Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP
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Novel CHOP activator LGH00168 induces necroptosis in A549 human lung cancer cells via ROS-mediated ER stress and NF-κB inhibitionAMPylation matches BiP activity to client protein load in the endoplasmic reticulum.Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains.N-glycosylation Triggers a Dual Selection Pressure in Eukaryotic Secretory Proteins.Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP).A disulfide-bonded DnaK dimer is maintained in an ATP-bound stateA Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Role of autophagy in cell-penetrating peptide transfection model.Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulationConformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.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.Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant.Cripto stabilizes GRP78 on the cell membrane.Pharmacological profiling of sigma 1 receptor ligands by novel receptor homomer assays.Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding.Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex.Glucose-regulated protein 78 substrate-binding domain alters its conformation upon EGCG inhibitor binding to nucleotide-binding domain: Molecular dynamics studies.Repurposing drugs to target the malaria parasite unfolding protein response.Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate releaseCochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
P2860
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P2860
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP
description
2015 nî lūn-bûn
@nan
2015 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
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2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
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name
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@ast
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@en
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@nl
type
label
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@ast
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@en
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@nl
prefLabel
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@ast
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@en
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@nl
P2093
P2860
P921
P3181
P1433
P1476
Close and Allosteric Opening o ...... in a Human Hsp70 Chaperone BiP
@en
P2093
Melesse Nune
Qinglian Liu
Yinong Zong
P2860
P304
P3181
P356
10.1016/J.STR.2015.10.012
P407
P50
P577
2015-11-19T00:00:00Z