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PDBsum entry 1pma

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protein Protein-protein interface(s) links
Protease PDB id
1pma
Jmol
Contents
Protein chains
(+ 8 more) 221 a.a. *
(+ 8 more) 203 a.a. *
* Residue conservation analysis
PDB id:
1pma
Name: Protease
Title: Proteasome from thermoplasma acidophilum
Structure: Proteasome. Chain: a, c, d, e, f, g, h, i, j, k, l, m, n, o. Synonym: prosome, multicatalytic protease, mcp, macropain. Engineered: yes. Proteasome. Chain: b, p, q, r, s, t, u, v, w, x, y, z, 1, 2. Synonym: prosome, multicatalytic protease, mcp, macropain. Engineered: yes
Source: Thermoplasma acidophilum. Organism_taxid: 2303. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: 28mer (from PQS)
Resolution:
3.40Å     R-factor:   0.221    
Authors: J.Loewe,D.Stock,B.Jap,P.Zwickl,W.Baumeister,R.Huber
Key ref: J.Löwe et al. (1995). Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science, 268, 533-539. PubMed id: 7725097 DOI: 10.1126/science.7725097
Date:
19-Dec-94     Release date:   20-Jun-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P25156  (PSA_THEAC) -  Proteasome subunit alpha
Seq:
Struc:
233 a.a.
221 a.a.
Protein chains
Pfam   ArchSchema ?
P28061  (PSB_THEAC) -  Proteasome subunit beta
Seq:
Struc:
211 a.a.
203 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2: E.C.3.4.25.1  - Proteasome endopeptidase complex.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleavage at peptide bonds with very broad specificity.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     proteasome complex   5 terms 
  Biological process     proteolysis   4 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1126/science.7725097 Science 268:533-539 (1995)
PubMed id: 7725097  
 
 
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
J.Löwe, D.Stock, B.Jap, P.Zwickl, W.Baumeister, R.Huber.
 
  ABSTRACT  
 
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23385464 S.O.Dahms, M.Kuester, C.Streb, C.Roth, N.Sträter, and M.E.Than (2013).
Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement.
  Acta Crystallogr D Biol Crystallogr, 69, 284-297.  
22183254 J.Maupin-Furlow (2012).
Proteasomes and protein conjugation across domains of life.
  Nat Rev Microbiol, 10, 100-111.  
21499243 A.R.Kusmierczyk, M.J.Kunjappu, R.Y.Kim, and M.Hochstrasser (2011).
A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding.
  Nat Struct Mol Biol, 18, 622-629.  
21335235 D.M.Smith, H.Fraga, C.Reis, G.Kafri, and A.L.Goldberg (2011).
ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle.
  Cell, 144, 526-538.  
21419622 F.A.Rey, and W.I.Sundquist (2011).
Macromolecular assemblages.
  Curr Opin Struct Biol, 21, 221-222.  
21111806 M.Gracanin, M.A.Lam, P.E.Morgan, K.J.Rodgers, C.L.Hawkins, and M.J.Davies (2011).
Amino acid, peptide, and protein hydroperoxides and their decomposition products modify the activity of the 26S proteasome.
  Free Radic Biol Med, 50, 389-399.  
21387143 N.Vigneron, and B.J.Van den Eynde (2011).
Insights into the processing of MHC class I ligands gained from the study of human tumor epitopes.
  Cell Mol Life Sci, 68, 1503-1520.  
20467919 X.Wang, S.Tu, J.Tan, T.Tian, L.Ran, J.F.Rodier, and G.Ren (2011).
REG gamma: a potential marker in breast cancer and effect on cell cycle and proliferation of breast cancer cell.
  Med Oncol, 28, 31-41.  
20814885 A.Baldisserotto, C.Franceschini, F.Scalambra, C.Trapella, M.Marastoni, F.Sforza, R.Gavioli, and R.Tomatis (2010).
Synthesis and proteasome inhibition of N-allyl vinyl ester-based peptides.
  J Pept Sci, 16, 659-663.  
20949307 A.M.Ruschak, A.Velyvis, and L.E.Kay (2010).
A simple strategy for ¹³C, ¹H labeling at the Ile-γ2 methyl position in highly deuterated proteins.
  J Biomol NMR, 48, 129-135.  
20944750 A.M.Ruschak, T.L.Religa, S.Breuer, S.Witt, and L.E.Kay (2010).
The proteasome antechamber maintains substrates in an unfolded state.
  Nature, 467, 868-871.  
20305655 B.G.Lee, E.Y.Park, K.E.Lee, H.Jeon, K.H.Sung, H.Paulsen, H.Rübsamen-Schaeff, H.Brötz-Oesterhelt, and H.K.Song (2010).
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.
  Nat Struct Mol Biol, 17, 471-478.
PDB codes: 3ktg 3kth 3kti 3ktj 3ktk
20676100 C.K.Chuang, B.Rockel, G.Seyit, P.J.Walian, A.M.Schönegge, J.Peters, P.H.Zwart, W.Baumeister, and B.K.Jap (2010).
Hybrid molecular structure of the giant protease tripeptidyl peptidase II.
  Nat Struct Mol Biol, 17, 990-996.
PDB code: 3lxu
20633347 D.Sheppard, R.Sprangers, and V.Tugarinov (2010).
Experimental approaches for NMR studies of side-chain dynamics in high-molecular-weight proteins.
  Prog Nucl Magn Reson Spectrosc, 56, 1.  
21125340 J.J.Driscoll, and R.Dechowdhury (2010).
Therapeutically targeting the SUMOylation, Ubiquitination and Proteasome pathways as a novel anticancer strategy.
  Target Oncol, 5, 281-289.  
20227375 K.Sadre-Bazzaz, F.G.Whitby, H.Robinson, T.Formosa, and C.P.Hill (2010).
Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
  Mol Cell, 37, 728-735.
PDB codes: 1vsy 3l5q
20010787 M.Groettrup, C.J.Kirk, and M.Basler (2010).
Proteasomes in immune cells: more than peptide producers?
  Nat Rev Immunol, 10, 73-78.  
20715286 M.Groll, N.Gallastegui, X.Maréchal, V.Le Ravalec, N.Basse, N.Richy, E.Genin, R.Huber, L.Moroder, J.Vidal, and M.Reboud-Ravaux (2010).
20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A.
  ChemMedChem, 5, 1701-1705.
PDB codes: 3nzj 3nzw 3nzx
20541423 N.Gallastegui, and M.Groll (2010).
The 26S proteasome: assembly and function of a destructive machine.
  Trends Biochem Sci, 35, 634-642.  
21098295 S.Bohn, F.Beck, E.Sakata, T.Walzthoeni, M.Beck, R.Aebersold, F.Förster, W.Baumeister, and S.Nickell (2010).
Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.
  Proc Natl Acad Sci U S A, 107, 20992-20997.  
20228196 S.E.Hensley, D.Zanker, B.P.Dolan, A.David, H.D.Hickman, A.C.Embry, C.N.Skon, K.M.Grebe, T.A.Griffin, W.Chen, J.R.Bennink, and J.W.Yewdell (2010).
Unexpected role for the immunoproteasome subunit LMP2 in antiviral humoral and innate immune responses.
  J Immunol, 184, 4115-4122.  
  20573219 S.Rothman (2010).
How is the balance between protein synthesis and degradation achieved?
  Theor Biol Med Model, 7, 25.  
20834233 S.S.Cha, Y.J.An, C.R.Lee, H.S.Lee, Y.G.Kim, S.J.Kim, K.K.Kwon, G.M.De Donatis, J.H.Lee, M.R.Maurizi, and S.G.Kang (2010).
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.
  EMBO J, 29, 3520-3530.
PDB code: 3k1j
20564558 T.Kinouchi, and N.Fujii (2010).
Structural consideration of mammalian D-aspartyl endopeptidase.
  Chem Biodivers, 7, 1403-1407.  
20360109 T.L.Religa, R.Sprangers, and L.E.Kay (2010).
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR.
  Science, 328, 98.
PDB codes: 2ku1 2ku2
20505154 X.Li, T.E.Wood, R.Sprangers, G.Jansen, N.E.Franke, X.Mao, X.Wang, Y.Zhang, S.E.Verbrugge, H.Adomat, Z.H.Li, S.Trudel, C.Chen, T.L.Religa, N.Jamal, H.Messner, J.Cloos, D.R.Rose, A.Navon, E.Guns, R.A.Batey, L.E.Kay, and A.D.Schimmer (2010).
Effect of noncompetitive proteasome inhibition on bortezomib resistance.
  J Natl Cancer Inst, 102, 1069-1082.  
20930034 Y.Xie (2010).
Structure, assembly and homeostatic regulation of the 26S proteasome.
  J Mol Cell Biol, 2, 308-317.  
20019667 Y.Yu, D.M.Smith, H.M.Kim, V.Rodriguez, A.L.Goldberg, and Y.Cheng (2010).
Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.
  EMBO J, 29, 692-702.
PDB code: 3ipm
19846313 A.K.Mittermaier, and L.E.Kay (2009).
Observing biological dynamics at atomic resolution using NMR.
  Trends Biochem Sci, 34, 601-611.  
19672456 A.M.Eleuteri, M.Amici, L.Bonfili, V.Cecarini, M.Cuccioloni, S.Grimaldi, L.Giuliani, M.Angeletti, and E.Fioretti (2009).
50 Hz extremely low frequency electromagnetic fields enhance protein carbonyl groups content in cancer cells: effects on proteasomal systems.
  J Biomed Biotechnol, 2009, 834239.  
19812037 A.Navon, and A.Ciechanover (2009).
The 26 S proteasome: from basic mechanisms to drug targeting.
  J Biol Chem, 284, 33713-33718.  
19067411 A.Visekruna, T.Joeris, N.Schmidt, M.Lawrenz, J.P.Ritz, H.J.Buhr, and U.Steinhoff (2009).
Comparative expression analysis and characterization of 20S proteasomes in human intestinal tissues: The proteasome pattern as diagnostic tool for IBD patients.
  Inflamm Bowel Dis, 15, 526-533.  
19841631 E.K.Schrader, K.G.Harstad, and A.Matouschek (2009).
Targeting proteins for degradation.
  Nat Chem Biol, 5, 815-822.  
19653995 F.Förster, K.Lasker, F.Beck, S.Nickell, A.Sali, and W.Baumeister (2009).
An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.
  Biochem Biophys Res Commun, 388, 228-233.  
19237538 F.I.Andersson, A.Tryggvesson, M.Sharon, A.V.Diemand, M.Classen, C.Best, R.Schmidt, J.Schelin, T.M.Stanne, B.Bukau, C.V.Robinson, S.Witt, A.Mogk, and A.K.Clarke (2009).
Structure and function of a novel type of ATP-dependent Clp protease.
  J Biol Chem, 284, 13519-13532.  
20041034 I.Lavelin, A.Beer, Z.Kam, V.Rotter, M.Oren, A.Navon, and B.Geiger (2009).
Discovery of novel proteasome inhibitors using a high-content cell-based screening system.
  PLoS One, 4, e8503.  
19821999 J.K.Agyin, B.Santhamma, H.B.Nair, S.S.Roy, and R.R.Tekmal (2009).
BU-32: a novel proteasome inhibitor for breast cancer.
  Breast Cancer Res, 11, R74.  
19483713 K.H.Darwin (2009).
Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis.
  Nat Rev Microbiol, 7, 485-491.  
19376868 M.A.Humbard, G.Zhou, and J.A.Maupin-Furlow (2009).
The N-terminal penultimate residue of 20S proteasome alpha1 influences its N(alpha) acetylation and protein levels as well as growth rate and stress responses of Haloferax volcanii.
  J Bacteriol, 191, 3794-3803.  
19006106 M.Cuccioloni, F.Montecchia, M.Amici, M.Mozzicafreddo, A.M.Eleuteri, and M.Angeletti (2009).
Co-chaperonin GroES as a modulator of proteasomal activity.
  J Mol Recognit, 22, 46-54.  
19109822 M.Groll, R.Huber, and L.Moroder (2009).
The persisting challenge of selective and specific proteasome inhibition.
  J Pept Sci, 15, 58-66.  
19363223 N.Medalia, A.Beer, P.Zwickl, O.Mihalache, M.Beck, O.Medalia, and A.Navon (2009).
Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase.
  J Biol Chem, 284, 22952-22960.  
19383601 P.Koodathingal, N.E.Jaffe, D.A.Kraut, S.Prakash, S.Fishbain, C.Herman, and A.Matouschek (2009).
ATP-dependent proteases differ substantially in their ability to unfold globular proteins.
  J Biol Chem, 284, 18674-18684.  
19580545 S.Liao, Q.Shang, X.Zhang, J.Zhang, C.Xu, and X.Tu (2009).
Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein.
  Biochem J, 422, 207-215.  
19165213 S.Murata, H.Yashiroda, and K.Tanaka (2009).
Molecular mechanisms of proteasome assembly.
  Nat Rev Mol Cell Biol, 10, 104-115.  
19581588 S.Nickell, F.Beck, S.H.Scheres, A.Korinek, F.Förster, K.Lasker, O.Mihalache, N.Sun, I.Nagy, A.Sali, J.M.Plitzko, J.M.Carazo, M.Mann, and W.Baumeister (2009).
Insights into the molecular architecture of the 26S proteasome.
  Proc Natl Acad Sci U S A, 106, 11943-11947.  
19254626 S.V.Rajkumar (2009).
Multiple myeloma.
  Curr Probl Cancer, 33, 7.  
19440739 S.Zhang, Y.Shi, H.Jin, Z.Liu, L.Zhang, and L.Zhang (2009).
Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: docking and molecular dynamics study.
  J Mol Model, 15, 1481-1490.  
  20047011 V.Milacic, and Q.P.Dou (2009).
The tumor proteasome as a novel target for gold(III) complexes: implications for breast cancer therapy.
  Coord Chem Rev, 253, 1649-1660.  
19022674 W.Fenical, P.R.Jensen, M.A.Palladino, K.S.Lam, G.K.Lloyd, and B.C.Potts (2009).
Discovery and development of the anticancer agent salinosporamide A (NPI-0052).
  Bioorg Med Chem, 17, 2175-2180.  
18754030 X.Mao, X.Li, R.Sprangers, X.Wang, A.Venugopal, T.Wood, Y.Zhang, D.A.Kuntz, E.Coe, S.Trudel, D.Rose, R.A.Batey, L.E.Kay, and A.D.Schimmer (2009).
Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma.
  Leukemia, 23, 585-590.  
19286367 Y.Cheng (2009).
Toward an atomic model of the 26S proteasome.
  Curr Opin Struct Biol, 19, 203-208.  
19500299 Y.Sonoda, K.Sako, Y.Maki, N.Yamazaki, H.Yamamoto, A.Ikeda, and J.Yamaguchi (2009).
Regulation of leaf organ size by the Arabidopsis RPT2a 19S proteasome subunit.
  Plant J, 60, 68-78.  
19915655 A.Bashan, and A.Yonath (2008).
The linkage between ribosomal crystallography, metal ions, heteropolytungstates and functional flexibility.
  J Mol Struct, 890, 289-294.  
18644121 A.U.Chouduri, T.Tokumoto, H.Dohra, T.Ushimaru, and S.Yamada (2008).
Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1.
  BMC Biochem, 9, 20.  
18656549 B.S.Moore, A.S.Eustáquio, and R.P.McGlinchey (2008).
Advances in and applications of proteasome inhibitors.
  Curr Opin Chem Biol, 12, 434-440.  
18186020 C.Chen, C.Huang, S.Chen, J.Liang, W.Lin, G.Ke, H.Zhang, B.Wang, J.Huang, Z.Han, L.Ma, K.Huo, X.Yang, P.Yang, F.He, and T.Tao (2008).
Subunit-subunit interactions in the human 26S proteasome.
  Proteomics, 8, 508-520.  
  18678936 E.Alexopoulos, U.Kanjee, J.Snider, W.A.Houry, and E.F.Pai (2008).
Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 700-706.  
18957208 F.Kriegenburg, M.Seeger, Y.Saeki, K.Tanaka, A.M.Lauridsen, R.Hartmann-Petersen, and K.B.Hendil (2008).
Mammalian 26S proteasomes remain intact during protein degradation.
  Cell, 135, 355-365.  
18829465 G.Lin, C.Tsu, L.Dick, X.K.Zhou, and C.Nathan (2008).
Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-acetyl tripeptide substrates.
  J Biol Chem, 283, 34423-34431.  
18931121 G.Zhou, D.Kowalczyk, M.A.Humbard, S.Rohatgi, and J.A.Maupin-Furlow (2008).
Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii.
  J Bacteriol, 190, 8096-8105.  
18292891 H.S.Lim, C.T.Archer, Y.C.Kim, T.Hutchens, and T.Kodadek (2008).
Rapid identification of the pharmacophore in a peptoid inhibitor of the proteasome regulatory particle.
  Chem Commun (Camb), (), 1064-1066.  
18505737 J.Chugh, S.Sharma, and R.V.Hosur (2008).
NMR insights into a megadalton-size protein self-assembly.
  Protein Sci, 17, 1319-1325.  
18482702 J.Hines, M.Groll, M.Fahnestock, and C.M.Crews (2008).
Proteasome inhibition by fellutamide B induces nerve growth factor synthesis.
  Chem Biol, 15, 501-512.
PDB code: 3d29
18500392 J.J.Chen, F.Lin, and Z.H.Qin (2008).
The roles of the proteasome pathway in signal transduction and neurodegenerative diseases.
  Neurosci Bull, 24, 183-194.  
18697939 J.Jiang, X.Zhang, Y.Chen, Y.Wu, Z.H.Zhou, Z.Chang, and S.F.Sui (2008).
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.
  Proc Natl Acad Sci U S A, 105, 11939-11944.  
18471981 J.Rabl, D.M.Smith, Y.Yu, S.C.Chang, A.L.Goldberg, and Y.Cheng (2008).
Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases.
  Mol Cell, 30, 360-368.
PDB codes: 3c91 3c92
  18931431 K.Felderer, M.Groves, J.Diez, E.Pohl, and S.Witt (2008).
Crystallization and preliminary X-ray analysis of the Thermoplasma acidophilum 20S proteasome in complex with protein substrates.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 899-902.  
18323626 K.Michalska, D.Borek, A.Hernández-Santoyo, and M.Jaskolski (2008).
Crystal packing of plant-type L-asparaginase from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 64, 309-320.
PDB codes: 1jn9 1k2x 2zak
18816064 L.D.Jennings, J.Bohon, M.R.Chance, and S.Licht (2008).
The ClpP N-terminus coordinates substrate access with protease active site reactivity.
  Biochemistry, 47, 11031-11040.  
  19802337 M.Gaczynska, and P.A.Osmulski (2008).
AFM of biological complexes: what can we learn?
  Curr Opin Colloid Interface Sci, 13, 351-367.  
18928262 M.Groll, E.P.Balskus, and E.N.Jacobsen (2008).
Structural analysis of spiro beta-lactone proteasome inhibitors.
  J Am Chem Soc, 130, 14981-14983.
PDB codes: 3dy3 3dy4
18824507 O.D.Ekici, M.Paetzel, and R.E.Dalbey (2008).
Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
  Protein Sci, 17, 2023-2037.  
18786393 P.C.Ramos, and R.J.Dohmen (2008).
PACemakers of proteasome core particle assembly.
  Structure, 16, 1296-1304.  
18534977 P.C.da Fonseca, and E.P.Morris (2008).
Structure of the human 26S proteasome: subunit radial displacements open the gate into the proteolytic core.
  J Biol Chem, 283, 23305-23314.  
18389302 R.E.Valas, and P.E.Bourne (2008).
Rethinking proteasome evolution: two novel bacterial proteasomes.
  J Mol Evol, 66, 494-504.  
18224667 W.Ma, H.Kantarjian, S.O'Brien, I.Jilani, X.Zhang, Z.Estrov, A.Ferrajoli, M.Keating, F.Giles, and M.Albitar (2008).
Enzymatic activity of circulating proteasomes correlates with clinical behavior in patients with chronic lymphocytic leukemia.
  Cancer, 112, 1306-1312.  
18578501 Y.Shen, K.K.Hixson, N.Tolić, D.G.Camp, S.O.Purvine, R.J.Moore, and R.D.Smith (2008).
Mass spectrometry analysis of proteome-wide proteolytic post-translational degradation of proteins.
  Anal Chem, 80, 5819-5828.  
17612489 A.Martin, T.A.Baker, and R.T.Sauer (2007).
Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.
  Mol Cell, 27, 41-52.  
18654266 A.Tinazli, J.Piehler, M.Beuttler, R.Guckenberger, and R.Tampé (2007).
Native protein nanolithography that can write, read and erase.
  Nat Nanotechnol, 2, 220-225.  
18075576 C.V.Robinson, A.Sali, and W.Baumeister (2007).
The molecular sociology of the cell.
  Nature, 450, 973-982.  
17803938 D.M.Smith, S.C.Chang, S.Park, D.Finley, Y.Cheng, and A.L.Goldberg (2007).
Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry.
  Mol Cell, 27, 731-744.  
17411433 J.B.Pereira-Leal, E.D.Levy, C.Kamp, and S.A.Teichmann (2007).
Evolution of protein complexes by duplication of homomeric interactions.
  Genome Biol, 8, R51.  
17455294 J.M.Hunter, M.Lesort, and G.V.Johnson (2007).
Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease.
  J Neurosci Res, 85, 1774-1788.  
17544279 K.Osanai, K.R.Landis-Piwowar, Q.P.Dou, and T.H.Chan (2007).
A para-amino substituent on the D-ring of green tea polyphenol epigallocatechin-3-gallate as a novel proteasome inhibitor and cancer cell apoptosis inducer.
  Bioorg Med Chem, 15, 5076-5082.  
17696779 L.Borissenko, and M.Groll (2007).
Diversity of proteasomal missions: fine tuning of the immune response.
  Biol Chem, 388, 947-955.  
17114253 L.S.Madding, J.K.Michel, K.R.Shockley, S.B.Conners, K.L.Epting, M.R.Johnson, and R.M.Kelly (2007).
Role of the beta1 subunit in the function and stability of the 20S proteasome in the hyperthermophilic archaeon Pyrococcus furiosus.
  J Bacteriol, 189, 583-590.  
17518699 M.Katsiki, N.Chondrogianni, I.Chinou, A.J.Rivett, and E.S.Gonos (2007).
The olive constituent oleuropein exhibits proteasome stimulatory properties in vitro and confers life span extension of human embryonic fibroblasts.
  Rejuvenation Res, 10, 157-172.  
17390294 O.Drews, C.Zong, and P.Ping (2007).
Exploring proteasome complexes by proteomic approaches.
  Proteomics, 7, 1047-1058.  
17103119 P.Voss, and T.Grune (2007).
The nuclear proteasome and the degradation of oxidatively damaged proteins.
  Amino Acids, 32, 527-534.  
17762877 R.Sprangers, A.Velyvis, and L.E.Kay (2007).
Solution NMR of supramolecular complexes: providing new insights into function.
  Nat Methods, 4, 697-703.  
17237764 R.Sprangers, and L.E.Kay (2007).
Quantitative dynamics and binding studies of the 20S proteasome by NMR.
  Nature, 445, 618-622.  
17960736 R.Weerasekera, Y.M.She, K.A.Markham, Y.Bai, N.Opalka, S.Orlicky, F.Sicheri, T.Kislinger, and G.Schmitt-Ulms (2007).
Interactome and interface protocol (2IP): a novel strategy for high sensitivity topology mapping of protein complexes.
  Proteomics, 7, 3835-3852.  
17941820 X.Wang, C.Guerrero, P.Kaiser, and L.Huang (2007).
Proteomics of proteasome complexes and ubiquitinated proteins.
  Expert Rev Proteomics, 4, 649-665.  
17462577 Y.K.Ho, P.Bargagna-Mohan, M.Wehenkel, R.Mohan, and K.B.Kim (2007).
LMP2-specific inhibitors: chemical genetic tools for proteasome biology.
  Chem Biol, 14, 419-430.  
17292836 Y.Nakamura, K.Nakano, T.Umehara, M.Kimura, Y.Hayashizaki, A.Tanaka, M.Horikoshi, B.Padmanabhan, and S.Yokoyama (2007).
Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome.
  Structure, 15, 179-189.
PDB codes: 2dvw 2dwz
  17329811 Y.Nakamura, T.Umehara, A.Tanaka, M.Horikoshi, B.Padmanabhan, and S.Yokoyama (2007).
Purification, crystallization and preliminary X-ray diffraction analysis of the non-ATPase subunit Nas6 in complex with the ATPase subunit Rpt3 of the 26S proteasome from Saccharomyces cerevisiae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 190-192.  
17157318 Y.Wang, and H.C.Guo (2007).
Crystallographic snapshot of a productive glycosylasparaginase-substrate complex.
  J Mol Biol, 366, 82-92.
PDB code: 2gl9
16321849 C.Bogner, C.Peschel, and T.Decker (2006).
Targeting the proteasome in mantle cell lymphoma: a promising therapeutic approach.
  Leuk Lymphoma, 47, 195-205.  
19617921 C.García-Echeverría (2006).
Peptide and Peptide-Like Modulators of 20S Proteasome Enzymatic Activity in Cancer Cells.
  Int J Pept Res Ther, 12, 49-64.  
16595883 D.Nandi, P.Tahiliani, A.Kumar, and D.Chandu (2006).
The ubiquitin-proteasome system.
  J Biosci, 31, 137-155.  
16487051 D.Poppek, and T.Grune (2006).
Proteasomal defense of oxidative protein modifications.
  Antioxid Redox Signal, 8, 173-184.  
17112313 E.D.Levy, J.B.Pereira-Leal, C.Chothia, and S.A.Teichmann (2006).
3D complex: a structural classification of protein complexes.
  PLoS Comput Biol, 2, e155.  
16713559 E.Lorentzen, and E.Conti (2006).
The exosome and the proteasome: nano-compartments for degradation.
  Cell, 125, 651-654.  
16468986 G.Hu, G.Lin, M.Wang, L.Dick, R.M.Xu, C.Nathan, and H.Li (2006).
Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate.
  Mol Microbiol, 59, 1417-1428.
PDB codes: 2fhg 2fhh
16468985 G.Lin, G.Hu, C.Tsu, Y.Z.Kunes, H.Li, L.Dick, T.Parsons, P.Li, Z.Chen, P.Zwickl, N.Weich, and C.Nathan (2006).
Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity.
  Mol Microbiol, 59, 1405-1416.  
16819825 H.Frase, J.Hudak, and I.Lee (2006).
Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease.
  Biochemistry, 45, 8264-8274.  
16222703 H.X.Wang, H.M.Wang, H.Y.Lin, Q.Yang, H.Zhang, B.K.Tsang, and C.Zhu (2006).
Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line.
  J Cell Physiol, 206, 616-623.  
16952374 J.Iwanczyk, K.Sadre-Bazzaz, K.Ferrell, E.Kondrashkina, T.Formosa, C.P.Hill, and J.Ortega (2006).
Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes.
  J Mol Biol, 363, 648-659.  
16446446 J.K.Kim, I.S.Yang, H.J.Shin, K.J.Cho, E.K.Ryu, S.H.Kim, S.S.Park, and K.H.Kim (2006).
Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
  Proc Natl Acad Sci U S A, 103, 1732-1737.
PDB codes: 2adv 2ae3 2ae4 2ae5
17008720 J.Wang, and E.R.Kantrowitz (2006).
Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine.
  Protein Sci, 15, 2395-2401.
PDB codes: 2g9y 2ga3
16858705 K.Schulze, A.Mulder, A.Tinazli, and R.Tampé (2006).
Controlling the activity of the 20S proteasome complex by synthetic gatekeepers.
  Angew Chem Int Ed Engl, 45, 5702-5705.  
16601692 M.A.Hoyt, J.Zich, J.Takeuchi, M.Zhang, C.Govaerts, and P.Coffino (2006).
Glycine-alanine repeats impair proper substrate unfolding by the proteasome.
  EMBO J, 25, 1720-1729.  
16950923 M.A.Humbard, S.M.Stevens, and J.A.Maupin-Furlow (2006).
Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii.
  J Bacteriol, 188, 7521-7530.  
16531229 M.Groll, C.R.Berkers, H.L.Ploegh, and H.Ovaa (2006).
Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome.
  Structure, 14, 451-456.
PDB code: 2f16
16537370 M.Groll, O.V.Larionov, R.Huber, and A.de Meijere (2006).
Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation.
  Proc Natl Acad Sci U S A, 103, 4576-4579.
PDB codes: 2fny 3e47
16402903 P.M.Voorhees, and R.Z.Orlowski (2006).
The proteasome and proteasome inhibitors in cancer therapy.
  Annu Rev Pharmacol Toxicol, 46, 189-213.  
16549793 P.Osterloh, K.Linkemann, S.Tenzer, H.G.Rammensee, M.P.Radsak, D.H.Busch, and H.Schild (2006).
Proteasomes shape the repertoire of T cells participating in antigen-specific immune responses.
  Proc Natl Acad Sci U S A, 103, 5042-5047.  
16987959 T.Shibatani, E.J.Carlson, F.Larabee, A.L.McCormack, K.Früh, and W.R.Skach (2006).
Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes.
  Mol Biol Cell, 17, 4962-4971.  
16672242 T.T.Baird, W.D.Wright, and C.S.Craik (2006).
Conversion of trypsin to a functional threonine protease.
  Protein Sci, 15, 1229-1238.  
16877706 T.V.Rotanova, I.Botos, E.E.Melnikov, F.Rasulova, A.Gustchina, M.R.Maurizi, and A.Wlodawer (2006).
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
  Protein Sci, 15, 1815-1828.  
16459078 W.Chiu, M.L.Baker, and S.C.Almo (2006).
Structural biology of cellular machines.
  Trends Cell Biol, 16, 144-150.  
15991207 A.Tinazli, J.Tang, R.Valiokas, S.Picuric, S.Lata, J.Piehler, B.Liedberg, and R.Tampé (2005).
High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies.
  Chemistry, 11, 5249-5259.  
15892698 B.B.Boonyaratanakornkit, A.J.Simpson, T.A.Whitehead, C.M.Fraser, N.M.El-Sayed, and D.S.Clark (2005).
Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock.
  Environ Microbiol, 7, 789-797.  
  17491658 C.Sia, and M.Weinem (2005).
Genetic susceptibility to type 1 diabetes in the intracellular pathway of antigen processing - a subject review and cross-study comparison.
  Rev Diabet Stud, 2, 40-52.  
16337593 D.M.Smith, G.Kafri, Y.Cheng, D.Ng, T.Walz, and A.L.Goldberg (2005).
ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins.
  Mol Cell, 20, 687-698.  
15665121 F.Luciani, C.Keşmir, M.Mishto, M.Or-Guil, and R.J.de Boer (2005).
A mathematical model of protein degradation by the proteasome.
  Biophys J, 88, 2422-2432.  
15790562 F.Shang, G.Deng, Q.Liu, W.Guo, A.L.Haas, B.Crosas, D.Finley, and A.Taylor (2005).
Lys6-modified ubiquitin inhibits ubiquitin-dependent protein degradation.
  J Biol Chem, 280, 20365-20374.  
16204847 I.Res, and O.Lichtarge (2005).
Character and evolution of protein-protein interfaces.
  Phys Biol, 2, S36-S43.  
16216576 J.A.Khan, B.M.Dunn, and L.Tong (2005).
Crystal structure of human Taspase1, a crucial protease regulating the function of MLL.
  Structure, 13, 1443-1452.
PDB codes: 2a8i 2a8j 2a8l 2a8m
15914020 J.A.Loo, B.Berhane, C.S.Kaddis, K.M.Wooding, Y.Xie, S.L.Kaufman, and I.V.Chernushevich (2005).
Electrospray ionization mass spectrometry and ion mobility analysis of the 20S proteasome complex.
  J Am Soc Mass Spectrom, 16, 998.  
15586024 J.M.Holzbeierlein, J.McIntosh, and J.B.Thrasher (2005).
The role of soy phytoestrogens in prostate cancer.
  Curr Opin Urol, 15, 17-22.  
15759099 K.Hanada, and J.C.Yang (2005).
Novel biochemistry: post-translational protein splicing and other lessons from the school of antigen processing.
  J Mol Med, 83, 420-428.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
15653075 M.Rechsteiner, and C.P.Hill (2005).
Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors.
  Trends Cell Biol, 15, 27-33.  
15837189 P.A.Leong, J.B.Heymann, and G.J.Jensen (2005).
Peach: a simple Perl-based system for distributed computation and its application to cryo-EM data processing.
  Structure, 13, 505-511.  
15757458 P.P.Klinger, and U.Schubert (2005).
The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy.
  Expert Rev Anti Infect Ther, 3, 61-79.  
16263929 R.Sprangers, A.Gribun, P.M.Hwang, W.A.Houry, and L.E.Kay (2005).
Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release.
  Proc Natl Acad Sci U S A, 102, 16678-16683.  
15766539 S.Dutta, and H.M.Berman (2005).
Large macromolecular complexes in the Protein Data Bank: a status report.
  Structure, 13, 381-388.  
16181327 T.A.Groothuis, A.C.Griekspoor, J.J.Neijssen, C.A.Herberts, and J.J.Neefjes (2005).
MHC class I alleles and their exploration of the antigen-processing machinery.
  Immunol Rev, 207, 60-76.  
15608126 W.Baumeister, and W.Baumeister (2005).
A voyage to the inner space of cells.
  Protein Sci, 14, 257-269.  
15312912 A.N.Hegde (2004).
Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity.
  Prog Neurobiol, 73, 311-357.  
14990998 C.M.Pickart, and R.E.Cohen (2004).
Proteasomes and their kin: proteases in the machine age.
  Nat Rev Mol Cell Biol, 5, 177-187.  
15201202 H.X.Wang, H.M.Wang, Q.L.Li, H.Y.Lin, D.Qian, and C.Zhu (2004).
Expression of proteasome subunits low molecular mass polypeptide (LMP) 2 and LMP7 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy.
  Biol Reprod, 71, 1317-1324.  
14739934 I.Velichutina, P.L.Connerly, C.S.Arendt, X.Li, and M.Hochstrasser (2004).
Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast.
  EMBO J, 23, 500-510.  
15368577 M.Kaiser, M.Groll, C.Siciliano, I.Assfalg-Machleidt, E.Weyher, J.Kohno, A.G.Milbradt, C.Renner, R.Huber, and L.Moroder (2004).
Binding mode of TMC-95A analogues to eukaryotic 20S proteasome.
  Chembiochem, 5, 1256-1266.  
15155224 M.Korsinczky, K.Fischer, N.Chen, J.Baker, K.Rieckmann, and Q.Cheng (2004).
Sulfadoxine resistance in Plasmodium vivax is associated with a specific amino acid in dihydropteroate synthase at the putative sulfadoxine-binding site.
  Antimicrob Agents Chemother, 48, 2214-2222.  
15233904 O.A.O'Connor (2004).
The emerging role of bortezomib in the treatment of indolent non-Hodgkin's and mantle cell lymphomas.
  Curr Treat Options Oncol, 5, 269-281.  
15105483 P.Cresswell (2004).
Cell biology. Cutting and pasting antigenic peptides.
  Science, 304, 525-527.  
15193311 R.B.Russell, F.Alber, P.Aloy, F.P.Davis, D.Korkin, M.Pichaud, M.Topf, and A.Sali (2004).
A structural perspective on protein-protein interactions.
  Curr Opin Struct Biol, 14, 313-324.  
15454077 R.T.Sauer, D.N.Bolon, B.M.Burton, R.E.Burton, J.M.Flynn, R.A.Grant, G.L.Hersch, S.A.Joshi, J.A.Kenniston, I.Levchenko, S.B.Neher, E.S.Oakes, S.M.Siddiqui, D.A.Wah, and T.A.Baker (2004).
Sculpting the proteome with AAA(+) proteases and disassembly machines.
  Cell, 119, 9.  
15175655 S.Hutschenreiter, A.Tinazli, K.Model, and R.Tampé (2004).
Two-substrate association with the 20S proteasome at single-molecule level.
  EMBO J, 23, 2488-2497.  
15361411 S.Mullapudi, L.Pullan, O.T.Bishop, H.Khalil, J.K.Stoops, R.Beckmann, P.M.Kloetzel, E.Krüger, and P.A.Penczek (2004).
Rearrangement of the 16S precursor subunits is essential for the formation of the active 20S proteasome.
  Biophys J, 87, 4098-4105.  
12941688 A.Förster, F.G.Whitby, and C.P.Hill (2003).
The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation.
  EMBO J, 22, 4356-4364.  
12581666 A.Matouschek (2003).
Protein unfolding--an important process in vivo?
  Curr Opin Struct Biol, 13, 98.  
12606569 C.Hirsch, D.Blom, and H.L.Ploegh (2003).
A role for N-glycanase in the cytosolic turnover of glycoproteins.
  EMBO J, 22, 1036-1046.  
12554931 D.Turk, and G.Guncar (2003).
Lysosomal cysteine proteases (cathepsins): promising drug targets.
  Acta Crystallogr D Biol Crystallogr, 59, 203-213.  
14633979 F.Schmitzberger, M.L.Kilkenny, C.M.Lobley, M.E.Webb, M.Vinkovic, D.Matak-Vinkovic, M.Witty, D.Y.Chirgadze, A.G.Smith, C.Abell, and T.L.Blundell (2003).
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.
  EMBO J, 22, 6193-6204.
PDB codes: 1ppy 1pqe 1pqf 1pqh 1pt0 1pt1 1pyq 1pyu
12930990 H.B.Olsen, M.R.Leuenberger-Fisher, W.Kadima, D.Borchardt, N.C.Kaarsholm, and M.F.Dunn (2003).
Structural signatures of the complex formed between 3-nitro-4-hydroxybenzoate and the Zn(II)-substituted R(6) insulin hexamer.
  Protein Sci, 12, 1902-1913.  
12948749 J.A.Maupin-Furlow, S.J.Kaczowka, C.J.Reuter, K.Zuobi-Hasona, and M.A.Gil (2003).
Archaeal proteasomes: potential in metabolic engineering.
  Metab Eng, 5, 151-163.  
12861018 J.Lundgren, P.Masson, C.A.Realini, and P.Young (2003).
Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13.
  Mol Cell Biol, 23, 5320-5330.  
12717035 J.Pei, and N.V.Grishin (2003).
Peptidase family U34 belongs to the superfamily of N-terminal nucleophile hydrolases.
  Protein Sci, 12, 1131-1135.  
12672453 M.Groll, and R.Huber (2003).
Substrate access and processing by the 20S proteasome core particle.
  Int J Biochem Cell Biol, 35, 606-616.  
14675543 M.Groll, and T.Clausen (2003).
Molecular shredders: how proteasomes fulfill their role.
  Curr Opin Struct Biol, 13, 665-673.  
12532325 M.Lu, R.P.Kitson, Y.Xue, and R.H.Goldfarb (2003).
Activation of multiple caspases and modification of cell surface fas (CD95) in proteasome inhibitor-induced apoptosis of rat natural killer cells.
  J Cell Biochem, 88, 482-492.  
12952558 S.B.Cannon, and N.D.Young (2003).
OrthoParaMap: distinguishing orthologs from paralogs by integrating comparative genome data and gene phylogenies.
  BMC Bioinformatics, 4, 35.  
12486053 S.J.Kaczowka, and J.A.Maupin-Furlow (2003).
Subunit topology of two 20S proteasomes from Haloferax volcanii.
  J Bacteriol, 185, 165-174.  
12794861 Z.Q.Yang, B.H.Kwok, S.Lin, M.A.Koldobskiy, C.M.Crews, and S.J.Danishefsky (2003).
Simplified synthetic TMC-95A/B analogues retain the potency of proteasome inhibitory activity.
  Chembiochem, 4, 508-513.  
12061900 A.R.Bahrami, R.Bastow, S.Rolfe, C.Price, and J.E.Gray (2002).
A role for nuclear localised proteasomes in mediating auxin action.
  Plant J, 30, 691-698.  
12391313 A.S.Frangakis, J.Böhm, F.Förster, S.Nickell, D.Nicastro, D.Typke, R.Hegerl, and W.Baumeister (2002).
Identification of macromolecular complexes in cryoelectron tomograms of phantom cells.
  Proc Natl Acad Sci U S A, 99, 14153-14158.  
  15803659 B.Franzetti, G.Schoehn, D.Garcia, R.W.Ruigrok, and G.Zaccai (2002).
Characterization of the proteasome from the extremely halophilic archaeon Haloarcula marismortui.
  Archaea, 1, 53-61.  
  15803660 D.E.Ward, K.R.Shockley, L.S.Chang, R.D.Levy, J.K.Michel, S.B.Conners, and R.M.Kelly (2002).
Proteolysis in hyperthermophilic microorganisms.
  Archaea, 1, 63-74.  
12153514 G.A.Enders (2002).
Mechanism of antigen presentation after hypertonic loading of soluble antigens.
  Immunology, 106, 511-516.  
12200039 G.Carrard, A.L.Bulteau, I.Petropoulos, and B.Friguet (2002).
Impairment of proteasome structure and function in aging.
  Int J Biochem Cell Biol, 34, 1461-1474.  
12133726 J.Adams (2002).
Preclinical and clinical evaluation of proteasome inhibitor PS-341 for the treatment of cancer.
  Curr Opin Chem Biol, 6, 493-500.  
12181345 M.Lafarga, M.T.Berciano, E.Pena, I.Mayo, J.G.Castaño, D.Bohmann, J.P.Rodrigues, J.P.Tavanez, and M.Carmo-Fonseca (2002).
Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, ubiquitin, and protein substrates of proteasome.
  Mol Biol Cell, 13, 2771-2782.  
12009902 M.R.Harpel, K.Y.Horiuchi, Y.Luo, L.Shen, W.Jiang, D.J.Nelson, K.C.Rogers, C.P.Decicco, and R.A.Copeland (2002).
Mutagenesis and mechanism-based inhibition of Streptococcus pyogenes Glu-tRNAGln amidotransferase implicate a serine-based glutaminase site.
  Biochemistry, 41, 6398-6407.  
12033938 P.A.Osmulski, and M.Gaczynska (2002).
Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition.
  Biochemistry, 41, 7047-7053.  
12374735 P.Goettig, M.Groll, J.S.Kim, R.Huber, and H.Brandstetter (2002).
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism.
  EMBO J, 21, 5343-5352.
PDB codes: 1mt3 1mtz 1mu0
12361801 R.A.Dunlop, K.J.Rodgers, and R.T.Dean (2002).
Recent developments in the intracellular degradation of oxidized proteins.
  Free Radic Biol Med, 33, 894-906.  
12169602 S.Chiba, Y.Akiyama, and K.Ito (2002).
Membrane protein degradation by FtsH can be initiated from either end.
  J Bacteriol, 184, 4775-4782.  
11919638 T.Krojer, M.Garrido-Franco, R.Huber, M.Ehrmann, and T.Clausen (2002).
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.
  Nature, 416, 455-459.
PDB code: 1ky9
12093752 V.Ustrell, L.Hoffman, G.Pratt, and M.Rechsteiner (2002).
PA200, a nuclear proteasome activator involved in DNA repair.
  EMBO J, 21, 3516-3525.  
11485623 A.D.Kelleher, B.L.Booth, A.K.Sewell, A.Oxenius, V.Cerundolo, A.J.McMichael, R.E.Phillips, and D.A.Price (2001).
Effects of retroviral protease inhibitors on proteasome function and processing of HIV-derived MHC class I-restricted cytotoxic T lymphocyte epitopes.
  AIDS Res Hum Retroviruses, 17, 1063-1066.  
11514224 A.F.Kisselev, and A.L.Goldberg (2001).
Proteasome inhibitors: from research tools to drug candidates.
  Chem Biol, 8, 739-758.  
11779508 A.Navon, and A.L.Goldberg (2001).
Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome.
  Mol Cell, 8, 1339-1349.  
11228406 B.J.Van den Eynde, and S.Morel (2001).
Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome.
  Curr Opin Immunol, 13, 147-153.  
11564559 B.M.Kessler, D.Tortorella, M.Altun, A.F.Kisselev, E.Fiebiger, B.G.Hekking, H.L.Ploegh, and H.S.Overkleeft (2001).
Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits.
  Chem Biol, 8, 913-929.  
11336713 C.Gieffers, P.Dube, J.R.Harris, H.Stark, and J.M.Peters (2001).
Three-dimensional structure of the anaphase-promoting complex.
  Mol Cell, 7, 907-913.  
11463387 C.Lee, M.P.Schwartz, S.Prakash, M.Iwakura, and A.Matouschek (2001).
ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal.
  Mol Cell, 7, 627-637.  
11726493 D.Turk, V.Janjić, I.Stern, M.Podobnik, D.Lamba, S.W.Dahl, C.Lauritzen, J.Pedersen, V.Turk, and B.Turk (2001).
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases.
  EMBO J, 20, 6570-6582.
PDB code: 1k3b
11170428 J.L.de Diego, J.M.Katz, P.Marshall, B.Gutiérrez, J.E.Manning, V.Nussenzweig, and J.González (2001).
The ubiquitin-proteasome pathway plays an essential role in proteolysis during Trypanosoma cruzi remodeling.
  Biochemistry, 40, 1053-1062.  
11295500 J.Li, and M.Rechsteiner (2001).
Molecular dissection of the 11S REG (PA28) proteasome activators.
  Biochimie, 83, 373-383.  
11432824 J.Li, X.Gao, J.Ortega, T.Nazif, L.Joss, M.Bogyo, A.C.Steven, and M.Rechsteiner (2001).
Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta.
  EMBO J, 20, 3359-3369.  
11410931 J.Myung, K.B.Kim, and C.M.Crews (2001).
The ubiquitin-proteasome pathway and proteasome inhibitors.
  Med Res Rev, 21, 245-273.  
11709174 J.Wang, J.J.Song, I.S.Seong, M.C.Franklin, S.Kamtekar, S.H.Eom, and C.H.Chung (2001).
Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU.
  Structure, 9, 1107-1116.
PDB codes: 1hqy 1ht1 1ht2
11250202 J.Wang, J.J.Song, M.C.Franklin, S.Kamtekar, Y.J.Im, S.H.Rho, I.S.Seong, C.S.Lee, C.H.Chung, and S.H.Eom (2001).
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism.
  Structure, 9, 177-184.
PDB codes: 1g4a 1g4b
11717526 M.C.Sousa, and D.B.McKay (2001).
Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
  Acta Crystallogr D Biol Crystallogr, 57, 1950-1954.
PDB code: 1jjw
11241606 M.Ziegler, J.J.Miranda, U.N.Andersen, D.W.Johnson, J.A.Leary, and K.N.Raymond (2001).
Combinatorial Libraries of Metal-Ligand Assemblies with an Encapsulated Guest Molecule Coordination Number Incommensurate Cluster Formation, Part 17. Financial support of this work was provided by NSF CHE-9709621 and a NATO-NSF exchange grant SRG 951516. We thank the Miller Foundation for a fellowship to M.Z. Part 16: R. M. Yeh, M. Ziegler, D. W. Johnson, A. J. Terpin, K. N. Raymond, Inorg. Chem. 2001, in press.
  Angew Chem Int Ed Engl, 40, 733-736.  
11295491 N.Benaroudj, E.Tarcsa, P.Cascio, and A.L.Goldberg (2001).
The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes.
  Biochimie, 83, 311-318.  
11325937 R.A.Larsen, T.M.Knox, and C.G.Miller (2001).
Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium.
  J Bacteriol, 183, 3089-3097.  
11514679 R.J.Frankenberg, T.S.Hsu, H.Yakota, R.Kim, and D.S.Clark (2001).
Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome.
  Protein Sci, 10, 1887-1896.  
11590019 S.J.Russell, F.Gonzalez, L.Joshua-Tor, and S.A.Johnston (2001).
Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases.
  Chem Biol, 8, 941-950.  
11287666 T.Ishikawa, F.Beuron, M.Kessel, S.Wickner, M.R.Maurizi, and A.C.Steven (2001).
Translocation pathway of protein substrates in ClpAP protease.
  Proc Natl Acad Sci U S A, 98, 4328-4333.  
11514661 W.A.Breyer, and B.W.Matthews (2001).
A structural basis for processivity.
  Protein Sci, 10, 1699-1711.  
11016885 A.J.Rivett, and R.C.Gardner (2000).
Proteasome inhibitors: from in vitro uses to clinical trials.
  J Pept Sci, 6, 478-488.  
10673442 C.Bompard-Gilles, V.Villeret, G.J.Davies, L.Fanuel, B.Joris, J.M.Frère, and J.Van Beeumen (2000).
A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi.
  Structure, 8, 153-162.
PDB code: 1b65
  11206054 C.Oinonen, and J.Rouvinen (2000).
Structural comparison of Ntn-hydrolases.
  Protein Sci, 9, 2329-2337.  
10940245 D.S.Goodsell, and A.J.Olson (2000).
Structural symmetry and protein function.
  Annu Rev Biophys Biomol Struct, 29, 105-153.  
10954757 E.W.Wang, B.M.Kessler, A.Borodovsky, B.F.Cravatt, M.Bogyo, H.L.Ploegh, and R.Glas (2000).
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
  Proc Natl Acad Sci U S A, 97, 9990-9995.  
11114186 H.K.Song, C.Hartmann, R.Ramachandran, M.Bochtler, R.Behrendt, L.Moroder, and R.Huber (2000).
Mutational studies on HslU and its docking mode with HslV.
  Proc Natl Acad Sci U S A, 97, 14103-14108.
PDB code: 1e94
10692374 H.L.Wilson, M.S.Ou, H.C.Aldrich, and J.Maupin-Furlow (2000).
Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome.
  J Bacteriol, 182, 1680-1692.  
11016878 J.Deadman (2000).
Proteinase inhibitors and activators strategic targets for therapeutic intervention.
  J Pept Sci, 6, 421-431.  
11163224 J.Ortega, S.K.Singh, T.Ishikawa, M.R.Maurizi, and A.C.Steven (2000).
Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP.
  Mol Cell, 6, 1515-1521.  
10922051 J.R.Hoskins, S.K.Singh, M.R.Maurizi, and S.Wickner (2000).
Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.
  Proc Natl Acad Sci U S A, 97, 8892-8897.  
10619848 J.S.Thrower, L.Hoffman, M.Rechsteiner, and C.M.Pickart (2000).
Recognition of the polyubiquitin proteolytic signal.
  EMBO J, 19, 94.  
11106733 M.C.Sousa, C.B.Trame, H.Tsuruta, S.M.Wilbanks, V.S.Reddy, and D.B.McKay (2000).
Crystal and solution structures of an HslUV protease-chaperone complex.
  Cell, 103, 633-643.
PDB codes: 1g3i 1g3k
10906271 M.H.Glickman (2000).
Getting in and out of the proteasome.
  Semin Cell Dev Biol, 11, 149-158.  
10652097 M.N.Pouch, B.Cournoyer, and W.Baumeister (2000).
Characterization of the 20S proteasome from the actinomycete Frankia.
  Mol Microbiol, 35, 368-377.  
10699313 M.Rao, and C.R.Alving (2000).
Delivery of lipids and liposomal proteins to the cytoplasm and Golgi of antigen-presenting cells. mangala.rao@na.amedd.army.mil.
  Adv Drug Deliv Rev, 41, 171-188.  
11001381 R.Z.Murray, and C.Norbury (2000).
Proteasome inhibitors as anti-cancer agents.
  Anticancer Drugs, 11, 407-417.  
10922052 S.K.Singh, R.Grimaud, J.R.Hoskins, S.Wickner, and M.R.Maurizi (2000).
Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
  Proc Natl Acad Sci U S A, 97, 8898-8903.  
10971134 T.C.Chang, W.Y.Chou, and G.G.Chang (2000).
Protein oxidation and turnover.
  J Biomed Sci, 7, 357-363.  
10903946 T.Nakai, T.Hasegawa, E.Yamashita, M.Yamamoto, T.Kumasaka, T.Ueki, H.Nanba, Y.Ikenaka, S.Takahashi, M.Sato, and T.Tsukihara (2000).
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases.
  Structure, 8, 729-737.
PDB code: 1erz
11076035 U.Kuckelkorn, C.Knuehl, B.Boes-Fabian, I.Drung, and P.M.Kloetzel (2000).
The effect of heat shock on 20S/26S proteasomes.
  Biol Chem, 381, 1017-1023.  
11114201 X.Du, I.G.Choi, R.Kim, W.Wang, J.Jancarik, H.Yokota, and S.H.Kim (2000).
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
  Proc Natl Acad Sci U S A, 97, 14079-14084.
PDB code: 1g2i
10357810 A.Kihara, Y.Akiyama, and K.Ito (1999).
Dislocation of membrane proteins in FtsH-mediated proteolysis.
  EMBO J, 18, 2970-2981.  
10500119 A.L.Horwich, E.U.Weber-Ban, and D.Finley (1999).
Chaperone rings in protein folding and degradation.
  Proc Natl Acad Sci U S A, 96, 11033-11040.  
10073263 A.L.Schwartz, and A.Ciechanover (1999).
The ubiquitin-proteasome pathway and pathogenesis of human diseases.
  Annu Rev Med, 50, 57-74.  
  10211841 A.Marina, P.M.Alzari, J.Bravo, M.Uriarte, B.Barcelona, I.Fita, and V.Rubio (1999).
Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.
  Protein Sci, 8, 934-940.
PDB codes: 1b7b 2we4 2we5
10089474 C.Bompard-Gilles, V.Villeret, L.Fanuel, B.Joris, J.M.Frère, and J.Van Beeumen (1999).
Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis.
  Acta Crystallogr D Biol Crystallogr, 55, 699-701.  
  10518749 C.P.Ponting, and M.J.Pallen (1999).
beta-propeller repeats and a PDZ domain in the tricorn protease: predicted self-compartmentalisation and C-terminal polypeptide-binding strategies of substrate selection.
  FEMS Microbiol Lett, 179, 447-451.  
10582238 C.R.Wilkinson, M.Penney, G.McGurk, M.Wallace, and C.Gordon (1999).
The 26S proteasome of the fission yeast Schizosaccharomyces pombe.
  Philos Trans R Soc Lond B Biol Sci, 354, 1523-1532.  
10393174 C.S.Arendt, and M.Hochstrasser (1999).
Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly.
  EMBO J, 18, 3575-3585.  
10872471 D.Voges, P.Zwickl, and W.Baumeister (1999).
The 26S proteasome: a molecular machine designed for controlled proteolysis.
  Annu Rev Biochem, 68, 1015-1068.  
10411654 F.Gardrat, B.Fraigneau, V.Montel, J.Raymond, and J.L.Azanza (1999).
Effect of high hydrostatic pressures on 20S proteasome activity.
  Eur J Biochem, 262, 900-906.  
10386971 G.Christie, R.E.Markwell, C.W.Gray, L.Smith, F.Godfrey, F.Mansfield, H.Wadsworth, R.King, M.McLaughlin, D.G.Cooper, R.V.Ward, D.R.Howlett, T.Hartmann, S.F.Lichtenthaler, K.Beyreuther, J.Underwood, S.K.Gribble, R.Cappai, C.L.Masters, A.Tamaoka, R.L.Gardner, A.J.Rivett, E.H.Karran, and D.Allsop (1999).
Alzheimer's disease: correlation of the suppression of beta-amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome.
  J Neurochem, 73, 195-204.  
10099130 G.Loidl, M.Groll, H.J.Musiol, L.Ditzel, R.Huber, and L.Moroder (1999).
Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes.
  Chem Biol, 6, 197-204.  
10417703 H.Fu, J.H.Doelling, D.M.Rubin, and R.D.Vierstra (1999).
Structural and functional analysis of the six regulatory particle triple-A ATPase subunits from the Arabidopsis 26S proteasome.
  Plant J, 18, 529-539.  
  10482525 H.L.Wilson, H.C.Aldrich, and J.Maupin-Furlow (1999).
Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis.
  J Bacteriol, 181, 5814-5824.  
10359790 H.Stahlberg, E.Kutejová, K.Suda, B.Wolpensinger, A.Lustig, G.Schatz, A.Engel, and C.K.Suzuki (1999).
Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.
  Proc Natl Acad Sci U S A, 96, 6787-6790.  
10200165 J.C.Milne, R.S.Roy, A.C.Eliot, N.L.Kelleher, A.Wokhlu, B.Nickels, and C.T.Walsh (1999).
Cofactor requirements and reconstitution of microcin B17 synthetase: a multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17.
  Biochemistry, 38, 4768-4781.  
10467138 J.Harms, A.Tocilj, I.Levin, I.Agmon, H.Stark, I.Kölln, M.van Heel, M.Cuff, F.Schlünzen, A.Bashan, F.Franceschi, and A.Yonath (1999).
Elucidating the medium-resolution structure of ribosomal particles: an interplay between electron cryo-microscopy and X-ray crystallograhy.
  Structure, 7, 931-941.  
10047537 K.Früh, and Y.Yang (1999).
Antigen presentation by MHC class I and its regulation by interferon gamma.
  Curr Opin Immunol, 11, 76-81.  
  10430571 K.J.Schmidt, K.E.Beck, and D.W.Grogan (1999).
UV stimulation of chromosomal marker exchange in Sulfolobus acidocaldarius: implications for DNA repair, conjugation and homologous recombination at extremely high temperatures.
  Genetics, 152, 1407-1415.  
10358773 K.L.Rock, and A.L.Goldberg (1999).
Degradation of cell proteins and the generation of MHC class I-presented peptides.
  Annu Rev Immunol, 17, 739-779.  
10410804 M.Bochtler, L.Ditzel, M.Groll, C.Hartmann, and R.Huber (1999).
The proteasome.
  Annu Rev Biophys Biomol Struct, 28, 295-317.  
10500111 M.Groll, W.Heinemeyer, S.Jäger, T.Ullrich, M.Bochtler, D.H.Wolf, and R.Huber (1999).
The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study.
  Proc Natl Acad Sci U S A, 96, 10976-10983.  
10582237 M.Hochstrasser, P.R.Johnson, C.S.Arendt, Amerik AYu, S.Swaminathan, R.Swanson, S.J.Li, J.Laney, R.Pals-Rylaarsdam, J.Nowak, and P.L.Connerly (1999).
The Saccharomyces cerevisiae ubiquitin-proteasome system.
  Philos Trans R Soc Lond B Biol Sci, 354, 1513-1522.  
10736750 M.Hoppert, and F.Mayer (1999).
Principles of macromolecular organization and cell function in bacteria and archaea.
  Cell Biochem Biophys, 31, 247-284.  
10508673 M.Schmidt, A.N.Lupas, and D.Finley (1999).
Structure and mechanism of ATP-dependent proteases.
  Curr Opin Chem Biol, 3, 584-591.  
10571008 N.N.Aronson (1999).
Aspartylglycosaminuria: biochemistry and molecular biology.
  Biochim Biophys Acta, 1455, 139-154.  
10404591 P.A.O'Farrell, F.Gonzalez, W.Zheng, S.A.Johnston, and L.Joshua-Tor (1999).
Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease.
  Structure, 7, 619-627.
PDB codes: 1cb5 2cb5
10582236 P.Zwickl, D.Voges, and W.Baumeister (1999).
The proteasome: a macromolecular assembly designed for controlled proteolysis.
  Philos Trans R Soc Lond B Biol Sci, 354, 1501-1511.  
10490104 Q.Xu, D.Buckley, C.Guan, and H.C.Guo (1999).
Structural insights into the mechanism of intramolecular proteolysis.
  Cell, 98, 651-661.
PDB codes: 9gaa 9gac 9gaf
10081087 R.De Mot, I.Nagy, J.Walz, and W.Baumeister (1999).
Proteasomes and other self-compartmentalizing proteases in prokaryotes.
  Trends Microbiol, 7, 88-92.  
10449745 R.Marino, R.De Santis, P.Giuliano, and M.R.Pinto (1999).
Follicle cell proteasome activity and acid extract from the egg vitelline coat prompt the onset of self-sterility in Ciona intestinalis oocytes.
  Proc Natl Acad Sci U S A, 96, 9633-9636.  
10394357 S.J.Russell, S.H.Reed, W.Huang, E.C.Friedberg, and S.A.Johnston (1999).
The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair.
  Mol Cell, 3, 687-695.  
  10049369 S.Li, J.L.Smith, and H.Zalkin (1999).
Mutational analysis of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase propeptide processing.
  J Bacteriol, 181, 1403-1408.  
10225950 W.C.Wigley, R.P.Fabunmi, M.G.Lee, C.R.Marino, S.Muallem, G.N.DeMartino, and P.J.Thomas (1999).
Dynamic association of proteasomal machinery with the centrosome.
  J Cell Biol, 145, 481-490.  
10411632 Y.Li, J.Chen, W.Jiang, X.Mao, G.Zhao, and E.Wang (1999).
In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130.
  Eur J Biochem, 262, 713-719.  
10220354 Z.Zhang, A.Krutchinsky, S.Endicott, C.Realini, M.Rechsteiner, and K.G.Standing (1999).
Proteasome activator 11S REG or PA28: recombinant REG alpha/REG beta hetero-oligomers are heptamers.
  Biochemistry, 38, 5651-5658.  
9666335 A.G.Murzin (1998).
How far divergent evolution goes in proteins.
  Curr Opin Struct Biol, 8, 380-387.  
9759494 A.Hershko, and A.Ciechanover (1998).
The ubiquitin system.
  Annu Rev Biochem, 67, 425-479.  
9770515 A.K.Nussbaum, T.P.Dick, W.Keilholz, M.Schirle, S.Stevanović, K.Dietz, W.Heinemeyer, M.Groll, D.H.Wolf, R.Huber, H.G.Rammensee, and H.Schild (1998).
Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.
  Proc Natl Acad Sci U S A, 95, 12504-12509.  
9437416 B.L.Stoddard, and S.Pietrokovski (1998).
Breaking up is hard to do.
  Nat Struct Biol, 5, 3-5.  
9822592 C.R.Wilkinson, M.Wallace, M.Morphew, P.Perry, R.Allshire, J.P.Javerzat, J.R.McIntosh, and C.Gordon (1998).
Localization of the 26S proteasome during mitosis and meiosis in fission yeast.
  EMBO J, 17, 6465-6476.  
9789328 D.H.Lee, and A.L.Goldberg (1998).
Proteasome inhibitors: valuable new tools for cell biologists.
  Trends Cell Biol, 8, 397-403.  
9724628 D.M.Rubin, M.H.Glickman, C.N.Larsen, S.Dhruvakumar, and D.Finley (1998).
Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome.
  EMBO J, 17, 4909-4919.  
9597133 E.Pamer, and P.Cresswell (1998).
Mechanisms of MHC class I--restricted antigen processing.
  Annu Rev Immunol, 16, 323-358.  
9737872 G.M.Adams, B.Crotchett, C.A.Slaughter, G.N.DeMartino, and E.P.Gogol (1998).
Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity.
  Biochemistry, 37, 12927-12932.  
  9611183 H.Fu, J.H.Doelling, C.S.Arendt, M.Hochstrasser, and R.D.Vierstra (1998).
Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana.
  Genetics, 149, 677-692.  
  9765579 I.Nagy, T.Tamura, J.Vanderleyden, W.Baumeister, and R.De Mot (1998).
The 20S proteasome of Streptomyces coelicolor.
  J Bacteriol, 180, 5448-5453.  
  9515917 J.A.Maupin-Furlow, H.C.Aldrich, and J.G.Ferry (1998).
Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila.
  J Bacteriol, 180, 1480-1487.  
9871688 J.F.Lynas, P.Harriott, A.Healy, M.A.McKervey, and B.Walker (1998).
Inhibitors of the chymotrypsin-like activity of proteasome based on di- and tri-peptidyl alpha-keto aldehydes (glyoxals).
  Bioorg Med Chem Lett, 8, 373-378.  
9914248 J.L.Smith (1998).
Glutamine PRPP amidotransferase: snapshots of an enzyme in action.
  Curr Opin Struct Biol, 8, 686-694.  
9770452 J.R.Hoskins, M.Pak, M.R.Maurizi, and S.Wickner (1998).
The role of the ClpA chaperone in proteolysis by ClpAP.
  Proc Natl Acad Sci U S A, 95, 12135-12140.  
9891777 J.S.Bonifacino, and A.M.Weissman (1998).
Ubiquitin and the control of protein fate in the secretory and endocytic pathways.
  Annu Rev Cell Dev Biol, 14, 19-57.  
9797452 K.Tanaka, and T.Chiba (1998).
The proteasome: a protein-destroying machine.
  Genes Cells, 3, 499-510.  
  9605331 L.Aravind, and C.P.Ponting (1998).
Homologues of 26S proteasome subunits are regulators of transcription and translation.
  Protein Sci, 7, 1250-1254.  
9529257 L.Lin, G.N.DeMartino, and W.C.Greene (1998).
Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome.
  Cell, 92, 819-828.  
9653549 M.Bogyo, S.Shin, J.S.McMaster, and H.L.Ploegh (1998).
Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes.
  Chem Biol, 5, 307-320.  
  9841670 M.D.Mendenhall, and A.E.Hodge (1998).
Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.
  Microbiol Mol Biol Rev, 62, 1191-1243.  
  9584156 M.H.Glickman, D.M.Rubin, V.A.Fried, and D.Finley (1998).
The regulatory particle of the Saccharomyces cerevisiae proteasome.
  Mol Cell Biol, 18, 3149-3162.  
9651672 M.R.Maurizi (1998).
Proteasome assembly: biting the hand.
  Curr Biol, 8, R453-R456.  
9845366 N.Tamura, F.Lottspeich, W.Baumeister, and T.Tamura (1998).
The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation.
  Cell, 95, 637-648.  
9491890 P.C.Ramos, J.Höckendorff, E.S.Johnson, A.Varshavsky, and R.J.Dohmen (1998).
Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly.
  Cell, 92, 489-499.  
10076530 R.T.Lum, S.S.Kerwar, S.M.Meyer, M.G.Nelson, S.R.Schow, D.Shiffman, M.M.Wick, and A.Joly (1998).
A new structural class of proteasome inhibitors that prevent NF-kappa B activation.
  Biochem Pharmacol, 55, 1391-1397.  
9615617 S.Yamada, J.Yamada, K.Sato, T.Tokumoto, M.Yasutomi, and K.Ishikawa (1998).
Irreversible potent activation and reversible inhibition of trypsin-like activity of 20S proteasome purified from Xenopus oocytes by fatty acid.
  Zoolog Sci, 15, 43-49.  
9601040 T.A.McCormack, A.A.Cruikshank, L.Grenier, F.D.Melandri, S.L.Nunes, L.Plamondon, R.L.Stein, and L.R.Dick (1998).
Kinetic studies of the branched chain amino acid preferring peptidase activity of the 20S proteasome: development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin beta-lactone.
  Biochemistry, 37, 7792-7800.  
9437427 T.Klabunde, S.Sharma, A.Telenti, W.R.Jacobs, and J.C.Sacchettini (1998).
Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing.
  Nat Struct Biol, 5, 31-36.
PDB code: 1am2
9628862 T.U.Mayer, T.Braun, and S.Jentsch (1998).
Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein.
  EMBO J, 17, 3251-3257.  
9521073 V.M.Braud, A.J.McMichael, and V.Cerundolo (1998).
Differential processing of influenza nucleoprotein in human and mouse cells.
  Eur J Immunol, 28, 625-635.  
  9472642 V.Spataro, C.Norbury, and A.L.Harris (1998).
The ubiquitin-proteasome pathway in cancer.
  Br J Cancer, 77, 448-455.  
9476896 W.Baumeister, J.Walz, F.Zühl, and E.Seemüller (1998).
The proteasome: paradigm of a self-compartmentalizing protease.
  Cell, 92, 367-380.  
9546396 W.Zheng, S.A.Johnston, and L.Joshua-Tor (1998).
The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
  Cell, 93, 103-109.
PDB codes: 1a6r 3gcb
  9721298 Y.S.Lee, and S.S.Park (1998).
Two-step autocatalytic processing of the glutaryl 7-aminocephalosporanic acid acylase from Pseudomonas sp. strain GK16.
  J Bacteriol, 180, 4576-4582.  
9501171 Z.Zhang, A.Clawson, C.Realini, C.C.Jensen, J.R.Knowlton, C.P.Hill, and M.Rechsteiner (1998).
Identification of an activation region in the proteasome activator REGalpha.
  Proc Natl Acad Sci U S A, 95, 2807-2811.  
9357316 A.Lupas, J.M.Flanagan, T.Tamura, and W.Baumeister (1997).
Self-compartmentalizing proteases.
  Trends Biochem Sci, 22, 399-404.  
  9165078 C.Ehlers, F.Kopp, and B.Dahlmann (1997).
Screening for molecules interacting with proteasomes in Thermoplasma acidophilum.
  Biol Chem, 378, 249-253.  
9390550 C.N.Larsen, and D.Finley (1997).
Protein translocation channels in the proteasome and other proteases.
  Cell, 91, 431-434.  
9207060 C.S.Arendt, and M.Hochstrasser (1997).
Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.
  Proc Natl Acad Sci U S A, 94, 7156-7161.  
9311996 D.Nandi, E.Woodward, D.B.Ginsburg, and J.J.Monaco (1997).
Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits.
  EMBO J, 16, 5363-5375.  
9321388 E.A.Reits, A.M.Benham, B.Plougastel, J.Neefjes, and J.Trowsdale (1997).
Dynamics of proteasome distribution in living cells.
  EMBO J, 16, 6087-6094.  
9096325 F.Kopp, K.B.Hendil, B.Dahlmann, P.Kristensen, A.Sobek, and W.Uerkvitz (1997).
Subunit arrangement in the human 20S proteasome.
  Proc Natl Acad Sci U S A, 94, 2939-2944.  
9221750 G.Niedermann, R.Grimm, E.Geier, M.Maurer, C.Realini, C.Gartmann, J.Soll, S.Omura, M.C.Rechsteiner, W.Baumeister, and K.Eichmann (1997).
Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system.
  J Exp Med, 186, 209-220.  
9005983 G.Tiao, S.Hobler, J.J.Wang, T.A.Meyer, F.A.Luchette, J.E.Fischer, and P.O.Hasselgren (1997).
Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle.
  J Clin Invest, 99, 163-168.  
9151663 H.B.McDonald, and B.Byers (1997).
A proteasome cap subunit required for spindle pole body duplication in yeast.
  J Cell Biol, 137, 539-553.  
9145098 J.A.Brannigan, and G.G.Dodson (1997).
A short cut for the immune system.
  Nat Struct Biol, 4, 334-338.  
  9233537 J.G.Ferry (1997).
Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila.
  Biofactors, 6, 25-35.  
  9165084 J.Knäblein, H.Dobbek, S.Ehlert, and F.Schneider (1997).
Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus.
  Biol Chem, 378, 293-302.  
9039771 J.O.Koopmann, G.J.Hämmerling, and F.Momburg (1997).
Generation, intracellular transport and loading of peptides associated with MHC class I molecules.
  Curr Opin Immunol, 9, 80-88.  
  9362069 J.Ozols (1997).
Degradation of hepatic stearyl CoA delta 9-desaturase.
  Mol Biol Cell, 8, 2281-2290.  
9659903 J.Walz, T.Tamura, N.Tamura, R.Grimm, W.Baumeister, and A.J.Koster (1997).
Tricorn protease exists as an icosahedral supermolecule in vivo.
  Mol Cell, 1, 59-65.  
9390554 J.Wang, J.A.Hartling, and J.M.Flanagan (1997).
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.
  Cell, 91, 447-456.
PDB code: 1tyf
9345628 K.Moffat, and Z.Ren (1997).
Synchrotron radiation applications to macromolecular crystallography.
  Curr Opin Struct Biol, 7, 689-696.  
9177170 M.Bochtler, L.Ditzel, M.Groll, and R.Huber (1997).
Crystal structure of heat shock locus V (HslV) from Escherichia coli.
  Proc Natl Acad Sci U S A, 94, 6070-6074.
PDB code: 1ned
9192616 M.Bogyo, J.S.McMaster, M.Gaczynska, D.Tortorella, A.L.Goldberg, and H.Ploegh (1997).
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors.
  Proc Natl Acad Sci U S A, 94, 6629-6634.  
9316392 M.Bogyo, M.Gaczynska, and H.L.Ploegh (1997).
Proteasome inhibitors and antigen presentation.
  Biopolymers, 43, 269-280.  
9256419 M.Groettrup, S.Standera, R.Stohwasser, and P.M.Kloetzel (1997).
The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome.
  Proc Natl Acad Sci U S A, 94, 8970-8975.  
9020589 M.Paetzel, and R.E.Dalbey (1997).
Catalytic hydroxyl/amine dyads within serine proteases.
  Trends Biochem Sci, 22, 28-31.  
9033594 M.Rohrwild, G.Pfeifer, U.Santarius, S.A.Müller, H.C.Huang, A.Engel, W.Baumeister, and A.L.Goldberg (1997).
The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome.
  Nat Struct Biol, 4, 133-139.  
  16535545 M.W.Bauer, S.H.Bauer, and R.M.Kelly (1997).
Purification and Characterization of a Proteasome from the Hyperthermophilic Archaeon Pyrococcus furiosus.
  Appl Environ Microbiol, 63, 1160-1164.  
9202072 N.E.Tawa, R.Odessey, and A.L.Goldberg (1997).
Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles.
  J Clin Invest, 100, 197-203.  
9060588 P.O.Hasselgren, and J.E.Fischer (1997).
The ubiquitin-proteasome pathway: review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions.
  Ann Surg, 225, 307-316.  
9174609 R.Stohwasser, S.Standera, I.Peters, P.M.Kloetzel, and M.Groettrup (1997).
Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tissue expression of interferon-gamma-modulated proteasome subunits.
  Eur J Immunol, 27, 1182-1187.  
  9385652 S.C.Johnston, F.G.Whitby, C.Realini, M.Rechsteiner, and C.P.Hill (1997).
The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer.
  Protein Sci, 6, 2469-2473.  
9390551 S.Gottesman, M.R.Maurizi, and S.Wickner (1997).
Regulatory subunits of energy-dependent proteases.
  Cell, 91, 435-438.  
9278475 S.Nouraini, D.Xu, S.Nelson, M.Lee, and J.D.Friesen (1997).
Genetic evidence for selective degradation of RNA polymerase subunits by the 20S proteasome in Saccharomyces cerevisiae.
  Nucleic Acids Res, 25, 3570-3579.  
  9398670 U.M.Gerlinger, R.Gückel, M.Hoffmann, D.H.Wolf, and W.Hilt (1997).
Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation.
  Mol Biol Cell, 8, 2487-2499.  
9094332 W.Baumeister, and A.Lupas (1997).
The proteasome.
  Curr Opin Struct Biol, 7, 273-278.  
  9165062 W.Baumeister, Z.Cejka, M.Kania, and E.Seemüller (1997).
The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
  Biol Chem, 378, 121-130.  
9115411 Y.Shao, and S.B.Kent (1997).
Protein splicing: occurrence, mechanisms and related phenomena.
  Chem Biol, 4, 187-194.  
8728645 A.A.Antson, E.J.Dodson, and G.G.Dodson (1996).
Circular assemblies.
  Curr Opin Struct Biol, 6, 142-150.  
8804825 A.G.Murzin (1996).
Structural classification of proteins: new superfamilies.
  Curr Opin Struct Biol, 6, 386-394.  
8631360 B.Ehring, T.H.Meyer, C.Eckerskorn, F.Lottspeich, and R.Tampé (1996).
Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes. Cleavage of proteins and antigenic peptides.
  Eur J Biochem, 235, 404-415.  
8794741 C.M.Benedict, and G.A.Clawson (1996).
Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes.
  Biochemistry, 35, 11612-11621.  
8768894 D.Stock, P.M.Nederlof, E.Seemüller, W.Baumeister, R.Huber, and J.Löwe (1996).
Proteasome: from structure to function.
  Curr Opin Biotechnol, 7, 376-385.  
  8655500 D.W.Grogan (1996).
Exchange of genetic markers at extremely high temperatures in the archaeon Sulfolobus acidocaldarius.
  J Bacteriol, 178, 3207-3211.  
8666915 E.A.Hughes, B.Ortmann, M.Surman, and P.Cresswell (1996).
The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum.
  J Exp Med, 183, 1569-1578.  
8681958 G.G.Mason, K.B.Hendil, and A.J.Rivett (1996).
Phosphorylation of proteasomes in mammalian cells. Identification of two phosphorylated subunits and the effect of phosphorylation on activity.
  Eur J Biochem, 238, 453-462.  
8710912 G.Niedermann, G.King, S.Butz, U.Birsner, R.Grimm, J.Shabanowitz, D.F.Hunt, and K.Eichmann (1996).
The proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex class I binding peptides.
  Proc Natl Acad Sci U S A, 93, 8572-8577.  
  9003765 G.Schmidtke, R.Kraft, S.Kostka, P.Henklein, C.Frömmel, J.Löwe, R.Huber, P.M.Kloetzel, and M.Schmidt (1996).
Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.
  EMBO J, 15, 6887-6898.  
8793968 H.G.Rammensee, and K.F.Lindhal (1996).
Less scholasticism, more exact immunology.
  Curr Opin Immunol, 8, 49-50.  
8666937 H.Hisamatsu, N.Shimbara, Y.Saito, P.Kristensen, K.B.Hendil, T.Fujiwara, E.Takahashi, N.Tanahashi, T.Tamura, A.Ichihara, and K.Tanaka (1996).
Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma.
  J Exp Med, 183, 1807-1816.  
  8830688 H.Kolmar, P.R.Waller, and R.T.Sauer (1996).
The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation.
  J Bacteriol, 178, 5925-5929.  
8743884 H.L.Pahl, and P.A.Baeuerle (1996).
Control of gene expression by proteolysis.
  Curr Opin Cell Biol, 8, 340-347.  
8717519 I.A.York, and K.L.Rock (1996).
Antigen processing and presentation by the class I major histocompatibility complex.
  Annu Rev Immunol, 14, 369-396.  
8619999 J.G.Castaño, E.Mahillo, P.Arizti, and J.Arribas (1996).
Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis.
  Biochemistry, 35, 3782-3789.  
  8764072 J.Huang, J.Kwong, E.C.Sun, and T.J.Liang (1996).
Proteasome complex as a potential cellular target of hepatitis B virus X protein.
  J Virol, 70, 5582-5591.  
8736550 J.Thygesen, S.Weinstein, F.Franceschi, and A.Yonath (1996).
The suitability of multi-metal clusters for phasing in crystallography of large macromolecular assemblies.
  Structure, 4, 513-518.  
  8816993 K.Yokota, S.Kagawa, Y.Shimizu, H.Akioka, C.Tsurumi, C.Noda, M.Fujimuro, H.Yokosawa, T.Fujiwara, E.Takahashi, M.Ohba, M.Yamasaki, G.N.DeMartino, C.A.Slaughter, A.Toh-e, and K.Tanaka (1996).
CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p.
  Mol Biol Cell, 7, 853-870.  
  8670888 L.M.Grimm, A.L.Goldberg, G.G.Poirier, L.M.Schwartz, and B.A.Osborne (1996).
Proteasomes play an essential role in thymocyte apoptosis.
  EMBO J, 15, 3835-3844.  
8696978 M.Chytil, and G.L.Verdine (1996).
The Rel family of eukaryotic transcription factors.
  Curr Opin Struct Biol, 6, 91.  
8625980 M.Groettrup, R.Kraft, S.Kostka, S.Standera, R.Stohwasser, and P.M.Kloetzel (1996).
A third interferon-gamma-induced subunit exchange in the 20S proteasome.
  Eur J Immunol, 26, 863-869.  
8982460 M.Hochstrasser (1996).
Ubiquitin-dependent protein degradation.
  Annu Rev Genet, 30, 405-439.  
8799160 M.Kasahara, M.Hayashi, K.Tanaka, H.Inoko, K.Sugaya, T.Ikemura, and T.Ishibashi (1996).
Chromosomal localization of the proteasome Z subunit gene reveals an ancient chromosomal duplication involving the major histocompatibility complex.
  Proc Natl Acad Sci U S A, 93, 9096-9101.  
8650174 M.Rohrwild, O.Coux, H.C.Huang, R.P.Moerschell, S.J.Yoo, J.H.Seol, C.H.Chung, and A.L.Goldberg (1996).
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome.
  Proc Natl Acad Sci U S A, 93, 5808-5813.  
8729447 P.J.Lehner, and P.Cresswell (1996).
Processing and delivery of peptides presented by MHC class I molecules.
  Curr Opin Immunol, 8, 59-67.  
8679541 P.R.Strack, L.Waxman, and J.M.Fagan (1996).
Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure.
  Biochemistry, 35, 7142-7149.  
8652597 R.H.Newman, P.Whitehead, J.Lally, A.Coffer, and P.Freemont (1996).
20S human proteasomes bind with a specific orientation to lipid monolayers in vitro.
  Biochim Biophys Acta, 1281, 111-116.  
8672420 R.L.Stein, F.Melandri, and L.Dick (1996).
Kinetic characterization of the chymotryptic activity of the 20S proteasome.
  Biochemistry, 35, 3899-3908.  
  8670796 R.Tikkanen, A.Riikonen, C.Oinonen, R.Rouvinen, and L.Peltonen (1996).
Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation.
  EMBO J, 15, 2954-2960.  
8753855 S.Abdulla, S.Beck, M.Belich, A.Jackson, T.Nakamura, and J.Trowsdale (1996).
Divergent intron arrangement in the MB1/LMP7 proteasome gene pair.
  Immunogenetics, 44, 254-258.  
  8626329 S.B.Halio, I.I.Blumentals, S.A.Short, B.M.Merrill, and R.M.Kelly (1996).
Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus.
  J Bacteriol, 178, 2605-2612.  
8901527 S.J.Yeung, S.H.Chen, and L.Chan (1996).
Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B.
  Biochemistry, 35, 13843-13848.  
8570648 S.van Nocker, Q.Deveraux, M.Rechsteiner, and R.D.Vierstra (1996).
Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome.
  Proc Natl Acad Sci U S A, 93, 856-860.  
  8641272 T.Biederer, C.Volkwein, and T.Sommer (1996).
Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.
  EMBO J, 15, 2069-2076.  
8962033 T.L.Blundell, and N.Srinivasan (1996).
Symmetry, stability, and dynamics of multidomain and multicomponent protein systems.
  Proc Natl Acad Sci U S A, 93, 14243-14248.  
8833236 T.Leeb, G.Rettenberger, J.Breech, H.Hameister, and B.Brenig (1996).
The porcine gene TBP10 encodes a protein homologous to the human tat-binding protein/26S protease subunit family.
  Mamm Genome, 7, 180-185.  
8882582 W.Hilt, and D.H.Wolf (1996).
Proteasomes: destruction as a programme.
  Trends Biochem Sci, 21, 96.  
  8878681 X.Yuan, M.Miller, and J.M.Belote (1996).
Duplicated proteasome subunit genes in Drosophila melanogaster encoding testes-specific isoforms.
  Genetics, 144, 147-157.  
8902577 Y.Yang, P.Sempé, and P.A.Peterson (1996).
Molecular mechanisms of class I major histocompatibility complex antigen processing and presentation.
  Immunol Res, 15, 208-233.  
  7588620 A.Carfi, S.Pares, E.Duée, M.Galleni, C.Duez, J.M.Frère, and O.Dideberg (1995).
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
  EMBO J, 14, 4914-4921.
PDB code: 1bmc
9383453 A.L.Goldberg, R.Stein, and J.Adams (1995).
New insights into proteasome function: from archaebacteria to drug development.
  Chem Biol, 2, 503-508.  
7553863 C.L.Ward, S.Omura, and R.R.Kopito (1995).
Degradation of CFTR by the ubiquitin-proteasome pathway.
  Cell, 83, 121-127.  
8846222 C.Oinonen, R.Tikkanen, J.Rouvinen, and L.Peltonen (1995).
Three-dimensional structure of human lysosomal aspartylglucosaminidase.
  Nat Struct Biol, 2, 1102-1108.
PDB codes: 1apy 1apz
7583150 C.Sibille, K.G.Gould, K.Willard-Gallo, S.Thomson, A.J.Rivett, S.Powis, G.W.Butcher, and P.De Baetselier (1995).
LMP2+ proteasomes are required for the presentation of specific antigens to cytotoxic T lymphocytes.
  Curr Biol, 5, 923-930.  
7583140 D.M.Rubin, and D.Finley (1995).
Proteolysis. The proteasome: a protein-degrading organelle?
  Curr Biol, 5, 854-858.  
8749362 J.L.Smith (1995).
Enzymes of nucleotide synthesis.
  Curr Opin Struct Biol, 5, 752-757.  
8618844 P.M.Nederlof, H.R.Wang, and W.Baumeister (1995).
Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro.
  Proc Natl Acad Sci U S A, 92, 12060-12064.  
7553848 S.Jentsch, and S.Schlenker (1995).
Selective protein degradation: a journey's end within the proteasome.
  Cell, 82, 881-884.  
7583123 T.Tamura, I.Nagy, A.Lupas, F.Lottspeich, Z.Cejka, G.Schoofs, K.Tanaka, R.De Mot, and W.Baumeister (1995).
The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus.
  Curr Biol, 5, 766-774.  
8574578 Z.Kelman, J.Finkelstein, and M.O'Donnell (1995).
Protein structure. Why have six-fold symmetry?
  Curr Biol, 5, 1239-1242.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.