Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
about
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumDifferent Poses for Ligand and Chaperone in Inhibitor-Bound Hsp90 and GRP94: Implications for Paralog-Specific Drug DesignAtomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenaseIdentification of subunit-subunit interaction sites in αA-WT crystallin and mutant αA-G98R crystallin using isotope-labeled cross-linker and mass spectrometrySaccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentationIntegrating mass spectrometry of intact protein complexes into structural proteomicsCollision-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 complexesMolecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modelingSelective 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 responsesConformational dynamics of the molecular chaperone Hsp90Experimental 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.
description
2006 nî lūn-bûn
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2006年の論文
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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
P2093
P2860
P356
P1433
P1476
Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
@en
P2093
Alma L Burlingame
Christopher V Nicchitta
Feixia Chu
Jason C Maynard
P2860
P304
P356
10.1110/PS.052065106
P577
2006-06-01T00:00:00Z