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

The Effects of PMM2-CDG-Causing Mutations on the Folding, Activity, and Stability of the PMM2 Protein.

Human mutation - 1 Sept 2015

Yuste-Checa Patricia, Gámez Alejandra, Brasil Sandra, Desviat Lourdes R, Ugarte Magdalena, Pérez-Cerdá Celia, Pérez Belén

Abstract excerpt

Congenital disorder of glycosylation type Ia (PMM2-CDG), the most common form of CDG, is caused by mutations in the PMM2 gene that reduce phosphomannomutase 2 (PMM2) activity. No curative treatment is available. The present work describes the functional analysis of nine human PMM2 mutant proteins frequently found in PMM2-CDG patients and also two murine Pmm2 mutations carried by the unique PMM2-CDG mouse model...

Read the complete abstract on PubMed

Topics

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

Share to Congenital Disorders of Glycosylation
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Fibroblasts

Share to Phosphotransferases (Phosphomutases)

Share to Protein Folding

Share to Protein Multimerization

Share to Proteolysis

Source

Identifiers

PMID: 26014514
DOI: 10.1002/humu.22817

Genes

PMM2

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Effects of PMM2-CDG-Causing Mutations on the Folding, Activity, and Stability of the PMM2 Protein.PMID 26014514Read ↗

Pharmacological Chaperoning: A Potential Treatment for PMM2-CDG.Semantic proximity Read ↗

A functional platform for the selection of pathogenic variants of PMM2 amenable to rescue via the use of pharmacological chaperones.Semantic proximity Read ↗

Functional significance of PMM2 mutations in mildly affected patients with congenital disorders of glycosylation Ia.Semantic proximity Read ↗

The Analysis of Variants in the General Population Reveals That PMM2 Is Extremely Tolerant to Missense Mutations and That Diagnosis of PMM2-CDG Can Benefit from the Identification of Modifiers.Semantic proximity Read ↗

Insight on molecular pathogenesis and pharmacochaperoning potential in phosphomannomutase 2 deficiency, provided by novel human phosphomannomutase 2 structures.Semantic proximity Read ↗

Proteostasis regulators as potential rescuers of PMM2 activity.Semantic proximity Read ↗

A mouse model of a human congenital disorder of glycosylation caused by loss of PMM2.Semantic proximity Read ↗

A new insight into PMM2 mutations in the French population.Semantic proximity Read ↗

Functional analysis of novel mutations in a congenital disorder of glycosylation Ia patient with mixed Asian ancestry.Semantic proximity Read ↗

HepG2 PMM2-CDG knockout model: A versatile platform for variant and therapeutic evaluation.Semantic proximity Read ↗

Yeast Models Of Phosphomannomutase 2 Deficiency, A Congenital Disorder Of GlycosylationSemantic proximity Read ↗

Clinical, laboratory and molecular findings and long-term follow-up data in 96 French patients with PMM2-CDG (phosphomannomutase 2-congenital disorder of glycosylation) and review of the literature.Semantic proximity Read ↗

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