Synergistic cooperation between two ClpB isoforms in aggregate reactivation. - Wikidata - awgldk - TriplyDB

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

http://www.wikidata.org/entity/Q33653831

about

Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis Substrate Discrimination by ClpB and Hsp104.Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans YjcC, a c-di-GMP phosphodiesterase protein, regulates the oxidative stress response and virulence of Klebsiella pneumoniae CG43.Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions.Aggregate reactivation mediated by the Hsp100 chaperones DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.N-terminomics identifies Prli42 as a membrane miniprotein conserved in Firmicutes and critical for stressosome activation in Listeria monocytogenes.Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.ClpL is a chaperone without auxiliary factors.Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic Spirochaete Leptospira interrogans.

P2860

Q28485543-11D84D91-753D-453F-8545-6D3B24BD7C95 Q28487701-E71852AE-F913-4147-AEAA-28957181722D Q33734726-34CF0FF1-ED4B-40C6-9027-7DAA9F2CEA1F Q33898027-D3EB1E00-FF98-49D9-BAAC-1E6CB926D2E7 Q34917638-40109FED-089F-471F-BDB1-323FB99C9A81 Q35191976-D281CAE5-FA89-41E3-963A-D9410286C716 Q35840288-E1A39FEA-7894-4506-9A50-3B345C65EF75 Q36217287-642B7180-29F9-4866-BA01-4BA765A0E9FE Q36365102-5AFD9423-D9E7-4973-8FE5-AC5BADB091CE Q36580607-D852ABFD-C1B7-4954-926B-752A8284E0E0 Q40335166-B86DBACB-D2B8-4956-AD06-1A8D1AFB0115 Q42264565-22176C5E-8057-4CEC-9203-79539F3B0C59 Q52324439-882B0C38-4589-41CF-8B11-309C0B34B191 Q53236221-4847A701-43C6-4748-84EA-E1E71D0A691A Q55038087-64930407-ABA6-42F4-A0CB-FAFCDE9AFA26

P2860

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

http://www.wikidata.org/entity/Q33653831

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

name

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@ast

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@en

type

label

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@ast

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@en

prefLabel

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@ast

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

@en

P1433

Q33653831-CA796334-AC62-4BB7-89B5-214F5689F648

P1476

Q33653831-9201DB75-4DAC-4793-8391-814FF117D3F0

P2093

Q33653831-4AA1CB77-2FE0-49FC-83C8-1DCDD01820F2

Q33653831-4E8C58AA-D44D-4B96-A161-02AC86FA52B9

Q33653831-55761492-5930-4982-873C-E7E40399E459

Q33653831-6FAA8833-2FB7-4BAD-8C3F-FF581FA29CF5

Q33653831-7E2042EA-1F97-496F-8872-B95F63B00645

Q33653831-DAC4846C-83F8-40D5-B071-B18A220CB281

P2860

Q33653831-019C1969-A1A8-45F3-91F9-915B0ABD9E9C

Q33653831-02C05994-AA41-4FFB-99D8-17EEFCFD103D

Q33653831-14F077E8-C317-4EC6-9A99-99C47B571E8E

Q33653831-1BC6CECA-319A-4017-8F14-50C0ABC078E4

Q33653831-2F67E701-59EF-4306-B57F-202E92D7A7B2

Q33653831-3C260946-6718-4D03-8F7D-F0108045BA84

Q33653831-3E32443D-7E10-4F29-AA43-809B80B3D245

Q33653831-45C3F926-1666-4A78-95C9-E8059AD61DDF

Q33653831-4C6B1FE9-DB98-4E20-88B5-14AC9053E62B

Q33653831-4E5D8C52-B352-4C9D-A6CC-56A9E95CC004

P304

Q33653831-99F485DF-8445-45F1-AC95-4A0C3105A60F

P31

Q33653831-7A5B19CA-4BFD-4FD4-851A-96107AEED823

P356

Q33653831-A65D6D0C-4BB7-49DA-9355-C8694A1C50EB

P407

Q33653831-31DDC592-A0DF-45B1-B6AB-ADEC25C37089

P433

Q33653831-9347E24A-C8E8-4D1B-8343-B39F0FE03495

P478

Q33653831-114E1C6F-4DC0-4B38-99A9-CEFFE30DD1FF

P50

Q33653831-DA8A290B-6362-4339-A7CC-40DED5370891

P577

Q33653831-61DCE686-6B54-4F15-AD28-D3AFCA1BC7A8

P5875

Q33653831-794C69A5-86CF-4705-B3DF-5B62DF539890

P698

Q33653831-07CEE427-939B-4EB5-BD62-F247AE2AE6C0

P932

Q33653831-3EF448D5-50E9-444B-8B8E-4E11C677E1A2

P356

J.JMB.2009.11.059

P1433

Journal of Molecular Biology

P1476

Synergistic cooperation between two ClpB isoforms in aggregate reactivation

@en

P2093

Izabela Guenther

http://www.w3.org/2001/XMLSchema#string

Maria I Zavodszky

http://www.w3.org/2001/XMLSchema#string

Maria Nagy

http://www.w3.org/2001/XMLSchema#string

Michal Zolkiewski

http://www.w3.org/2001/XMLSchema#string

Micheal E Barnett

http://www.w3.org/2001/XMLSchema#string

Vladimir Akoyev

http://www.w3.org/2001/XMLSchema#string

P2860

Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex.

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

AAA+ superfamily ATPases: common structure--diverse function

ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.

P304

697-707

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.JMB.2009.11.059

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

396

http://www.w3.org/2001/XMLSchema#string

P50

Sabina Kędzierska-Mieszkowska

P577

2009-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

40448850

http://www.w3.org/2001/XMLSchema#string

P698

19961856

http://www.w3.org/2001/XMLSchema#string

P932

2822101

http://www.w3.org/2001/XMLSchema#string