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

4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition.

Biochimica et biophysica acta - 1 Oct 2012

Riedel Travis J, Knight John, Murray Michael S, Milliner Dawn S, Holmes Ross P, Lowther W Todd

Abstract excerpt

Mutations in the gene encoding for 4-hydroxy-2-oxoglutarate aldolase (HOGA) are associated with an excessive production of oxalate in Primary Hyperoxaluria type 3 (PH3). This enzyme is the final step of the hydroxyproline degradation pathway within the mitochondria and catalyzes the cleavage of 4...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Oxidoreductases
Share to CHO Cells
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutarates

Share to Hydroxyproline

Share to Hyperoxaluria, Primary

Share to Ketoglutaric Acids

Share to Oxo-Acid-Lyases

Source

Open in PubMed Open full text

Identifiers

PMID: 22771891
DOI: 10.1016/j.bbadis.2012.06.014
PMCID: PMC3418427

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22771891-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

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

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition.PMID 22771891Read ↗

Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.Semantic proximity Read ↗

The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type 3.Semantic proximity Read ↗

Genetic basis of primary hyperoxaluria type II.Semantic proximity Read ↗

Human glyoxylate metabolism revisited: New insights pointing to multi-organ involvement with implications for siRNA-based therapies in primary hyperoxaluria.Semantic proximity Read ↗

Primary hyperoxalurias: disorders of glyoxylate detoxification.Semantic proximity Read ↗

The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type IISemantic proximity Read ↗

Primary HyperoxaluriaSemantic proximity Read ↗

CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type ISemantic proximity Read ↗

Molecular analysis of the glyoxylate reductase (GRHPR) gene and description of mutations underlying primary hyperoxaluria type 2.Semantic proximity Read ↗

Late diagnosis of primary hyperoxaluria type III.Semantic proximity Read ↗

A molecular journey on the pathogenesis of primary hyperoxaluria.Semantic proximity Read ↗

Renal function can be impaired in children with primary hyperoxaluria type 3.Semantic proximity Read ↗

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