About: Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 16 July 2002

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 2002 (uk) im Juli 2002 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en juillet 2002 (fr) artículu científicu espublizáu en xunetu de 2002 (ast) scientific article published on 16 July 2002 (en)
publication date	wds:Q74472513-CF2F1983-BE7E-4BD0-9489-E1CA5326FE26
publication date	2002-07-16 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q74472513-46181863-A149-48CE-BC92-D5CD66F68DA7
language of work or name	English
cites work	wds:Q74472513-22A6080C-1E99-42D6-A095-C92B3E8B85C4 wds:Q74472513-2F0D7D04-7585-4C72-B561-C0FFD57A138C wds:Q74472513-30C87593-5471-4BCF-95A5-C7F640BE2D0B wds:Q74472513-355F6336-8C1C-4435-9AAA-3D6563B48817 wds:Q74472513-3F3B5CC2-5760-41D2-ADC5-8453573F914F wds:Q74472513-4427ED3D-1E7B-4DB4-9D2B-1AFC14943489 wds:Q74472513-4BD3CFBA-305A-493D-850C-0C12E299DE4F wds:Q74472513-51329A15-3718-4207-A788-0ED82D08EFE7 wds:Q74472513-52E55987-09E1-4D58-86E2-7E82DDA13422 wds:Q74472513-550CE049-F8BC-4CBC-844C-8EA242565D30 wds:Q74472513-640EFC81-8E5B-4E2A-919B-53E306978F75 wds:Q74472513-6A8BCFB1-23EA-4C10-83FE-DB9F70F26F46 wds:Q74472513-759C9E3E-EA13-4A74-B890-EEB0B597B98D wds:Q74472513-791D96FF-3A1C-4F96-923E-61AA03447254 wds:Q74472513-7A693CEB-74AA-445D-84BE-F9B89BF60B2E wds:Q74472513-7EBDABB5-DA3A-4759-96E2-AF6DEF52CEF3 wds:Q74472513-80977764-2FD3-4FCD-93B9-079656579BE2 wds:Q74472513-8C953E83-44FA-43E8-B475-BFD28871F6FE wds:Q74472513-907DE927-FD1E-4101-A3E3-8E45B0058EB1 wds:Q74472513-91069DAB-31FC-4936-AD3B-345626F65A57 wds:Q74472513-9A3B52D0-1000-471D-AE4B-DD2A407B1675 wds:Q74472513-9B1F4759-C821-4203-AAD9-066C6DFBD45F wds:Q74472513-9F34B5BD-388D-4F0E-B3E6-650A8C496E00 wds:Q74472513-A3021F80-7E6A-44DF-999B-CBCA2827AA17 wds:Q74472513-A758E315-25EB-42AE-B192-02BCC73225F0 wds:Q74472513-ACF2E8E4-6E66-4EC1-8727-69A0C40028B4 wds:Q74472513-B1BF11BE-362A-4C42-AD66-3BFE0323A96E wds:Q74472513-B4088E10-02DD-4E2D-8320-F437E9C45DFB wds:Q74472513-B748195D-0ECC-4A36-A4C0-DC19A0F683A6 wds:Q74472513-BF9576D1-FC09-44A4-B14B-1B07586EF239 wds:Q74472513-C6C57D91-01F3-44BB-A536-49255507CD01 wds:Q74472513-CD7776BE-33D4-485F-98CD-F6E7C8EC4774 wds:Q74472513-DB4CF18F-B51E-4300-824D-39E4978B68F6 wds:Q74472513-DBC46CE1-8A77-48C5-B4FD-E221F4B6C67F wds:Q74472513-DD7968BF-1CC5-4DCF-94C0-CE6979378E6F wds:Q74472513-DE49F2D1-FD44-46D3-B7A9-80679422FFC2 wds:Q74472513-E72170AC-C4FD-4EB0-A229-F864C9AF35ED wds:Q74472513-E7926EFE-F878-42C0-8883-FE26208651CB wds:Q74472513-E86AF923-F116-4B9F-AB7F-BF129D7AD499 wds:Q74472513-F449FD90-06E8-4829-BFCD-4F44E2043B71 wds:Q74472513-FA22F70D-92C9-4674-9758-901893FE13B6
cites work	A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase Mechanism of dimer formation of the 90-kDa heat-shock protein The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation Steroid receptor interactions with heat shock protein and immunophilin chaperones Nucleotides and two functional states of hsp90 The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase Dimerization characteristics of the 94-kDa glucose-regulated protein. The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins Modulation of Akt kinase activity by binding to Hsp90 Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins Isolation of Hsp90 mutants by screening for decreased steroid receptor function The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains The charged region of Hsp90 modulates the function of the N-terminal domain Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein Cdc37 is a molecular chaperone with specific functions in signal transduction Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast Interaction between casein kinase II and the 90-kDa stress protein, HSP90 The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones Dynamic activation of endothelial nitric oxide synthase by Hsp90. Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae Heat-induced chaperone activity of HSP90. Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family Liberation of the intramolecular interaction as the mechanism of heat-induced activation of HSP90 molecular chaperone The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47 Identification of dimeric structure of proteins by use of the glutathione S-transferase-fusion expression system Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells
author name string	wds:Q74472513-028547CC-6821-4F4C-9BE5-BCCDB10374E9 wds:Q74472513-22150B0B-EE4E-421F-9B03-FD9945EAE287 wds:Q74472513-2F29DB0E-4CA1-45E5-A2AC-749CA9963109 wds:Q74472513-30FBF4CB-AB29-4E85-AA2D-8143E3E21EDD wds:Q74472513-40AEB0F2-D171-44B7-9A6E-3C0866F2EE99 wds:Q74472513-773BA0CA-88E0-4D5A-B3F1-CA730B7D14B5 wds:Q74472513-7AD6E0F7-A156-4CDF-AC5E-3EAAFA3827B0

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 172 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software