The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition. - Wikidata - wikimedia - TriplyDB

The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.

The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.

http://www.wikidata.org/entity/Q33906613

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Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3 The role of the central flexible region on the aggregation and conformational properties of human ataxin-3 Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3 Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes Deubiquitinating enzymes in cellular signaling and disease regulation Cell biology of spinocerebellar ataxia Investigation of the Josephin Domain protein-protein interaction by molecular dynamics Crystal Structure of the Peptidase Domain of Streptococcus ComA, a Bifunctional ATP-binding Cassette Transporter Involved in the Quorum-sensing Pathway NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity Aggresome formation and neurodegenerative diseases: therapeutic implications Proteotoxic stress increases nuclear localization of ataxin-3 Deranged calcium signaling and neurodegeneration in spinocerebellar ataxia type 3 Therapeutic prospects for spinocerebellar ataxia type 2 and 3.Trinucleotide repeats: a structural perspective Josephin Domain Structural Conformations Explored by Metadynamics in Essential Coordinates.Ubiquitin domain proteins in disease.The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias Ataxin-3 plays a role in mouse myogenic differentiation through regulation of integrin subunit levels Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3.The challenge of producing ubiquitinated proteins for structural studies A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation.Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117.Functional interactions as a survival strategy against abnormal aggregation Ubiquitin-binding site 2 of ataxin-3 prevents its proteasomal degradation by interacting with Rad23 A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected Dominant negative effect of polyglutamine expansion perturbs normal function of ataxin-3 in neuronal cells.Characterization of the conformational fluctuations in the Josephin domain of ataxin-3.The Josephin domain determines the morphological and mechanical properties of ataxin-3 fibrils.Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.Balancing act: deubiquitinating enzymes in the nervous system.Energy landscapes of functional proteins are inherently risky.Allosteric regulation of deubiquitylase activity through ubiquitination.Toward understanding Machado-Joseph disease Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.A mutant ataxin-3 fragment results from processing at a site N-terminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice.Enhanced molecular mobility of ordinarily structured regions drives polyglutamine disease

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The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.

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P2860

Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B

The Protein Data Bank

Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution

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

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structural basis for the specificity of ubiquitin C-terminal hydrolases

Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a

A Ca(2+) switch aligns the active site of calpain

Structural basis for development of cathepsin B-specific noncovalent-type inhibitor: crystal structure of cathepsin B-E64c complex

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

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