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Article

XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.

PloS one - 1 Jan 2014

Wright Katharine M, Wu Kuanlin, Babatunde Omotolani, Du Haijuan, Massiah Michael A

Abstract excerpt

MID1 catalyzes the ubiquitination of the protein alpha4 and the catalytic subunit of protein phosphatase 2A. Mutations within the MID1 Bbox1 domain are associated with X-linked Opitz G syndrome (XLOS). Our functional assays have shown that mutations of Ala130 to Val or Thr, Cys142 to Ser and Cys1...

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Source

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Identifiers

PMID: 25216264
DOI: 10.1371/journal.pone.0107537
PMCID: PMC4162623

Genes

MID1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25216264-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Research trail→

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XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.PMID 25216264Read ↗

Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.Semantic proximity Read ↗

Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.Semantic proximity Read ↗

Mechanism of midline defect-causing mutation P151L in MID1 revealed.Semantic proximity Read ↗

New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome.Semantic proximity Read ↗

Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1.Semantic proximity Read ↗

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation.Semantic proximity Read ↗

A structure-function study of MID1 mutations associated with a mild Opitz phenotype.Semantic proximity Read ↗

X-linked Opitz syndrome: novel mutations in the MID1 gene and redefinition of the clinical spectrum.Semantic proximity Read ↗

DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding.Semantic proximity Read ↗

Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the carboxy-terminal domain.Semantic proximity Read ↗

Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.Semantic proximity Read ↗

Nox4 B-loop creates an interface between the transmembrane and dehydrogenase domains.Semantic proximity Read ↗

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