about
Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of boneUbiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switchDefective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD.Structural insights into specificity and diversity in mechanisms of ubiquitin recognition by ubiquitin-binding domains.Independent interactions of ubiquitin-binding domains in a ubiquitin-mediated ternary complex.Characterization of a non-UBA domain missense mutation of sequestosome 1 (SQSTM1) in Paget's disease of bone.Mutant p62/SQSTM1 UBA domains linked to Paget's disease of bone differ in their abilities to function as stabilization signals.Novel UBA domain mutations of SQSTM1 in Paget's disease of bone: genotype phenotype correlation, functional analysis, and structural consequences.On the role of STAT1 and STAT6 ADP-ribosylation in the regulation of macrophage activation.Loss of Ubiquitin-Binding Associated With Paget's Disease of Bone p62 (SQSTM1) Mutations
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P50
description
researcher ORCID ID = 0000-0003-4515-0515
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wetenschapper
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name
James R Cavey
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James R Cavey
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James R Cavey
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James R Cavey
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type
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James R Cavey
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James R Cavey
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James R Cavey
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James R Cavey
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James Cavey
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James R Cavey
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James R Cavey
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James R Cavey
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James R Cavey
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6603132807
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0000-0003-4515-0515