Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
about
Bleach activates a redox-regulated chaperone by oxidative protein unfoldingExploiting thiol modificationsThe roles of conditional disorder in redox proteinsTranscriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutaseThe crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.Thiol-based redox switchesRedox-regulated chaperones.Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli.Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneConditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.Expanding the proteome: disordered and alternatively folded proteins.Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC.Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.Protein quality control under oxidative stress conditions.Order out of disorder: working cycle of an intrinsically unfolded chaperone.A thermodynamic definition of protein domainsBeyond transcription--new mechanisms for the regulation of molecular chaperones.Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperonesProtein unfolding as a switch from self-recognition to high-affinity client bindingOxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia.Reactive oxygen species and cellular oxygen sensingRegulated unfolding of proteins in signalingThe redox-switch domain of Hsp33 functions as dual stress sensorTranscriptional and phenotypic responses of Listeria monocytogenes to chlorine dioxide.Proteomic methods unravel the protein quality control in Escherichia coli.Disorder in the lifetime of a proteinBile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS.Interplay between redox and protein homeostasis.Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions.Theoretical insights into the mechanism of redox switch in heat shock protein Hsp33.Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis.HSP33 in eukaryotes - an evolutionary tale of a chaperone adapted to photosynthetic organisms.Oxidant stress during simulated ischemia primes cardiomyocytes for cell death during reperfusion.Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.
P2860
Q24643056-295C181A-FB69-4085-839C-9C8EA4F03911Q24793687-0FFFC5BF-414E-4942-9826-DFDBD6D96D0BQ27026679-590184DA-B071-48C7-8D62-79AE3E9EC278Q27937674-39E64FAA-9BC6-4E68-8AE3-4F67957E2424Q30418692-7E36BB34-B192-41A6-B404-E68240278417Q33762400-CF792FA3-4C33-4082-BD91-C713C18B3731Q33766707-AE792F98-6AE4-4566-A9B0-47EB1B6511B8Q33766713-ADC64963-F557-42AB-9CCC-757F5EA37B95Q33799664-C0847F0C-3523-4C2B-9F06-4CA8790C96D3Q33875537-3E851C06-6E59-43C4-9D1A-45960E01B8C3Q34065998-47121CFD-558B-4B5B-8257-096BED9EA125Q34197530-F2030C7B-7D23-4F2A-9EDC-0836D8FD74F6Q34537224-C1D81177-D5CC-48E7-B656-D754A4802D6CQ35104234-40AAC884-99BA-494D-BFE2-1910BC849243Q35129032-FB3FFA70-7E13-4DF0-A09A-C233D4493618Q35171206-8609FD2D-B15D-4E05-BD4C-FA1D568E71E9Q36038114-EC6D3888-5C3C-4F78-96F4-360E7D278E35Q36066412-CCA21498-9B8E-4DD9-842D-5EEF93F8C82DQ36069364-5EDE1966-8905-4182-AE49-349BE8EBF9A4Q36492826-B1A98494-0B72-4799-9B93-E3A747050E86Q36528501-BD6489A7-45A1-421D-B2A2-CDF126A15CB9Q36542391-B52AAA9D-A543-4007-8C18-C9D4B87FB1C8Q36950679-55299BD7-2736-46D4-97BD-FBAD2759392EQ36983557-7832675E-1F49-4742-A90A-169F505169E4Q37436690-710D7D94-04F3-4542-9094-47F6BB9842A1Q37713123-1EAF838F-2C95-4F69-ABDA-A251894CF8A4Q37895211-47FA3E2C-5A33-468F-BECF-7526980ED8D3Q38779717-03AB8EC4-6F5B-49A9-A67D-8200F33979B5Q38808637-46AB60A1-2F11-4927-BDD4-FA05283524D7Q38888594-7B2DF28A-E4F3-44BA-8563-298625833017Q40285963-F65C3385-91A1-429C-952F-7683EFC45409Q41503117-078F6429-7268-4F3D-835D-292E0A729374Q45115040-F60F634B-40AC-4A97-A86E-EE9CF57910A1Q46740761-C09DBB64-428B-419F-B555-0BC054B44D47Q50684490-AEFA873E-E87E-43B1-9F0C-C92BFF66F83DQ53441134-05DBD175-5E37-4305-B559-4C8CF0D00956Q54343806-91AD6F7F-5F52-49A9-A10E-E55DA711BD08
P2860
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@en
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@nl
type
label
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@en
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@nl
prefLabel
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@en
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
@nl
P2093
P2860
P50
P356
P1476
Activation of the redox-regulated chaperone Hsp33 by domain unfolding
@en
P2093
Hauke Lilie
Maria Martinez-Yamout
Ursula Jakob
P2860
P304
20529-20538
P356
10.1074/JBC.M401764200
P407
P577
2004-03-15T00:00:00Z