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PDBsum entry 1f16

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protein links
Apoptosis PDB id
1f16
Jmol
Contents
Protein chain
192 a.a. *
* Residue conservation analysis
PDB id:
1f16
Name: Apoptosis
Title: Solution structure of a pro-apoptotic protein bax
Structure: Protein (apoptosis regulator bax, membrane isoform alpha). Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: M.Suzuki,R.J.Youle,N.Tjandra
Key ref:
M.Suzuki et al. (2000). Structure of Bax: coregulation of dimer formation and intracellular localization. Cell, 103, 645-654. PubMed id: 11106734 DOI: 10.1016/S0092-8674(00)00167-7
Date:
18-May-00     Release date:   22-Nov-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q07812  (BAX_HUMAN) -  Apoptosis regulator BAX
Seq:
Struc:
192 a.a.
192 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   17 terms 
  Biological process     viral reproduction   107 terms 
  Biochemical function     protein binding     7 terms  

 

 
DOI no: 10.1016/S0092-8674(00)00167-7 Cell 103:645-654 (2000)
PubMed id: 11106734  
 
 
Structure of Bax: coregulation of dimer formation and intracellular localization.
M.Suzuki, R.J.Youle, N.Tjandra.
 
  ABSTRACT  
 
Apoptosis is stimulated by the insertion of Bax from the cytosol into mitochondrial membranes. The solution structure of Bax, including the putative transmembrane domain at the C terminus, was determined in order to understand the regulation of its subcellular location. Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor, Bcl-x(L). The C-terminal alpha 9 helix occupies the hydrophobic pocket proposed previously to mediate heterodimer formation and bioactivity of opposing members of the Bcl-2 family. The Bax structure shows that the orientation of helix alpha 9 provides simultaneous control over its mitochondrial targeting and dimer formation.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Structure Comparison between Bax and Bcl-x[L]Two different views of (A) Bax, (B) Bcl-x[L], and (C) Bcl-x[L] complexed with Bak BH3 peptide are presented, a view straight down the central hydrophobic helix α5 (top panels) and a view from the side of the protein (bottom panels). The atomic coordinates of Bcl-x[L] and the Bcl-x[L]–peptide complex were obtained from the Protein Data Bank with ID codes 1MAZ and 1BXL, respectively. The BH1, BH2, BH3, and BH4 domains are shown in cyan, magenta, red, and blue, respectively. Helix α1 in Bax, which corresponds to BH4 containing helix in Bcl-x[L], is shown in purple. The C-terminal helix of Bax and the Bak BH3 peptide are shown in green. The C-terminal 24 residues of Bcl-x[L] were deleted in both structural studies of free and complexed Bcl-x[L]. The side chain of hydrophobic residues of Bak BH3 peptide (Val^74, Leu^78, Ile^81, and Ile^85) for stabilizing the complex formation between Bcl-x[L] and Bak BH3 peptide and those of corresponding hydrophobic residues of Bax BH3 domain (Leu^60, Leu^63, Ile^66, Leu^70) are represented by balls and sticks.
Figure 6.
Figure 6. The Orientation of the C-terminal HelixA close-up view of the Bax C-terminal helix and the hydrophobic pocket is shown. The side chains of the residues in the C-terminal helix are represented by balls and sticks. Solvent exposed side chains are shown in cyan. Magenta balls represent oxygen atom in threonines and serine. A surface representation of the pocket is colored red, purple, and yellow to represent negative, positive, and hydrophobic residues, respectively.
 
  The above figures are reprinted by permission from Cell Press: Cell (2000, 103, 645-654) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21060336 B.Ku, C.Liang, J.U.Jung, and B.H.Oh (2011).
Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX.
  Cell Res, 21, 627-641.
PDB code: 2xa0
21195116 D.Westphal, G.Dewson, P.E.Czabotar, and R.M.Kluck (2011).
Molecular biology of Bax and Bak activation and action.
  Biochim Biophys Acta, 1813, 521-531.  
21440528 E.Martínez-Abundis, F.Correa, E.Rodríguez, E.Soria-Castro, J.S.Rodríguez-Zavala, D.Pacheco-Alvarez, and C.Zazueta (2011).
A CRAC-like motif in BAX sequence: relationship with protein insertion and pore activity in liposomes.
  Biochim Biophys Acta, 1808, 1888-1895.  
21031486 F.J.Tan, J.E.Zuckerman, R.C.Wells, and R.B.Hill (2011).
The C. elegans B-cell lymphoma 2 (Bcl-2) homolog cell death abnormal 9 (CED-9) associates with and remodels LIPID membranes.
  Protein Sci, 20, 62-74.  
21182587 F.Zhou, Y.Yang, and D.Xing (2011).
Bcl-2 and Bcl-xL play important roles in the crosstalk between autophagy and apoptosis.
  FEBS J, 278, 403-413.  
21056595 J.Lindsay, M.D.Esposti, and A.P.Gilmore (2011).
Bcl-2 proteins and mitochondria--specificity in membrane targeting for death.
  Biochim Biophys Acta, 1813, 532-539.  
20966963 L.Lalier, P.F.Cartron, C.Olivier, C.Logé, G.Bougras, J.M.Robert, L.Oliver, and F.M.Vallette (2011).
Prostaglandins antagonistically control Bax activation during apoptosis.
  Cell Death Differ, 18, 528-537.  
20941706 L.Prieto, and T.Lazaridis (2011).
Computational studies of colicin insertion into membranes: the closed state.
  Proteins, 79, 126-141.  
20888373 M.Crimi, and M.D.Esposti (2011).
Apoptosis-induced changes in mitochondrial lipids.
  Biochim Biophys Acta, 1813, 551-557.  
21419810 S.Desai, P.Pillai, H.Win-Piazza, and M.Acevedo-Duncan (2011).
PKC-ι promotes glioblastoma cell survival by phosphorylating and inhibiting BAD through a phosphatidylinositol 3-kinase pathway.
  Biochim Biophys Acta, 1813, 1190-1197.  
21183949 X.Q.Zhang, Z.Yang, and W.F.Benedict (2011).
Direct gene transfer of adenoviral-mediated interferon α into human bladder cancer cells but not the bystander factors produced induces endoplasmic reticulum stress-related cytotoxicity.
  Cancer Gene Ther, 18, 260-264.  
20077016 A.C.Johansson, H.Appelqvist, C.Nilsson, K.Kågedal, K.Roberg, and K.Ollinger (2010).
Regulation of apoptosis-associated lysosomal membrane permeabilization.
  Apoptosis, 15, 527-540.  
21070973 E.Gavathiotis, D.E.Reyna, M.L.Davis, G.H.Bird, and L.D.Walensky (2010).
BH3-triggered structural reorganization drives the activation of proapoptotic BAX.
  Mol Cell, 40, 481-492.  
20480043 G.J.Rautureau, C.L.Day, and M.G.Hinds (2010).
Intrinsically disordered proteins in bcl-2 regulated apoptosis.
  Int J Mol Sci, 11, 1808-1824.  
19653066 J.D.Qiu, S.H.Luo, J.H.Huang, X.Y.Sun, and R.P.Liang (2010).
Predicting subcellular location of apoptosis proteins based on wavelet transform and support vector machine.
  Amino Acids, 38, 1201-1208.  
21166696 J.D.Xu, T.Furuya, X.X.Cao, X.L.Liu, Q.Q.Li, W.J.Wang, J.W.Xu, Z.D.Xu, K.Sasaki, and X.P.Liu (2010).
Loss of BCL2L10 protein expression as prognostic predictor for poor clinical outcome in gastric carcinoma.
  Histopathology, 57, 814-824.  
20959805 J.L.Fox, F.Ismail, A.Azad, N.Ternette, S.Leverrier, M.J.Edelmann, B.M.Kessler, I.M.Leigh, S.Jackson, and A.Storey (2010).
Tyrosine dephosphorylation is required for Bak activation in apoptosis.
  EMBO J, 29, 3853-3868.  
21209886 L.Sborgi, S.Barrera-Vilarmau, P.Obregón, and E.de Alba (2010).
Characterization of a novel interaction between Bcl-2 members Diva and Harakiri.
  PLoS One, 5, e15575.  
20798979 L.Shu, K.L.Cheung, T.O.Khor, C.Chen, and A.N.Kong (2010).
Phytochemicals: cancer chemoprevention and suppression of tumor onset and metastasis.
  Cancer Metastasis Rev, 29, 483-502.  
19880508 N.M.George, N.Targy, J.J.Evans, L.Zhang, and X.Luo (2010).
Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven process.
  J Biol Chem, 285, 1384-1392.  
20642852 R.Kanthan, J.L.Senger, and D.Diudea (2010).
Malignant mixed Mullerian tumors of the uterus: histopathological evaluation of cell cycle and apoptotic regulatory proteins.
  World J Surg Oncol, 8, 60.  
20160031 R.L.Smoot, B.R.Blechacz, N.W.Werneburg, S.F.Bronk, F.A.Sinicrope, A.E.Sirica, and G.J.Gores (2010).
A Bax-mediated mechanism for obatoclax-induced apoptosis of cholangiocarcinoma cells.
  Cancer Res, 70, 1960-1969.  
20148665 R.S.Whelan, V.Kaplinskiy, and R.N.Kitsis (2010).
Cell death in the pathogenesis of heart disease: mechanisms and significance.
  Annu Rev Physiol, 72, 19-44.  
20008353 S.Bleicken, M.Classen, P.V.Padmavathi, T.Ishikawa, K.Zeth, H.J.Steinhoff, and E.Bordignon (2010).
Molecular details of Bax activation, oligomerization, and membrane insertion.
  J Biol Chem, 285, 6636-6647.  
20683470 S.W.Tait, and D.R.Green (2010).
Mitochondria and cell death: outer membrane permeabilization and beyond.
  Nat Rev Mol Cell Biol, 11, 621-632.  
20101465 V.Ganesan, M.N.Perera, D.Colombini, D.Datskovskiy, K.Chadha, and M.Colombini (2010).
Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane.
  Apoptosis, 15, 553-562.  
20140092 Y.Guillemin, J.Lopez, D.Gimenez, G.Fuertes, J.G.Valero, L.Blum, P.Gonzalo, J.Salgado, A.Girard-Egrot, and A.Aouacheria (2010).
Active fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergence.
  PLoS One, 5, e9066.  
20093356 Z.Wang, A.Havasi, J.Gall, R.Bonegio, Z.Li, H.Mao, J.H.Schwartz, and S.C.Borkan (2010).
GSK3beta promotes apoptosis after renal ischemic injury.
  J Am Soc Nephrol, 21, 284-294.  
19439192 A.Jourdain, and J.C.Martinou (2009).
Mitochondrial outer-membrane permeabilization and remodelling in apoptosis.
  Int J Biochem Cell Biol, 41, 1884-1889.  
19239902 A.Strasser, P.J.Jost, and S.Nagata (2009).
The many roles of FAS receptor signaling in the immune system.
  Immunity, 30, 180-192.  
19759007 G.Brien, A.L.Debaud, X.Robert, L.Oliver, M.C.Trescol-Biemont, N.Cauquil, O.Geneste, N.Aghajari, F.M.Vallette, R.Haser, and N.Bonnefoy-Berard (2009).
C-terminal residues regulate localization and function of the antiapoptotic protein Bfl-1.
  J Biol Chem, 284, 30257-30263.  
19795525 G.Dewson, and R.M.Kluck (2009).
Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis.
  J Cell Sci, 122, 2801-2808.  
19917256 H.Kim, H.C.Tu, D.Ren, O.Takeuchi, J.R.Jeffers, G.P.Zambetti, J.J.Hsieh, and E.H.Cheng (2009).
Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.
  Mol Cell, 36, 487-499.  
19169652 H.Lin, H.Wang, H.Ding, Y.L.Chen, and Q.Z.Li (2009).
Prediction of subcellular localization of apoptosis protein using Chou's pseudo amino acid composition.
  Acta Biotheor, 57, 321-330.  
19383470 H.W.Huang (2009).
Free energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptides.
  Biophys J, 96, 3263-3272.  
19265193 H.Yamaguchi, N.T.Woods, L.G.Piluso, H.H.Lee, J.Chen, K.N.Bhalla, A.Monteiro, X.Liu, M.C.Hung, and H.G.Wang (2009).
p53 Acetylation Is Crucial for Its Transcription-independent Proapoptotic Functions.
  J Biol Chem, 284, 11171-11183.  
19701793 J.Peng, J.Ding, C.Tan, B.Baggenstoss, Z.Zhang, S.M.Lapolla, and J.Lin (2009).
Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid.
  Apoptosis, 14, 1145-1153.  
  19334571 J.Peng, S.M.Lapolla, Z.Zhang, and J.Lin (2009).
The cytosolic domain of Bcl-2 forms small pores in model mitochondrial outer membrane after acidic pH-induced membrane association.
  Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, 26, 130-137.  
  19634687 J.Peng, S.M.Lapolla, Z.Zhang, and J.Lin (2009).
The cytosolic domain of Bcl-2 oligomerizes to form pores in model mitochondrial outer membrane at acidic pH.
  Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, 26, 631-637.  
  19813621 J.Peng, S.M.Lapolla, Z.Zhang, and J.Lin (2009).
The Bax BH3 peptide H2-H3 promotes apoptosis by inhibiting Bcl-2's pore-forming and anti-Bax activities in the membrane.
  Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, 26, 829-835.  
19823588 M.D.Shortridge, and R.Powers (2009).
Structural and functional similarity between the bacterial type III secretion system needle protein PrgI and the eukaryotic apoptosis Bcl-2 proteins.
  PLoS One, 4, e7442.  
19521421 M.Ott, E.Norberg, B.Zhivotovsky, and S.Orrenius (2009).
Mitochondrial targeting of tBid/Bax: a role for the TOM complex?
  Cell Death Differ, 16, 1075-1082.  
19278624 M.Sadidi, S.I.Lentz, and E.L.Feldman (2009).
Hydrogen peroxide-induced Akt phosphorylation regulates Bax activation.
  Biochimie, 91, 577-585.  
19150424 N.Y.Fu, S.K.Sukumaran, S.Y.Kerk, and V.C.Yu (2009).
Baxbeta: a constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanism.
  Mol Cell, 33, 15-29.  
19564333 O.Ivashyna, A.J.García-Sáez, J.Ries, E.T.Christenson, P.Schwille, and P.H.Schlesinger (2009).
Detergent-activated BAX protein is a monomer.
  J Biol Chem, 284, 23935-23946.  
19557009 P.E.Czabotar, P.M.Colman, and D.C.Huang (2009).
Bax activation by Bim?
  Cell Death Differ, 16, 1187-1191.  
19255832 S.Bleicken, and K.Zeth (2009).
Conformational changes and protein stability of the pro-apoptotic protein Bax.
  J Bioenerg Biomembr, 41, 29-40.  
19123183 S.J.Ralph, and J.Neuzil (2009).
Mitochondria as targets for cancer therapy.
  Mol Nutr Food Res, 53, 9.  
19380879 T.Gallenne, F.Gautier, L.Oliver, E.Hervouet, B.Noël, J.A.Hickman, O.Geneste, P.F.Cartron, F.M.Vallette, S.Manon, and P.Juin (2009).
Bax activation by the BH3-only protein Puma promotes cell dependence on antiapoptotic Bcl-2 family members.
  J Cell Biol, 185, 279-290.  
19805544 T.K.Rostovtseva, H.Boukari, A.Antignani, B.Shiu, S.Banerjee, A.Neutzner, and R.J.Youle (2009).
Bax activates endophilin B1 oligomerization and lipid membrane vesiculation.
  J Biol Chem, 284, 34390-34399.  
19466402 V.G.Veresov, and A.I.Davidovskii (2009).
Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations.
  Eur Biophys J, 38, 941-960.  
19247369 V.Gama, J.A.Gomez, L.D.Mayo, M.W.Jackson, D.Danielpour, K.Song, A.L.Haas, M.J.Laughlin, and S.Matsuyama (2009).
Hdm2 is a ubiquitin ligase of Ku70-Akt promotes cell survival by inhibiting Hdm2-dependent Ku70 destabilization.
  Cell Death Differ, 16, 758-769.  
19386024 W.Wisessmith, P.Phansuwan-Pujito, P.Govitrapong, and B.Chetsawang (2009).
Melatonin reduces induction of Bax, caspase and cell death in methamphetamine-treated human neuroblastoma SH-SY5Y cultured cells.
  J Pineal Res, 46, 433-440.  
19917244 Y.Yao, and F.M.Marassi (2009).
BAX and BAK caught in the act.
  Mol Cell, 36, 353-354.  
19182807 Z.J.Shen, S.Esnault, A.Schinzel, C.Borner, and J.S.Malter (2009).
The peptidyl-prolyl isomerase Pin1 facilitates cytokine-induced survival of eosinophils by suppressing Bax activation.
  Nat Immunol, 10, 257-265.  
18307410 A.J.Valentijn, J.P.Upton, and A.P.Gilmore (2008).
Analysis of endogenous Bax complexes during apoptosis using blue native PAGE: implications for Bax activation and oligomerization.
  Biochem J, 412, 347-357.  
18437166 A.J.Valentijn, J.P.Upton, N.Bates, and A.P.Gilmore (2008).
Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms.
  Cell Death Differ, 15, 1243-1254.  
18026176 A.Strasser, H.Puthalakath, L.A.O'Reilly, and P.Bouillet (2008).
What do we know about the mechanisms of elimination of autoreactive T and B cells and what challenges remain.
  Immunol Cell Biol, 86, 57-66.  
18344566 C.Nie, C.Tian, L.Zhao, P.X.Petit, M.Mehrpour, and Q.Chen (2008).
Cysteine 62 of Bax is critical for its conformational activation and its proapoptotic activity in response to H2O2-induced apoptosis.
  J Biol Chem, 283, 15359-15369.  
18452209 D.Lama, and R.Sankararamakrishnan (2008).
Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: comparative molecular dynamics simulations.
  Proteins, 73, 492-514.  
17724463 D.Neise, V.Graupner, B.F.Gillissen, P.T.Daniel, K.Schulze-Osthoff, R.U.Jänicke, and F.Essmann (2008).
Activation of the mitochondrial death pathway is commonly mediated by a preferential engagement of Bak.
  Oncogene, 27, 1387-1396.  
18948940 D.R.Green, and J.E.Chipuk (2008).
Apoptosis: Stabbed in the BAX.
  Nature, 455, 1047-1049.  
18178565 D.Zhai, C.Jin, Z.Huang, A.C.Satterthwait, and J.C.Reed (2008).
Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1.
  J Biol Chem, 283, 9580-9586.  
18948948 E.Gavathiotis, M.Suzuki, M.L.Davis, K.Pitter, G.H.Bird, S.G.Katz, H.C.Tu, H.Kim, E.H.Cheng, N.Tjandra, and L.D.Walensky (2008).
BAX activation is initiated at a novel interaction site.
  Nature, 455, 1076-1081.
PDB code: 2k7w
19070569 G.C.Shore, and M.Nguyen (2008).
Bcl-2 proteins and apoptosis: choose your partner.
  Cell, 135, 1004-1006.  
18471982 G.Dewson, T.Kratina, H.W.Sim, H.Puthalakath, J.M.Adams, P.M.Colman, and R.M.Kluck (2008).
To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.
  Mol Cell, 30, 369-380.  
  19077196 H.A.Harrington, K.L.Ho, S.Ghosh, and K.C.Tung (2008).
Construction and analysis of a modular model of caspase activation in apoptosis.
  Theor Biol Med Model, 5, 26.  
18271938 H.Saito, T.Minamisawa, T.Yamori, and K.Shiba (2008).
Motif-programmed artificial protein induces apoptosis in several cancer cells by disrupting mitochondria.
  Cancer Sci, 99, 398-406.  
18362212 J.C.Reed (2008).
Bcl-2-family proteins and hematologic malignancies: history and future prospects.
  Blood, 111, 3322-3330.  
19074266 J.E.Chipuk, J.C.Fisher, C.P.Dillon, R.W.Kriwacki, T.Kuwana, and D.R.Green (2008).
Mechanism of apoptosis induction by inhibition of the anti-apoptotic BCL-2 proteins.
  Proc Natl Acad Sci U S A, 105, 20327-20332.  
18981409 J.I.Fletcher, S.Meusburger, C.J.Hawkins, D.T.Riglar, E.F.Lee, W.D.Fairlie, D.C.Huang, and J.M.Adams (2008).
Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax.
  Proc Natl Acad Sci U S A, 105, 18081-18087.  
18214681 J.Thompson, K.Finlayson, E.Salvo-Chirnside, D.MacDonald, J.McCulloch, L.Kerr, and J.Sharkey (2008).
Characterisation of the Bax-nucleophosmin interaction: the importance of the Bax C-terminus.
  Apoptosis, 13, 394-403.  
17766334 J.Y.Zheng, Y.C.Tsai, P.Kadimcherla, R.Zhang, J.Shi, G.A.Oyler, and N.N.Boustany (2008).
The C-terminal transmembrane domain of Bcl-xL mediates changes in mitochondrial morphology.
  Biophys J, 94, 286-297.  
19641510 L.P.Billen, A.Shamas-Din, and D.W.Andrews (2008).
Bid: a Bax-like BH3 protein.
  Oncogene, 27, S93-104.  
18547146 L.P.Billen, C.L.Kokoski, J.F.Lovell, B.Leber, and D.W.Andrews (2008).
Bcl-XL inhibits membrane permeabilization by competing with Bax.
  PLoS Biol, 6, e147.  
17965970 L.Yang, Y.Mei, Q.Xie, X.Han, F.Zhang, L.Gu, Y.Zhang, Y.Chen, G.Li, and Z.Gao (2008).
Acidification induces Bax translocation to the mitochondria and promotes ultraviolet light-induced apoptosis.
  Cell Mol Biol Lett, 13, 119-129.  
19641498 M.Giam, D.C.Huang, and P.Bouillet (2008).
BH3-only proteins and their roles in programmed cell death.
  Oncogene, 27, S128-S136.  
18195012 O.Terrones, A.Etxebarria, A.Landajuela, O.Landeta, B.Antonsson, and G.Basañez (2008).
BIM and tBID are not mechanistically equivalent when assisting BAX to permeabilize bilayer membranes.
  J Biol Chem, 283, 7790-7803.  
18331646 P.Feng, T.Li, Z.Guan, R.B.Franklin, and L.C.Costello (2008).
The involvement of Bax in zinc-induced mitochondrial apoptogenesis in malignant prostate cells.
  Mol Cancer, 7, 25.  
18097445 R.J.Youle, and A.Strasser (2008).
The BCL-2 protein family: opposing activities that mediate cell death.
  Nat Rev Mol Cell Biol, 9, 47-59.  
18691924 R.Yamaguchi, L.Lartigue, G.Perkins, R.T.Scott, A.Dixit, Y.Kushnareva, T.Kuwana, M.H.Ellisman, and D.D.Newmeyer (2008).
Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization.
  Mol Cell, 31, 557-569.  
18987313 S.Qian, W.Wang, L.Yang, and H.W.Huang (2008).
Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores.
  Proc Natl Acad Sci U S A, 105, 17379-17383.  
18375382 X.Cao, R.L.Bennett, and W.S.May (2008).
c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis.
  J Biol Chem, 283, 14490-14496.  
17384234 A.E.Douglas, K.D.Corbett, J.M.Berger, G.McFadden, and T.M.Handel (2007).
Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2.
  Protein Sci, 16, 695-703.
PDB code: 2o42
17416629 A.J.García-Sáez, S.Chiantia, J.Salgado, and P.Schwille (2007).
Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM.
  Biophys J, 93, 103-112.  
16909120 A.L.Nouvion, J.Thibaut, O.D.Lohez, S.Venet, P.Colas, G.Gillet, and P.Lalle (2007).
Modulation of Nr-13 antideath activity by peptide aptamers.
  Oncogene, 26, 701-710.  
17496930 A.L.Pauleau, N.Larochette, F.Giordanetto, S.R.Scholz, D.Poncet, N.Zamzami, V.S.Goldmacher, and G.Kroemer (2007).
Structure-function analysis of the interaction between Bax and the cytomegalovirus-encoded protein vMIA.
  Oncogene, 26, 7067-7080.  
17294078 A.Rasola, and P.Bernardi (2007).
The mitochondrial permeability transition pore and its involvement in cell death and in disease pathogenesis.
  Apoptosis, 12, 815-833.  
17517961 A.Weber, S.A.Paschen, K.Heger, F.Wilfling, T.Frankenberg, H.Bauerschmitt, B.M.Seiffert, S.Kirschnek, H.Wagner, and G.Häcker (2007).
BimS-induced apoptosis requires mitochondrial localization but not interaction with anti-apoptotic Bcl-2 proteins.
  J Cell Biol, 177, 625-636.  
17453159 B.Leber, J.Lin, and D.W.Andrews (2007).
Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes.
  Apoptosis, 12, 897-911.  
17699158 B.Sot, S.M.Freund, and A.R.Fersht (2007).
Comparative biophysical characterization of p53 with the pro-apoptotic BAK and the anti-apoptotic BCL-xL.
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16927372 C.N.Im, J.S.Lee, Y.Zheng, and J.S.Seo (2007).
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16946732 F.W.Peyerl, S.Dai, G.A.Murphy, F.Crawford, J.White, P.Marrack, and J.W.Kappler (2007).
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PDB code: 2g5b
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17911107 H.Arokium, H.Ouerfelli, G.Velours, N.Camougrand, F.M.Vallette, and S.Manon (2007).
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17559379 H.Zhang, D.C.Fang, C.H.Lan, and Y.H.Luo (2007).
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17486058 H.Zhou, Q.Hou, J.L.Hansen, and Y.T.Hsu (2007).
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17927731 J.Choi, D.Zhai, X.Zhou, A.Satterthwait, J.C.Reed, and F.M.Marassi (2007).
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17593526 K.Chen, and N.Tjandra (2007).
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17827721 K.Futami, A.Shimamoto, and Y.Furuichi (2007).
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PDB code: 2uxe
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PDB code: 1wsx
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Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak.
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The cell death machinery controlled by Bax and Bcl-XL is evolutionarily conserved in Ciona intestinalis.
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Structural basis for redox regulation of Yap1 transcription factor localization.
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PDB code: 1sse
  19003251 M.M.Godlewski, M.Gorka, M.Lamparska-Przybysz, and T.Motyl (2004).
Minute kinetics of proapoptotic proteins: BAX and Smac/DIABLO in living tumor cells revealed by homeostatic confocal microscopy.
  Cytotechnology, 45, 141-153.  
15138279 O.Terrones, B.Antonsson, H.Yamaguchi, H.G.Wang, J.Liu, R.M.Lee, A.Herrmann, and G.Basañez (2004).
Lipidic pore formation by the concerted action of proapoptotic BAX and tBID.
  J Biol Chem, 279, 30081-30091.  
14681224 P.F.Cartron, L.Oliver, P.Juin, K.Meflah, and F.M.Vallette (2004).
The p18 truncated form of Bax behaves like a Bcl-2 homology domain 3-only protein.
  J Biol Chem, 279, 11503-11512.  
15574335 P.F.Cartron, T.Gallenne, G.Bougras, F.Gautier, F.Manero, P.Vusio, K.Meflah, F.M.Vallette, and P.Juin (2004).
The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.
  Mol Cell, 16, 807-818.  
15149601 P.K.Kim, M.G.Annis, P.J.Dlugosz, B.Leber, and D.W.Andrews (2004).
During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria.
  Mol Cell, 14, 523-529.  
14766748 S.J.Gardai, D.A.Hildeman, S.K.Frankel, B.B.Whitlock, S.C.Frasch, N.Borregaard, P.Marrack, D.L.Bratton, and P.M.Henson (2004).
Phosphorylation of Bax Ser184 by Akt regulates its activity and apoptosis in neutrophils.
  J Biol Chem, 279, 21085-21095.  
15008953 S.L.Chan, and V.C.Yu (2004).
Proteins of the bcl-2 family in apoptosis signalling: from mechanistic insights to therapeutic opportunities.
  Clin Exp Pharmacol Physiol, 31, 119-128.  
15131699 S.Y.Jeong, B.Gaume, Y.J.Lee, Y.T.Hsu, S.W.Ryu, S.H.Yoon, and R.J.Youle (2004).
Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers.
  EMBO J, 23, 2146-2155.  
14729675 T.K.Rostovtseva, B.Antonsson, M.Suzuki, R.J.Youle, M.Colombini, and S.M.Bezrukov (2004).
Bid, but not Bax, regulates VDAC channels.
  J Biol Chem, 279, 13575-13583.  
14729175 T.Kaufmann, A.Schinzel, and C.Borner (2004).
Bcl-w(edding) with mitochondria.
  Trends Cell Biol, 14, 8.  
14730312 T.Ohtsuka, H.Ryu, Y.A.Minamishima, S.Macip, J.Sagara, K.I.Nakayama, S.A.Aaronson, and S.W.Lee (2004).
ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway.
  Nat Cell Biol, 6, 121-128.  
15123718 X.M.Gong, J.Choi, C.M.Franzin, D.Zhai, J.C.Reed, and F.M.Marassi (2004).
Conformation of membrane-associated proapoptotic tBid.
  J Biol Chem, 279, 28954-28960.  
15383280 Y.J.Nam, K.Mani, A.W.Ashton, C.F.Peng, B.Krishnamurthy, Y.Hayakawa, P.Lee, S.J.Korsmeyer, and R.N.Kitsis (2004).
Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions.
  Mol Cell, 15, 901-912.  
15322047 Y.Xiao, Y.Zhong, W.Greene, F.Dong, and G.Zhong (2004).
Chlamydia trachomatis infection inhibits both Bax and Bak activation induced by staurosporine.
  Infect Immun, 72, 5470-5474.  
15302859 Z.Zhang, S.M.Lapolla, M.G.Annis, M.Truscott, G.J.Roberts, Y.Miao, Y.Shao, C.Tan, J.Peng, A.E.Johnson, X.C.Zhang, D.W.Andrews, and J.Lin (2004).
Bcl-2 homodimerization involves two distinct binding surfaces, a topographic arrangement that provides an effective mechanism for Bcl-2 to capture activated Bax.
  J Biol Chem, 279, 43920-43928.  
12576135 A.Clerk, S.M.Cole, T.E.Cullingford, J.G.Harrison, M.Jormakka, and D.M.Valks (2003).
Regulation of cardiac myocyte cell death.
  Pharmacol Ther, 97, 223-261.  
12925707 A.J.Valentijn, A.D.Metcalfe, J.Kott, C.H.Streuli, and A.P.Gilmore (2003).
Spatial and temporal changes in Bax subcellular localization during anoikis.
  J Cell Biol, 162, 599-612.  
12752673 A.Strasser, and P.Bouillet (2003).
The control of apoptosis in lymphocyte selection.
  Immunol Rev, 193, 82-92.  
12651847 A.Y.Denisov, M.S.Madiraju, G.Chen, A.Khadir, P.Beauparlant, G.Attardo, G.C.Shore, and K.Gehring (2003).
Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix.
  J Biol Chem, 278, 21124-21128.
PDB code: 1mk3
12732850 B.Guo, D.Zhai, E.Cabezas, K.Welsh, S.Nouraini, A.C.Satterthwait, and J.C.Reed (2003).
Humanin peptide suppresses apoptosis by interfering with Bax activation.
  Nature, 423, 456-461.  
12642586 C.Moreau, P.F.Cartron, A.Hunt, K.Meflah, D.R.Green, G.Evan, F.M.Vallette, and P.Juin (2003).
Minimal BH3 peptides promote cell death by antagonizing anti-apoptotic proteins.
  J Biol Chem, 278, 19426-19435.  
12941691 D.Arnoult, B.Gaume, M.Karbowski, J.C.Sharpe, F.Cecconi, and R.J.Youle (2003).
Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization.
  EMBO J, 22, 4385-4399.  
12881569 E.H.Cheng, T.V.Sheiko, J.K.Fisher, W.J.Craigen, and S.J.Korsmeyer (2003).
VDAC2 inhibits BAK activation and mitochondrial apoptosis.
  Science, 301, 513-517.  
14532263 E.S.Sulistijo, T.M.Jaszewski, and K.R.MacKenzie (2003).
Sequence-specific dimerization of the transmembrane domain of the "BH3-only" protein BNIP3 in membranes and detergent.
  J Biol Chem, 278, 51950-51956.  
12471598 G.P.Zhou, and K.Doctor (2003).
Subcellular location prediction of apoptosis proteins.
  Proteins, 50, 44-48.  
14580191 H.Feng, J.Takei, R.Lipsitz, N.Tjandra, and Y.Bai (2003).
Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding.
  Biochemistry, 42, 12461-12465.
PDB codes: 1yyj 1yza
14522999 J.A.Yethon, R.F.Epand, B.Leber, R.M.Epand, and D.W.Andrews (2003).
Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis.
  J Biol Chem, 278, 48935-48941.  
12379660 J.Usuda, S.M.Chiu, E.S.Murphy, M.Lam, A.L.Nieminen, and N.L.Oleinick (2003).
Domain-dependent photodamage to Bcl-2. A membrane anchorage region is needed to form the target of phthalocyanine photosensitization.
  J Biol Chem, 278, 2021-2029.  
12952938 J.Wilson-Annan, L.A.O'Reilly, S.A.Crawford, G.Hausmann, J.G.Beaumont, L.P.Parma, L.Chen, M.Lackmann, T.Lithgow, M.G.Hinds, C.L.Day, J.M.Adams, and D.C.Huang (2003).
Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity.
  J Cell Biol, 162, 877-887.  
12654255 L.Coultas, and A.Strasser (2003).
The role of the Bcl-2 protein family in cancer.
  Semin Cancer Biol, 13, 115-123.  
12660157 M.G.Hinds, M.Lackmann, G.L.Skea, P.J.Harrison, D.C.Huang, and C.L.Day (2003).
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity.
  EMBO J, 22, 1497-1507.
PDB code: 1o0l
12652309 M.Sawada, P.Hayes, and S.Matsuyama (2003).
Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70.
  Nat Cell Biol, 5, 352-357.  
12652308 M.Sawada, W.Sun, P.Hayes, K.Leskov, D.A.Boothman, and S.Matsuyama (2003).
Ku70 suppresses the apoptotic translocation of Bax to mitochondria.
  Nat Cell Biol, 5, 320-329.  
12821639 N.Borgese, S.Colombo, and E.Pedrazzini (2003).
The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane.
  J Cell Biol, 161, 1013-1019.  
12529375 P.F.Cartron, M.Priault, L.Oliver, K.Meflah, S.Manon, and F.M.Vallette (2003).
The N-terminal end of Bax contains a mitochondrial-targeting signal.
  J Biol Chem, 278, 11633-11641.  
12721291 S.C.Ruffolo, and G.C.Shore (2003).
BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization.
  J Biol Chem, 278, 25039-25045.  
12515824 T.Kaufmann, S.Schlipf, J.Sanz, K.Neubert, R.Stein, and C.Borner (2003).
Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane.
  J Cell Biol, 160, 53-64.  
14644193 T.Kuwana, and D.D.Newmeyer (2003).
Bcl-2-family proteins and the role of mitochondria in apoptosis.
  Curr Opin Cell Biol, 15, 691-699.  
12898509 T.Subramanian, and G.Chinnadurai (2003).
Pro-apoptotic activity of transiently expressed BCL-2 occurs independent of BAX and BAK.
  J Cell Biochem, 89, 1102-1114.  
12454021 V.Mikhailov, M.Mikhailova, K.Degenhardt, M.A.Venkatachalam, E.White, and P.Saikumar (2003).
Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release.
  J Biol Chem, 278, 5367-5376.  
12414721 V.S.Marsden, and A.Strasser (2003).
Control of apoptosis in the immune system: Bcl-2, BH3-only proteins and more.
  Annu Rev Immunol, 21, 71.  
12974619 Y.Ren, L.Xiong, and J.R.Wu (2003).
Induction of mitochondrion-mediated apoptosis of CHO cells by tripchlorolide.
  Cell Res, 13, 295-300.  
12111869 B.C.Baliga, and S.Kumar (2002).
Role of Bcl-2 family of proteins in malignancy.
  Hematol Oncol, 20, 63-74.  
12042767 C.Jin, and J.C.Reed (2002).
Yeast and apoptosis.
  Nat Rev Mol Cell Biol, 3, 453-459.  
11836425 D.S.Bellows, M.Howell, C.Pearson, S.A.Hazlewood, and J.M.Hardwick (2002).
Epstein-Barr virus BALF1 is a BCL-2-like antagonist of the herpesvirus antiapoptotic BCL-2 proteins.
  J Virol, 76, 2469-2479.  
11918810 D.Ye, and S.R.Blanke (2002).
Functional complementation reveals the importance of intermolecular monomer interactions for Helicobacter pylori VacA vacuolating activity.
  Mol Microbiol, 43, 1243-1253.  
11842081 F.Tsuruta, N.Masuyama, and Y.Gotoh (2002).
The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria.
  J Biol Chem, 277, 14040-14047.  
12381734 G.Basañez, J.C.Sharpe, J.Galanis, T.B.Brandt, J.M.Hardwick, and J.Zimmerberg (2002).
Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature.
  J Biol Chem, 277, 49360-49365.  
11980919 G.V.Putcha, C.A.Harris, K.L.Moulder, R.M.Easton, C.B.Thompson, and E.M.Johnson (2002).
Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice.
  J Cell Biol, 157, 441-453.  
12198137 H.Yamaguchi, and H.G.Wang (2002).
Bcl-XL protects BimEL-induced Bax conformational change and cytochrome C release independent of interacting with Bax or BimEL.
  J Biol Chem, 277, 41604-41612.  
12450324 J.Salgado, A.J.García-Sáez, G.Malet, I.Mingarro, and E.Pérez-Payá (2002).
Peptides in apoptosis research.
  J Pept Sci, 8, 543-560.  
11836241 K.Degenhardt, R.Sundararajan, T.Lindsten, C.Thompson, and E.White (2002).
Bax and Bak independently promote cytochrome C release from mitochondria.
  J Biol Chem, 277, 14127-14134.  
11997495 M.Marani, T.Tenev, D.Hancock, J.Downward, and N.R.Lemoine (2002).
Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis.
  Mol Cell Biol, 22, 3577-3589.  
12423342 M.Priault, J.J.Bessoule, A.Grelaud-Coq, N.Camougrand, and S.Manon (2002).
Bax-induced cell death in yeast depends on mitochondrial lipid oxidation.
  Eur J Biochem, 269, 5440-5450.  
11904405 Q.Huang, A.M.Petros, H.W.Virgin, S.W.Fesik, and E.T.Olejniczak (2002).
Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus.
  Proc Natl Acad Sci U S A, 99, 3428-3433.
PDB code: 1k3k
12209154 S.Cory, and J.M.Adams (2002).
The Bcl2 family: regulators of the cellular life-or-death switch.
  Nat Rev Cancer, 2, 647-656.  
12133724 S.E.Rutledge, J.W.Chin, and A.Schepartz (2002).
A view to a kill: ligands for Bcl-2 family proteins.
  Curr Opin Chem Biol, 6, 479-485.  
12419244 T.Kuwana, M.R.Mackey, G.Perkins, M.H.Ellisman, M.Latterich, R.Schneiter, D.R.Green, and D.D.Newmeyer (2002).
Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane.
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12401491 Z.Huang (2002).
The chemical biology of apoptosis. Exploring protein-protein interactions and the life and death of cells with small molecules.
  Chem Biol, 9, 1059-1072.  
11724809 A.Degterev, M.Boyce, and J.Yuan (2001).
The channel of death.
  J Cell Biol, 155, 695-698.  
11248023 A.M.Petros, A.Medek, D.G.Nettesheim, D.H.Kim, H.S.Yoon, K.Swift, E.D.Matayoshi, T.Oltersdorf, and S.W.Fesik (2001).
Solution structure of the antiapoptotic protein bcl-2.
  Proc Natl Acad Sci U S A, 98, 3012-3017.
PDB codes: 1g5m 1g5o 1gjh
11402069 A.Nechushtan, C.L.Smith, I.Lamensdorf, S.H.Yoon, and R.J.Youle (2001).
Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis.
  J Cell Biol, 153, 1265-1276.  
11772248 C.M.Rodrigues, and C.J.Steer (2001).
The therapeutic effects of ursodeoxycholic acid as an anti-apoptotic agent.
  Expert Opin Investig Drugs, 10, 1243-1253.  
11533027 C.N.O'Donovan, D.Tobin, and T.G.Cotter (2001).
Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells.
  J Biol Chem, 276, 43516-43523.  
11583631 E.H.Cheng, M.C.Wei, S.Weiler, R.A.Flavell, T.W.Mak, T.Lindsten, and S.J.Korsmeyer (2001).
BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis.
  Mol Cell, 8, 705-711.  
11707402 G.W.Makin, B.M.Corfe, G.J.Griffiths, A.Thistlethwaite, J.A.Hickman, and C.Dive (2001).
Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate.
  EMBO J, 20, 6306-6315.  
11165519 J.M.Adams, and S.Cory (2001).
Life-or-death decisions by the Bcl-2 protein family.
  Trends Biochem Sci, 26, 61-66.  
11413234 K.L.Jin, S.H.Graham, X.O.Mao, X.He, T.Nagayama, R.P.Simon, and D.A.Greenberg (2001).
Bax kappa, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death.
  J Neurochem, 77, 1508-1519.  
11489880 L.Dubrez, J.L.Coll, A.Hurbin, E.Solary, and M.C.Favrot (2001).
Caffeine sensitizes human H358 cell line to p53-mediated apoptosis by inducing mitochondrial translocation and conformational change of BAX protein.
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11546793 N.S.Wang, M.T.Unkila, E.Z.Reineks, and C.W.Distelhorst (2001).
Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death.
  J Biol Chem, 276, 44117-44128.  
11462023 R.Sundararajan, and E.White (2001).
E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis.
  J Virol, 75, 7506-7516.  
11591332 Y.Lazebnik (2001).
Why do regulators of apoptosis look like bacterial toxins?
  Curr Biol, 11, R767-R768.  
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 code is shown on the right.