Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The FEBS journal - 1 Jul 2017

Wright Katharine M, Du Haijuan, Massiah Michael A

Abstract excerpt

Mutations of human MID1 are associated with X-linked Opitz G Syndrome (XLOS), which is characterized by midline birth defects. XLOS-observed mutations within the MID1 B-box1 domain are associated with cleft lip/palate, wide-spaced eyes and hyperspadias. Three of the four XLOS-observed mutations in the B-box1 domain results in unfolding but the structural and functional effects of the P151L mutation is not...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cleft Palate
Share to Esophagus
Share to Genetic Diseases, X-Linked

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hypertelorism

Share to Hypospadias

Share to Microtubule Proteins

Share to Protein Phosphatase 2

Share to Ubiquitination

Source

Identifiers

PMID: 28548391
DOI: 10.1111/febs.14121

Genes

MID1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.PMID 28548391Read ↗

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

The MID1 gene product in physiology and disease.Semantic proximity Read ↗

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

The MID1 protein is a central player during development and in disease.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 ↗

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

Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22.Semantic proximity Read ↗

Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A.Semantic proximity Read ↗

Complex rearrangement of the exon 6 genomic region among Opitz G/BBB Syndrome MID1 alterations.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.