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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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response to stress
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2 terms
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Biochemical function
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unfolded protein binding
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2 terms
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DOI no:
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J Cell Biol
143:901-910
(1998)
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PubMed id:
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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
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W.M.Obermann,
H.Sondermann,
A.A.Russo,
N.P.Pavletich,
F.U.Hartl.
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ABSTRACT
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Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic
cytosol, is involved in the folding of a set of cell regulatory proteins and in
the re-folding of stress-denatured polypeptides. The basic mechanism of action
of Hsp90 is not yet understood. In particular, it has been debated whether Hsp90
function is ATP dependent. A recent crystal structure of the NH2-terminal domain
of yeast Hsp90 established the presence of a conserved nucleotide binding site
that is identical with the binding site of geldanamycin, a specific inhibitor of
Hsp90. The functional significance of nucleotide binding by Hsp90 has remained
unclear. Here we present evidence for a slow but clearly detectable ATPase
activity in purified Hsp90. Based on a new crystal structure of the NH2-terminal
domain of human Hsp90 with bound ADP-Mg and on the structural homology of this
domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of
Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified.
The corresponding mutations were made in the yeast Hsp90 homologue, Hsp82, and
tested for their ability to functionally replace wild-type Hsp82. Our results
show that both ATP binding and hydrolysis are required for Hsp82 function in
vivo. The mutant Hsp90 proteins tested are defective in the binding and ATP
hydrolysis-dependent cycling of the co-chaperone p23, which is thought to
regulate the binding and release of substrate polypeptide from Hsp90.
Remarkably, the complete Hsp90 protein is required for ATPase activity and for
the interaction with p23, suggesting an intricate allosteric communication
between the domains of the Hsp90 dimer. Our results establish Hsp90 as an
ATP-dependent chaperone.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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T.Taldone,
D.Zatorska,
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J.H.Ahn,
K.Moulick,
M.L.Guzman,
and
G.Chiosis
(2011).
Design, synthesis, and evaluation of small molecule Hsp90 probes.
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Bioorg Med Chem, 19,
2603-2614.
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C.S.Chua,
H.Low,
K.S.Goo,
and
T.S.Sim
(2010).
Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90.
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Cell Mol Life Sci, 67,
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H.Bansal,
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Heat shock protein 90 regulates the expression of Wilms tumor 1 protein in myeloid leukemias.
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Circadian input kinases and their homologs in cyanobacteria: evolutionary constraints versus architectural diversification.
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J Mol Evol, 70,
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A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
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Mol Cell Proteomics, 9,
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K.D.Corbett,
and
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Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.
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Proteins, 78,
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PDB code:
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M.Mollapour,
S.Tsutsumi,
A.C.Donnelly,
K.Beebe,
M.J.Tokita,
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D.Bourboulia,
B.T.Scroggins,
G.Colombo,
B.S.Blagg,
B.Panaretou,
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J.B.Trepel,
P.W.Piper,
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L.H.Pearl,
and
L.Neckers
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Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.
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Mol Cell, 37,
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Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.
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J Biol Chem, 285,
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K.H.Huang,
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P.M.Steed,
A.F.Barabasz,
B.Foley,
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J.M.Partridge,
J.Rice,
A.Scott,
L.G.Dubois,
T.A.Freed,
M.A.Silinski,
T.E.Barta,
P.F.Hughes,
A.Ommen,
W.Ma,
E.D.Smith,
A.W.Spangenberg,
J.Eaves,
G.J.Hanson,
L.Hinkley,
M.Jenks,
M.Lewis,
J.Otto,
G.J.Pronk,
K.Verleysen,
T.A.Haystead,
and
S.E.Hall
(2010).
Application of chemoproteomics to drug discovery: identification of a clinical candidate targeting hsp90.
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Chem Biol, 17,
686-694.
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PDB code:
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T.O.Street,
K.A.Krukenberg,
J.Rosgen,
D.W.Bolen,
and
D.A.Agard
(2010).
Osmolyte-induced conformational changes in the Hsp90 molecular chaperone.
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Protein Sci, 19,
57-65.
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V.E.Cotton,
E.R.Hoffmann,
and
R.H.Borts
(2010).
Distinct regulation of Mlh1p heterodimers in meiosis and mitosis in Saccharomyces cerevisiae.
|
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Genetics, 185,
459-467.
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Z.Popovic,
and
D.M.Templeton
(2010).
Interaction of iron regulatory protein-1 (IRP-1) with ATP/ADP maintains a non-IRE-binding state.
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Biochem J, 430,
315-324.
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C.Graf,
M.Stankiewicz,
G.Kramer,
and
M.P.Mayer
(2009).
Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.
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EMBO J, 28,
602-613.
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C.K.Vaughan,
P.W.Piper,
L.H.Pearl,
and
C.Prodromou
(2009).
A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s.
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FEBS J, 276,
199-209.
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D.A.Hubert,
Y.He,
B.C.McNulty,
P.Tornero,
and
J.L.Dangl
(2009).
Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone function in plant NB-LRR disease resistance protein regulation.
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Proc Natl Acad Sci U S A, 106,
9556-9563.
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G.E.Brandt,
and
B.S.Blagg
(2009).
Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.
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Curr Top Med Chem, 9,
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I.Yang,
S.Han,
and
A.T.Parsa
(2009).
Heat-shock protein vaccines as active immunotherapy against human gliomas.
|
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Expert Rev Anticancer Ther, 9,
1577-1582.
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J.K.McCleese,
M.D.Bear,
S.L.Fossey,
R.M.Mihalek,
K.P.Foley,
W.Ying,
J.Barsoum,
and
C.A.London
(2009).
The novel HSP90 inhibitor STA-1474 exhibits biologic activity against osteosarcoma cell lines.
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Int J Cancer, 125,
2792-2801.
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J.R.Smith,
P.A.Clarke,
E.de Billy,
and
P.Workman
(2009).
Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors.
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Oncogene, 28,
157-169.
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J.Y.Cha,
N.Ermawati,
M.H.Jung,
M.Su'udi,
K.Y.Kim,
J.Y.Kim,
C.D.Han,
K.H.Lee,
and
D.Son
(2009).
Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein.
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Cell Stress Chaperones, 14,
233-243.
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J.Y.Song,
E.S.Kim,
D.W.Kim,
S.E.Jensen,
and
K.J.Lee
(2009).
A gene located downstream of the clavulanic acid gene cluster in Streptomyces clavuligerus ATCC 27064 encodes a putative response regulator that affects clavulanic acid production.
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J Ind Microbiol Biotechnol, 36,
301-311.
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M.Hessling,
K.Richter,
and
J.Buchner
(2009).
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.
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| |
Nat Struct Mol Biol, 16,
287-293.
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M.Retzlaff,
M.Stahl,
H.C.Eberl,
S.Lagleder,
J.Beck,
H.Kessler,
and
J.Buchner
(2009).
Hsp90 is regulated by a switch point in the C-terminal domain.
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| |
EMBO Rep, 10,
1147-1153.
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M.Sgobba,
and
G.Rastelli
(2009).
Structure-based and in silico design of Hsp90 inhibitors.
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ChemMedChem, 4,
1399-1409.
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M.W.Amolins,
and
B.S.Blagg
(2009).
Natural product inhibitors of Hsp90: potential leads for drug discovery.
|
| |
Mini Rev Med Chem, 9,
140-152.
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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.
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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.
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R.I.Feldman,
B.Mintzer,
D.Zhu,
J.M.Wu,
S.L.Biroc,
S.Yuan,
K.Emayan,
Z.Chang,
D.Chen,
D.O.Arnaiz,
J.Bryant,
X.S.Ge,
M.Whitlow,
M.Adler,
M.A.Polokoff,
W.W.Li,
M.Ferrer,
T.Sato,
J.M.Gu,
J.Shen,
J.L.Tseng,
H.Dinter,
and
B.Buckman
(2009).
Potent triazolothione inhibitor of heat-shock protein-90.
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Chem Biol Drug Des, 74,
43-50.
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PDB code:
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A.K.McCollum,
C.J.TenEyck,
B.Stensgard,
B.W.Morlan,
K.V.Ballman,
R.B.Jenkins,
D.O.Toft,
and
C.Erlichman
(2008).
P-Glycoprotein-mediated resistance to Hsp90-directed therapy is eclipsed by the heat shock response.
|
| |
Cancer Res, 68,
7419-7427.
|
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A.K.McCollum,
K.B.Lukasiewicz,
C.J.Teneyck,
W.L.Lingle,
D.O.Toft,
and
C.Erlichman
(2008).
Cisplatin abrogates the geldanamycin-induced heat shock response.
|
| |
Mol Cancer Ther, 7,
3256-3264.
|
|
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|
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|
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A.Yan,
G.H.Grant,
and
W.G.Richards
(2008).
Dynamics of conserved waters in human Hsp90: implications for drug design.
|
| |
J R Soc Interface, 5,
S199-S205.
|
|
|
|
|
|
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C.F.Cheng,
J.Fan,
M.Fedesco,
S.Guan,
Y.Li,
B.Bandyopadhyay,
A.M.Bright,
D.Yerushalmi,
M.Liang,
M.Chen,
Y.P.Han,
D.T.Woodley,
and
W.Li
(2008).
Transforming growth factor alpha (TGFalpha)-stimulated secretion of HSP90alpha: using the receptor LRP-1/CD91 to promote human skin cell migration against a TGFbeta-rich environment during wound healing.
|
| |
Mol Cell Biol, 28,
3344-3358.
|
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C.Liu,
C.Erlichman,
C.J.McDonald,
J.N.Ingle,
P.Zollman,
I.Iankov,
S.J.Russell,
and
E.Galanis
(2008).
Heat shock protein inhibitors increase the efficacy of measles virotherapy.
|
| |
Gene Ther, 15,
1024-1034.
|
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|
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G.Colombo,
G.Morra,
M.Meli,
and
G.Verkhivker
(2008).
Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution.
|
| |
Proc Natl Acad Sci U S A, 105,
7976-7981.
|
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|
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K.Rose,
S.Pallast,
S.Klumpp,
and
J.Krieglstein
(2008).
ATP-binding on fibroblast growth factor 2 partially overlaps with the heparin-binding domain.
|
| |
J Biochem, 144,
343-347.
|
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K.Schmid,
M.Haslbeck,
J.Buchner,
and
V.Somoza
(2008).
Induction of heat shock proteins and the proteasome system by casein-N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)lysine in Caco-2 cells.
|
| |
Ann N Y Acad Sci, 1126,
257-261.
|
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M.Averna,
R.Stifanese,
R.De Tullio,
M.Passalacqua,
F.Salamino,
S.Pontremoli,
and
E.Melloni
(2008).
Functional role of HSP90 complexes with endothelial nitric-oxide synthase (eNOS) and calpain on nitric oxide generation in endothelial cells.
|
| |
J Biol Chem, 283,
29069-29076.
|
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|
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M.Kosmaoglou,
N.Schwarz,
J.S.Bett,
and
M.E.Cheetham
(2008).
Molecular chaperones and photoreceptor function.
|
| |
Prog Retin Eye Res, 27,
434-449.
|
|
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|
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|
|
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.
|
|
|
|
|
|
|
R.I.Morimoto
(2008).
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging.
|
| |
Genes Dev, 22,
1427-1438.
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S.Arias,
E.R.Olivera,
M.Arcos,
G.Naharro,
and
J.M.Luengo
(2008).
Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U.
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| |
Environ Microbiol, 10,
413-432.
|
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S.Taguwa,
T.Okamoto,
T.Abe,
Y.Mori,
T.Suzuki,
K.Moriishi,
and
Y.Matsuura
(2008).
Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replication.
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| |
J Virol, 82,
2631-2641.
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T.Y.Huang,
L.S.Minamide,
J.R.Bamburg,
and
G.M.Bokoch
(2008).
Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation.
|
| |
Dev Cell, 15,
691-703.
|
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|
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|
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|
Y.Fukuyo,
M.Inoue,
T.Nakajima,
R.Higashikubo,
N.T.Horikoshi,
C.Hunt,
A.Usheva,
M.L.Freeman,
and
N.Horikoshi
(2008).
Oxidative stress plays a critical role in inactivating mutant BRAF by geldanamycin derivatives.
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| |
Cancer Res, 68,
6324-6330.
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|
C.Konstantinou-Kirtay,
J.B.Mitchell,
and
J.A.Lumley
(2007).
Scoring functions and enrichment: a case study on Hsp90.
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| |
BMC Bioinformatics, 8,
27.
|
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D.E.Dollins,
J.J.Warren,
R.M.Immormino,
and
D.T.Gewirth
(2007).
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.
|
| |
Mol Cell, 28,
41-56.
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PDB codes:
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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.
|
|
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|
|
P.L.Yeyati,
R.M.Bancewicz,
J.Maule,
and
V.van Heyningen
(2007).
Hsp90 selectively modulates phenotype in vertebrate development.
|
| |
PLoS Genet, 3,
e43.
|
|
|
|
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|
|
Q.C.Guo,
J.N.Shen,
S.Jin,
J.Wang,
G.Huang,
L.J.Zhang,
G.Huang,
J.Q.Yin,
C.Y.Zou,
and
M.T.Li
(2007).
Comparative proteomic analysis of human osteosarcoma and SV40-immortalized normal osteoblastic cell lines.
|
| |
Acta Pharmacol Sin, 28,
850-858.
|
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|
T.M.Buck,
C.M.Wright,
and
J.L.Brodsky
(2007).
The activities and function of molecular chaperones in the endoplasmic reticulum.
|
| |
Semin Cell Dev Biol, 18,
751-761.
|
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|
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A.Chadli,
J.D.Graham,
M.G.Abel,
T.A.Jackson,
D.F.Gordon,
W.M.Wood,
S.J.Felts,
K.B.Horwitz,
and
D.Toft
(2006).
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
|
| |
Mol Cell Biol, 26,
1722-1730.
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B.Chen,
D.Zhong,
and
A.Monteiro
(2006).
Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms.
|
| |
BMC Genomics, 7,
156.
|
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|
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F.Chu,
J.C.Maynard,
G.Chiosis,
C.V.Nicchitta,
and
A.L.Burlingame
(2006).
Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
|
| |
Protein Sci, 15,
1260-1269.
|
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|
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J.Moreno-Farre,
Y.Asad,
S.Pacey,
P.Workman,
and
F.I.Raynaud
(2006).
Development and validation of a liquid chromatography/tandem mass spectrometry method for the determination of the novel anticancer agent 17-DMAG in human plasma.
|
| |
Rapid Commun Mass Spectrom, 20,
2845-2850.
|
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|
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K.Terasawa,
K.Yoshimatsu,
S.Iemura,
T.Natsume,
K.Tanaka,
and
Y.Minami
(2006).
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases.
|
| |
Mol Cell Biol, 26,
3378-3389.
|
|
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|
|
L.H.Pearl,
and
C.Prodromou
(2006).
Structure and mechanism of the Hsp90 molecular chaperone machinery.
|
| |
Annu Rev Biochem, 75,
271-294.
|
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|
|
|
|
|
M.M.Ali,
S.M.Roe,
C.K.Vaughan,
P.Meyer,
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P.W.Piper,
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P.Hawle,
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PDB codes:
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PDB codes:
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Nature, 425,
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Integrin alphavbeta3, requirement for VEGFR2-mediated activation of SAPK2/p38 and for Hsp90-dependent phosphorylation of focal adhesion kinase in endothelial cells activated by VEGF.
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Cell Stress Chaperones, 8,
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Eur J Biochem, 270,
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EMBO J, 22,
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Mol Cell Biol, 23,
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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.
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Mol Cell, 11,
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PDB code:
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B.Panaretou,
G.Siligardi,
P.Meyer,
A.Maloney,
J.K.Sullivan,
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The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor.
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Cell Stress Chaperones, 6,
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PDB codes:
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J.Buchner
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Hsp90 & Co. - a holding for folding.
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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.
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|
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