spacer
spacer

PDBsum entry 1elr

Go to PDB code: 
protein ligands metals links
Chaperone PDB id
1elr
Jmol PyMol
Contents
Protein chain
128 a.a. *
Ligands
ACE-MET-GLU-GLU-
VAL-ASP
Metals
_NI
Waters ×151
* Residue conservation analysis
PDB id:
1elr
Name: Chaperone
Title: Crystal structure of the tpr2a domain of hop in complex with the hsp90 peptide meevd
Structure: Tpr2a-domain of hop. Chain: a. Fragment: middle domain. Engineered: yes. Hsp90-peptide meevd. Chain: b. Fragment: c-terminal pentapeptide. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence occurs naturally in humans
Biol. unit: Dimer (from PQS)
Resolution:
1.90Å     R-factor:   0.181     R-free:   0.219
Authors: C.Scheufler,A.Brinker,F.U.Hartl,I.Moarefi
Key ref:
C.Scheufler et al. (2000). Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell, 101, 199-210. PubMed id: 10786835 DOI: 10.1016/S0092-8674(00)80830-2
Date:
14-Mar-00     Release date:   26-Apr-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31948  (STIP1_HUMAN) -  Stress-induced-phosphoprotein 1
Seq:
Struc:
 
Seq:
Struc:
543 a.a.
128 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1016/S0092-8674(00)80830-2 Cell 101:199-210 (2000)
PubMed id: 10786835  
 
 
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
C.Scheufler, A.Brinker, G.Bourenkov, S.Pegoraro, L.Moroder, H.Bartunik, F.U.Hartl, I.Moarefi.
 
  ABSTRACT  
 
The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Interaction of the TPR1 Domain of Hop with Hsc70/Hsp70
Figure 4.
Figure 4. Schematic Representation of the TPR–Peptide Interactions
 
  The above figures are reprinted by permission from Cell Press: Cell (2000, 101, 199-210) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22343721 A.M.Ellisdon, L.Dimitrova, E.Hurt, and M.Stewart (2012).
Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.
  Nat Struct Mol Biol, 19, 328-336.
PDB codes: 3t5v 3t5x
21114539 A.Allegra, E.Sant'antonio, G.Penna, A.Alonci, A.D'Angelo, S.Russo, A.Cannavò, D.Gerace, and C.Musolino (2011).
Novel therapeutic strategies in multiple myeloma: role of the heat shock protein inhibitors.
  Eur J Haematol, 86, 93.  
21397190 C.F.Lee, A.V.Hauenstein, J.K.Fleming, W.C.Gasper, V.Engelke, B.Sankaran, S.I.Bernstein, and T.Huxford (2011).
X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.
  Structure, 19, 397-408.
PDB code: 3now
21776078 F.U.Hartl, A.Bracher, and M.Hayer-Hartl (2011).
Molecular chaperones in protein folding and proteostasis.
  Nature, 475, 324-332.  
21426241 I.L.Cockburn, E.R.Pesce, J.M.Pryzborski, M.T.Davies-Coleman, P.G.Clark, R.A.Keyzers, L.L.Stephens, and G.L.Blatch (2011).
Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1.
  Biol Chem, 392, 431-438.  
21170051 J.Li, K.Richter, and J.Buchner (2011).
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.
  Nat Struct Mol Biol, 18, 61-66.  
21377533 K.H.Skjærven, P.A.Olsvik, R.N.Finn, E.Holen, and K.Hamre (2011).
Ontogenetic expression of maternal and zygotic genes in Atlantic cod embryos under ambient and thermally stressed conditions.
  Comp Biochem Physiol A Mol Integr Physiol, 159, 196-205.  
21119664 L.Li, Z.Lou, and L.Wang (2011).
The role of FKBP5 in cancer aetiology and chemoresistance.
  Br J Cancer, 104, 19-23.  
21235734 T.Horibe, M.Kohno, M.Haramoto, K.Ohara, and K.Kawakami (2011).
Designed hybrid TPR peptide targeting Hsp90 as a novel anticancer agent.
  J Transl Med, 9, 8.  
20888775 V.M.Bolanos-Garcia, and T.L.Blundell (2011).
BUB1 and BUBR1: multifaceted kinases of the cell cycle.
  Trends Biochem Sci, 36, 141-150.  
20504278 A.C.Fan, L.M.Gava, C.H.Ramos, and J.C.Young (2010).
Human mitochondrial import receptor Tom70 functions as a monomer.
  Biochem J, 429, 553-563.  
20089039 A.L.Cortajarena, J.Wang, and L.Regan (2010).
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.
  FEBS J, 277, 1058-1066.
PDB code: 3kd7
20856808 B.D.Prasad, S.Goel, and P.Krishna (2010).
In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70.
  PLoS One, 5, e12761.  
  20944222 C.Bakolitsa, Q.Xu, C.L.Rife, P.Abdubek, T.Astakhova, H.L.Axelrod, D.Carlton, C.Chen, H.J.Chiu, T.Clayton, D.Das, M.C.Deller, L.Duan, K.Ellrott, C.L.Farr, J.Feuerhelm, J.C.Grant, A.Grzechnik, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, P.Kozbial, S.S.Krishna, A.Kumar, W.W.Lam, D.Marciano, D.McMullan, M.D.Miller, A.T.Morse, E.Nigoghossian, A.Nopakun, L.Okach, C.Puckett, R.Reyes, H.J.Tien, C.B.Trame, H.van den Bedem, D.Weekes, K.O.Hodgson, J.Wooley, M.A.Elsliger, A.M.Deacon, A.Godzik, S.A.Lesley, and I.A.Wilson (2010).
Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1274-1280.
PDB code: 3cgh
20421385 C.H.Teng, Y.T.Tseng, R.Maruvada, D.Pearce, Y.Xie, M.Paul-Satyaseela, and K.S.Kim (2010).
NlpI contributes to Escherichia coli K1 strain RS218 interaction with human brain microvascular endothelial cells.
  Infect Immun, 78, 3090-3096.  
20159471 C.L.Keiski, M.Harwich, S.Jain, A.M.Neculai, P.Yip, H.Robinson, J.C.Whitney, L.Riley, L.L.Burrows, D.E.Ohman, and P.L.Howell (2010).
AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.
  Structure, 18, 265-273.
PDB code: 3e4b
20855544 D.Forget, A.A.Lacombe, P.Cloutier, R.Al-Khoury, A.Bouchard, M.Lavallée-Adam, D.Faubert, C.Jeronimo, M.Blanchette, and B.Coulombe (2010).
The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II.
  Mol Cell Proteomics, 9, 2827-2839.  
20850366 F.Wang, E.C.Brown, G.Mak, J.Zhuang, and V.Denic (2010).
A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.
  Mol Cell, 40, 159-171.  
19866486 F.Yi, I.Doudevski, and L.Regan (2010).
HOP is a monomer: investigation of the oligomeric state of the co-chaperone HOP.
  Protein Sci, 19, 19-25.  
20874569 H.Feng, L.Wang, Y.Liu, L.He, M.Li, W.Lu, and C.Xue (2010).
Molecular characterization and expression of a heat shock protein gene (HSP90) from the carmine spider mite, Tetranychus cinnabarinus (Boisduval).
  J Insect Sci, 10, 112.  
20617406 H.Kubota, S.Yamamoto, E.Itoh, Y.Abe, A.Nakamura, Y.Izumi, H.Okada, M.Iida, H.Nanjo, H.Itoh, and Y.Yamamoto (2010).
Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma.
  Cell Stress Chaperones, 15, 1003-1011.  
21087465 J.C.Ahn, D.W.Kim, Y.N.You, M.S.Seok, J.M.Park, H.Hwang, B.G.Kim, S.Luan, H.S.Park, and H.S.Cho (2010).
Classification of rice (Oryza sativa L. Japonica nipponbare) immunophilins (FKBPs, CYPs) and expression patterns under water stress.
  BMC Plant Biol, 10, 253.  
  20023401 J.L.Rao, P.S.Reddy, R.N.Mishra, D.Gupta, D.Sahal, N.Tuteja, S.K.Sopory, and M.K.Reddy (2010).
Thermo and pH stable ATP-independent chaperone activity of heat-inducible Hsp70 from Pennisetum glaucum.
  Plant Signal Behav, 5, 110-121.  
20184891 J.Tao, K.Petrova, D.Ron, and B.Sha (2010).
Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.
  J Mol Biol, 397, 1307-1315.
PDB code: 3ieg
19913553 L.Kundrat, and L.Regan (2010).
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.
  J Mol Biol, 395, 587-594.  
20404152 M.A.Morales, R.Watanabe, M.Dacher, P.Chafey, J.Osorio y Fortéa, D.A.Scott, S.M.Beverley, G.Ommen, J.Clos, S.Hem, P.Lenormand, J.C.Rousselle, A.Namane, and G.F.Späth (2010).
Phosphoproteome dynamics reveal heat-shock protein complexes specific to the Leishmania donovani infectious stage.
  Proc Natl Acad Sci U S A, 107, 8381-8386.  
20479121 M.Reidy, and D.C.Masison (2010).
Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.
  Mol Cell Biol, 30, 3542-3552.  
20453924 P.Cloutier, and B.Coulombe (2010).
New insights into the biogenesis of nuclear RNA polymerases?
  Biochem Cell Biol, 88, 211-221.  
19768775 S.N.Witt (2010).
Hsp70 molecular chaperones and Parkinson's disease.
  Biopolymers, 93, 218-228.  
20553226 T.Tamura, J.C.Sunryd, and D.N.Hebert (2010).
Sorting things out through endoplasmic reticulum quality control.
  Mol Membr Biol, 27, 412-427.  
20304973 T.Z.Grove, M.Hands, and L.Regan (2010).
Creating novel proteins by combining design and selection.
  Protein Eng Des Sel, 23, 449-455.  
20354811 T.Z.Lu, Y.Quan, and Z.P.Feng (2010).
Multifaceted role of heat shock protein 70 in neurons.
  Mol Neurobiol, 42, 114-123.  
19940115 V.E.Walker, M.J.Wong, R.Atanasiu, C.Hantouche, J.C.Young, and A.Shrier (2010).
Hsp40 chaperones promote degradation of the HERG potassium channel.
  J Biol Chem, 285, 3319-3329.  
19768774 V.Grimminger-Marquardt, and H.A.Lashuel (2010).
Structure and function of the molecular chaperone Hsp104 from yeast.
  Biopolymers, 93, 252-276.  
20696833 X.Yang, T.R.Lenhart, T.Kariu, J.Anguita, D.R.Akins, and U.Pal (2010).
Characterization of unique regions of Borrelia burgdorferi surface-located membrane protein 1.
  Infect Immun, 78, 4477-4487.  
19689428 A.J.Ramsey, L.C.Russell, and M.Chinkers (2009).
C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins.
  Biochem J, 423, 411-419.  
19192245 A.Ludwig, J.Blume, T.M.Diep, J.Yuan, J.M.Mateos, K.Leuthäuser, M.Steuble, P.Streit, and P.Sonderegger (2009).
Calsyntenins Mediate TGN Exit of APP in a Kinesin-1-Dependent Manner.
  Traffic, 10, 572-589.  
19875982 C.Roodveldt, C.W.Bertoncini, A.Andersson, A.T.van der Goot, S.T.Hsu, R.Fernández-Montesinos, J.de Jong, T.J.van Ham, E.A.Nollen, D.Pozo, J.Christodoulou, and C.M.Dobson (2009).
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.
  EMBO J, 28, 3758-3770.  
19519514 D.Sharma, and D.C.Masison (2009).
Hsp70 structure, function, regulation and influence on yeast prions.
  Protein Pept Lett, 16, 571-581.  
19693936 E.Iakhiaeva, C.S.Hinck, A.P.Hinck, and C.Zwieb (2009).
Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis.
  Protein Sci, 18, 2183-2195.  
19491934 F.U.Hartl, and M.Hayer-Hartl (2009).
Converging concepts of protein folding in vitro and in vivo.
  Nat Struct Mol Biol, 16, 574-581.  
19211782 F.Yi, P.Zhu, N.Southall, J.Inglese, C.P.Austin, W.Zheng, and L.Regan (2009).
An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction.
  J Biomol Screen, 14, 273-281.  
19082595 G.Watanabe, K.E.Behrns, J.S.Kim, and R.D.Kim (2009).
Heat shock protein 90 inhibition abrogates hepatocellular cancer growth through cdc2-mediated G2/M cell cycle arrest and apoptosis.
  Cancer Chemother Pharmacol, 64, 433-443.  
18987995 J.Hernández Torres, N.Papandreou, and J.Chomilier (2009).
Sequence analyses reveal that a TPR-DP module, surrounded by recombinable flanking introns, could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins.
  Cell Stress Chaperones, 14, 281-289.  
18636345 J.L.Johnson, and C.Brown (2009).
Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.
  Cell Stress Chaperones, 14, 83-94.  
19581297 J.Li, X.Qian, J.Hu, and B.Sha (2009).
Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.
  J Biol Chem, 284, 23852-23859.
PDB codes: 3fp2 3fp3 3fp4
19014346 K.Shirasu (2009).
The HSP90-SGT1 chaperone complex for NLR immune sensors.
  Annu Rev Plant Biol, 60, 139-164.  
19444470 K.W.Modisakeng, M.Jiwaji, E.R.Pesce, J.Robert, C.T.Amemiya, R.A.Dorrington, and G.L.Blatch (2009).
Isolation of a Latimeria menadoensis heat shock protein 70 (Lmhsp70) that has all the features of an inducible gene and encodes a functional molecular chaperone.
  Mol Genet Genomics, 282, 185-196.  
20003465 K.Watanabe, M.Tachibana, S.Kim, and M.Watarai (2009).
EEVD motif of heat shock cognate protein 70 contributes to bacterial uptake by trophoblast giant cells.
  J Biomed Sci, 16, 113.  
19286558 M.Bayer, T.Nawy, C.Giglione, M.Galli, T.Meinnel, and W.Lukowitz (2009).
Paternal control of embryonic patterning in Arabidopsis thaliana.
  Science, 323, 1485-1488.  
19309728 M.E.Jackrel, R.Valverde, and L.Regan (2009).
Redesign of a protein-peptide interaction: characterization and applications.
  Protein Sci, 18, 762-774.
PDB code: 3fwv
19362536 M.E.Matyskiela, and D.O.Morgan (2009).
Analysis of activator-binding sites on the APC/C supports a cooperative substrate-binding mechanism.
  Mol Cell, 34, 68-80.  
19478065 M.Lunelli, R.K.Lokareddy, A.Zychlinsky, and M.Kolbe (2009).
IpaB-IpgC interaction defines binding motif for type III secretion translocator.
  Proc Natl Acad Sci U S A, 106, 9661-9666.
PDB codes: 3gyz 3gz1
19553156 M.R.Arkin, and A.Whitty (2009).
The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions.
  Curr Opin Chem Biol, 13, 284-290.  
19553666 O.Hainzl, M.C.Lapina, J.Buchner, and K.Richter (2009).
The charged linker region is an important regulator of Hsp90 function.
  J Biol Chem, 284, 22559-22567.  
19198901 O.Mirus, T.Bionda, A.von Haeseler, and E.Schleiff (2009).
Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria.
  J Mol Model, 15, 971-982.  
19553200 O.Ostrovsky, C.A.Makarewich, E.L.Snapp, and Y.Argon (2009).
An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.
  Proc Natl Acad Sci U S A, 106, 11600-11605.  
19691130 R.Alag, N.Bharatham, A.Dong, T.Hills, A.Harikishore, A.A.Widjaja, S.G.Shochat, R.Hui, and H.S.Yoon (2009).
Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
  Protein Sci, 18, 2115-2124.
PDB code: 2fbn
19302411 R.Bhowmick, M.Li, J.Sun, S.A.Baker, C.Insinna, and J.C.Besharse (2009).
Photoreceptor IFT complexes containing chaperones, guanylyl cyclase 1 and rhodopsin.
  Traffic, 10, 648-663.  
19028997 R.F.Waller, C.Jabbour, N.C.Chan, N.Celik, V.A.Likic, T.D.Mulhern, and T.Lithgow (2009).
Evidence of a reduced and modified mitochondrial protein import apparatus in microsporidian mitosomes.
  Eukaryot Cell, 8, 19-26.  
19399909 S.H.Millson, J.M.Nuttall, M.Mollapour, and P.W.Piper (2009).
The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae.
  Yeast, 26, 339-347.  
19860737 S.Patury, Y.Miyata, and J.E.Gestwicki (2009).
Pharmacological targeting of the Hsp70 chaperone.
  Curr Top Med Chem, 9, 1337-1351.  
19849724 T.Gkouvitsas, D.Kontogiannatos, and A.Kourti (2009).
Expression of the Hsp83 gene in response to diapause and thermal stress in the moth Sesamia nonagrioides.
  Insect Mol Biol, 18, 759-768.  
19586912 T.Kajander, J.N.Sachs, A.Goldman, and L.Regan (2009).
Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering.
  J Biol Chem, 284, 25364-25374.
PDB code: 3esk
19141287 V.M.Bolanos-Garcia, T.Kiyomitsu, S.D'Arcy, D.Y.Chirgadze, J.G.Grossmann, D.Matak-Vinkovic, A.R.Venkitaraman, M.Yanagida, C.V.Robinson, and T.L.Blundell (2009).
The crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochores.
  Structure, 17, 105-116.
PDB code: 3esl
19277710 Y.Chen, M.Zhao, S.Wang, J.Chen, Y.Wang, Q.Cao, W.Zhou, J.Liu, Z.Xu, G.Tong, and J.Li (2009).
A novel role for DYX1C1, a chaperone protein for both Hsp70 and Hsp90, in breast cancer.
  J Cancer Res Clin Oncol, 135, 1265-1276.  
19179103 Y.Li, T.Zhang, S.J.Schwartz, and D.Sun (2009).
New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.
  Drug Resist Updat, 12, 17-27.  
18771283 A.Banerjee, S.Periyasamy, I.M.Wolf, T.D.Hinds, W.Yong, W.Shou, and E.R.Sanchez (2008).
Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins.
  Biochemistry, 47, 10471-10480.  
18991631 A.Donnelly, and B.S.Blagg (2008).
Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.
  Curr Med Chem, 15, 2702-2717.  
18808717 A.M.Nicola, R.V.Andrade, A.S.Dantas, P.A.Andrade, F.B.Arraes, L.Fernandes, I.Silva-Pereira, and M.S.Felipe (2008).
The stress responsive and morphologically regulated hsp90 gene from Paracoccidioides brasiliensis is essential to cell viability.
  BMC Microbiol, 8, 158.  
18922470 C.K.Vaughan, M.Mollapour, J.R.Smith, A.Truman, B.Hu, V.M.Good, B.Panaretou, L.Neckers, P.A.Clarke, P.Workman, P.W.Piper, C.Prodromou, and L.H.Pearl (2008).
Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.
  Mol Cell, 31, 886-895.  
19075114 D.Baird, C.Stefan, A.Audhya, S.Weys, and S.D.Emr (2008).
Assembly of the PtdIns 4-kinase Stt4 complex at the plasma membrane requires Ypp1 and Efr3.
  J Cell Biol, 183, 1061-1074.  
17803240 D.Han, K.Kim, J.Oh, J.Park, and Y.Kim (2008).
TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7.
  Proteins, 70, 900-914.
PDB code: 2e2e
18725399 E.A.Champion, B.H.Lane, M.E.Jackrel, L.Regan, and S.J.Baserga (2008).
A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21 is essential for efficient pre-rRNA processing.
  Mol Cell Biol, 28, 6547-6556.  
18452231 E.Rousselet, A.Martelli, M.Chevallet, H.Diemer, A.Van Dorsselaer, T.Rabilloud, and J.M.Moulis (2008).
Zinc adaptation and resistance to cadmium toxicity in mammalian cells: molecular insight by proteomic analysis.
  Proteomics, 8, 2244-2255.  
18458105 F.Ran, M.Bali, and C.A.Michels (2008).
Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant alleles.
  Genetics, 179, 331-343.  
18320024 G.Crevel, D.Bennett, and S.Cotterill (2008).
The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.
  PLoS ONE, 3, e0001737.  
18408180 J.Hidalgo-de-Quintana, R.J.Evans, M.E.Cheetham, and J.van der Spuy (2008).
The Leber congenital amaurosis protein AIPL1 functions as part of a chaperone heterocomplex.
  Invest Ophthalmol Vis Sci, 49, 2878-2887.  
18776008 J.Koo, S.Tammam, S.Y.Ku, L.M.Sampaleanu, L.L.Burrows, and P.L.Howell (2008).
PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.
  J Bacteriol, 190, 6961-6969.
PDB code: 2ho1
  18827603 J.Okamoto, I.Mikami, Y.Tominaga, K.M.Kuchenbecker, Y.C.Lin, D.T.Bravo, G.Clement, A.Yagui-Beltran, M.R.Ray, K.Koizumi, B.He, and D.M.Jablons (2008).
Inhibition of Hsp90 leads to cell cycle arrest and apoptosis in human malignant pleural mesothelioma.
  J Thorac Oncol, 3, 1089-1095.  
  18259061 J.Tao, Y.Wu, D.Ron, and B.Sha (2008).
Preliminary X-ray crystallographic studies of mouse UPR responsive protein P58(IPK) TPR fragment.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 108-110.  
18266909 J.W.Hammond, K.Griffin, G.T.Jih, J.Stuckey, and K.J.Verhey (2008).
Co-operative versus independent transport of different cargoes by Kinesin-1.
  Traffic, 9, 725-741.  
18215318 L.Brocchieri, E.Conway de Macario, and A.J.Macario (2008).
hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions.
  BMC Evol Biol, 8, 19.  
18326487 L.Liu, R.Srikakulam, and D.A.Winkelmann (2008).
Unc45 activates Hsp90-dependent folding of the myosin motor domain.
  J Biol Chem, 283, 13185-13193.  
18490186 M.Kosmaoglou, N.Schwarz, J.S.Bett, and M.E.Cheetham (2008).
Molecular chaperones and photoreceptor function.
  Prog Retin Eye Res, 27, 434-449.  
17634984 M.Palaiomylitou, A.Tartas, D.Vlachakis, D.Tzamarias, and M.Vlassi (2008).
Investigating the structural stability of the Tup1-interaction domain of Ssn6: evidence for a conformational change on the complex.
  Proteins, 70, 72-82.  
18373550 M.Sgobba, G.Degliesposti, A.M.Ferrari, and G.Rastelli (2008).
Structural models and binding site prediction of the C-terminal domain of human Hsp90: a new target for anticancer drugs.
  Chem Biol Drug Des, 71, 420-433.  
18037921 P.Taylor, E.Blackburn, Y.G.Sheng, S.Harding, K.Y.Hsin, D.Kan, S.Shave, and M.D.Walkinshaw (2008).
Ligand discovery and virtual screening using the program LIDAEUS.
  Br J Pharmacol, 153, S55-S67.  
18587674 Q.Liu, J.Gao, X.Chen, Y.Chen, J.Chen, S.Wang, J.Liu, X.Liu, and J.Li (2008).
HBP21: a novel member of TPR motif family, as a potential chaperone of heat shock protein 70 in proliferative vitreoretinopathy (PVR) and breast cancer.
  Mol Biotechnol, 40, 231-240.  
18923554 R.A.Daly, and C.P.Lostroh (2008).
Genetic analysis of the Salmonella transcription factor HilA.
  Can J Microbiol, 54, 854-860.  
18478096 R.Srikakulam, L.Liu, and D.A.Winkelmann (2008).
Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain.
  PLoS ONE, 3, e2137.  
18268103 R.Zhao, Y.Kakihara, A.Gribun, J.Huen, G.Yang, M.Khanna, M.Costanzo, R.L.Brost, C.Boone, T.R.Hughes, C.M.Yip, and W.A.Houry (2008).
Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.
  J Cell Biol, 180, 563-578.  
18699990 S.Cao, G.H.Ho, and V.C.Lin (2008).
Tetratricopeptide repeat domain 9A is an interacting protein for tropomyosin Tm5NM-1.
  BMC Cancer, 8, 231.  
18412542 S.H.Millson, C.K.Vaughan, C.Zhai, M.M.Ali, B.Panaretou, P.W.Piper, L.H.Pearl, and C.Prodromou (2008).
Chaperone ligand-discrimination by the TPR-domain protein Tah1.
  Biochem J, 413, 261-268.  
18182494 S.J.Du, H.Li, Y.Bian, and Y.Zhong (2008).
Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos.
  Proc Natl Acad Sci U S A, 105, 554-559.  
18442971 S.K.Wandinger, K.Richter, and J.Buchner (2008).
The Hsp90 chaperone machinery.
  J Biol Chem, 283, 18473-18477.  
18669640 S.Shimamoto, M.Takata, M.Tokuda, F.Oohira, H.Tokumitsu, and R.Kobayashi (2008).
Interactions of S100A2 and S100A6 with the tetratricopeptide repeat proteins, Hsp90/Hsp70-organizing protein and kinesin light chain.
  J Biol Chem, 283, 28246-28258.  
18069675 T.Sakiyama, H.Fujita, and H.Tsubouchi (2008).
Autoantibodies against ubiquitination factor E4A (UBE4A) are associated with severity of Crohn's disease.
  Inflamm Bowel Dis, 14, 310-317.  
18566891 V.A.Jarymowycz, A.L.Cortajarena, L.Regan, and M.J.Stone (2008).
Comparison of the backbone dynamics of a natural and a consensus designed 3-TPR domain.
  J Biomol NMR, 41, 169-178.  
17079733 A.Bracale, F.Cesca, V.E.Neubrand, T.P.Newsome, M.Way, and G.Schiavo (2007).
Kidins220/ARMS is transported by a kinesin-1-based mechanism likely to be involved in neuronal differentiation.
  Mol Biol Cell, 18, 142-152.  
17485476 C.H.Tung, and J.M.Yang (2007).
fastSCOP: a fast web server for recognizing protein structural domains and SCOP superfamilies.
  Nucleic Acids Res, 35, W438-W443.  
17380304 C.Wang, Q.Tian, Z.Hou, M.Mucha, M.Aukerman, and O.A.Olsen (2007).
The Arabidopsis thaliana AT PRP39-1 gene, encoding a tetratricopeptide repeat protein with similarity to the yeast pre-mRNA processing protein PRP39, affects flowering time.
  Plant Cell Rep, 26, 1357-1366.  
18158900 E.M.Dunleavy, A.L.Pidoux, M.Monet, C.Bonilla, W.Richardson, G.L.Hamilton, K.Ekwall, P.J.McLaughlin, and R.C.Allshire (2007).
A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its deposition at fission yeast centromeres.
  Mol Cell, 28, 1029-1044.  
17101799 J.L.Johnson, A.Halas, and G.Flom (2007).
Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.
  Mol Cell Biol, 27, 768-776.  
17080288 K.Aviezer-Hagai, J.Skovorodnikova, M.Galigniana, O.Farchi-Pisanty, E.Maayan, S.Bocovza, Y.Efrat, P.von Koskull-Döring, N.Ohad, and A.Breiman (2007).
Arabidopsis immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit tissue specificity, are heat-stress induced, and bind HSP90.
  Plant Mol Biol, 63, 237-255.  
17283040 K.M.Hatle, W.Neveu, O.Dienz, S.Rymarchyk, R.Barrantes, S.Hale, N.Farley, K.M.Lounsbury, J.P.Bond, D.Taatjes, and M.Rincón (2007).
Methylation-controlled J protein promotes c-Jun degradation to prevent ABCB1 transporter expression.
  Mol Cell Biol, 27, 2952-2966.  
17826744 M.A.Brown, L.Zhu, C.Schmidt, and P.W.Tucker (2007).
Hsp90--from signal transduction to cell transformation.
  Biochem Biophys Res Commun, 363, 241-246.  
18049904 M.D.Heitzer, I.M.Wolf, E.R.Sanchez, S.F.Witchel, and D.B.DeFranco (2007).
Glucocorticoid receptor physiology.
  Rev Endocr Metab Disord, 8, 321-330.  
17825565 M.J.Baker, A.E.Frazier, J.M.Gulbis, and M.T.Ryan (2007).
Mitochondrial protein-import machinery: correlating structure with function.
  Trends Cell Biol, 17, 456-464.  
17596514 M.K.Bhangoo, S.Tzankov, A.C.Fan, K.Dejgaard, D.Y.Thomas, and J.C.Young (2007).
Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.
  Mol Biol Cell, 18, 3414-3428.  
17199898 M.R.Karpenahalli, A.N.Lupas, and J.Söding (2007).
TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences.
  BMC Bioinformatics, 8, 2.  
17573546 M.Ren, A.Santhanam, P.Lee, A.Caplan, and S.Garrett (2007).
Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.
  Eukaryot Cell, 6, 1363-1372.  
17884824 R.C.Wells, L.K.Picton, S.C.Williams, F.J.Tan, and R.B.Hill (2007).
Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm.
  J Biol Chem, 282, 33769-33775.  
17441508 S.T.Liou, M.Y.Cheng, and C.Wang (2007).
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.
  Cell Stress Chaperones, 12, 59-70.  
17569659 V.E.Walker, R.Atanasiu, H.Lam, and A.Shrier (2007).
Co-chaperone FKBP38 promotes HERG trafficking.
  J Biol Chem, 282, 23509-23516.  
17386263 Y.Bai, T.C.Auperin, C.Y.Chou, G.G.Chang, J.L.Manley, and L.Tong (2007).
Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursors.
  Mol Cell, 25, 863-875.
PDB codes: 2ond 2ooe
17998537 Y.Zhang, and D.C.Chan (2007).
Structural basis for recruitment of mitochondrial fission complexes by Fis1.
  Proc Natl Acad Sci U S A, 104, 18526-18530.
PDB codes: 2pqn 2pqr
16757946 A.Bracher, and F.U.Hartl (2006).
Hsp90 structure: when two ends meet.
  Nat Struct Mol Biol, 13, 478-480.  
16968702 A.C.Fan, M.K.Bhangoo, and J.C.Young (2006).
Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import.
  J Biol Chem, 281, 33313-33324.  
16253993 A.Gasch, S.Wiesner, P.Martin-Malpartida, X.Ramirez-Espain, L.Ruiz, and M.J.Macias (2006).
The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domains.
  J Biol Chem, 281, 356-364.
PDB code: 2b7e
17005566 A.J.Bredemeyer, P.E.Carrigan, T.A.Fehniger, D.F.Smith, and T.J.Ley (2006).
Hop cleavage and function in granzyme B-induced apoptosis.
  J Biol Chem, 281, 37130-37141.  
16461275 A.J.Perry, J.M.Hulett, V.A.Likić, T.Lithgow, and P.R.Gooley (2006).
Convergent evolution of receptors for protein import into mitochondria.
  Curr Biol, 16, 221-229.
PDB code: 1zu2
16760430 A.Konecna, R.Frischknecht, J.Kinter, A.Ludwig, M.Steuble, V.Meskenaite, M.Indermühle, M.Engel, C.Cen, J.M.Mateos, P.Streit, and P.Sonderegger (2006).
Calsyntenin-1 docks vesicular cargo to kinesin-1.
  Mol Biol Cell, 17, 3651-3663.  
16641492 A.L.Cortajarena, and L.Regan (2006).
Ligand binding by TPR domains.
  Protein Sci, 15, 1193-1198.  
16807248 B.H.Kang, and D.C.Altieri (2006).
Regulation of survivin stability by the aryl hydrocarbon receptor-interacting protein.
  J Biol Chem, 281, 24721-24727.  
16385039 C.Bongiorni, R.Stoessel, D.Shoemaker, and M.Perego (2006).
Rap phosphatase of virulence plasmid pXO1 inhibits Bacillus anthracis sporulation.
  J Bacteriol, 188, 487-498.  
16822835 C.H.Chou, R.S.Lee, and H.F.Yang-Yen (2006).
An internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathway.
  Mol Biol Cell, 17, 3952-3963.  
16219779 G.Flom, J.Weekes, J.J.Williams, and J.L.Johnson (2006).
Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae.
  Genetics, 172, 41-51.  
16897471 H.Yoshida, K.L.Wang, C.M.Chang, K.Mori, E.Uchida, and J.R.Ecker (2006).
The ACC synthase TOE sequence is required for interaction with ETO1 family proteins and destabilization of target proteins.
  Plant Mol Biol, 62, 427-437.  
16438680 J.P.Burnie, T.L.Carter, S.J.Hodgetts, and R.C.Matthews (2006).
Fungal heat-shock proteins in human disease.
  FEMS Microbiol Rev, 30, 53-88.  
16687570 J.Xiao, L.S.Kim, and T.R.Graham (2006).
Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo.
  Mol Biol Cell, 17, 3281-3290.  
16756493 L.H.Pearl, and C.Prodromou (2006).
Structure and mechanism of the Hsp90 molecular chaperone machinery.
  Annu Rev Biochem, 75, 271-294.  
16477027 L.J.Alderwick, V.Molle, L.Kremer, A.J.Cozzone, T.R.Dafforn, G.S.Besra, and K.Fütterer (2006).
Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis.
  Proc Natl Acad Sci U S A, 103, 2558-2563.
PDB codes: 2fez 2ff4
17201776 M.A.Theodoraki, and A.C.Mintzas (2006).
cDNA cloning, heat shock regulation and developmental expression of the hsp83 gene in the Mediterranean fruit fly Ceratitis capitata.
  Insect Mol Biol, 15, 839-852.  
16531226 M.J.Cliff, R.Harris, D.Barford, J.E.Ladbury, and M.A.Williams (2006).
Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90.
  Structure, 14, 415-426.
PDB code: 2bug
17158958 M.L.Chou, C.C.Chu, L.J.Chen, M.Akita, and H.M.Li (2006).
Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts.
  J Cell Biol, 175, 893-900.  
16625188 M.M.Ali, S.M.Roe, C.K.Vaughan, P.Meyer, B.Panaretou, P.W.Piper, C.Prodromou, and L.H.Pearl (2006).
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.
  Nature, 440, 1013-1017.
PDB codes: 2cg9 2cge
16452615 P.E.Carrigan, L.A.Sikkink, D.F.Smith, and M.Ramirez-Alvarado (2006).
Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.
  Protein Sci, 15, 522-532.  
16682404 R.F.Nelson, K.A.Glenn, V.M.Miller, H.Wen, and H.L.Paulson (2006).
A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control.
  J Biol Chem, 281, 20242-20251.  
16421106 R.K.Allan, D.Mok, B.K.Ward, and T.Ratajczak (2006).
Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.
  J Biol Chem, 281, 7161-7171.  
16407978 S.K.Wandinger, M.H.Suhre, H.Wegele, and J.Buchner (2006).
The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90.
  EMBO J, 25, 367-376.  
16723661 S.Liu, R.Rauhut, H.P.Vornlocher, and R.Lührmann (2006).
The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP.
  RNA, 12, 1418-1430.  
16923392 S.Oyadomari, C.Yun, E.A.Fisher, N.Kreglinger, G.Kreibich, M.Oyadomari, H.P.Harding, A.G.Goodman, H.Harant, J.L.Garrison, J.Taunton, M.G.Katze, and D.Ron (2006).
Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload.
  Cell, 126, 727-739.  
16619024 S.Qbadou, T.Becker, O.Mirus, I.Tews, J.Soll, and E.Schleiff (2006).
The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64.
  EMBO J, 25, 1836-1847.  
16803880 S.R.Bushell, S.P.Bottomley, J.Rossjohn, and T.Beddoe (2006).
Tracking the unfolding pathway of a multirepeat protein via tryptophan scanning: evidence of localized instability in the mitochondrial import receptor Tom70.
  J Biol Chem, 281, 24345-24350.  
16921518 S.Sonoda, K.Fukumoto, Y.Izumi, H.Yoshida, and H.Tsumuki (2006).
Cloning of heat shock protein genes (hsp90 and hsc70) and their expression during larval diapause and cold tolerance acquisition in the rice stem borer, Chilo suppressalis Walker.
  Arch Insect Biochem Physiol, 63, 36-47.  
16703614 S.Sonoda, M.Ashfaq, and H.Tsumuki (2006).
Cloning and nucleotide sequencing of three heat shock protein genes (hsp90, hsc70, and hsp19.5) from the diamondback moth, Plutella xylostella (L.) and their expression in relation to developmental stage and temperature.
  Arch Insect Biochem Physiol, 62, 80-90.  
17024179 T.Okamoto, Y.Nishimura, T.Ichimura, K.Suzuki, T.Miyamura, T.Suzuki, K.Moriishi, and Y.Matsuura (2006).
Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90.
  EMBO J, 25, 5015-5025.  
16314389 T.S.Kim, C.Y.Jang, H.D.Kim, J.Y.Lee, B.Y.Ahn, and J.Kim (2006).
Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation.
  Mol Biol Cell, 17, 824-833.  
16880507 Y.Liao, R.D.Moir, and I.M.Willis (2006).
Interactions of Brf1 peptides with the tetratricopeptide repeat-containing subunit of TFIIIC inhibit and promote preinitiation complex assembly.
  Mol Cell Biol, 26, 5946-5956.  
16299395 Y.Tutar, Y.Song, and D.C.Masison (2006).
Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.
  Genetics, 172, 851-861.  
16767096 Y.Wu, and B.Sha (2006).
Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p.
  Nat Struct Mol Biol, 13, 589-593.
PDB code: 2gw1
15968044 C.Bongiorni, S.Ishikawa, S.Stephenson, N.Ogasawara, and M.Perego (2005).
Synergistic regulation of competence development in Bacillus subtilis by two Rap-Phr systems.
  J Bacteriol, 187, 4353-4361.  
15634341 C.G.Wilson, T.Kajander, and L.Regan (2005).
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
  FEBS J, 272, 166-179.
PDB code: 1xnf
15831501 D.C.David, S.Hauptmann, I.Scherping, K.Schuessel, U.Keil, P.Rizzu, R.Ravid, S.Dröse, U.Brandt, W.E.Müller, A.Eckert, and J.Götz (2005).
Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice.
  J Biol Chem, 280, 23802-23814.  
15871019 G.Flom, J.Weekes, and J.L.Johnson (2005).
Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.
  Curr Genet, 47, 368-380.  
16015602 G.W.Jones, and M.F.Tuite (2005).
Chaperoning prions: the cellular machinery for propagating an infectious protein?
  Bioessays, 27, 823-832.  
16091151 H.Yoshida, M.Nagata, K.Saito, K.L.Wang, and J.R.Ecker (2005).
Arabidopsis ETO1 specifically interacts with and negatively regulates type 2 1-aminocyclopropane-1-carboxylate synthases.
  BMC Plant Biol, 5, 14.  
15935782 J.Kim, S.Sitaraman, A.Hierro, B.M.Beach, G.Odorizzi, and J.H.Hurley (2005).
Structural basis for endosomal targeting by the Bro1 domain.
  Dev Cell, 8, 937-947.
PDB code: 1zb1
16038411 J.R.Hwang, C.Zhang, and C.Patterson (2005).
C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis.
  Cell Stress Chaperones, 10, 147-156.  
15577939 J.Yang, S.M.Roe, M.J.Cliff, M.A.Williams, J.E.Ladbury, P.T.Cohen, and D.Barford (2005).
Molecular basis for TPR domain-mediated regulation of protein phosphatase 5.
  EMBO J, 24, 1.
PDB code: 1wao
15782428 L.Moroder (2005).
Isosteric replacement of sulfur with other chalcogens in peptides and proteins.
  J Pept Sci, 11, 187-214.  
16175177 L.Whitesell, and S.L.Lindquist (2005).
HSP90 and the chaperoning of cancer.
  Nat Rev Cancer, 5, 761-772.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
15770419 M.P.Mayer, and B.Bukau (2005).
Hsp70 chaperones: cellular functions and molecular mechanism.
  Cell Mol Life Sci, 62, 670-684.  
16307917 M.Zhang, M.Windheim, S.M.Roe, M.Peggie, P.Cohen, C.Prodromou, and L.H.Pearl (2005).
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
  Mol Cell, 20, 525-538.
PDB codes: 2c2l 2c2v
15632128 P.E.Carrigan, D.L.Riggs, M.Chinkers, and D.F.Smith (2005).
Functional comparison of human and Drosophila Hop reveals novel role in steroid receptor maturation.
  J Biol Chem, 280, 8906-8911.  
16869789 P.Workman (2005).
Drugging the cancer kinome: progress and challenges in developing personalized molecular cancer therapeutics.
  Cold Spring Harb Symp Quant Biol, 70, 499-515.  
16027977 R.Bruggmann, O.Abderhalden, P.Reymond, and R.Dudler (2005).
Analysis of epidermis- and mesophyll-specific transcript accumulation in powdery mildew-inoculated wheat leaves.
  Plant Mol Biol, 58, 247-267.  
15766533 R.Zhao, M.Davey, Y.C.Hsu, P.Kaplanek, A.Tong, A.B.Parsons, N.Krogan, G.Cagney, D.Mai, J.Greenblatt, C.Boone, A.Emili, and W.A.Houry (2005).
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.
  Cell, 120, 715-727.  
16333321 R.Zhao, and W.A.Houry (2005).
Hsp90: a chaperone for protein folding and gene regulation.
  Biochem Cell Biol, 83, 703-710.  
15381148 T.H.Davies, and E.R.Sánchez (2005).
FKBP52.
  Int J Biochem Cell Biol, 37, 42-47.  
16194281 T.J.Magliery, and L.Regan (2005).
Sequence variation in ligand binding sites in proteins.
  BMC Bioinformatics, 6, 240.  
16040755 V.M.Bolanos-Garcia, S.Beaufils, A.Renault, J.G.Grossmann, S.Brewerton, M.Lee, A.Venkitaraman, and T.L.Blundell (2005).
The conserved N-terminal region of the mitotic checkpoint protein BUBR1: a putative TPR motif of high surface activity.
  Biophys J, 89, 2640-2649.  
16841168 V.M.Carr (2005).
Induced and constitutive heat shock protein expression in the olfactory system--a review, new findings, and some perspectives.
  J Neurocytol, 34, 269-293.  
16100115 Y.Song, and D.C.Masison (2005).
Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).
  J Biol Chem, 280, 34178-34185.  
15497503 A.Carrello, R.K.Allan, S.L.Morgan, B.A.Owen, D.Mok, B.K.Ward, R.F.Minchin, D.O.Toft, and T.Ratajczak (2004).
Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.
  Cell Stress Chaperones, 9, 167-181.  
15107424 B.He, S.Bai, A.T.Hnat, R.I.Kalman, J.T.Minges, C.Patterson, and E.M.Wilson (2004).
An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP).
  J Biol Chem, 279, 30643-30653.  
15159550 B.Wu, P.Li, Y.Liu, Z.Lou, Y.Ding, C.Shu, S.Ye, M.Bartlam, B.Shen, and Z.Rao (2004).
3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.
  Proc Natl Acad Sci U S A, 101, 8348-8353.
PDB codes: 1p5q 1q1c 1qz2
14970196 C.Kamm, H.Boston, J.Hewett, J.Wilbur, D.P.Corey, P.I.Hanson, V.Ramesh, and X.O.Breakefield (2004).
The early onset dystonia protein torsinA interacts with kinesin light chain 1.
  J Biol Chem, 279, 19882-19892.  
15497498 D.F.Smith (2004).
Tetratricopeptide repeat cochaperones in steroid receptor complexes.
  Cell Stress Chaperones, 9, 109-121.  
15082786 G.Jones, Y.Song, S.Chung, and D.C.Masison (2004).
Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding.
  Mol Cell Biol, 24, 3928-3937.  
14705031 J.A.Dohm, S.J.Lee, J.M.Hardwick, R.B.Hill, and A.G.Gittis (2004).
Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold.
  Proteins, 54, 153-156.
PDB code: 1nzn
14998780 J.Burnie, and R.Matthews (2004).
Genetically recombinant antibodies: new therapeutics against candidiasis.
  Expert Opin Biol Ther, 4, 233-241.  
15459659 J.C.Young, V.R.Agashe, K.Siegers, and F.U.Hartl (2004).
Pathways of chaperone-mediated protein folding in the cytosol.
  Nat Rev Mol Cell Biol, 5, 781-791.  
15036203 J.M.Barral, S.A.Broadley, G.Schaffar, and F.U.Hartl (2004).
Roles of molecular chaperones in protein misfolding diseases.
  Semin Cell Dev Biol, 15, 17-29.  
15611333 J.M.Younger, H.Y.Ren, L.Chen, C.Y.Fan, A.Fields, C.Patterson, and D.M.Cyr (2004).
A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase.
  J Cell Biol, 167, 1075-1085.  
15347646 J.van der Spuy, and M.E.Cheetham (2004).
The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments.
  J Biol Chem, 279, 48038-48047.  
15456868 L.B.Lingelbach, and K.B.Kaplan (2004).
The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly.
  Mol Cell Biol, 24, 8938-8950.  
15028727 L.Shaner, A.Trott, J.L.Goeckeler, J.L.Brodsky, and K.A.Morano (2004).
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.
  J Biol Chem, 279, 21992-22001.  
15361863 M.Jínek, J.Rehwinkel, B.D.Lazarus, E.Izaurralde, J.A.Hanover, and E.Conti (2004).
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha.
  Nat Struct Mol Biol, 11, 1001-1007.
PDB code: 1w3b
15456751 M.Pekkala, R.Hieta, U.Bergmann, K.I.Kivirikko, R.K.Wierenga, and J.Myllyharju (2004).
The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues.
  J Biol Chem, 279, 52255-52261.
PDB code: 1tjc
15044454 O.Hainzl, H.Wegele, K.Richter, and J.Buchner (2004).
Cns1 is an activator of the Ssa1 ATPase activity.
  J Biol Chem, 279, 23267-23273.  
15382137 O.O.Odunuga, V.M.Longshaw, and G.L.Blatch (2004).
Hop: more than an Hsp70/Hsp90 adaptor protein.
  Bioessays, 26, 1058-1068.  
14960564 P.E.Carrigan, G.M.Nelson, P.J.Roberts, J.Stoffer, D.L.Riggs, and D.F.Smith (2004).
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
  J Biol Chem, 279, 16185-16193.  
14760739 P.Forrer, H.K.Binz, M.T.Stumpp, and A.Plückthun (2004).
Consensus design of repeat proteins.
  Chembiochem, 5, 183-189.  
14739935 P.Meyer, C.Prodromou, C.Liao, B.Hu, S.Mark Roe, C.K.Vaughan, I.Vlasic, B.Panaretou, P.W.Piper, and L.H.Pearl (2004).
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
  EMBO J, 23, 511-519.  
14610072 R.Nikolay, T.Wiederkehr, W.Rist, G.Kramer, M.P.Mayer, and B.Bukau (2004).
Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity.
  J Biol Chem, 279, 2673-2678.  
15274928 S.F.Harris, A.K.Shiau, and D.A.Agard (2004).
The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.
  Structure, 12, 1087-1097.
PDB code: 1sf8
15189447 S.Hatakeyama, M.Matsumoto, M.Yada, and K.I.Nakayama (2004).
Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones.
  Genes Cells, 9, 533-548.  
15316022 T.Beddoe, S.R.Bushell, M.A.Perugini, T.Lithgow, T.D.Mulhern, S.P.Bottomley, and J.Rossjohn (2004).
A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway.
  J Biol Chem, 279, 46448-46454.  
14761955 Y.T.Lee, J.Jacob, W.Michowski, M.Nowotny, J.Kuznicki, and W.J.Chazin (2004).
Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain.
  J Biol Chem, 279, 16511-16517.
PDB code: 1rl1
15538384 Y.Tateishi, Y.Kawabe, T.Chiba, S.Murata, K.Ichikawa, A.Murayama, K.Tanaka, T.Baba, S.Kato, and J.Yanagisawa (2004).
Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.
  EMBO J, 23, 4813-4823.  
12612599 A.J.Caplan, S.Jackson, and D.Smith (2003).
Hsp90 reaches new heights. Conference on the Hsp90 chaperone machine.
  EMBO Rep, 4, 126-130.  
14504384 A.Takahashi, C.Casais, K.Ichimura, and K.Shirasu (2003).
HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.
  Proc Natl Acad Sci U S A, 100, 11777-11782.  
12773536 C.C.Chou, F.Forouhar, Y.H.Yeh, H.L.Shr, C.Wang, and C.D.Hsiao (2003).
Crystal structure of the C-terminal 10-kDa subdomain of Hsc70.
  J Biol Chem, 278, 30311-30316.
PDB code: 1ud0
12538866 C.R.Sinars, J.Cheung-Flynn, R.A.Rimerman, J.G.Scammell, D.F.Smith, and J.Clardy (2003).
Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes.
  Proc Natl Acad Sci U S A, 100, 868-873.
PDB codes: 1kt0 1kt1
12795688 D.G.Cole (2003).
The intraflagellar transport machinery of Chlamydomonas reinhardtii.
  Traffic, 4, 435-442.  
12948778 E.R.Main, S.E.Jackson, and L.Regan (2003).
The folding and design of repeat proteins: reaching a consensus.
  Curr Opin Struct Biol, 13, 482-489.  
12737816 E.R.Main, Y.Xiong, M.J.Cocco, L.D'Andrea, and L.Regan (2003).
Design of stable alpha-helical arrays from an idealized TPR motif.
  Structure, 11, 497-508.
PDB codes: 1na0 1na3
12810716 G.B.Bolger, A.H.Peden, M.R.Steele, C.MacKenzie, D.G.McEwan, D.A.Wallace, E.Huston, G.S.Baillie, and M.D.Houslay (2003).
Attenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2.
  J Biol Chem, 278, 33351-33363.  
12671002 G.J.Gatto, and J.M.Berg (2003).
Nonrandom tripeptide sequence distributions at protein carboxyl termini.
  Genome Res, 13, 617-623.  
14627198 G.M.Nelson, H.Huffman, and D.F.Smith (2003).
Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip.
  Cell Stress Chaperones, 8, 125-133.  
12604615 G.P.Lotz, H.Lin, A.Harst, and W.M.Obermann (2003).
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.
  J Biol Chem, 278, 17228-17235.  
  12618389 G.W.Jones, and D.C.Masison (2003).
Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+].
  Genetics, 163, 495-506.  
12956947 H.C.Vodermaier, C.Gieffers, S.Maurer-Stroh, F.Eisenhaber, and J.M.Peters (2003).
TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1.
  Curr Biol, 13, 1459-1468.  
12716905 H.Wegele, M.Haslbeck, J.Reinstein, and J.Buchner (2003).
Sti1 is a novel activator of the Ssa proteins.
  J Biol Chem, 278, 25970-25976.  
14559183 J.C.Young, J.M.Barral, and F.Ulrich Hartl (2003).
More than folding: localized functions of cytosolic chaperones.
  Trends Biochem Sci, 28, 541-547.  
12526792 J.C.Young, N.J.Hoogenraad, and F.U.Hartl (2003).
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.
  Cell, 112, 41-50.  
12611898 J.Cheung-Flynn, P.J.Roberts, D.L.Riggs, and D.F.Smith (2003).
C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90.
  J Biol Chem, 278, 17388-17394.  
12525481 K.Richter, P.Muschler, O.Hainzl, J.Reinstein, and J.Buchner (2003).
Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle.
  J Biol Chem, 278, 10328-10333.  
12950917 L.Core, and M.Perego (2003).
TPR-mediated interaction of RapC with ComA inhibits response regulator-DNA binding for competence development in Bacillus subtilis.
  Mol Microbiol, 49, 1509-1522.  
12837759 M.J.Lees, D.J.Peet, and M.L.Whitelaw (2003).
Defining the role for XAP2 in stabilization of the dioxin receptor.
  J Biol Chem, 278, 35878-35888.  
12799000 M.J.Pallen, M.S.Francis, and K.Fütterer (2003).
Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators.
  FEMS Microbiol Lett, 223, 53-60.
PDB codes: 1ool 1oom 1ooo 1oor 1oos
12805212 M.L.Chou, L.M.Fitzpatrick, S.L.Tu, G.Budziszewski, S.Potter-Lewis, M.Akita, J.Z.Levin, K.Keegstra, and H.M.Li (2003).
Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon.
  EMBO J, 22, 2970-2980.  
12788914 M.Tesic, J.A.Marsh, S.B.Cullinan, and R.F.Gaber (2003).
Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.
  J Biol Chem, 278, 32692-32701.  
12482845 O.O.Odunuga, J.A.Hornby, C.Bies, R.Zimmermann, D.J.Pugh, and G.L.Blatch (2003).
Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.
  J Biol Chem, 278, 6896-6904.  
14622256 P.W.Piper, S.H.Millson, M.Mollapour, B.Panaretou, G.Siligardi, L.H.Pearl, and C.Prodromou (2003).
Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast.
  Eur J Biochem, 270, 4689-4695.  
14532117 Q.Dai, C.Zhang, Y.Wu, H.McDonough, R.A.Whaley, V.Godfrey, H.H.Li, N.Madamanchi, W.Xu, L.Neckers, D.Cyr, and C.Patterson (2003).
CHIP activates HSF1 and confers protection against apoptosis and cellular stress.
  EMBO J, 22, 5446-5458.  
14984055 S.Alberti, C.Esser, and J.Höhfeld (2003).
BAG-1--a nucleotide exchange factor of Hsc70 with multiple cellular functions.
  Cell Stress Chaperones, 8, 225-231.  
12878599 S.Tobaben, F.Varoqueaux, N.Brose, B.Stahl, and G.Meyer (2003).
A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein.
  J Biol Chem, 278, 38376-38383.  
12571865 S.Wax, M.Piecyk, B.Maritim, and P.Anderson (2003).
Geldanamycin inhibits the production of inflammatory cytokines in activated macrophages by reducing the stability and translation of cytokine transcripts.
  Arthritis Rheum, 48, 541-550.  
12492485 S.Yamada, T.Ono, A.Mizuno, and T.K.Nemoto (2003).
A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone.
  Eur J Biochem, 270, 146-154.  
12482863 U.Schmidt, G.M.Wochnik, M.C.Rosenhagen, J.C.Young, F.U.Hartl, F.Holsboer, and T.Rein (2003).
Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptor.
  J Biol Chem, 278, 4926-4931.  
12930823 Y.Liao, I.M.Willis, and R.D.Moir (2003).
The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to overlapping sites in the tetratricopeptide repeats of Tfc4.
  J Biol Chem, 278, 44467-44474.  
11877417 A.Brinker, C.Scheufler, F.Von Der Mulbe, B.Fleckenstein, C.Herrmann, G.Jung, I.Moarefi, and F.U.Hartl (2002).
Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.
  J Biol Chem, 277, 19265-19275.  
11969423 A.J.Ramsey, and M.Chinkers (2002).
Identification of potential physiological activators of protein phosphatase 5.
  Biochemistry, 41, 5625-5632.  
12270919 A.V.Kajava (2002).
What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome.
  J Biol Chem, 277, 49791-49798.  
12145316 B.K.Ward, R.K.Allan, D.Mok, S.E.Temple, P.Taylor, J.Dornan, P.J.Mark, D.J.Shaw, P.Kumar, M.D.Walkinshaw, and T.Ratajczak (2002).
A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90.
  J Biol Chem, 277, 40799-40809.  
12456005 C.Dubacq, R.Guerois, R.Courbeyrette, K.Kitagawa, and C.Mann (2002).
Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast.
  Eukaryot Cell, 1, 568-582.  
12114026 D.M.Cyr, J.Höhfeld, and C.Patterson (2002).
Protein quality control: U-box-containing E3 ubiquitin ligases join the fold.
  Trends Biochem Sci, 27, 368-375.  
11916974 G.Siligardi, B.Panaretou, P.Meyer, S.Singh, D.N.Woolfson, P.W.Piper, L.H.Pearl, and C.Prodromou (2002).
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.
  J Biol Chem, 277, 20151-20159.  
11739742 H.Dumay-Odelot, J.Acker, R.Arrebola, A.Sentenac, and C.Marck (2002).
Multiple roles of the tau131 subunit of yeast transcription factor IIIC (TFIIIC) in TFIIIB assembly.
  Mol Cell Biol, 22, 298-308.  
11809970 J.M.Barral, A.H.Hutagalung, A.Brinker, F.U.Hartl, and H.F.Epstein (2002).
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin.
  Science, 295, 669-671.  
12005211 J.Poland, D.Schadendorf, H.Lage, M.Schnölzer, J.E.Celis, and P.Sinha (2002).
Study of therapy resistance in cancer cells with functional proteome analysis.
  Clin Chem Lab Med, 40, 221-234.  
12456884 K.Aoki, F.Kragler, B.Xoconostle-Cazares, and W.J.Lucas (2002).
A subclass of plant heat shock cognate 70 chaperones carries a motif that facilitates trafficking through plasmodesmata.
  Proc Natl Acad Sci U S A, 99, 16342-16347.  
12161444 M.P.Hernández, W.P.Sullivan, and D.O.Toft (2002).
The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.
  J Biol Chem, 277, 38294-38304.  
11687574 M.Velten, N.Gomez-Vrielynck, A.Chaffotte, and M.M.Ladjimi (2002).
Domain structure of the HSC70 cochaperone, HIP.
  J Biol Chem, 277, 259-266.  
12499358 P.Lee, J.Rao, A.Fliss, E.Yang, S.Garrett, and A.J.Caplan (2002).
The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.
  J Cell Biol, 159, 1051-1059.  
11684692 R.D.Moir, K.V.Puglia, and I.M.Willis (2002).
Autoinhibition of TFIIIB70 binding by the tetratricopeptide repeat-containing subunit of TFIIIC.
  J Biol Chem, 277, 694-701.  
12167707 R.D.Moir, K.V.Puglia, and I.M.Willis (2002).
A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding.
  Mol Cell Biol, 22, 6131-6141.  
11923303 S.Ishikawa, L.Core, and M.Perego (2002).
Biochemical characterization of aspartyl phosphate phosphatase interaction with a phosphorylated response regulator and its inhibition by a pentapeptide.
  J Biol Chem, 277, 20483-20489.  
12491239 S.Walter, and J.Buchner (2002).
Molecular chaperones--cellular machines for protein folding.
  Angew Chem Int Ed Engl, 41, 1098-1113.  
12437126 T.Abbas-Terki, P.A.Briand, O.Donzé, and D.Picard (2002).
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
  Biol Chem, 383, 1335-1342.  
12356871 T.Becker, F.U.Hartl, and F.Wieland (2002).
CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes.
  J Cell Biol, 158, 1277-1285.  
12410806 T.Kamphausen, J.Fanghänel, D.Neumann, B.Schulz, and J.U.Rahfeld (2002).
Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90.
  Plant J, 32, 263-276.  
11914729 T.Kirchhausen (2002).
Single-handed recognition of a sorting traffic motif by the GGA proteins.
  Nat Struct Biol, 9, 241-244.  
11790321 T.Wiederkehr, B.Bukau, and A.Buchberger (2002).
Protein turnover: a CHIP programmed for proteolysis.
  Curr Biol, 12, R26-R28.  
  11973290 W.Zhu, I.R.Rainville, M.Ding, M.Bolus, N.H.Heintz, and D.S.Pederson (2002).
Evidence that the pre-mRNA splicing factor Clf1p plays a role in DNA replication in Saccharomyces cerevisiae.
  Genetics, 160, 1319-1333.  
11959502 X.Zhang, F.Beuron, and P.S.Freemont (2002).
Machinery of protein folding and unfolding.
  Curr Opin Struct Biol, 12, 231-238.  
11259606 A.Kazlauskas, S.Sundström, L.Poellinger, and I.Pongratz (2001).
The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.
  Mol Cell Biol, 21, 2594-2607.  
11511361 C.Demonacos, M.Krstic-Demonacos, and N.B.La Thangue (2001).
A TPR motif cofactor contributes to p300 activity in the p53 response.
  Mol Cell, 8, 71-84.  
11545740 C.Mazza, M.Ohno, A.Segref, I.W.Mattaj, and S.Cusack (2001).
Crystal structure of the human nuclear cap binding complex.
  Mol Cell, 8, 383-396.
PDB code: 1h6k
11590142 C.Morris-Desbois, S.Réty, M.Ferro, J.Garin, and P.Jalinot (2001).
The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3.
  J Biol Chem, 276, 45988-45995.  
11709169 C.Steegborn, O.Danot, R.Huber, and T.Clausen (2001).
Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization.
  Structure, 9, 1051-1060.
PDB code: 1hz4
11470816 J.C.Young, I.Moarefi, and F.U.Hartl (2001).
Hsp90: a specialized but essential protein-folding tool.
  J Cell Biol, 154, 267-273.  
11395418 J.Frydman (2001).
Folding of newly translated proteins in vivo: the role of molecular chaperones.
  Annu Rev Biochem, 70, 603-647.  
11600451 J.Höhfeld, D.M.Cyr, and C.Patterson (2001).
From the cradle to the grave: molecular chaperones that may choose between folding and degradation.
  EMBO Rep, 2, 885-890.  
11238452 K.J.Verhey, D.Meyer, R.Deehan, J.Blenis, B.J.Schnapp, T.A.Rapoport, and B.Margolis (2001).
Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules.
  J Cell Biol, 152, 959-970.  
11551791 K.J.Verhey, and T.A.Rapoport (2001).
Kinesin carries the signal.
  Trends Biochem Sci, 26, 545-550.  
11473354 K.Richter, and J.Buchner (2001).
Hsp90: chaperoning signal transduction.
  J Cell Physiol, 188, 281-290.  
11524682 K.S.Wendt, H.C.Vodermaier, U.Jacob, C.Gieffers, M.Gmachl, J.M.Peters, R.Huber, and P.Sondermann (2001).
Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex.
  Nat Struct Biol, 8, 784-788.
PDB code: 1jhj
11137038 M.Chinkers (2001).
Protein phosphatase 5 in signal transduction.
  Trends Endocrinol Metab, 12, 28-32.  
11377203 P.Taylor, J.Dornan, A.Carrello, R.F.Minchin, T.Ratajczak, and M.D.Walkinshaw (2001).
Two structures of cyclophilin 40: folding and fidelity in the TPR domains.
  Structure, 9, 431-438.
PDB codes: 1ihg 1iip
11604493 T.Abbas-Terki, O.Donzé, P.A.Briand, and D.Picard (2001).
Hsp104 interacts with Hsp90 cochaperones in respiring yeast.
  Mol Cell Biol, 21, 7569-7575.  
  11553703 Y.Du, M.Pypaert, P.Novick, and S.Ferro-Novick (2001).
Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae.
  Mol Biol Cell, 12, 2614-2628.  
11144355 A.Kamal, G.B.Stokin, Z.Yang, C.H.Xia, and L.S.Goldstein (2000).
Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I.
  Neuron, 28, 449-459.  
11060043 J.C.Young, and F.U.Hartl (2000).
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.
  EMBO J, 19, 5930-5940.  
  11090627 K.Lapouge, S.J.Smith, P.A.Walker, S.J.Gamblin, S.J.Smerdon, and K.Rittinger (2000).
Structure of the TPR domain of p67phox in complex with Rac.GTP.
  Mol Cell, 6, 899-907.
PDB code: 1e96
11106732 R.Siegert, M.R.Leroux, C.Scheufler, F.U.Hartl, and I.Moarefi (2000).
Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.
  Cell, 103, 621-632.
PDB code: 1fxk
11154072 V.M.Longshaw, H.W.Dirr, G.L.Blatch, and M.Lässle (2000).
The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34cdc2-NLS (CcN) motif.
  Biol Chem, 381, 1133-1138.  
11084334 W.E.Gall, M.A.Higginbotham, C.Chen, M.F.Ingram, D.M.Cyr, and T.R.Graham (2000).
The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast.
  Curr Biol, 10, 1349-1358.  
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.

 

spacer

spacer