Specificity in intracellular protein aggregation and inclusion body formation. - Wikidata - wikimedia - TriplyDB

Specificity in intracellular protein aggregation and inclusion body formation.

Specificity in intracellular protein aggregation and inclusion body formation.

http://www.wikidata.org/entity/Q33949081

about

Hook2 contributes to aggresome formation Sequence determinants of protein aggregation: tools to increase protein solubility.Macromolecule-assisted de novo protein folding The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Proteomic characterization of an isolated fraction of synthetic proteasome inhibitor (PSI)-induced inclusions in PC12 cells might offer clues to aggresomes as a cellular defensive response against proteasome inhibition by PSI.Delayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation.Aggresomes do not represent a general cellular response to protein misfolding in mammalian cells Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation.Rescue of photoreceptor degeneration by curcumin in transgenic rats with P23H rhodopsin mutation.Quality control of protein folding in extracellular space.Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions.The importance of sequence diversity in the aggregation and evolution of proteins.The common inhaled anesthetic isoflurane increases aggregation of huntingtin and alters calcium homeostasis in a cell model of Huntington's disease Deciphering structural intermediates and genotoxic fibrillar aggregates of albumins: a molecular mechanism underlying for degenerative diseases.Probing mechanisms of photoreceptor degeneration in a new mouse model of the common form of autosomal dominant retinitis pigmentosa due to P23H opsin mutations.A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila.Variables and strategies in development of therapeutic post-transcriptional gene silencing agents Tracking protein aggregate interactions.Polyglutamine expansion alters the dynamics and molecular architecture of aggregates in dentatorubropallidoluysian atrophy Identifying polyglutamine protein species in situ that best predict neurodegeneration Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling Bottlenecks in development of retinal therapeutic post-transcriptional gene silencing agents De novo design of a biologically active amyloid.Misfolded opsin mutants display elevated β-sheet structure.Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences Do amyloid oligomers act as traps for misfolded proteins? A hypothesis Recovery of bioactive protein from bacterial inclusion bodies using trifluoroethanol as solubilization agent The last tangle of tau.Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae.Elovl4 5-bp deletion knock-in mouse model for Stargardt-like macular degeneration demonstrates accumulation of ELOVL4 and lipofuscin Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.X chromosome reactivation perturbs intracellular self/not-self discrimination.Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro Amyloid oligomers: dynamics and toxicity in the cytosol and nucleus.Proteomic analysis of mitochondrial dysfunction in neurodegenerative diseases.An in vitro perspective on the molecular mechanisms underlying mutant huntingtin protein toxicity Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease.

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P2860

Specificity in intracellular protein aggregation and inclusion body formation.

http://www.wikidata.org/entity/Q33949081

description

2001 nî lūn-bûn

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2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2001 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

Specificity in intracellular protein aggregation and inclusion body formation.

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Specificity in intracellular protein aggregation and inclusion body formation.

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type

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Specificity in intracellular protein aggregation and inclusion body formation.

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Specificity in intracellular protein aggregation and inclusion body formation.

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prefLabel

Specificity in intracellular protein aggregation and inclusion body formation.

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Specificity in intracellular protein aggregation and inclusion body formation.

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Proceedings of the National Academy of Sciences of the United States of America

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Specificity in intracellular protein aggregation and inclusion body formation.

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Bence NF

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

Illing ME

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Kopito RR

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Rajan RS

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P2860

The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription

Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1

Rhodopsin mutations in autosomal dominant retinitis pigmentosa

A new technique for the assay of infectivity of human adenovirus 5 DNA

The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media

Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin

Aggresomes: a cellular response to misfolded proteins

Aggresomes, inclusion bodies and protein aggregation

Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells

Biosynthesis of surfactant protein C: characterization of aggresome formation by EGFP chimeras containing propeptide mutants lacking conserved cysteine residues.

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98

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