Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. - Wikidata - wikimedia - TriplyDB

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

http://www.wikidata.org/entity/Q34488383

about

Molecular chaperones: guardians of the proteome in normal and disease states Metazoan Hsp70-based protein disaggregases: emergence and mechanisms How Polyomaviruses Exploit the ERAD Machinery to Cause Infection The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.The stress protein heat shock cognate 70 (Hsc70) inhibits the Transient Receptor Potential Vanilloid type 1 (TRPV1) channel A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Human cyclophilin 40 unravels neurotoxic amyloids.Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils.Hallmarks of therapeutic management of the cystic fibrosis functional landscape.Chaperone-Assisted Protein Folding Is Critical for Yellow Fever Virus NS3/4A Cleavage and Replication.Engineering therapeutic protein disaggregases.Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110 Heat Shock Proteins Promote Cancer: It's a Protection Racket Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome.ArHsp40, a type 1 J-domain protein, is developmentally regulated and stress inducible in post-diapause Artemia franciscana.Hyperthermia enhances 17-DMAG efficacy in hepatocellular carcinoma cells with aggravated DNA damage and impaired G2/M transition Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Progranulin Recruits HSP70 to β-Glucocerebrosidase and Is Therapeutic Against Gaucher Disease.Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Prions and Protein Assemblies that Convey Biological Information in Health and Disease.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer.Chaperone-Driven Degradation of a Misfolded Proinsulin Mutant in Parallel With Restoration of Wild-Type Insulin Secretion.ɑ-Synuclein strains and the variable pathologies of synucleinopathies.Possible Function of Molecular Chaperones in Diseases Caused by Propagating Amyloid Aggregates.Induction of heat shock proteins in differentiated human neuronal cells following co-application of celastrol and arimoclomol.DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins.Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Interplay between redox and protein homeostasis.How Do J-Proteins Get Hsp70 to Do So Many Different Things?Role of sHsps in organizing cytosolic protein aggregation and disaggregation.Designer protein disaggregases to counter neurodegenerative disease.Protein-Remodeling Factors As Potential Therapeutics for Neurodegenerative Disease.Shaping proteostasis at the cellular, tissue, and organismal level.Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis

P2860

Q26766168-4BE6A3E0-10C6-4B9D-9547-2213C34F4978 Q26779046-790315B3-19AE-49B8-845E-F7279E3A23A5 Q27468807-F796B2B2-0B7F-46D1-A25F-5EC1D934BBA4 Q27936206-D7535C40-7764-40A1-B71B-235B28ECB372 Q28828381-DBE7F566-9943-4495-844F-834915D53F38 Q30402024-97C14A0F-3ECB-496A-AD52-4E89B5FFCB95 Q33715895-46A24319-54D7-4D51-B309-06929DF6E38A Q33842022-9ADE8A4B-C7AC-4C5D-A01B-C32C184DA65B Q35753373-F8C99958-556D-4B5A-B291-5EBDCD4F06A8 Q36279553-17F549EF-9318-46AC-B6B1-C2B247A92430 Q36736579-343A42DC-4802-46A2-B05E-BB58BDEE777A Q36896295-E693A4B0-5457-40FA-89D4-7E6A24CCBDCE Q36905019-F4CC10C0-03C4-464E-A7AA-C451566C1745 Q37013952-CD475B58-128B-4C6D-83EE-5617717C1975 Q37079732-88998629-FF28-4003-AF12-59649F510472 Q37214887-47A80BC7-51E4-428A-94F0-A46D613E8D59 Q37372970-BCED261B-517B-4C20-B412-245A7E317561 Q37464190-95073B9F-B161-42FF-81FD-5DDAE3AB5229 Q37493185-5470D492-B169-4F15-B1E9-1C6378C1B2B4 Q37604580-53312D7E-F601-4323-9F93-0DC8DD15FD7A Q37719263-0E35C8F3-A0E5-46E8-B03E-D3D7192BDAA1 Q37739093-A60D4818-240B-4349-83BF-F349B01F6A02 Q38336025-56C2F217-767D-4949-9B93-DB56524EAE2F Q38648239-2F2715B8-B118-4B13-8F97-513950FA9F20 Q38698836-E996653E-C0D3-4E89-BF03-47E1CCA36359 Q38724059-A37C8255-6851-4A45-8DDC-FB6EA00E7FE5 Q38753941-F3A5317B-E9AF-4F70-B272-5CFBA206B4B0 Q38755364-425B08B2-20A7-4466-8CB4-218F671AEEE0 Q38765994-EA98B837-A538-4567-997B-C414B52F10E0 Q38766640-4CFCC13B-1BBE-4F53-B1D4-E8A49A575097 Q38818474-5074DE64-FE66-4ED1-8ADA-31D1E79DF926 Q38888594-6FB5B9C0-CD4F-4D18-9C91-3A2FD97010F6 Q38897201-556A5E1B-E063-48A9-AC5C-3D1AC941BF94 Q39102253-7F3BEB09-B30B-4173-9178-D84C17496362 Q39139060-8CDCBD40-2752-4F58-9E5C-169B4BDB8F77 Q39178504-23A3FE3C-E548-4A38-919E-4CE563DCD879 Q39235911-4DB30389-13C6-4A59-B1AD-F703AB345038 Q39251180-03EE21C8-0DE0-47AC-AC6F-6C475B736543 Q39349922-794077DD-FD65-4964-B576-FD8E7A0770E5 Q39430414-1250BD19-54AC-4C7A-ACE0-D8A09D52F0D6

P2860

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

http://www.wikidata.org/entity/Q34488383

description

2015 nî lūn-bûn

@nan

2015 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@ast

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@en

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@nl

type

label

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@ast

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@en

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@nl

prefLabel

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@ast

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@en

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@nl

P1433

Q34488383-C0E247A7-EB13-46B3-AF81-E6490286ABF0

P1476

Q34488383-ADE0F3B1-F576-41AC-9903-CAAB8B36970D

P2093

Q34488383-433E1BE4-A642-4BF4-A864-760683751C33

Q34488383-6CFF4779-1D95-4921-9214-C7612683822B

Q34488383-8AEA323F-DDA2-4D5E-B45D-169FEE8E2FC9

Q34488383-A015EDAE-2E7A-4A0A-9FB6-C808001C626D

Q34488383-D3FD2389-70BB-4004-8595-8E74309BC531

Q34488383-E67B00A9-0811-4189-BED3-23B8B4A9F551

Q34488383-E6B3C937-03EF-45CD-B253-5F2ED8A89E25

Q34488383-FE189D45-1BE1-4CD4-A986-7348B148A212

P2860

Q34488383-02115782-99F5-43CF-BA87-E1B9C214087A

Q34488383-03FEC968-2193-4E06-B997-B96FA1CFA919

Q34488383-047A3AD4-28A0-4D48-BD3C-DC1DFE98F489

Q34488383-07B05E6B-23FC-462C-BA00-40DCD97F770C

Q34488383-0E7E8535-C131-460F-89A4-4F8B6DDE8D7B

Q34488383-141FF6DA-FAF0-4835-A0DA-E92A68DB988D

Q34488383-17F1E9D4-7208-47D6-9209-0940E693519C

Q34488383-210449FB-2B8B-407B-85B2-51E96C5ECB3F

Q34488383-264FBF47-10D3-4EFC-98C1-031345BE6061

Q34488383-276A8690-19F9-49D7-A827-E7CC568C6593

P2888

Q34488383-23F8EF20-EEC6-4530-9CEC-288C3BF97116

P304

Q34488383-CF8E9F09-F65E-412F-8DA2-5AA50476D0EB

P31

Q34488383-F4132257-D8B3-4AAE-A0E7-31F5632B1108

P356

Q34488383-B824126D-51A2-4635-BC99-A7090C8D1BD8

P407

Q34488383-CFF04CCE-87D3-4292-8C89-DD3F25EBF057

P433

Q34488383-144B5D9B-B791-427E-AA3E-C9BDBC400AB3

P478

Q34488383-7A20B362-1CEF-4C05-923D-3699ECF7656C

P50

Q34488383-049BD3DC-7D98-462F-91D7-CFBD008FDA78

Q34488383-0E67D225-DE82-4D87-9EAF-F36260C07DBF

Q34488383-54DAF244-749D-489C-A9C2-E28E5608AB6E

Q34488383-79B53639-E5F3-47FB-9F00-741A34C0B42E

Q34488383-997DAEDA-5BF2-4F33-91EA-D1FFA3D0F95A

Q34488383-9A8AE97B-9A2D-4772-B04B-B4FECEDFAF25

Q34488383-A9BA1DB2-347A-4533-957A-42EC8D218284

P577

Q34488383-57A84960-DADB-48A4-8F4F-B0BD4FECD233

P5875

Q34488383-4BD42CD8-3789-4835-A6B1-3B60A73BF0C3

P698

Q34488383-D914654E-B5F4-4C5A-A2DC-0E6F69F3C246

P921

Q34488383-8FEA6B9E-323C-43F2-A979-F1D8FA4615AC

P932

Q34488383-21BB5325-18B0-4023-A394-6559D872420D

P356

P1433

P1476

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

@en

P2093

Anna Szlachcic

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

Annika Scior

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

Antonia Stank

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

D Lys Guilbride

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

Kristin Arnsburg

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

Mykhaylo Berynskyy

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

Richard I Morimoto

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

Xuechao Gao

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

P2860

The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models

Hsp70 chaperones: cellular functions and molecular mechanism

The SWISS-MODEL Repository and associated resources

The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate

Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70

Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ

Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

WHAT IF: a molecular modeling and drug design program

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

P2888

P304

247-251

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

P31

scholarly article

P356

10.1038/NATURE14884

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

P407

P433

7564

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

P478

524

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

P50

Matthias P. Mayer

Janine Kirstein

Florian Stengel

Nadinath B Nillegoda

Ruedi Aebersold

P577

2015-08-05T00:00:00Z

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

P5875

280723126

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

P698

26245380

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

P921

molecular chaperones

P932

4830470

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