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Article

Mutations in p97/VCP induce unfolding activity.

FEBS letters - 20 Mar 2007

Rothballer Andrea, Tzvetkov Nikolay, Zwickl Peter

Abstract excerpt

A comparison of the protein sequences of various two-domain AAA+ ATPases revealed a striking difference in the residues lining the central pore of the D1 domain. The protein unfoldases of the bacterial Clp family and the archaeal VAT protein have at least one aromatic residue in the central D1 pore. In contrast, none of the members of the eukaryotic p97/VCP protein family has an aromatic residue in the D1 pore....

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Topics

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Share to Adenosine Triphosphatases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17346713
DOI: 10.1016/j.febslet.2007.02.031

Genes

VCP

Provenance

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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in p97/VCP induce unfolding activity.PMID 17346713Read ↗

VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.Semantic proximity Read ↗

Allosteric activation of VCP, a AAA unfoldase, by small molecule mimicrySemantic 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 ↗

Characterization of the aggregation-prevention activity of p97/valosin-containing protein.Semantic proximity Read ↗

Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation.Semantic proximity Read ↗

Structure and function of the AAA+ ATPase p97/Cdc48p.Semantic proximity Read ↗

ATPase activity of p97/valosin-containing protein is regulated by oxidative modification of the evolutionally conserved cysteine 522 residue in Walker A motif.Semantic proximity Read ↗

Conserved L464 in p97 D1-D2 linker is critical for p97 cofactor regulated ATPase activity.Semantic proximity Read ↗

Crystal structure of the catalytic D2 domain of the AAA+ ATPase p97 reveals a putative helical split-washer-type mechanism for substrate unfolding.Semantic proximity Read ↗

Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains.Semantic proximity Read ↗

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

p97/valosin-containing protein (VCP) is highly modulated by phosphorylation and acetylation.Semantic proximity Read ↗

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