ErbB2 degradation mediated by the co-chaperone protein CHIP
about
sameAs
Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradationCHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradationEndoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligaseCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesRegulation of death-associated protein kinase. Stabilization by HSP90 heterocomplexesQuality control and fate determination of Hsp90 client proteinsRINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesisTargeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseasesProtein homeostasis at the plasma membraneA 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 survivalDefining the role for XAP2 in stabilization of the dioxin receptorThe E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradationHeat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytesFunctional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesisMarked enhancement of lysosomal targeting and efficacy of ErbB2-targeted drug delivery by HSP90 inhibitionRegulation of the Src family kinase Lck by Hsp90 and ubiquitinationClathrin-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 compartmentsThe 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 EGFRExpression 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 malignancymiR-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 degradationA 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 diseasesMechanisms of Trastuzumab resistance in ErbB2-driven breast cancer and newer opportunities to overcome therapy resistance.
P2860
Q24297095-3E4697BB-FF9A-4D50-B356-D17DDAC496CBQ24298589-715BC319-CA97-4976-9F7E-ADCA7CA7A3F6Q24320293-68E7DDB0-AFFF-4FBA-A918-63D0A51BA416Q24338386-5D3589BD-6C83-4533-8DCA-BDC23F2532E3Q24646541-167DF2E7-384C-426E-9D5B-C3F2381D5EE5Q26853052-19759166-8130-4701-9AA9-52578D2F9A3FQ26853207-3BBD0876-383E-4CDC-B26B-440B66EE0DE8Q26859909-AC897D77-46B0-4DEA-928A-81F693111C79Q27009009-9E6382FE-843E-489C-A54C-05851C1342E2Q28078724-F693450B-4133-43FC-8389-37C9EE5E32F4Q28183470-05D684CB-993B-487A-B77A-651A70F46954Q28184153-DD7A4540-C209-47CD-A662-1BB33D423483Q28511737-7ACA116E-4DDF-4318-B418-0395F0AA1792Q28572341-BF46DDD3-DEE6-482F-ABAD-D82A574AC7DFQ28593080-21FEF2AE-7A6B-468C-B3D4-05816596DC23Q28829301-3E776E14-794E-443C-BD3F-113072B0F9F5Q30164012-06A7FE73-C45F-4D31-8FC2-B941EB5F6674Q30439237-A4E2AC9E-B02C-4DAC-A9B4-92EBEF0C0376Q30479942-2CF42B49-FC5E-4C20-91E9-56A97BE54875Q31107044-4FDEA567-041A-4966-B0AC-C243813D4AD8Q33384289-C7B85EE3-7C8D-420C-8124-DE5510827E4EQ33444766-B47AF1F6-BD00-473B-BA15-84AD5718A7E4Q33688445-50FE6126-F230-488F-BACB-ADD12A18878BQ33743601-B5164206-CA79-48AE-9B37-9A7654955BE2Q33820676-956A2541-086D-4BBC-8DD7-A64F350F9360Q33831775-01F71CD2-F7B2-42CA-8E5D-147B1C9F2E0EQ34104101-352B0AFA-FB9E-4326-B07D-7EE874C96372Q34260429-265DBFA4-330F-431A-B68D-B9EB16B0F91EQ34349106-577D4528-BD0C-45E6-AF66-1CB7E2CE4D1BQ34380963-45AB2205-09A7-4E44-9CC2-396D17843C36Q34408829-AA26BB40-D650-4FF4-8E87-007E62D43812Q34412404-93FD6A8C-71B0-43D7-8844-C0AB7528D407Q34427505-0E3B03F4-EE49-468C-820A-19D95910DB59Q34430965-4E4ECA03-4233-476B-BECC-5F2FE043A444Q34472013-4862CD31-1475-4268-B730-3B10D5E825BAQ34611621-B11F087F-FDA0-410E-98AC-148A16391842Q34616517-D7682DC3-ED86-4149-BCA6-93AF120EE99DQ34627681-6F67D365-0250-41EB-B935-CA63DE8D46B9Q35053633-9E06D8C0-EC2B-4B98-8F07-8FF1CD4AF7D0Q35624814-F3798128-2829-46FE-A845-F7E232C6B3DF
P2860
ErbB2 degradation mediated by the co-chaperone protein CHIP
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
P2093
P2860
P3181
P356
P1476
ErbB2 degradation mediated by the co-chaperone protein CHIP
@en
P2093
Alagarsamy Lakku Reddi
David E Wazer
Hamid Band
Howard Safran
Ingrid L Dodge
Norvin Fernandes
Pengcheng Zhou
Thomas A DiPetrillo
P2860
P304
P3181
P356
10.1074/JBC.M209640200
P407
P50
P577
2003-04-18T00:00:00Z