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Functional interactions as a survival strategy against abnormal aggregation

Functional interactions as a survival strategy against abnormal aggregation

http://www.wikidata.org/entity/Q34421847

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The role of the central flexible region on the aggregation and conformational properties of human ataxin-3 Investigation of the Josephin Domain protein-protein interaction by molecular dynamics Protein-protein interactions as a strategy towards protein-specific drug design: the example of ataxin-1 Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase Trinucleotide repeats: a structural perspective Josephin Domain Structural Conformations Explored by Metadynamics in Essential Coordinates.N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42 An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.Chemical shift assignment of the ataxin-1 AXH domain in complex with a CIC ligand peptide.The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected Evolutionary capacitance and control of protein stability in protein-protein interaction networks.The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils.Toward understanding Machado-Joseph disease Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.Enhanced molecular mobility of ordinarily structured regions drives polyglutamine disease The importance of serine 776 in Ataxin-1 partner selection: a FRET analysis.Ataxin-3 phosphorylation decreases neuronal defects in spinocerebellar ataxia type 3 models Cellular strategies for regulating functional and nonfunctional protein aggregation.Early folding events protect aggregation-prone regions of a β-rich protein.Thermodynamic and kinetic stability of the Josephin Domain closed arrangement: evidences from replica exchange molecular dynamics Kaleidoscopic protein-protein interactions in the life and death of ataxin-1: new strategies against protein aggregation.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Evolutionary selection for protein aggregation.Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein Examination of Ataxin-3 (atx-3) Aggregation by Structural Mass Spectrometry Techniques: A Rationale for Expedited Aggregation upon Polyglutamine (polyQ) Expansion.A tale of a tail: Structural insights into the conformational properties of the polyglutamine protein ataxin-3.Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Destabilizing the AXH Tetramer by Mutations: Mechanisms and Potential Antiaggregation Strategies.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms

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Functional interactions as a survival strategy against abnormal aggregation

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2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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name

Functional interactions as a survival strategy against abnormal aggregation

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Functional interactions as a survival strategy against abnormal aggregation

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Functional interactions as a survival strategy against abnormal aggregation

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Functional interactions as a survival strategy against abnormal aggregation

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Giuseppe Nicastro

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Laura Masino

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Lesley Calder

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P2860

An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.

Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis

Protein misfolding, functional amyloid, and human disease

Adapting proteostasis for disease intervention

Protein misfolding, evolution and disease

Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities

Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature

Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors

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