Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes. - Wikidata - awgldk - TriplyDB

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

http://www.wikidata.org/entity/Q37079732

about

Proline isomerization in the C-terminal region of HSP27.Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20 The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer.A disulfide-bonded DnaK dimer is maintained in an ATP-bound state Bacterial Hsp90 ATPase Assays.Molecular dynamics simulations of Hsp40 J-domain mutants identifies disruption of the critical HPD-motif as the key factor for impaired curing in vivo of the yeast prion [URE3].Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development.Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.Fingerprints of Conformational States of Human Hsp70 at Sub-THz Frequencies Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium

P2860

Q33779914-8783CCE1-19DA-4658-8FC6-B305AB725E28 Q33920604-839D3D81-FCBD-4DD6-8F94-744283C0AFC1 Q37590176-F6A3BDA4-94F5-4830-8EC0-4B3D47E95DFF Q38698836-5F906EB5-D11E-47B0-880F-BE1E540F5403 Q41834098-5E96ADB7-89CF-4D38-9105-AF4EB1846260 Q47362593-94AD20BB-AAAB-45BB-9F04-987CC8C2E25D Q48001128-AB66C39F-870F-411A-B016-F2894DE9AD4C Q48118580-B52FD5D6-2665-451B-855C-57AABC9525C5 Q51237852-473C22F7-5FEC-4CD0-B347-46A32933C671 Q57154138-0698F3D1-ADF2-4B3C-B595-C7863925677D Q58765325-40E4A6BE-A905-4EBE-9403-3B0BC690AC99

P2860

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

http://www.wikidata.org/entity/Q37079732

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 23 June 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@en

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@nl

type

label

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@en

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@nl

prefLabel

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@en

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.

@nl

P1433

Q37079732-3DCE7049-B01A-474E-867B-BB5A909FB9B4

P1476

Q37079732-4473F771-C95F-4103-9BCA-186D2E9AB68A

P2093

Q37079732-2EF6A3B0-BB0C-4D1A-B024-A59AE97B1B9A

P2860

Q37079732-0008D115-86AE-4600-AFDE-68EE6458B32F

Q37079732-042142DB-73D5-4BE7-A905-5F1B6226A4D0

Q37079732-09D635D3-0ED3-457A-8A93-52F00370B723

Q37079732-0CEE3B25-3BC8-42BD-8A5B-6BEDE62C8F46

Q37079732-0F11FB5A-5E95-4CAC-87FF-0872D8CE91C3

Q37079732-111B750F-69AD-4A0B-A427-439611AF5919

Q37079732-115D706C-9303-4A93-BD74-008F8800CC6C

Q37079732-129A3D93-761A-421A-8848-9841B845F4D9

Q37079732-14049BCE-66F6-45F2-8855-F6CF9662AA09

Q37079732-18B16171-3C2E-4842-9E60-6B8FF212D31B

P304

Q37079732-239B1ED0-4263-43E6-A157-54DF1652A134

P31

Q37079732-1A713AF7-0E9B-4F0E-9050-406633E7BD08

P356

Q37079732-A69BF5C2-91DC-4FA7-BB21-DEC61D1AC544

P433

Q37079732-26356712-DE35-4E79-92F2-A870838428F6

P478

Q37079732-754865FD-5B05-4225-9B1B-AE9DD5AFBA34

P50

Q37079732-E06ED648-6F68-470C-8680-A82EDFEDA578

Q37079732-ED408B7A-635F-4825-9E98-86677054C0F7

P577

Q37079732-402FC10A-CA41-40B4-9AAF-73B75E94FD7B

P698

Q37079732-F263465A-C603-4F46-97F4-2EE90B080972

P932

Q37079732-3D372FD8-353C-4D5E-9412-6EEEF801D5C8

P356

J.STR.2016.05.011

P1433

P1476

Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes

@en

P2093

John Lute Markley

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

P2860

Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles

Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer

Hsp70 chaperones: cellular functions and molecular mechanism

Discovery of molecular chaperones

Molecular mechanism of allosteric communication in Hsp70 revealed by molecular dynamics simulations

The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ

Structural insights into substrate binding by the molecular chaperone DnaK

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG

Structural Basis of J Cochaperone Binding and Regulation of Hsp70

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

P304

1014-1030

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

P31

scholarly article

P356

10.1016/J.STR.2016.05.011

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

P433

7

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

P478

24

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

P50

T Reid Alderson

P577

2016-06-23T00:00:00Z

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

P698

27345933

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

P932

4938735

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