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

Functional and structural analysis of five mutations identified in methylmalonic aciduria cblB type.

Human mutation - 1 Sept 2010

Jorge-Finnigan Ana, Aguado Cristina, Sánchez-Alcudia Rocio, Abia David, Richard Eva, Merinero Begoña, Gámez Alejandra, Banerjee Ruma, Desviat Lourdes R, Ugarte Magdalena, Pérez Belen

Abstract excerpt

ATP:cob(I)alamin adenosyltransferase (ATR, E.C.2.5.1.17) converts reduced cob(I)alamin to the adenosylcobalamin cofactor. Mutations in the MMAB gene encoding ATR are responsible for the cblB type methylmalonic aciduria. Here we report the functional analysis of five cblB mutations to determine the underlying molecular basis of the dysfunction. The transcriptional profile along with minigenes analysis revealed...

Read the complete abstract on PubMed

Topics

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

Share to Alkyl and Aryl Transferases
Share to Amino Acid Metabolism, Inborn Errors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genome, Human

Share to Mutant Proteins

Share to Mutation, Missense

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Share to RNA Splicing

Source

Open in PubMed Open full text

Identifiers

PMID: 20556797
DOI: 10.1002/humu.21307
PMCID: PMC2932867

Genes

ATR
MMAB

Variants

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional and structural analysis of five mutations identified in methylmalonic aciduria cblB type.PMID 20556797Read ↗

Methylmalonic aciduria cblB type: characterization of two novel mutations and mitochondrial dysfunction studies.Semantic proximity Read ↗

Spectrum and characterization of bi-allelic variants in MMAB causing cblB-type methylmalonic aciduria.Semantic proximity Read ↗

Protein destabilization and loss of protein-protein interaction are fundamental mechanisms in cblA-type methylmalonic aciduria.Semantic proximity Read ↗

Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions.Semantic proximity Read ↗

Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria.Semantic proximity Read ↗

Mutation and biochemical analysis of patients belonging to the cblB complementation class of vitamin B12-dependent methylmalonic aciduria.Semantic proximity Read ↗

Hepatocyte-like cells differentiated from methylmalonic aciduria cblB type induced pluripotent stem cells: A platform for the evaluation of pharmacochaperoning.Semantic proximity Read ↗

Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function.Semantic proximity Read ↗

Modulation of conformational features and oligomerization of MMACHC by cobalamin variants: impact of the R161Q mutation in cblC disease.Semantic proximity Read ↗

Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism.Semantic proximity Read ↗

Combined methylmalonic acidemia and homocystinuria, cblC type. I. Clinical presentations, diagnosis and management.Semantic proximity Read ↗

Functional Characterization and Categorization of Missense Mutations that Cause Methylmalonyl‐ <scp>C</scp> o <scp>A</scp> Mutase ( <scp>MUT</scp> ) DeficiencySemantic proximity Read ↗

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