ErbB2 degradation mediated by the co-chaperone protein CHIP - Test2 - elhamkhani - TriplyDB

ErbB2 degradation mediated by the co-chaperone protein CHIP

ErbB2 degradation mediated by the co-chaperone protein CHIP

http://www.wikidata.org/entity/Q28208008

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Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation CHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates Regulation of death-associated protein kinase. Stabilization by HSP90 heterocomplexes Quality control and fate determination of Hsp90 client proteins RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Protein homeostasis at the plasma membrane A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival Defining the role for XAP2 in stabilization of the dioxin receptor The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradation Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis Marked enhancement of lysosomal targeting and efficacy of ErbB2-targeted drug delivery by HSP90 inhibition Regulation of the Src family kinase Lck by Hsp90 and ubiquitination Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells.Endocytic down-regulation of ErbB2 is stimulated by cleavage of its C-terminus.The HSP90 inhibitor geldanamycin perturbs endosomal structure and drives recycling ErbB2 and transferrin to modified MVBs/lysosomal compartments The UPS: a promising target for breast cancer treatment.Regulation of ErbB2 receptor status by the proteasomal DUB POH1.CHIP is a novel tumor suppressor in pancreatic cancer through targeting EGFR Expression of t-DARPP mediates trastuzumab resistance in breast cancer cells.ErbB2 trafficking and degradation associated with K48 and K63 polyubiquitination.Ubiquitinylation of α-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5).Engineered ubiquitin ligase PTB-U-box targets insulin/insulin-like growth factor receptor for degradation and coordinately inhibits cancer malignancy miR-764-5p promotes osteoblast differentiation through inhibition of CHIP/STUB1 expression.E3 ubiquitin ligases in ErbB receptor quantity control.Prognostic implications of carboxyl-terminus of Hsc70 interacting protein and lysyl-oxidase expression in human breast cancer.Role of Erbin in ErbB2-dependent breast tumor growth.Quality control for unfolded proteins at the plasma membrane.Geldanamycin selectively targets the nascent form of ERBB3 for degradation A kinase inhibitor screen reveals protein kinase C-dependent endocytic recycling of ErbB2 in breast cancer cells.A heat-shock protein axis regulates VEGFR2 proteolysis, blood vessel development and repair.Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.Anticancer activity of Celastrol in combination with ErbB2-targeted therapeutics for treatment of ErbB2-overexpressing breast cancers.Regulation of FSP27 protein stability by AMPK and HSC70.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseases Mechanisms of Trastuzumab resistance in ErbB2-driven breast cancer and newer opportunities to overcome therapy resistance.

P2860

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P2860

ErbB2 degradation mediated by the co-chaperone protein CHIP

http://www.wikidata.org/entity/Q28208008

description

2003 nî lūn-bûn

@nan

2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

ErbB2 degradation mediated by the co-chaperone protein CHIP

@ast

ErbB2 degradation mediated by the co-chaperone protein CHIP

@en

ErbB2 degradation mediated by the co-chaperone protein CHIP

@nl

type

label

ErbB2 degradation mediated by the co-chaperone protein CHIP

@ast

ErbB2 degradation mediated by the co-chaperone protein CHIP

@en

ErbB2 degradation mediated by the co-chaperone protein CHIP

@nl

prefLabel

ErbB2 degradation mediated by the co-chaperone protein CHIP

@ast

ErbB2 degradation mediated by the co-chaperone protein CHIP

@en

ErbB2 degradation mediated by the co-chaperone protein CHIP

@nl

P1433

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P1476

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P2860

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P356

P1433

Journal of Biological Chemistry

P1476

ErbB2 degradation mediated by the co-chaperone protein CHIP

@en

P2093

Alagarsamy Lakku Reddi

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

David E Wazer

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

Hamid Band

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

Howard Safran

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

Ingrid L Dodge

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

Navin Rao

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

Norvin Fernandes

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

Pengcheng Zhou

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

Thomas A DiPetrillo

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

P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

U box proteins as a new family of ubiquitin-protein ligases

Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product

Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90

Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells

The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation.

P304

13829-37

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

P31

scholarly article

P3181

611399

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

P356

10.1074/JBC.M209640200

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

P407

P433

16

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

P478

278

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

P50

P577

2003-04-18T00:00:00Z

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

P698

12574167

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

P921

molecular chaperones