Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97. - Wikidata - wikimedia - TriplyDB

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

http://www.wikidata.org/entity/Q40775969

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Structural analysis of the UBA domain of X-linked inhibitor of apoptosis protein reveals different surfaces for ubiquitin-binding and self-association Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis An arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG Structural basis for UBA-mediated dimerization of c-Cbl ubiquitin ligase Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer Altered cofactor regulation with disease-associated p97/VCP mutations Conformational changes in the AAA ATPase p97-p47 adaptor complex Ubiquitin-binding domains Ubiquitin-binding domains Data-driven docking for the study of biomolecular complexes.Structural insights into the p97-Ufd1-Npl4 complex.Multiple UBXN family members inhibit retrovirus and lentivirus production and canonical NFκΒ signaling by stabilizing IκBα.Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1.The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L.Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b.Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin.The arabidopsis histone methyltransferase SUVR4 binds ubiquitin via a domain with a four-helix bundle structure.The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.The defective proteasome but not substrate recognition function is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10 Targeted Disruption of Calcium/NFAT Signaling Reveals a Left-Right Determination Disorder in the Pharyngeal Arch Artery

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P2860

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

http://www.wikidata.org/entity/Q40775969

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2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

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type

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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

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SJ.EMBOJ.7600152

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The EMBO Journal

P1476

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

@en

P2093

Carol Robinson

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

Catherine Keetch

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

Ciaran McKeown

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

Hisao Kondo

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

Peter Simpson

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

Stephen Matthews

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

Xuemei Yuan

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

P2860

Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains

p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins

SMART: a web-based tool for the study of genetically mobile domains.

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.

Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.

SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation.

A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways

VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo

The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle

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

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