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

Primary hyperoxaluria type 1: AGT mistargeting highlights the fundamental differences between the peroxisomal and mitochondrial protein import pathways.

Biochimica et biophysica acta - 1 Dec 2006

Danpure Christopher J

Abstract excerpt

Primary hyperoxaluria type 1 (PH1) is an atypical peroxisomal disorder, as befits a deficiency of alanine:glyoxylate aminotransferase (AGT), which is itself an atypical peroxisomal enzyme. PH1 is characterized by excessive synthesis and excretion of the metabolic end-product oxalate and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract. Disease in many patients is caused by...

Read the complete abstract on PubMed

Topics

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

Share to Hyperoxaluria, Primary
Share to Kidney Calculi

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

Share to Mitochondria

Share to Peroxisome-Targeting Signal 1 Receptor

Share to Peroxisomes

Share to Protein Transport

Share to Receptors, Cytoplasmic and Nuclear

Share to Transaminases

Source

Identifiers

PMID: 17027096
DOI: 10.1016/j.bbamcr.2006.08.021

Genes

AGT

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Primary hyperoxaluria type 1: AGT mistargeting highlights the fundamental differences between the peroxisomal and mitochondrial protein import pathways.PMID 17027096Read ↗

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

A unique molecular basis for enzyme mistargeting in primary hyperoxaluria type 1.Semantic proximity Read ↗

Liver peroxisomal alanine:glyoxylate aminotransferase and the effects of mutations associated with Primary Hyperoxaluria Type I: An overview.Semantic proximity Read ↗

Molecular Aetiology of Primary Hyperoxaluria Type 1Semantic proximity Read ↗

Primary hyperoxaluria type 1: genotypic and phenotypic heterogeneity.Semantic proximity Read ↗

Molecular insights into primary hyperoxaluria Type I pathogenesisSemantic proximity Read ↗

Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease.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 ↗

Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation.Semantic proximity Read ↗

Pharmacologic rescue of an enzyme-trafficking defect in primary hyperoxaluria 1.Semantic proximity Read ↗

Molecular etiology of primary hyperoxaluria type 1: new directions for treatment.Semantic proximity Read ↗

Molecular aetiology of primary hyperoxaluria and its implications for clinical management.Semantic proximity Read ↗

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