About: The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation

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About: The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation Goto Sponge NotDistinct Permalink

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scientific article published on 20 February 2019

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) artículu científicu espublizáu en febreru de 2019 (ast) наукова стаття, опублікована в лютому 2019 (uk) scientific article published on 20 February 2019 (en)
publication date	wds:Q91760261-74B29275-B7FE-4879-B28A-F3A269D4C6BD
publication date	2019-02-20 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q91760261-3053A2BA-6B1F-4B43-9703-041E938A6262
language of work or name	English
cites work	wds:Q91760261-05D9411C-0CD6-4B63-B97A-30457D5980F6 wds:Q91760261-1219A412-3ADF-4E7A-BB2C-BDD9580D4B5E wds:Q91760261-1C01ACAD-5E62-466B-873B-78D1AE4249D6 wds:Q91760261-1DDA46DE-E25B-4B48-AA4E-CD826723CBA7 wds:Q91760261-1F67BBCD-B7FB-45B0-806D-BABA80DB74F4 wds:Q91760261-245AF60B-75C3-461C-9C08-BB541FFCD8E5 wds:Q91760261-271419FF-5655-401E-9711-0BDE75D1901B wds:Q91760261-3D48734C-4A1D-469A-8194-2AC4691B47CC wds:Q91760261-3F66D47C-7006-4C7A-A1A9-D03DE7A24F24 wds:Q91760261-4397A529-B556-46C1-ADFD-5898F2F38C7F wds:Q91760261-49ADB7EF-17CD-4B8C-A683-2315833FE150 wds:Q91760261-4B905A2C-78A8-402D-9B75-466309916173 wds:Q91760261-4BABB6CE-E602-4EBF-B27E-019879DB46CD wds:Q91760261-5B04F40D-914D-46EF-8620-1A44C9CB53E9 wds:Q91760261-723953C2-C9CC-4B9E-ACE4-0FF8F963C710 wds:Q91760261-74D22DC9-C31A-42CE-B916-B87F63BD6B57 wds:Q91760261-774EBA14-2C90-430E-8C15-FF3820FE394D wds:Q91760261-77A02B1D-4EEE-4B0C-A19D-BD6BCE0DA990 wds:Q91760261-79972561-0A52-483F-A0E3-F2F780F6524A wds:Q91760261-7C135CDB-24BC-466A-BCFA-28F697AEA3C3 wds:Q91760261-7E7211D8-83EC-476E-815A-996B3F47EE0D wds:Q91760261-8BCF1802-422A-43BD-BD0A-8494A8BFE0BE wds:Q91760261-8D74B6AE-8342-43E1-9CFA-1A8767DDF559 wds:Q91760261-9281CC33-A73B-4415-9F70-74F6226AAEF1 wds:Q91760261-94000CB0-428C-4CD8-B103-0A2EA8482C1D wds:Q91760261-9B420BB9-CAEF-464D-BE8C-47528A058F64 wds:Q91760261-9F8A590F-3454-460F-949B-253B731C2CD1 wds:Q91760261-ABF152FE-37CA-4147-B586-452DFF2B0BA4 wds:Q91760261-BF394522-4AA9-405B-9A06-24A5E2E7DAA2 wds:Q91760261-C709A988-F3FA-4245-8C7A-9D2D50E3AC00 wds:Q91760261-C9E300B1-EA8F-4A99-B4D6-BD43FC95154C wds:Q91760261-E2FE4FF2-20D2-4D3F-AB84-9AF362754F2B wds:Q91760261-ECF9005B-263B-4D6A-AC6A-850A6BF8EA35 wds:Q91760261-F3F248B9-A704-4971-9E75-7C01CE2F0E72 wds:Q91760261-F52B8F9A-50A9-43BC-A04D-DB9FC4246D62 wds:Q91760261-F5638B84-842C-464B-9750-2B7A92532949 wds:Q91760261-F8B4A804-8ACF-4003-95F9-AF36E1B7812A wds:Q91760261-F8F8D5F1-C380-4F02-9838-C66F567916BF
cites work	Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex An interaction map of endoplasmic reticulum chaperones and foldases The CCPN data model for NMR spectroscopy: development of a software pipeline An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78 Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation Interconversion of three differentially modified and assembled forms of BiP Modulation of the ATPase cycle of BiP by peptides and proteins Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket Substrate transfer from the chaperone Hsp70 to Hsp90. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. Crowding Activates Heat Shock Protein 90. The ClusPro web server for protein-protein docking Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker 2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling Functional and physical interaction between yeast Hsp90 and Hsp70. Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site. Dancing with the Diva: Hsp90-Client Interactions. 5'-N-ethylcarboxamidoadenosine is not a paralog-specific Hsp90 inhibitor
author name string	wds:Q91760261-1A14F7AC-032F-4128-91E5-23066BA4C207 wds:Q91760261-775162E0-9DDA-4092-943C-DB5247F865CA wds:Q91760261-C636AC12-8B91-4325-9784-E5B52540D68C
author name string	Ming Sun Shanshan Liu Judy L M Kotler
rdfs:label	The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (en) The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (nl)
skos:prefLabel	The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (en) The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (nl)
name	The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (en) The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation (nl)
author	wds:Q91760261-56D64EBA-4D05-411A-AFE8-46A183791A67
author	Timothy O Street
title	wds:Q91760261-BC096D41-0D87-42F9-BA9A-5D79EE032B96

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