Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94. - Wikidata - wikimedia - TriplyDB

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

http://www.wikidata.org/entity/Q36458429

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GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Different Poses for Ligand and Chaperone in Inhibitor-Bound Hsp90 and GRP94: Implications for Paralog-Specific Drug Design Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase Identification of subunit-subunit interaction sites in αA-WT crystallin and mutant αA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry Saccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentation Integrating mass spectrometry of intact protein complexes into structural proteomics Collision-induced dissociation of Lys-Lys intramolecular crosslinked peptides.Finding chimeras: a bioinformatics strategy for identification of cross-linked peptides.Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Decarbonylated cyclophilin A Cpr1 protein protects Saccharomyces cerevisiae KNU5377Y when exposed to stress induced by menadione.The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modeling Selective enrichment and identification of azide-tagged cross-linked peptides using chemical ligation and mass spectrometry.An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells.GRP94 in ER quality control and stress responses Conformational dynamics of the molecular chaperone Hsp90 Experimental Anti-Inflammatory Drug Semapimod Inhibits TLR Signaling by Targeting the TLR Chaperone gp96.Optimized Fragmentation Regime for Diazirine Photo-Cross-Linked Peptides.Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.Fragmentation features of intermolecular cross-linked peptides using N-hydroxy- succinimide esters by MALDI- and ESI-MS/MS for use in structural proteomics.

P2860

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P2860

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

http://www.wikidata.org/entity/Q36458429

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh

2006年學術文章

@zh-hant

name

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@ast

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@en

type

label

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@ast

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@en

prefLabel

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@ast

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@en

P1433

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P1433

Protein Science

P1476

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

@en

P2093

Alma L Burlingame

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

Christopher V Nicchitta

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

Feixia Chu

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

Jason C Maynard

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

P2860

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Structures of the two 3D domain-swapped RNase A trimers

Antibody multispecificity mediated by conformational diversity

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

P304

1260-1269

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scholarly article

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10.1110/PS.052065106

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6

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15

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Gabriela Chiosis

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2006-06-01T00:00:00Z

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7050823

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16731965

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P921

molecular chaperones

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2242539

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