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PDBsum entry 1a4h
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Contents |
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* Residue conservation analysis
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DOI no:
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Cell
90:65-75
(1997)
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PubMed id:
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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.
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C.Prodromou,
S.M.Roe,
R.O'Brien,
J.E.Ladbury,
P.W.Piper,
L.H.Pearl.
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ABSTRACT
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Hsp90 molecular chaperones in eukaryotic cells play essential roles in the
folding and activation of a range of client proteins involved in cell cycle
regulation, steroid hormone responsiveness, and signal transduction. The
biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP
in particular is controversial. Crystal structures of complexes between the
N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously
identify a specific adenine nucleotide binding site homologous to the
ATP-binding site of DNA gyrase B. This site is the same as that identified for
the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking
the binding of nucleotides to Hsp90 and not the binding of incompletely folded
client polypeptides as previously suggested. These results finally resolve the
question of the direct involvement of ATP in Hsp90 function.
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Selected figure(s)
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Figure 3.
Figure 3. Comparison of Bound Nucleotide Conformations in
Hsc70 and Hsp90Conformations of ADP bound to (a) Hsc70 ([13])
and (b) Hsp90. The N1, N6, which make specific contacts in the
ADP/ATP-binding pocket, are indicated, as is the adenine base C8
atom, which is unhindered in the Hsc70-bound conformation but
hindered in the Hsp90-bound conformation.
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Figure 6.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1997,
90,
65-75)
copyright 1997.
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Figures were
selected
by an automated process.
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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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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.
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Eur J Haematol,
86,
93.
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J.King-Scott,
P.V.Konarev,
S.Panjikar,
R.Jordanova,
D.I.Svergun,
and
P.A.Tucker
(2011).
Structural characterization of the multidomain regulatory protein Rv1364c from Mycobacterium tuberculosis.
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Structure,
19,
56-69.
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K.A.Krukenberg,
T.O.Street,
L.A.Lavery,
and
D.A.Agard
(2011).
Conformational dynamics of the molecular chaperone Hsp90.
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Q Rev Biophys,
44,
229-255.
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L.García-Descalzo,
A.Alcazar,
F.Baquero,
and
C.Cid
(2011).
Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.
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Cell Stress Chaperones,
16,
203-218.
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M.T.Guarnieri,
B.S.Blagg,
and
R.Zhao
(2011).
A high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinases.
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Assay Drug Dev Technol,
9,
174-183.
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N.Wang,
I.Whang,
J.S.Lee,
and
J.Lee
(2011).
Molecular characterization and expression analysis of a heat shock protein 90 gene from disk abalone (Haliotis discus).
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Mol Biol Rep,
38,
3055-3060.
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S.Minagawa,
Y.Kondoh,
K.Sueoka,
H.Osada,
and
H.Nakamoto
(2011).
Cyclic lipopeptide antibiotics bind to the N-terminal domain of the prokaryotic Hsp90 to inhibit the chaperone activity.
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Biochem J,
435,
237-246.
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W.Zhao,
L.Chen,
J.Qin,
P.Wu,
F.Zhang,
E.Li,
and
B.Tang
(2011).
MnHSP90 cDNA characterization and its expression during the ovary development in oriental river prawn, Macrobrachium nipponense.
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Mol Biol Rep,
38,
1399-1406.
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A.Chadli,
S.J.Felts,
Q.Wang,
W.P.Sullivan,
M.V.Botuyan,
A.Fauq,
M.Ramirez-Alvarado,
and
G.Mer
(2010).
Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23.
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J Biol Chem,
285,
4224-4231.
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A.Giménez Ortiz,
and
J.Montalar Salcedo
(2010).
Heat shock proteins as targets in oncology.
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Clin Transl Oncol,
12,
166-173.
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A.K.Mandal,
P.A.Gibney,
N.B.Nillegoda,
M.A.Theodoraki,
A.J.Caplan,
and
K.A.Morano
(2010).
Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.
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Mol Biol Cell,
21,
1439-1448.
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A.Orthwein,
A.M.Patenaude,
e.l. .B.Affar,
A.Lamarre,
J.C.Young,
and
J.M.Di Noia
(2010).
Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.
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J Exp Med,
207,
2751-2765.
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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,
1675-1686.
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I.E.Wrona,
A.Gozman,
T.Taldone,
G.Chiosis,
and
J.S.Panek
(2010).
Synthesis of reblastatin, autolytimycin, and non-benzoquinone analogues: potent inhibitors of heat shock protein 90.
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J Org Chem,
75,
2820-2835.
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J.E.Day,
S.Y.Sharp,
M.G.Rowlands,
W.Aherne,
P.Workman,
and
C.J.Moody
(2010).
Targeting the Hsp90 chaperone: synthesis of novel resorcylic acid macrolactone inhibitors of Hsp90.
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Chemistry,
16,
2758-2763.
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J.E.Day,
S.Y.Sharp,
M.G.Rowlands,
W.Aherne,
W.Lewis,
S.M.Roe,
C.Prodromou,
L.H.Pearl,
P.Workman,
and
C.J.Moody
(2010).
Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies.
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Chemistry,
16,
10366-10372.
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PDB code:
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J.R.Porter,
C.C.Fritz,
and
K.M.Depew
(2010).
Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy.
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Curr Opin Chem Biol,
14,
412-420.
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K.D.Corbett,
and
J.M.Berger
(2010).
Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.
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Proteins,
78,
2738-2744.
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PDB code:
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L.Moleda,
L.Jurzik,
M.Froh,
E.Gäbele,
C.Hellerbrand,
R.H.Straub,
J.Schölmerich,
and
R.Wiest
(2010).
Role of HSP-90 for increased nNOS-mediated vasodilation in mesenteric arteries in portal hypertension.
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World J Gastroenterol,
16,
1837-1844.
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L.Vozzolo,
B.Loh,
P.J.Gane,
M.Tribak,
L.Zhou,
I.Anderson,
E.Nyakatura,
R.G.Jenner,
D.Selwood,
and
A.Fassati
(2010).
Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein.
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J Biol Chem,
285,
39314-39328.
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M.Mollapour,
S.Tsutsumi,
A.C.Donnelly,
K.Beebe,
M.J.Tokita,
M.J.Lee,
S.Lee,
G.Morra,
D.Bourboulia,
B.T.Scroggins,
G.Colombo,
B.S.Blagg,
B.Panaretou,
W.G.Stetler-Stevenson,
J.B.Trepel,
P.W.Piper,
C.Prodromou,
L.H.Pearl,
and
L.Neckers
(2010).
Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.
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Mol Cell,
37,
333-343.
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M.Taipale,
D.F.Jarosz,
and
S.Lindquist
(2010).
HSP90 at the hub of protein homeostasis: emerging mechanistic insights.
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Nat Rev Mol Cell Biol,
11,
515-528.
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M.Zhang,
Y.Kadota,
C.Prodromou,
K.Shirasu,
and
L.H.Pearl
(2010).
Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors.
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Mol Cell,
39,
269-281.
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PDB code:
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N.Boufaied,
M.A.Wioland,
P.Falardeau,
and
H.Gourdeau
(2010).
TLN-4601, a novel anticancer agent, inhibits Ras signaling post Ras prenylation and before MEK activation.
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Anticancer Drugs,
21,
543-552.
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P.Fadden,
K.H.Huang,
J.M.Veal,
P.M.Steed,
A.F.Barabasz,
B.Foley,
M.Hu,
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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R.Zhao,
E.Leung,
S.Grüner,
M.Schapira,
and
W.A.Houry
(2010).
Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity.
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PLoS One,
5,
e9934.
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V.Kvardova,
R.Hrstka,
D.Walerych,
P.Muller,
E.Matoulkova,
V.Hruskova,
D.Stelclova,
P.Sova,
and
B.Vojtesek
(2010).
The new platinum(IV) derivative LA-12 shows stronger inhibitory effect on Hsp90 function compared to cisplatin.
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Mol Cancer,
9,
147.
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W.B.Pratt,
Y.Morishima,
H.M.Peng,
and
Y.Osawa
(2010).
Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.
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Exp Biol Med (Maywood),
235,
278-289.
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X.Sun,
E.A.Barlow,
S.Ma,
S.R.Hagemeier,
S.J.Duellman,
R.R.Burgess,
J.Tellam,
R.Khanna,
and
S.C.Kenney
(2010).
Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism.
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Proc Natl Acad Sci U S A,
107,
3146-3151.
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X.Sun,
and
S.C.Kenney
(2010).
Hsp90 inhibitors: a potential treatment for latent EBV infection?
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Cell Cycle,
9,
1665-1666.
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X.Wang,
D.M.Heuvelman,
J.A.Carroll,
D.R.Dufield,
and
J.L.Masferrer
(2010).
Geldanamycin-induced PCNA degradation in isolated Hsp90 complex from cancer cells.
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Cancer Invest,
28,
635-641.
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Y.Yu,
A.Hamza,
T.Zhang,
M.Gu,
P.Zou,
B.Newman,
Y.Li,
A.A.Gunatilaka,
C.G.Zhan,
and
D.Sun
(2010).
Withaferin A targets heat shock protein 90 in pancreatic cancer cells.
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Biochem Pharmacol,
79,
542-551.
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A.Ito,
H.Saito,
K.Mitobe,
Y.Minamiya,
N.Takahashi,
K.Maruyama,
S.Motoyama,
Y.Katayose,
and
J.Ogawa
(2009).
Inhibition of heat shock protein 90 sensitizes melanoma cells to thermosensitive ferromagnetic particle-mediated hyperthermia with low Curie temperature.
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Cancer Sci,
100,
558-564.
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B.H.Kang,
and
D.C.Altieri
(2009).
Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones.
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Oncogene,
28,
3681-3688.
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B.T.Scroggins,
and
L.Neckers
(2009).
Just say NO: nitric oxide regulation of Hsp90.
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EMBO Rep,
10,
1093-1094.
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C.B.Clark,
M.J.Rane,
D.El Mehdi,
C.J.Miller,
L.R.Sachleben,
and
E.Gozal
(2009).
Role of oxidative stress in geldanamycin-induced cytotoxicity and disruption of Hsp90 signaling complex.
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Free Radic Biol Med,
47,
1440-1449.
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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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E.S.Ehrlich,
T.Wang,
K.Luo,
Z.Xiao,
A.M.Niewiadomska,
T.Martinez,
W.Xu,
L.Neckers,
and
X.F.Yu
(2009).
Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase.
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Proc Natl Acad Sci U S A,
106,
20330-20335.
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F.Cervantes-Gomez,
R.Nimmanapalli,
and
V.Gandhi
(2009).
Transcription inhibition of heat shock proteins: a strategy for combination of 17-allylamino-17-demethoxygeldanamycin and actinomycin d.
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Cancer Res,
69,
3947-3954.
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M.W.Amolins,
and
B.S.Blagg
(2009).
Natural product inhibitors of Hsp90: potential leads for drug discovery.
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Mini Rev Med Chem,
9,
140-152.
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R.L.van Montfort,
and
P.Workman
(2009).
Structure-based design of molecular cancer therapeutics.
|
| |
Trends Biotechnol,
27,
315-328.
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S.Eichner,
H.G.Floss,
F.Sasse,
and
A.Kirschning
(2009).
New, highly active nonbenzoquinone geldanamycin derivatives by using mutasynthesis.
|
| |
Chembiochem,
10,
1801-1805.
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S.Jiang,
L.Qiu,
F.Zhou,
J.Huang,
Y.Guo,
and
K.Yang
(2009).
Molecular cloning and expression analysis of a heat shock protein (Hsp90) gene from black tiger shrimp (Penaeus monodon).
|
| |
Mol Biol Rep,
36,
127-134.
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T.Taldone,
W.Sun,
and
G.Chiosis
(2009).
Discovery and development of heat shock protein 90 inhibitors.
|
| |
Bioorg Med Chem,
17,
2225-2235.
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T.Wenyong,
L.Lu,
C.Daozhen,
Y.Weidong,
and
H.Ying
(2009).
An experimental study on the antitumor effect of (131)I-17-AAG in vitro and in vivo.
|
| |
Ann Nucl Med,
23,
113-122.
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T.Zhang,
Y.Li,
Y.Yu,
P.Zou,
Y.Jiang,
and
D.Sun
(2009).
Characterization of celastrol to inhibit hsp90 and cdc37 interaction.
|
| |
J Biol Chem,
284,
35381-35389.
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X.Chen,
H.Kang,
and
F.Zou
(2009).
Low concentration of GA activates a preconditioning response in HepG2 cells during oxidative stress-roles of Hsp90 and vimentin.
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| |
Cell Stress Chaperones,
14,
381-389.
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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.
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Y.Li,
T.Zhang,
Y.Jiang,
H.F.Lee,
S.J.Schwartz,
and
D.Sun
(2009).
(-)-Epigallocatechin-3-gallate inhibits Hsp90 function by impairing Hsp90 association with cochaperones in pancreatic cancer cell line Mia Paca-2.
|
| |
Mol Pharm,
6,
1152-1159.
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Z.Chang
(2009).
Posttranslational modulation on the biological activities of molecular chaperones.
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| |
Sci China C Life Sci,
52,
515-520.
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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.
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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.
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| |
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.
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| |
Mol Cancer Ther,
7,
3256-3264.
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A.Leskovar,
H.Wegele,
N.D.Werbeck,
J.Buchner,
and
J.Reinstein
(2008).
The ATPase cycle of the mitochondrial Hsp90 analog Trap1.
|
| |
J Biol Chem,
283,
11677-11688.
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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.
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| |
BMC Microbiol,
8,
158.
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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.Liu,
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Proc Natl Acad Sci U S A,
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PDB code:
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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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