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Article

The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97.

The FEBS journal - 1 Nov 2006

Shiozawa Kumiko, Goda Natsuko, Shimizu Toshiyuki, Mizuguchi Kenji, Kondo Naomi, Shimozawa Nobuyuki, Shirakawa Masahiro, Hiroaki Hidekazu

Abstract excerpt

PEX1 is a type II AAA-ATPase that is indispensable for biogenesis and maintenance of the peroxisome, an organelle responsible for the primary metabolism of lipids, such as beta-oxidation and lipid biosynthesis. Recently, we demonstrated a striking structural similarity between its N-terminal domain and those of other membrane-related AAA-ATPases, such as valosine-containing protein (p97). The N-terminal domain of...

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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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Share to Hydrophobic and Hydrophilic Interactions

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Source

Identifiers

PMID: 17018057
DOI: 10.1111/j.1742-4658.2006.05494.x

Genes

PEX1
VCP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97.PMID 17018057Read ↗

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