Molecular chaperone targeting and regulation by BAG family proteins - sprookjes - yvandenbroek - TriplyDB

Molecular chaperone targeting and regulation by BAG family proteins

Molecular chaperone targeting and regulation by BAG family proteins

http://www.wikidata.org/entity/Q28190053

about

Comparative analysis of apoptosis and inflammation genes of mice and humans Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3 Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain Tid1, a cochaperone of the heat shock 70 protein and the mammalian counterpart of the Drosophila tumor suppressor l(2)tid, is critical for early embryonic development and cell survival Hsp70 chaperones: cellular functions and molecular mechanism The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor Activities of the cochaperones Hap46/BAG-1M and Hap50/BAG-1L and isoforms Chemical communication threatened by endocrine-disrupting chemicals The nucleotide exchange factors of Hsp70 molecular chaperones BAG4/SODD protein contains a short BAG domain Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2 Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.BAG3: a new player in the heart failure paradigm BAG3 protein controls B-chronic lymphocytic leukaemia cell apoptosis Regulation by heavy metals and temperature of the human BAG-3 gene, a modulator of Hsp70 activity CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase Ricin triggers apoptotic morphological changes through caspase-3 cleavage of BAT3 Regulation of the cytoplasmic quality control protein degradation pathway by BAG2 BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress Myofibrillar myopathies A novel, non-apoptotic role for Scythe/BAT3: a functional switch between the pro- and anti-proliferative roles of p21 during the cell cycle A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein BAG-6 is essential for selective elimination of defective proteasomal substrates CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis Bag1 is essential for differentiation and survival of hematopoietic and neuronal cells.BAG3 deficiency results in fulminant myopathy and early lethality The reaper-binding protein scythe modulates apoptosis and proliferation during mammalian development Regulation of osteoblast development by Bcl-2-associated athanogene-1 (BAG-1)Influence of common genetic variation on lung cancer risk: meta-analysis of 14 900 cases and 29 485 controls The HSP70 chaperone machinery: J proteins as drivers of functional specificity Pathways of chaperone-mediated protein folding in the cytosol Hsp70-Bag3 interactions regulate cancer-related signaling networks HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Thioflavin S (NSC71948) interferes with Bcl-2-associated athanogene (BAG-1)-mediated protein-protein interactions.

P2860

Q24306056-EBE70645-D06E-4A2A-B07E-8643AF73EF70 Q24312452-99BB0C12-1E23-48F3-8873-07911D2DFCD9 Q24312870-38B07692-589F-4CB2-9FE3-5EF88A9CA979 Q24321127-11587EF8-BCF6-46E2-8E45-BB91B5F2E6FD Q24321761-6381ECAD-E0E8-453B-AB62-AA2842D7A19B Q24537245-84ACE46F-9667-411F-83BF-839997BA53D0 Q24629776-F9673964-CDD7-4F58-B346-D13BC06328DC Q24644472-DEEB70CB-5663-45EB-98B0-9A849931CD29 Q24652993-78238AE0-7EF6-4687-9582-2F1647B06AF1 Q24680043-79B84FC6-D053-44AC-9F57-E061A6EE895A Q24812060-72729E1A-FDA9-424D-AB2D-12AA783A1941 Q26766367-C482B062-F426-45E3-AB5E-4797AE2A718D Q27639158-AF4513B1-9F66-4103-988A-6E7D09585447 Q27652982-D686C73D-154D-4440-81F0-FB4B2203D325 Q27931293-807923AD-A237-4FA0-A5C4-F145B2D98BAC Q27931383-F9450276-AAA3-4C09-83AC-862ABE2CFEE0 Q28088321-4C2209D2-D084-496C-A1E4-A77D69B706DB Q28191626-F90DE70B-8171-454B-9BD0-5AC2C839DDBF Q28198421-5284A744-92E5-4DE1-A74E-E10DBCEB677A Q28204432-42C573FE-7B7A-4470-A785-0BE30DFDA36E Q28213524-1F1F2680-7334-4602-8CD2-927F5DBA0422 Q28242315-2D3BF84B-5DF9-4604-A170-61B54AD458C8 Q28244908-ADEE83DB-0359-442A-93B7-AD7DEBE7B133 Q28272894-AF934398-D6F0-4579-AFF3-093B9834C00D Q28294601-AFFE076F-FF9F-4E4E-9E0C-9B443023BC02 Q28303812-740581DF-B36F-47E9-826B-6FE3C617222B Q28385780-D1771843-37A9-44BC-9414-D66A2BDC267F Q28504634-9211B31C-274E-4369-931F-398238E4D893 Q28505838-6FBED265-BEB8-40F4-B100-F2F3F1FB0BEB Q28508530-7EA8A942-DF9E-4C65-9AA5-2FEF4C2EED47 Q28585194-5D608C93-A7C7-4E33-B2DC-CA18A17205FF Q28585764-A9BE75C6-B954-4BC1-9D34-CA11A4174702 Q28586611-43CBFFE5-B0F4-47EA-ABC0-2347E58D3500 Q28830055-394FC3EA-D320-4787-B0EE-69BB88EBD904 Q29417049-3B16A1D9-31B0-4163-B7FD-EBD366FB74DC Q29616140-5FC0FD4B-1036-466D-8839-CC51D1B48054 Q29618887-D2B2AA49-2ACE-4AAF-BACF-A2F193507D79 Q30009385-39C8788E-7B72-4E39-BB59-AE8E3908E49B Q30354473-F814C2B0-DF0A-47BF-9D05-96932C6F836B Q33494790-F22DC839-8060-4A07-AC56-F2833A416E64

P2860

Molecular chaperone targeting and regulation by BAG family proteins

http://www.wikidata.org/entity/Q28190053

description

2001 nî lūn-bûn

@nan

2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Molecular chaperone targeting and regulation by BAG family proteins

@ast

Molecular chaperone targeting and regulation by BAG family proteins

@en

Molecular chaperone targeting and regulation by BAG family proteins

@nl

type

label

Molecular chaperone targeting and regulation by BAG family proteins

@ast

Molecular chaperone targeting and regulation by BAG family proteins

@en

Molecular chaperone targeting and regulation by BAG family proteins

@nl

prefLabel

Molecular chaperone targeting and regulation by BAG family proteins

@ast

Molecular chaperone targeting and regulation by BAG family proteins

@en

Molecular chaperone targeting and regulation by BAG family proteins

@nl

P1433

Q28190053-39C14E6C-F744-4906-94C9-2889571D2802

P1476

Q28190053-3AB9C992-D13E-4D63-9EB6-ABCD87EAC815

P2093

Q28190053-091BDCE7-8224-4554-805D-AC5D1352309F

Q28190053-7EE0DE1D-610D-4A1B-947E-38EDB231D2C9

P2860

Q28190053-029B2CDF-8D4E-4EC5-BBFC-D3AD34073E38

Q28190053-02D30828-6790-4073-BD79-0F6F0D3CCC04

Q28190053-04781C6F-04D4-4DF5-AA65-F6BE9426F8C6

Q28190053-08F605E0-C44A-47FF-BB4A-B5D0CB0BFE43

Q28190053-134783C4-8498-4191-AE72-6D9EA01CB43E

Q28190053-14793C06-8F12-4209-A055-9D14300C0464

Q28190053-150E89DB-0606-49C6-A490-A72137ED9206

Q28190053-1600FDE1-0583-4901-A7A9-46D8228276EC

Q28190053-18357799-6B72-406F-9C42-ECC1BFD2FB74

Q28190053-1886893C-9B3F-4544-84BF-D4D5D63A5D1A

P2888

Q28190053-33B2FE73-0802-449C-8B3A-90DB0C93CAFE

P304

Q28190053-F86E4AB7-D2BE-4793-827B-A8D261828E70

P31

Q28190053-C0A369F5-378C-47B3-AE7D-8E42B2285D0F

P3181

Q28190053-6A27B49E-3791-4AD1-BEF7-24A8FBEAB61B

P356

Q28190053-9600EB32-9B1E-4703-950E-730579055A9C

P407

Q28190053-1847C266-0085-4F07-A5FF-EF880114F360

P433

Q28190053-9EF5ADF9-40DF-4A94-9ABC-78488F332A5B

P478

Q28190053-44A1C820-175C-4206-958F-40896BEE663A

P577

Q28190053-28CDF361-A9FB-42CC-A495-DC2F1FBA51A8

P6179

Q28190053-72BC97CE-2486-4B55-9ED3-3B76AEB2DB24

P698

Q28190053-2D629A2D-05AA-44A5-AD2B-5D589F59C677

P921

Q28190053-43670698-BEB8-44E9-857C-10974D91B2ED

P3181

P356

P1433

Nature Cell Biology

P1476

Molecular chaperone targeting and regulation by BAG family proteins

@en

P2093

J C Reed

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

S Takayama

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

P2860

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

Prevention of constitutive TNF receptor 1 signaling by silencer of death domains

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death

BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation

p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1.

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper

A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning

P2888

P304

E237-41

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

P31

scholarly article

P3181

2717906

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

P356

10.1038/NCB1001-E237

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

P407

P433

10

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

P478

3

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

P577

2001-10-01T00:00:00Z

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

P6179

1005299981

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

P698

11584289

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

P921

molecular chaperones