Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.
about
Insights into the molecular mechanism of allostery in Hsp70s.BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATPClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machineryPathways of allosteric regulation in Hsp70 chaperones.Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonanceCombining MFD and PIE for accurate single-pair Förster resonance energy transfer measurements.The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Dissection of structural and functional requirements that underlie the interaction of ERdj3 protein with substrates in the endoplasmic reticulum.Alternative modes of client binding enable functional plasticity of Hsp70.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.Sil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretionDecipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum.Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK).Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linkerComputational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationAMPylation matches BiP activity to client protein load in the endoplasmic reticulum.Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2ERdj3 regulates BiP occupancy in living cells.Endoplasmic reticulum (ER) stress response and its physiological roles in plants.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.Proteins improving recombinant antibody production in mammalian cells.Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Structural mechanisms of chaperone mediated protein disaggregation.The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer.The chaperone toolbox at the single-molecule level: From clamping to confining.BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP.Monitoring conformational heterogeneity of the lid of DnaK substrate-binding domain during its chaperone cycle.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum.Cellular Signature of SIL1 Depletion: Disease Pathogenesis due to Alterations in Protein Composition Beyond the ER Machinery.Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET.
P2860
Q26779247-CDAC7FDD-0A35-484B-AA8A-C82407A8679CQ26825679-7651452A-27C5-4451-B63A-4ACAF488E26EQ27678317-2CE96FE0-7366-47FF-A2B8-1A25688E87EEQ28270851-9F0C3774-DFF0-4943-B6D3-DF01AB4FF299Q28587463-2227749B-06CB-4E85-A2C5-76BB1086A86EQ30667048-26630874-157F-4B71-8E2F-1F20BF95B295Q33737717-C46B54B9-D05D-4BD8-B5F3-521002B8D024Q34181177-5705F821-9697-499D-ACAF-8A93FFD83990Q34221854-0D074BD2-F5BE-43D7-BE97-8EDA66622D29Q34283395-C415691D-EBCA-48F7-BB66-BC940A30BE68Q34543463-6F7430ED-8A03-4162-A867-160AAFCDEE57Q34808252-A4372870-E306-4D26-AFA0-4C9AA9A9ED08Q34923990-DFBD2AF9-3FEC-4287-AF9E-4704B915690FQ35027549-59185C9E-0EEA-474C-985C-C45D135F6535Q35069132-D0DBE15A-CF08-4246-9777-873B3018D499Q35671627-1FEF54B8-4AA7-41B5-9436-459C9AAA4AD4Q35854620-9EB81A16-06A2-4642-8557-B8EBA219BF2CQ35855961-60020B87-2736-4C73-8C1A-1E331702317CQ36058976-A0BBD11E-37A9-453A-8C13-15081DAC21AAQ36145748-7095F562-B21E-4EC2-A5BC-D9AF649B81A3Q36169640-9150C8AA-95F8-4EBB-A7D4-CE6F3A6F939AQ36251118-BEFA53C6-6BD1-434C-BF66-C4020D8A97ECQ36539715-77016409-8D0D-406E-B9F3-39978723343EQ36801199-1E9A84AB-4400-4995-985C-25B2E0246D3CQ36815730-247D4F0C-52AD-4A1E-9721-17E51A7C81C0Q36820563-E6AF0874-80FF-4D1F-B2BB-9FD970C95645Q37079732-D5E69E95-06E9-4F3B-A179-8E0D0C5CED74Q37368632-EF478494-C8F5-483F-9DAF-60527B1D1712Q38170315-CFFD03AA-EF10-49D8-B659-F335E844B05EQ38190542-70B7B852-130F-4847-964E-FA3B535BACEAQ38356312-9D5603A1-E60A-4A21-BAC2-E2D842FF17D2Q38490755-FF8DADED-0C9E-4223-9AB3-2D01E58C7D0AQ38698836-54284DA6-1A84-4DB6-8FC6-870EE09066D7Q39200186-8531E977-D8C5-4905-B506-D97E6378690FQ39692774-95B38457-613B-4B7C-A16B-E2BE7AFA8D13Q39719019-161849AF-3557-4471-9F2D-111207DDD034Q39795700-77642828-3BEB-4BE1-81A1-F6C79D1BD07CQ40289318-AD2E31C2-E41D-4FD4-B78E-EC3000E064E8Q40430593-27527796-A2B5-4740-A2FC-2D693471B00DQ41460745-088E2C2F-4AB6-4118-B162-19B79C41DB64
P2860
Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Substrate discrimination of th ...... ed conformational transitions.
@en
type
label
Substrate discrimination of th ...... ed conformational transitions.
@en
prefLabel
Substrate discrimination of th ...... ed conformational transitions.
@en
P2093
P2860
P921
P356
P1476
Substrate discrimination of th ...... ted conformational transitions
@en
P2093
Danae Baerend
Johannes Buchner
Matthias Höller
Moritz Marcinowski
P2860
P2888
P304
P356
10.1038/NSMB.1970
P577
2011-01-09T00:00:00Z