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Article

Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers.

European journal of cell biology - 1 Jan 2000

Rijal Ramesh, Arhzaouy Khalid, Strucksberg Karl-Heinz, Cross Megan, Hofmann Andreas, Schröder Rolf, Clemen Christoph S, Eichinger Ludwig

Abstract excerpt

p97 (VCP) is a homo-hexameric triple-A ATPase that exerts a plethora of cellular processes. Heterozygous missense mutations of p97 cause at least five human neurodegenerative disorders. However, the specific molecular consequences of p97 mutations are hitherto widely unknown. Our in silico structural models of human and Dictyostelium p97 showed that the disease-causing human R93C, R155H, and R155C as well as...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 27132113
DOI: 10.1016/j.ejcb.2016.03.004

Genes

VCP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutant p97 exhibits species-specific changes of its ATPase activity and compromises the UBXD9-mediated monomerisation of p97 hexamers.PMID 27132113Read ↗

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Valosin-Containing Protein (VCP)/p97 Oligomerization.Semantic proximity Read ↗

D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP.Semantic proximity Read ↗

Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants.Semantic proximity Read ↗

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