Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition. - Wikidata - wikimedia - TriplyDB

Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.

Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.

http://www.wikidata.org/entity/Q35205006

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Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast DNAJs: more than substrate delivery to HSPA Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport A method to rapidly create protein aggregates in living cells.Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.Degradation-mediated protein quality control at the inner nuclear membrane Modularity and determinants of a (bi-)polarization control system from free-living and obligate intracellular bacteria Ribosomal proteins produced in excess are degraded by the ubiquitin-proteasome system Protein misfolding specifies recruitment to cytoplasmic inclusion bodies A simple microfluidic platform to study age-dependent protein abundance and localization changes in Saccharomyces cerevisiae.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress Protein aggregation as a mechanism of adaptive cellular responses.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Border Safety: Quality Control at the Nuclear Envelope.Prions are affected by evolution at two levels Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast Hsp90 Maintains Proteostasis of the Galactose Utilization Pathway To Prevent Cell Lethality Rqc1 and Ltn1 Prevent C-terminal Alanine-Threonine Tail (CAT-tail)-induced Protein Aggregation by Efficient Recruitment of Cdc48 on Stalled 60S Subunits.Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux.LC3A Silencing Hinders Aggresome Vimentin Cage Clearance in Primary Choroid Plexus Carcinoma Fusion, fission, and transport control asymmetric inheritance of mitochondria and protein aggregates.Walking the tightrope: proteostasis and neurodegenerative disease.Protein quality control in the nucleus.Protein Quality Control in Health and Disease.Hitchhiking vesicular transport routes to the vacuole: Amyloid recruitment to the Insoluble Protein Deposit (IPOD)Restricted access: spatial sequestration of damaged proteins during stress and aging.Proteasome dynamics between proliferation and quiescence stages of Saccharomyces cerevisiae.Prions, Chaperones, and Proteostasis in Yeast.Role of sHsps in organizing cytosolic protein aggregation and disaggregation.The Emerging Roles of Early Protein Folding Events in the Secretory Pathway in the Development of Neurodegenerative Maladies.The Upsides and Downsides of Organelle Interconnectivity.Asymmetric Inheritance of Aggregated Proteins and Age Reset in Yeast Are Regulated by Vac17-Dependent Vacuolar Functions.Protein aggregates are associated with replicative aging without compromising protein quality control.CELL BIOLOGY. Disrupted nuclear import-export in neurodegeneration.Spatial regulation of coalesced protein assemblies: Lessons from yeast to diseases.Prioritized Expression of BTN2 of Saccharomyces cerevisiae under Pronounced Translation Repression Induced by Severe Ethanol Stress.Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers.CHIP as a membrane-shuttling proteostasis sensor.

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P2860

Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.

http://www.wikidata.org/entity/Q35205006

description

2015 nî lūn-bûn

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2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

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2015年論文

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2015年论文

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name

Compartment-specific aggregase ...... oplasmic aggregate deposition.

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Compartment-specific aggregase ...... oplasmic aggregate deposition.

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type

label

Compartment-specific aggregase ...... oplasmic aggregate deposition.

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Compartment-specific aggregase ...... oplasmic aggregate deposition.

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prefLabel

Compartment-specific aggregase ...... oplasmic aggregate deposition.

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Compartment-specific aggregase ...... oplasmic aggregate deposition.

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P1433

The EMBO Journal

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Compartment-specific aggregase ...... oplasmic aggregate deposition.

@en

P2093

Annett Neuner

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

Chi-Ting Ho

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

D Lys Guilbride

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Elmar Schiebel

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Juliane Winkler

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Karsten Richter

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Maria Khokhrina

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Mohamed Y H Mohamed

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Stephanie B M Miller

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P2860

The complete spectrum of yeast chromosome instability genes identifies candidate CIN cancer genes and functional roles for ASTRA complex components

Hook2 contributes to aggresome formation

Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

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

Misfolded proteins partition between two distinct quality control compartments

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Sorting out the trash: the spatial nature of eukaryotic protein quality control

Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes

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778-797

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10.15252/EMBJ.201489524

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6

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34

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25672362

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4369314

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