Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.
about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Anti-inflammatory peptide regulates the supply of heat shock protein 70 monomers: implications for aging and age-related diseaseMulti-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperonesQuantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPsGroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATPHsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.The CNGCb and CNGCd genes from Physcomitrella patens moss encode for thermosensory calcium channels responding to fluidity changes in the plasma membrane.Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides.Co-evolutionary analysis implies auxiliary functions of HSP110 in Plasmodium falciparum.Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of TauopathySystems-wide analysis of acclimation responses to long-term heat stress and recovery in the photosynthetic model organism Chlamydomonas reinhardtii.
P2860
Q26779046-7B953D50-875F-4B80-934F-97CD609FA080Q28286034-53E42807-1089-4F7E-993E-4FA27BE321B8Q34038270-ECC3139A-DDFB-483E-AF7A-328FD4123691Q35485951-9700504F-6CD4-43FB-AD42-3204C0E8E38FQ35686747-CC6F16B5-F326-479E-A70F-48457D05BF4DQ35725189-7679BE53-CC4D-4897-982B-ED0CADECD6A4Q36820063-6EEC4B16-C5C4-4DE3-B200-5EC9BAF06C89Q37175214-6410E1A8-8945-41CF-8370-2F3F1DB814F9Q37378889-3FF7235A-88D7-4315-A437-E984E26183AEQ38107685-277C979E-8539-4BB1-994A-51DB21982EB6Q40860270-5978A432-995F-47A4-A8D2-19E276C87982Q41493996-B4826E2B-A7B3-4C19-ABC2-077CF20F92E7Q43528508-56339387-ECDD-41D5-90D2-276AC4182215
P2860
Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Probing the different chaperon ...... molabile luciferase substrate.
@en
Probing the different chaperon ...... molabile luciferase substrate.
@nl
type
label
Probing the different chaperon ...... molabile luciferase substrate.
@en
Probing the different chaperon ...... molabile luciferase substrate.
@nl
prefLabel
Probing the different chaperon ...... molabile luciferase substrate.
@en
Probing the different chaperon ...... molabile luciferase substrate.
@nl
P2860
P356
P1433
P1476
Probing the different chaperon ...... molabile luciferase substrate.
@en
P2093
Paolo De Los Rios
Pierre Goloubinoff
P2860
P304
P356
10.1002/PROT.23024
P407
P577
2011-04-12T00:00:00Z