Elucidation of the Hsp90 C-terminal inhibitor binding site - Wikidata - thesis-toulmin - TriplyDB

Elucidation of the Hsp90 C-terminal inhibitor binding site

Elucidation of the Hsp90 C-terminal inhibitor binding site

http://www.wikidata.org/entity/Q28236934

about

Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling The 'active life' of Hsp90 complexes GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Targeting Hsp90 in urothelial carcinoma Gambogic acid identifies an isoform-specific druggable pocket in the middle domain of Hsp90β Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.Hsp90 C-terminal inhibitors exhibit antimigratory activity by disrupting the Hsp90α/Aha1 complex in PC3-MM2 cells.Design, synthesis, and biological evaluation of ring-constrained novobiocin analogues as hsp90 C-terminal inhibitors C-terminal heat shock protein 90 inhibitor decreases hyperglycemia-induced oxidative stress and improves mitochondrial bioenergetics in sensory neurons.Synthesis and evaluation of novologues as C-terminal Hsp90 inhibitors with cytoprotective activity against sensory neuron glucotoxicity.Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach.Development of Noviomimetics as C-Terminal Hsp90 Inhibitors Potential C-terminal-domain inhibitors of heat shock protein 90 derived from a C-terminal peptide helix.Synthesis and Biological Evaluation of Novobiocin Core Analogues as Hsp90 Inhibitors.In Vivo Conformational Dynamics of Hsp90 and Its Interactors.Synthesis and biological evaluation of coumarin replacements of novobiocin as Hsp90 inhibitors.Heat-shock protein 90 (Hsp90) as anticancer target for drug discovery: an ample computational perspective.Design, synthesis and biological evaluation of alkylamino biphenylamides as Hsp90 C-terminal inhibitors.Targeting the Diabetic Chaperome to Improve Peripheral Neuropathy.A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease.Development of radamide analogs as Grp94 inhibitors Cruentaren A binds F1F0 ATP synthase to modulate the Hsp90 protein folding machinery Alternative approaches to Hsp90 modulation for the treatment of cancer.Therapeutic Strategies for Restoring Tau Homeostasis.Synthesis and biological evaluation of arylated novobiocin analogs as Hsp90 inhibitors.Identification of a new scaffold for hsp90 C-terminal inhibition Design, synthesis and biological evaluation of biphenylamide derivatives as Hsp90 C-terminal inhibitors Exploiting conformational dynamics in drug discovery: design of C-terminal inhibitors of Hsp90 with improved activities.Synthesis and structure-activity relationships of EGCG analogues, a recently identified Hsp90 inhibitor Diverging Novobiocin Anti-Cancer Activity from Neuroprotective Activity through Modification of the Amide Tail.Triazole Containing Novobiocin and Biphenyl Amides as Hsp90 C-Terminal Inhibitors.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Computational Modeling of the Hsp90 Interactions with Cochaperones and Small-Molecule Inhibitors.Development of noviomimetics that modulate molecular chaperones and manifest neuroprotective effects.Synthesis and Biological Evaluation of Stilbene Analogues as Hsp90 C-Terminal Inhibitors.Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.

P2860

Q26801686-3663829F-BB9E-4444-81B7-C9BA81E0E892 Q26829003-DD45C353-B0E4-4EF0-865A-53019500D7F0 Q26860153-DE359052-928D-4777-8DA6-29D77287E4A7 Q27023406-1C59EE6E-5BD5-4EE0-AC5E-3275920B20EF Q28829208-ACDD3DD3-74FB-433B-ADA3-238D5C463633 Q30353164-2C5A221A-444B-476D-B956-6107B30C64AD Q30358343-5B1D2A6D-FF83-40C0-AF80-B233DF19F8D3 Q30363516-BF15002D-68A8-4E1B-96A4-766FC0631E7F Q34280087-DD3EFCC6-7489-47CC-9AE7-7A4E4E39E5EA Q34915636-4917F4CF-92FE-44D2-B403-6E7A5882DDFE Q35121121-024DB610-8364-4108-90C2-332BB9C4844B Q35564420-2D6C40BB-7358-419F-BD40-BA5FCF9C3CE5 Q35898056-E4D48E77-367B-4934-B849-B57D784C3193 Q36077840-525A74B4-72C1-49F6-9EAD-EA8747492198 Q36095575-A0B023F3-F069-4EC2-8773-2F936D93E1D2 Q36473154-C91C9EFA-36B1-4B1A-80CB-E8E9712CFD3F Q36844176-A271F579-F44E-4A8B-AF29-1238F36281F8 Q37130692-B07244F8-EA85-4932-BD34-50A4B33DB4F7 Q37233917-9CA7BECC-8E8A-46D4-B7F2-5C945E3D127A Q38428349-AE0492A2-725D-4619-8DD8-9EBD0A9EF11B Q38469746-C4A77975-DF06-495C-AE42-CF687E2404AF Q38727743-B2CB7FE0-8584-446B-8A0B-52AC7872B237 Q38869328-CA91D808-F499-4235-8919-CB56844D1649 Q38911503-8AF3595F-EF5F-4FCE-B611-11E7DE113F5C Q38975022-8ACD6503-1D7C-436A-BAC9-47B68B02416D Q39031940-0C9E5715-FE97-41A6-8A07-4230B46E8A07 Q39103704-C540A6DA-D0B4-4EB2-990D-B0BCC9E338C2 Q39118898-C019B125-1A7E-4EDD-B1FE-03A86644836E Q39455379-BA71081E-6523-4618-88F9-74EB585A4D43 Q39786880-EA9E6290-7B1D-4E7E-8B3C-DDB1F3B527E2 Q39867588-1A4A15FC-4332-40C3-B38C-00A585758363 Q41856020-2F9089CB-1BE8-4E12-A4A6-30B6E94B3F6F Q41873320-E4610C93-2D58-4FBB-899F-77A27ACD4D47 Q42358762-AB9B2371-9369-4727-9439-7B219C6BADE0 Q42945545-CA10EE75-9341-4174-ADF1-3C6AEEBE5953 Q47265199-98B302AF-B508-4323-B497-A204A52FA94A Q47362549-01ADF52D-9DE6-43E9-B59E-54E5D529E674 Q47403043-92C917B0-C180-4161-A0B1-4BEF8517CAFE Q47616767-4D90501A-4AC6-4B7C-9A9A-72A84E5B1371 Q48118580-8EEE56C9-56E4-4494-88FC-A5C348AB5373

P2860

Elucidation of the Hsp90 C-terminal inhibitor binding site

http://www.wikidata.org/entity/Q28236934

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Elucidation of the Hsp90 C-terminal inhibitor binding site

@ast

Elucidation of the Hsp90 C-terminal inhibitor binding site

@en

Elucidation of the Hsp90 C-terminal inhibitor binding site

@nl

type

label

Elucidation of the Hsp90 C-terminal inhibitor binding site

@ast

Elucidation of the Hsp90 C-terminal inhibitor binding site

@en

Elucidation of the Hsp90 C-terminal inhibitor binding site

@nl

prefLabel

Elucidation of the Hsp90 C-terminal inhibitor binding site

@ast

Elucidation of the Hsp90 C-terminal inhibitor binding site

@en

Elucidation of the Hsp90 C-terminal inhibitor binding site

@nl

P1433

Q28236934-F9B8336A-2739-4FF5-9D7D-1415944194CB

P1476

Q28236934-EB73E72F-5238-4240-B591-354BC04B02A5

P2093

Q28236934-1FCA486A-FE81-482C-9208-059C30BEF955

Q28236934-24C3E3B0-FDFB-45E4-AE78-F8088C08FD67

Q28236934-55FA8430-DE5C-405A-B220-FF2C3ACBDA7D

Q28236934-61E3CE3F-8222-4473-9EE9-5A9D39F0D86B

Q28236934-71EDF7BD-3D77-4644-BBD6-1FACB6168121

Q28236934-AB50C7B1-FF93-4928-BE7F-D51F68DEB131

Q28236934-C1566693-5596-4358-91FE-E3C3523FE0E6

Q28236934-F709F457-8133-4425-BDCB-21E0766B27DD

P2860

Q28236934-017DF5F1-0E6F-48E9-A27C-65AFA4DD43C9

Q28236934-08BDCDFB-8FE5-47DF-803F-0206EDCCF89B

Q28236934-0E094000-289A-4567-9587-DFCE4BCF8FBD

Q28236934-0E819BDF-0C2A-4073-B7DA-CBE6EA455495

Q28236934-0F10CFF8-D5E8-4E63-B10B-71EC2EE86606

Q28236934-1FB70487-968B-4576-9E6E-C98B4DB6DBDB

Q28236934-246FF8DA-83E1-406C-AD61-3916CC355309

Q28236934-34009F84-23B6-4559-92DA-44B5A87AFE39

Q28236934-35494735-3027-4114-AAC2-2283795CF141

Q28236934-405ED7BB-0CBF-469F-BE1E-75FB21F71429

P304

Q28236934-CBF53523-E8AD-4D3A-9FAD-780A039E7FE7

P31

Q28236934-2689388C-1C4C-46CF-8080-827FD529F09C

P356

Q28236934-BB9545C5-00C8-4190-868C-E10FAC89562F

P407

Q28236934-3E5555AB-62AD-4F8F-92DF-3DD6BDDB3B4C

P433

Q28236934-9FFC0102-6433-417D-A9D0-53E3B41709BC

P478

Q28236934-83EE07FB-144C-42B8-AA6A-F58C1DC858CE

P50

Q28236934-E3CC8739-D088-493B-85AE-B9CE31534895

P577

Q28236934-1308062E-59FA-4FA0-96E2-03B5DC737772

P5875

Q28236934-EF063AEB-B568-4779-981C-3FBE60FA1D8B

P698

Q28236934-5FB9599B-7FE5-482E-A3DD-4C996DED2A7D

P932

Q28236934-E56B0344-FC75-4DCC-87D4-2E64FDF2C42C

P356

P1433

ACS Chemical Biology

P1476

Elucidation of the Hsp90 C-terminal inhibitor binding site

@en

P2093

Anshuman Dixit

http://www.w3.org/2001/XMLSchema#string

Brian S J Blagg

http://www.w3.org/2001/XMLSchema#string

Laura B Peterson

http://www.w3.org/2001/XMLSchema#string

Liang Sun

http://www.w3.org/2001/XMLSchema#string

Palgunan Kalyanaraman

http://www.w3.org/2001/XMLSchema#string

Robert L Matts

http://www.w3.org/2001/XMLSchema#string

Steve D Hartson

http://www.w3.org/2001/XMLSchema#string

Sudhakar Voruganti

http://www.w3.org/2001/XMLSchema#string

P2860

The Hallmarks of Cancer

Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase

Basic local alignment search tool

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

Clustal W and Clustal X version 2.0

Scalable molecular dynamics with NAMD

Comparative protein modelling by satisfaction of spatial restraints

Hsp90 is regulated by a switch point in the C-terminal domain

P304

800-807

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/CB200052X

http://www.w3.org/2001/XMLSchema#string

P407

P433

8

http://www.w3.org/2001/XMLSchema#string

P478

6

http://www.w3.org/2001/XMLSchema#string

P50

Gennady Verkhivker

P577

2011-05-17T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51104062

http://www.w3.org/2001/XMLSchema#string

P698

21548602

http://www.w3.org/2001/XMLSchema#string

P932

3164513

http://www.w3.org/2001/XMLSchema#string