PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.
about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsIntracellular Dynamics of the Ubiquitin-Proteasome-SystemNuclear Import of Yeast ProteasomesDNAJs: more than substrate delivery to HSPAThe many faces of autophagy dysfunction in Huntington's disease: from mechanism to therapySorting out the trash: the spatial nature of eukaryotic protein quality controlAutophagy in polyglutamine disease: Imposing order on disorder or contributing to the chaos?Protein quality control in the nucleusPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportThe protein quality control machinery regulates its misassembled proteasome subunitsModulation of the maladaptive stress response to manage diseases of protein foldingPrefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress.DNAJB6 Myopathies: Focused Review on an Emerging and Expanding Group of MyopathiesRole of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative DiseasesA chaperome subnetwork safeguards proteostasis in aging and neurodegenerative diseaseArtificial targeting of misfolded cytosolic proteins to endoplasmic reticulum as a mechanism for clearance.Ethosuximide ameliorates neurodegenerative disease phenotypes by modulating DAF-16/FOXO target gene expressionProtein misfolding specifies recruitment to cytoplasmic inclusion bodiesThe BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins.Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thalianaCharacterizing the altered cellular proteome induced by the stress-independent activation of heat shock factor 1.Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Elevation of proteasomal substrate levels sensitizes cells to apoptosis induced by inhibition of proteasomal deubiquitinases.Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.How the nucleus copes with proteotoxic stress.Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition.The biology of proteostasis in aging and disease.Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Protein aggregation as a mechanism of adaptive cellular responses.Defining the limits: Protein aggregation and toxicity in vivoSpatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.Roles of intramolecular and intermolecular interactions in functional regulation of the Hsp70 J-protein co-chaperone Sis1.Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.
P2860
Q26779046-21B9A048-423D-4F6A-A72B-B6B6EC3DD450Q26784629-3660A5AB-F96D-4974-804F-CC4843585913Q26799309-0B48DCD4-CA6C-4053-B786-DF1422A947F9Q26801509-4F4F12FC-CD38-4731-8E7C-08FACC2D7E69Q26823365-415EC4D2-7DD9-46CF-9AEE-240EA7BACF47Q26849685-4A219A4A-AA32-47DC-A7E8-E5BD1B0F6636Q27011387-A679A4C3-1EFD-4625-A4BC-01E3F7EB1E5CQ27023202-EBFC68EF-F99A-4BE8-B81F-8608FD752419Q27307839-1F364D54-9F1F-43AE-A5F3-D6F4AA1946B9Q27311236-6E40398C-0C40-43DD-B4EA-C020DA196EABQ27313626-CAF45E5C-1703-4DF5-B802-60AC1CAF9BD8Q27933637-3083DBEA-68F8-4F82-AC63-92E27D984372Q27936206-31AA5DDF-2718-47AE-A4C3-E0B598E3A1EBQ27937702-D0FBBE85-AFBE-4F19-9282-4EB19B5C1E1EQ28071332-6D6BCAED-193E-4AC2-9802-975129B06B6BQ28082714-6F131366-D6EB-4253-A6BB-4C2E89A9C689Q28252463-5DA44565-E670-46E5-9235-BA7F233CE503Q30657635-E7393A36-7E8F-475B-9C35-28CDC8966B1BQ30666205-44631D50-365E-48E3-8B03-B475CFA135ABQ30826780-6A11BE67-362F-46AF-A60A-781D0CB7C71AQ33556224-658C4924-16EB-4BA1-98EC-F91020EA2538Q33609884-697CFA24-7FAF-4CE2-A0FC-82BB6A53D5B1Q33614771-DF929A15-66E2-4873-8525-30A6B5945A5BQ33769272-A319FEB5-F45F-46CB-A461-1C72BDEBFCBDQ33807686-9BB89881-5252-4070-B32B-603A4CAF1446Q33824789-F893C532-3763-47CB-AEE9-8D11C8230930Q34082859-BEAD3104-55FA-46CC-BE71-54EDA09C4119Q34115717-6A91206A-210C-4443-9696-CD2C8A7A1F66Q34294233-38480CFE-D3FD-4175-9286-153692B6A490Q34388290-5807090A-4F12-4C21-A2D2-3F14FA14A138Q34391566-4E1E8EB8-5F58-473A-BE41-DB97F844D366Q34413909-FAEB6A91-53E0-4025-A528-9A105D6850C7Q34467650-E3A6B62D-BAA5-467A-B078-EA34582DE324Q34519909-7374BCD6-6F82-4733-99CA-94D6AA1A0388Q34520461-C822E5E3-F782-4336-981F-73FB04378A0BQ34549351-21CD5144-D7FF-4953-B34B-C61CB219E367Q34729587-FD1427E8-6442-4DC0-AB57-1729148F1C9DQ34793446-5C94C43F-3F8E-47B7-8D43-A37FDEEDAE7DQ35171087-A17D6811-9C80-4D6C-8883-BC7B6BAADE5FQ35205006-906B6BB1-5562-42F9-901A-4CE64D794537
P2860
PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@ast
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@en
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@nl
type
label
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@ast
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@en
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@nl
prefLabel
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@ast
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@en
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@nl
P2093
P50
P3181
P1433
P1476
PolyQ proteins interfere with ...... uestering the Sis1p chaperone.
@en
P2093
Ayano Konagai
Rajat Gupta
Sae-Hun Park
Taotao Chen
Yury Kukushkin
P304
P3181
P356
10.1016/J.CELL.2013.06.003
P407
P577
2013-07-03T00:00:00Z