Misfolded proteins partition between two distinct quality control compartments - Test2 - elhamkhani - TriplyDB

Misfolded proteins partition between two distinct quality control compartments

Misfolded proteins partition between two distinct quality control compartments

http://www.wikidata.org/entity/Q24651093

about

Localization of protein aggregation in Escherichia coli is governed by diffusion and nucleoid macromolecular crowding effect Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3 Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae Glycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics)Spatial protein quality control and the evolution of lineage-specific ageing Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast Intracellular Dynamics of the Ubiquitin-Proteasome-System Sup35 methionine oxidation is a trigger for de novo [PSI(+)] prion formation Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes Nuclear Import of Yeast Proteasomes Protein Folding and Mechanisms of Proteostasis Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Sorting out the trash: the spatial nature of eukaryotic protein quality control Particle-rich cytoplasmic structure (PaCS): identification, natural history, role in cell biology and pathology Role of asymmetric cell division in lifespan control in Saccharomyces cerevisiae Yeast prions: structure, biology, and prion-handling systems Hijacked then lost in translation: the plight of the recombinant host cell in membrane protein structural biology projects INS-gene mutations: from genetics and beta cell biology to clinical disease Therapeutic Approaches for Inhibition of Protein Aggregation in Huntington's Disease The Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality Control Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport Recruitment of the oncoprotein v-ErbA to aggresomes.The protein quality control machinery regulates its misassembled proteasome subunits An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates Fusion of protein aggregates facilitates asymmetric damage segregation A method to rapidly create protein aggregates in living cells.Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease Rapid flow cytometric measurement of protein inclusions and nuclear trafficking.Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi Widespread protein aggregation as an inherent part of aging in C. elegans Structure of Minimal Tetratricopeptide Repeat Domain Protein Tah1 Reveals Mechanism of Its Interaction with Pih1 and Hsp90 Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis.

P2860

Q21563476-26EDA708-4193-4D4B-9899-4B205D4931D6 Q24312870-C6AC2478-1C3A-4C8B-8F71-91A2E2303B11 Q24564356-B6DEFC9F-AB74-4241-B2C8-44543B358036 Q24610346-3F1AB42F-3B72-400C-9ACC-1AF463001558 Q24610496-BB389A85-93F5-4878-9533-79139918B471 Q24629545-E546D28E-91EB-425D-BC56-BD11724A84FE Q24631476-CA0D88BD-7496-4E56-A825-12127D089420 Q24650675-66027EA6-10F2-40B5-AFEA-5313A6B47E26 Q24655821-2CCC65F2-0F67-412C-BED4-4D32A941FCE2 Q26778771-9CC48A31-BA67-41D9-9529-5774C93D6EA4 Q26784629-5E57338E-B46E-4DB5-9A17-381F17D6D647 Q26798417-A513F203-AE7B-467A-842D-47CAE48AF0A1 Q26799208-7832F23A-234F-400A-8C32-6F37457944F1 Q26799309-D8A476B8-71B6-416D-BC54-5A149E8C5204 Q26801512-A5943982-0303-4201-B78D-34E3D2F766C9 Q26824733-E1BF3AF4-B6A2-402B-A053-D23EC6D00774 Q26849685-1DA1CF9A-8F4E-4370-9CE9-F89EAACEF483 Q26998855-18EEC8FC-467A-48D2-9B8A-DDD4576968C7 Q27006778-D3B98BBE-D7F1-44B8-98D5-D07B4280C26B Q27007482-F9F6F743-FD93-4AB8-9452-BE35037D0F2C Q27008341-B57127FF-2470-40D8-BF27-521C61DC90EE Q27013618-1B6B171C-876D-4F79-98CA-75A0F39882D0 Q27022757-F05CCAED-40DE-4E16-91F6-7803A42AB910 Q27027216-2517ED30-6D8E-46DF-B16E-830C292687FB Q27307839-2F171D11-A42B-425B-84D6-7FC79671FE27 Q27308854-C38AEB23-41A9-4992-AF01-ABDFACC4902C Q27311236-69575A2D-2BAB-4C4F-BCF9-C20C53946ACF Q27313222-023F3A4C-1D1D-4D2B-9FC6-B1B3B3791903 Q27314554-024633E8-E877-42B1-9729-87592B7FE792 Q27314757-81028AC7-414F-4AC2-B873-4B209223F2DD Q27315894-ACE8E8FD-527C-4D94-8911-F77731CCE781 Q27316174-59223A60-A8EE-42DB-9D56-53654ACB7ACF Q27319135-947059C1-7D1B-400B-BA67-EDB78DB516BD Q27320799-E5EC277C-B9DE-40EF-83CF-F58E7DF58845 Q27323997-600B7BC1-7738-4D66-BAE3-D7A39A460173 Q27676285-F88C8AEF-86E1-4203-BDAD-95080276071D Q27929853-31CA3EFB-C020-4A9F-B8DA-69C5EF38CCC3 Q27930363-D18E4155-7222-43CF-8BA1-F1765C74B340 Q27933148-55992EE7-A292-4943-95CD-F9B16DCF3EB6 Q27933360-E9850B6C-6DC3-4157-96EA-14EDA8D78BB6

P2860

Misfolded proteins partition between two distinct quality control compartments

http://www.wikidata.org/entity/Q24651093

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Misfolded proteins partition between two distinct quality control compartments

@ast

Misfolded proteins partition between two distinct quality control compartments

@en

Misfolded proteins partition between two distinct quality control compartments

@nl

type

label

Misfolded proteins partition between two distinct quality control compartments

@ast

Misfolded proteins partition between two distinct quality control compartments

@en

Misfolded proteins partition between two distinct quality control compartments

@nl

prefLabel

Misfolded proteins partition between two distinct quality control compartments

@ast

Misfolded proteins partition between two distinct quality control compartments

@en

Misfolded proteins partition between two distinct quality control compartments

@nl

P1433

Q24651093-63F45E79-E85F-4E63-8C9B-ACC335CFA544

P1476

Q24651093-DF2E7E2A-A961-44F9-B499-6B89D08E8D1F

P2093

Q24651093-136B1931-3545-4518-9793-4BE9AE74750B

Q24651093-30C5055E-C391-4C6F-8C2B-148CB2031606

P2860

Q24651093-02964C42-9044-4931-BED0-1B5581227342

Q24651093-07BD340B-18EE-4D52-B8C9-8250B5FA4F62

Q24651093-087D52EF-CAD0-4E89-A508-16C894A7CF12

Q24651093-0BFFB037-023F-42FD-98F9-20129D26CA75

Q24651093-0C3F578A-3583-4FCF-953C-3402808E6EEE

Q24651093-0DFD2015-2454-4F3C-8BC5-FAA620268BF7

Q24651093-0E803D7F-BE56-4A6F-832E-04DE2D9C4102

Q24651093-0F305CA6-D13B-4A45-97BC-37B24C7100D4

Q24651093-1142ABE6-3DA6-44A5-BEF9-91E9E48D33AD

Q24651093-11901888-2185-4DC3-A9FD-CF57B4217CC4

P2888

Q24651093-67A3AC6F-7573-4703-B2B3-C458067D7CE6

P304

Q24651093-9366519C-C4B9-4266-92F3-19E0B977148D

P31

Q24651093-C5D8A8FF-4DC7-449C-8F3C-AB59DD724B94

P3181

Q24651093-84EF0EEC-A451-454D-891B-E582C7A693DD

P356

Q24651093-1E559E9C-15F5-455C-BBF5-7B593F7940D3

P407

Q24651093-2E9D6F43-99DC-4E3E-AB79-9E2EAB469634

P433

Q24651093-98E79C68-4EAE-4946-BFBA-E0B0646C499F

P478

Q24651093-2A8D3EA4-7A7A-4E87-B2BA-56786A8E4C50

P50

Q24651093-9B976B2C-AB88-4CB4-90EA-7D1F64AC0077

P577

Q24651093-B9EFCB90-59AD-4A1D-A9E4-A323705F6B5F

P5875

Q24651093-03C55631-9B90-4D85-82D3-1875F8BEB4E5

P6179

Q24651093-71124DAB-6340-48F4-B02E-725CA29F2576

P698

Q24651093-23A6ADA2-86D7-4D86-A889-54C304C1A9E6

P921

Q24651093-EBAF957E-1E76-4CCD-98E6-A2FA6A59FBBA

P932

Q24651093-6AFA34F7-4AC1-4561-813F-77A9750EE080

P3181

P356

P1433

P1476

Misfolded proteins partition between two distinct quality control compartments

@en

P2093

Daniel Kaganovich

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

Ron Kopito

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

P2860

p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy

Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.

Autophagy: molecular machinery for self-eating

Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein

Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast.

Protein misfolding, functional amyloid, and human disease

Adapting proteostasis for disease intervention

The roles of intracellular protein-degradation pathways in neurodegeneration

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

P2888

P304

1088-95

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

P31

scholarly article

P3181

746293

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

P356

10.1038/NATURE07195

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

P407

P433

7208

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

P478

454

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

P50

P577

2008-08-28T00:00:00Z

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

P5875

23222624

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

P6179

1035244952

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

P698

18756251

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

P921

quality control

P932

2746971

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