Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. - Wikidata - wikimedia - TriplyDB

Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.

Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.

http://www.wikidata.org/entity/Q42564287

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Protein Folding and Mechanisms of Proteostasis Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation Protein quality control in the nucleus The roles of conditional disorder in redox proteins Functional diversity and structural disorder in the human ubiquitination pathway A conserved deubiquitinating enzyme controls cell growth by regulating RNA polymerase I stability.Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation Physical and genetic associations of the Irc20 ubiquitin ligase with Cdc48 and SUMO.Degradation-mediated protein quality control at the inner nuclear membrane Signalling scaffolds and local organization of cellular behaviour The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability Reporter-based growth assay for systematic analysis of protein degradation Dynamic Sumoylation of a Conserved Transcription Corepressor Prevents Persistent Inclusion Formation during Hyperosmotic Stress Uncertainty analysis in protein disorder prediction.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP)Posttranslational modification of mitochondrial transcription factor A in impaired mitochondria biogenesis: implications in diabetic retinopathy and metabolic memory phenomenon.Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus.Redesigning the NEDD8 pathway with a bacterial genetic screen for ubiquitin-like molecule transfer.The N-end rule pathway and regulation by proteolysis Conditional disorder in chaperone action.How the nucleus copes with proteotoxic stress.Roles of mitochondrial ubiquitin ligase MITOL/MARCH5 in mitochondrial dynamics and diseases.Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity Ligand-switchable substrates for a ubiquitin-proteasome system Tight regulation of the unfolded protein sensor Ire1 by its intramolecularly antagonizing subdomain.Ubiquitination of newly synthesized proteins at the ribosome.Molecular evolution and in vitro characterization of Botryllus histocompatibility factor.Dissecting seipin function: the localized accumulation of phosphatidic acid at ER/LD junctions in the absence of seipin is suppressed by Sei1p(ΔNterm) only in combination with Ldb16p A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in Yeast Distinct transcriptional responses elicited by unfolded nuclear or cytoplasmic protein in mammalian cells.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Proteasome inhibition rescues clinically significant unstable variants of the mismatch repair protein Msh2.

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P2860

Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.

http://www.wikidata.org/entity/Q42564287

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Disorder targets misorder in n ...... izes its misfolded substrates.

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Disorder targets misorder in n ...... izes its misfolded substrates.

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Disorder targets misorder in n ...... izes its misfolded substrates.

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Disorder targets misorder in n ...... izes its misfolded substrates.

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Disorder targets misorder in n ...... izes its misfolded substrates.

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J.MOLCEL.2010.12.004

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Disorder targets misorder in n ...... nizes its misfolded substrates

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Carrie M Garrett-Engele

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Daniel E Gottschling

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Elizabeth D Hetrick

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Eric K Fredrickson

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Joel C Rosenbaum

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Michelle L Oeser

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Thomas I Milac

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Zara W Nelson

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Hsp70 chaperones: cellular functions and molecular mechanism

Using circular dichroism spectra to estimate protein secondary structure

One step at a time: endoplasmic reticulum-associated degradation

PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

Crystal structure and assembly of a eukaryotic small heat shock protein

Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.

A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation.

Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.

Degradation-mediated protein quality control in the nucleus.

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93-106

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scholarly article

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10.1016/J.MOLCEL.2010.12.004

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1

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41

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Richard G Gardner

Melissa N Locke

Lauren A Richardson

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2011-01-01T00:00:00Z

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49734021

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21211726

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nuclear protein quality control by the ubiquitin-proteasome system

quality control

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3042722

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