ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.
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Intracellular Mono-ADP-Ribosylation in Signaling and DiseaseBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsThe Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and HistonesFive Questions (with their Answers) on ER-Associated DegradationClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPFormation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative StressExperimental reconstitution of chronic ER stress in the liver reveals feedback suppression of BiP mRNA expressionNew Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Proteasome regulation by ADP-ribosylationHow viruses hijack the ERAD tuning machinery.Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.Generation of human ER chaperone BiP in yeast Saccharomyces cerevisiaeNew PARP targets for cancer therapyPhysiological modulation of BiP activity by trans-protomer engagement of the interdomain linkerAMPylation matches BiP activity to client protein load in the endoplasmic reticulum.Endoplasmic reticulum stress sensing in the unfolded protein responseOn the importance of oxidative folding in the evolution of conotoxins: cysteine codon preservation through gene duplication and adaptation.Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology.Selective inhibition of the unfolded protein response: targeting catalytic sites for Schiff base modification.The human NAD metabolome: Functions, metabolism and compartmentalization.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumrAMPing Up Stress Signaling: Protein AMPylation in Metazoans.FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.A first line of defense against ER stress.A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Unfolded protein responses with or without unfolded proteins?Surveying the floodgates: estimating protein flux into the endoplasmic reticulum lumen in Saccharomyces cerevisiae.Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.ARTC1-mediated ADP-ribosylation of GRP78/BiP: a new player in endoplasmic-reticulum stress responses.The protein kinase PERK/EIF2AK3 regulates proinsulin processing not via protein synthesis but by controlling endoplasmic reticulum chaperones.
P2860
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P2860
ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.
description
2012 nî lūn-bûn
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2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
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name
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@ast
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@en
type
label
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@ast
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@en
prefLabel
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@ast
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@en
P2860
P50
P356
P1476
ADP ribosylation adapts an ER ...... ions in unfolded protein load.
@en
P2093
Giulia Tomba
Kseniya Petrova
P2860
P304
P356
10.1083/JCB.201202005
P407
P577
2012-08-01T00:00:00Z