about
Insights into the molecular mechanism of allostery in Hsp70s.Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingThe novolactone natural product disrupts the allosteric regulation of Hsp70An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly.Pathways of allosteric regulation in Hsp70 chaperones.Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.Chaperone action at the single-molecule level.Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.Alternative modes of client binding enable functional plasticity of Hsp70.Hsp70 chaperone machines.Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling.Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils.Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityCharged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activityRecruitment of Hsp70 chaperones: a crucial part of viral survival strategies.Mechanism of substrate recognition by Hsp70 chaperones.c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Hsp70 chaperone dynamics and molecular mechanism.The universe of Hsp90.Hsp90: breaking the symmetry.Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux.The oxidation state of the cytoplasmic glutathione redox system does not correlate with replicative lifespan in yeastMolecular mechanism of thermosensory function of human heat shock transcription factor Hsf1.Analyzing protein dynamics using hydrogen exchange mass spectrometry.Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37.Phosphotyrosine confers client specificity to Hsp90.Backbone circularization of Bacillus subtilis family 11 xylanase increases its thermostability and its resistance against aggregation.Differences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insightsSmall Molecule Inhibitors Targeting Tec Kinase Block Unconventional Secretion of Fibroblast Growth Factor 2HIV-Tat Protein Forms Phosphoinositide-dependent Membrane Pores Implicated in Unconventional Protein SecretionModeling Hsp70-mediated protein folding.Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.Analysis of subsecond protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setupSpatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interactionThe chaperone network connected to human ribosome-associated complexA model for handling cell stress.The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway.Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones.
P50
Q26779247-82B1B5E0-57B3-41C4-8414-66F6833F2B0BQ27667685-E15E567F-9D7A-4F06-8B80-70D0DADEEE1FQ27697073-EEBFCC62-51F0-4FD2-A804-529BB96C5351Q30273576-24272D72-3985-4854-8A4B-07E91FE7998FQ30667048-012B0A81-690D-4AFA-BE43-178755C0A1E2Q33575042-5D3D5E7D-4BAF-403C-97C3-4AAB68F81BE6Q34368326-CDB68AE0-AAFA-4757-A7BC-8DF127902AE1Q34488383-049BD3DC-7D98-462F-91D7-CFBD008FDA78Q34543463-4B4773A9-002B-4CC1-B432-F9FFE6889538Q34545594-1F47757E-B4E2-49D7-B975-675811040BE0Q34660530-F7F41186-602F-4E83-9A55-F6910786E742Q35753373-B7A972B4-C2F1-40E4-AEDD-0D4C1EBC9B4AQ35764464-6E831140-39B0-4F30-94C6-1FBCE6E943EAQ35779397-E3151B3D-03F4-4922-9F2E-AFC5DAEA6F9CQ35831258-EC2384D2-0066-4033-AB0A-CA7E1DCE4828Q35843735-40D1F4BA-8E25-46DA-ADC5-9659ED9A50F1Q36652870-3420E555-4A80-445D-B1FE-4839C7436C2EQ37479435-3FF12F89-8AC1-4DAA-B486-10138334A41BQ38135145-305F2FD0-7492-4EDB-A452-93673EB6DDD8Q38273054-08096FE9-0428-4851-AA9A-126924A0DBEBQ38403781-D31BAB88-10AD-48ED-ACF7-2C4C3FD5C6B1Q38616124-8BD9D362-6A17-4187-9B92-14BB2993B63EQ38673040-3BA3B190-F9AF-4DC3-92C9-F4E7142C635CQ38729074-031C4D1C-D508-4A54-AB63-D46029393783Q38833669-BB2F7676-DB11-4F06-A05D-F0A0AE597D85Q39007736-688D0876-6081-4606-A14B-F8A4CA98FEB0Q39738901-B21ACEE1-D888-47C9-AA54-05F4AB6384FAQ40469561-E02D5824-5029-4467-81EE-9D1FFAD2259CQ40568581-A72BF1E3-D282-4D40-9D10-E0C225643EFCQ41046189-386CA332-8967-4A99-B06F-F32F31B5F21FQ41578290-D97C0B00-EDBA-48F7-B4F2-CECC4415CCD1Q41666510-DD6C2284-C083-4ED4-8B68-BFC12BA01133Q41791552-A7DBCA33-B7B5-41F4-BD3B-82042696EC36Q41872561-049C409C-3F9A-4239-BFAF-A01DFD619508Q41898566-9EE10C51-AFD9-44B0-A603-C21E53B62610Q41933973-A7223CCE-1833-4E27-9E56-DC6E24C75F41Q42083091-A82F45A1-2238-4A0D-B6C3-CDC36174FB5BQ42362084-0098C201-31E2-4D52-BBF1-3CB992F7AA95Q42378832-624EB968-0E8F-414B-B97D-E42DEF982333Q42524938-2E429EFD-14B5-412D-A063-E5DFD47483EA
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Matthias P. Mayer
@ast
Matthias P. Mayer
@en
Matthias P. Mayer
@es
Matthias P. Mayer
@nl
Matthias P. Mayer
@sl
type
label
Matthias P. Mayer
@ast
Matthias P. Mayer
@en
Matthias P. Mayer
@es
Matthias P. Mayer
@nl
Matthias P. Mayer
@sl
prefLabel
Matthias P. Mayer
@ast
Matthias P. Mayer
@en
Matthias P. Mayer
@es
Matthias P. Mayer
@nl
Matthias P. Mayer
@sl
P106
P1153
7402464877
P21
P214
3924155044868972520007
P31
P3762
P496
0000-0002-7859-3112
P734
P735
P7859
viaf-3924155044868972520007