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

Topics Community

Article

Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I.

Proceedings of the National Academy of Sciences of the United States of America - 16 Feb 2010

Cellini Barbara, Montioli Riccardo, Paiardini Alessandro, Lorenzetto Antonio, Maset Fabio, Bellini Tiziana, Oppici Elisa, Voltattorni Carla Borri

Abstract excerpt

G41 is an interfacial residue located within the alpha-helix 34-42 of alanine:glyoxylate aminotransferase (AGT). Its mutations on the major (AGT-Ma) or the minor (AGT-Mi) allele give rise to the variants G41R-Ma, G41R-Mi, and G41V-Ma causing hyperoxaluria type 1. Impairment of dimerization in these variants has been suggested to be responsible for immunoreactivity deficiency, intraperoxisomal aggregation, and...

Topics

Alanine
Chromatography, Gel
Dimerization
Glycine
Humans
Hyperoxaluria, Primary
Kinetics
Mass Spectrometry
Models, Molecular
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nephelometry and Turbidimetry

Transaminases

Source

Open in PubMed Open full text

Identifiers

PMID: 20133649
DOI: 10.1073/pnas.0908565107
PMCID: PMC2840350

Genes

AGT

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I.PMID 20133649Read ↗

Effects of interface mutations on the dimerization of alanine glyoxylate aminotransferase and implications in the mistargeting of the pathogenic variants F152I and I244T.Semantic proximity Read ↗

Cryptic genetic variations of alanine:glyoxylate aminotransferase shape its fitness and dynamicsSemantic proximity Read ↗

Correlation between the molecular effects of mutations at the dimer interface of alanine-glyoxylate aminotransferase leading to primary hyperoxaluria type I and the cellular response to vitamin B6.Semantic proximity Read ↗

Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants.Semantic proximity Read ↗

Structural dynamics shape the fitness window of alanine:glyoxylate aminotransferase.Semantic proximity Read ↗

Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.Semantic proximity Read ↗

Biochemical and cellular effects of a novel missense mutation of the AGXT gene associated with Primary Hyperoxaluria Type 1.Semantic proximity Read ↗

The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I.Semantic proximity Read ↗

The ILE56 mutation on different genetic backgrounds of alanine:glyoxylate aminotransferase: Clinical features and biochemical characterization.Semantic proximity Read ↗

The molecular basis of alanine: glyoxylate aminotransferase mistargeting: the most common single cause of primary hyperoxaluria type 1.Semantic proximity Read ↗

Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with primary hyperoxaluria type I.Semantic proximity Read ↗

Natural and Unnatural Compounds Rescue Folding Defects of Human Alanine: Glyoxylate Aminotransferase Leading to Primary Hyperoxaluria Type I.Semantic proximity Read ↗

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