Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation - Wikidata - wikimedia - TriplyDB

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

http://www.wikidata.org/entity/Q27650298

about

Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate Molecular chaperones: guardians of the proteome in normal and disease states The nucleotide exchange factors of Hsp70 molecular chaperones Insights into the molecular mechanism of allostery in Hsp70s.BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions Extrapolation of Inter Domain Communications and Substrate Binding Cavity of Camel HSP70 1A: A Molecular Modeling and Dynamics Simulation Study Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Biochemical and structural studies on the high affinity of Hsp70 for ADP Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Crystal Structure of DnaK Protein Complexed with Nucleotide Exchange Factor GrpE in DnaK Chaperone System: INSIGHT INTO INTERMOLECULAR COMMUNICATION Allostery in the Hsp70 chaperone proteins Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Structural analysis of polarizing indels: an emerging consensus on the root of the tree of life Small molecule DnaK modulators targeting the beta-domain.Kinetic and structural characterization of human mortalin Overproduction and biophysical characterization of human HSP70 proteins.Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Interaction of heat shock protein 70 with membranes depends on the lipid environment.Heat shock proteins in association with heat tolerance in grasses.A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker Mechanisms of the Hsp70 chaperone system.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.Chaperone-client interactions: Non-specificity engenders multifunctionality.ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1.Monitoring conformational heterogeneity of the lid of DnaK substrate-binding domain during its chaperone cycle.Hsc70-induced changes in clathrin-auxilin cage structure suggest a role for clathrin light chains in cage disassembly.Modeling of the Full-Size 3D Structure of Human Chaperone Hsp70 and Study of Its Interdomain Interactions.Expression of DnaJ gene in Alicyclobacillus acidoterrestris under stress conditions by quantitative real-time PCR.A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum.Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Homology model and potential virus-capsid binding site of a putative HEV receptor Grp78.Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation.The chloroplast DnaJ homolog CDJ1 of Chlamydomonas reinhardtii is part of a multichaperone complex containing HSP70B, CGE1, and HSP90C.

P2860

Q21090602-5BDFFC8F-3CCD-44C1-BDCA-5CDBD4A19A4C Q26766168-8F34F043-DC95-4E80-BDCD-13C8DF1EB323 Q26766367-2941FF30-72C8-4FDA-9012-0A034B58E55F Q26779247-94829DB1-D3D6-4BD6-9801-9E9025DCA1EC Q26825679-BE9964C2-B4A4-4E33-844D-BF20C36FDEBA Q27321339-72E4B5B9-1FFC-4562-868D-BA7091E34CCA Q27655465-21007536-D634-45E6-BD52-B7FD46746626 Q27667975-F5C1BF23-284D-471C-A966-6223CB18350E Q27678317-30BC460A-3FD0-4486-953C-9CB38A59C239 Q27678812-925FEEF7-68EF-4CCA-B3E5-477DB721A029 Q28266387-5F054A7F-EA54-4BB4-8DAB-57C80E66E1D4 Q28270851-954E3CC1-793F-4E35-AC08-DA5EB81B7C88 Q30354473-CC31123B-EEE3-4E04-BBDF-81A32A1E60F9 Q30380105-F6EE1245-C139-4F17-9D31-DA4952746936 Q33495332-1DD44B14-A37D-438F-9500-493B1D57F8BC Q33919575-13343778-A2D5-401A-AF69-C21E89749D89 Q34588883-F70B58DD-6BE4-411D-ACC9-054831E32B11 Q34673896-1410CCA4-5333-4553-98AE-F910CB01237B Q34808252-81BA6BF4-4015-42FB-B5D9-2413B89E6480 Q35319529-BE2A6C3B-3695-46A6-800A-C02220616933 Q35431324-C94AE5A6-212C-499F-8145-AA812A1E27AE Q35580778-6ECFC9C1-85A9-4D85-A079-AF584B820E94 Q35606383-433421C4-C5DF-4FAF-B1D9-3B3921C60145 Q35855961-5429CB35-7889-4137-B7D7-C8B81B225D01 Q36169640-109D3EDD-41D1-4195-8DD8-1A47B97479A5 Q37746993-C11BB030-D818-4393-8A4A-501BC5D9DE60 Q38356312-483D447F-D2D1-48E6-9EFC-E9310C438206 Q38611961-5D08F013-4EE3-49CD-A41F-4EC74B7DDDC0 Q39376939-C88D99DF-29FC-4DF4-81B5-CE871FC5DCD8 Q39538987-375564D5-7EB2-4FD6-9C24-36B6F42B5AD1 Q39719019-B03E7941-22F4-4AD4-8442-98600BEBF2ED Q41610914-D24645D7-811A-4C0E-83F1-801B21A092C0 Q42071121-C1E6CF33-EAE2-4A68-8CEC-8AFB27E5D59B Q42656197-A88220C5-D981-4B5E-A346-2341050EED54 Q43125499-BC094C2D-F458-4B95-AEAF-A5CBA90DA11B Q44710284-6DE29914-8E5B-46F2-9C5B-C868099DE69E Q44967706-F95E4BEC-13D7-4664-A507-350D0E52A559 Q45273095-68525DC9-00B9-4D88-A771-6E6279E888C7 Q46446808-F3510900-AFF5-4A4E-9DB0-02DBFF7030A9 Q46521725-021D0D98-E438-45FD-924D-C66F4564DF73

P2860

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

http://www.wikidata.org/entity/Q27650298

description

2008 nî lūn-bûn

@nan

2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@ast

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@en

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@nl

type

label

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@ast

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@en

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@nl

prefLabel

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@ast

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@en

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

@nl

P1433

Q27650298-666770E1-2293-416B-9A3E-AEFF686AABED

P1476

Q27650298-8CC452F6-E3BD-439C-851D-15772556984D

P2093

Q27650298-DCC92490-02F2-4C41-8040-1FD826B700D3

Q27650298-ECDEFC9B-5FB5-41AB-AB15-F05278A7BC24

Q27650298-F0F04084-EB3E-4AD5-9774-80A70233E342

P2860

Q27650298-028A457A-8A37-45AC-B05C-34082BB79ECC

Q27650298-056752CF-02CE-4297-85DA-528620F44998

Q27650298-0A86A199-3394-4D67-AF79-D2BE471A110C

Q27650298-0EEA82D5-A8B1-4435-AD96-04A359AEE0B8

Q27650298-10F3CB8D-F238-432D-BD61-EB9E263AF4E6

Q27650298-17CAB3CE-C365-49C1-808D-74455DEEFA2C

Q27650298-1C42CB82-C30B-4B29-9663-93C7D5778019

Q27650298-1F2E89AE-5A42-4D03-9173-6C2649149465

Q27650298-2A847AC6-5C4D-4927-B3FE-A1FF8725115C

Q27650298-2ABD0B2E-6516-4115-B056-C4CD0271764F

P304

Q27650298-DA524958-64F7-42AE-9ABC-44381A7DC4B0

P31

Q27650298-25B6C45C-EC6F-4966-939B-456D1C2A1D6E

P356

Q27650298-3D69AB07-B1E3-4151-BB25-18E52A015ACA

P407

Q27650298-38330A71-C154-4C8F-B1C4-89FD9EF04747

P433

Q27650298-E3C062CD-53F5-4804-B123-424384D6568C

P478

Q27650298-57953E13-576C-4EFA-A315-28C8627EBC69

P50

Q27650298-BD70C745-0F3D-4A0A-ACC7-D6B3BA5F21C6

P577

Q27650298-8194F32B-0102-4455-9E5E-AFB0BBA1A76C

P698

Q27650298-E01B3603-DF26-467D-B3A4-BF385C89F18C

P921

Q27650298-5020B35F-A050-4CEB-A8E1-F1101454C564

Q27650298-E20D726B-1B0F-4AE0-B520-FBF434FCEB97

Q27650298-FC638775-583E-464B-888E-9C51D42538CF

P932

Q27650298-9359B60A-4FFF-4C39-B336-A45653996392

P356

P1433

Journal of Biological Chemistry

P1476

Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation

@en

P2093

Chung Wang

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

Chwan-Deng Hsiao

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

Yuh-Ju Sun

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

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the C-terminal 10-kDa subdomain of Hsc70

Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Structural analysis of substrate binding by the molecular chaperone DnaK

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

P304

15502-15511

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

P31

scholarly article

P356

10.1074/JBC.M708992200

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

P407

P433

22

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

P478

283

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

P50

P577

2008-04-08T00:00:00Z

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

P698

18400763

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

P921

crystal structure

P932

3258884

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