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

Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-phosphotransferase.

The Journal of biological chemistry - 29 Aug 2003

Yaghootfam Afshin, Schestag Frank, Dierks Thomas, Gieselmann Volkmar

Abstract excerpt

The critical step for sorting of lysosomal enzymes is the recognition by a Golgi-located phosphotransferase. The topogenic structure common to all lysosomal enzymes essential for this recognition is still not well defined, except that lysine residues seem to play a critical role. Here we have substituted surface-located lysine residues of lysosomal arylsulfatases A and B. In lysosomal arylsulfatase A only...

Read the complete abstract on PubMed

Topics

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

Share to Cerebroside-Sulfatase
Share to Cricetinae

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

Share to Glycosylation

Share to Lysine

Share to Lysosomes

Share to Oligosaccharides

Share to Precipitin Tests

Share to Transferases (Other Substituted Phosphate Groups)

Source

Identifiers

PMID: 12783870
DOI: 10.1074/jbc.M304865200

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

Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-phosphotransferase.PMID 12783870Read ↗

Deficient glycosylation of arylsulfatase A in pseudo arylsulfatase-A deficiency.Semantic proximity Read ↗

Processing of normal lysosomal and mutant N-acetylgalactosamine 4-sulphatase: BiP (immunoglobulin heavy-chain binding protein) may interact with critical protein contact sites.Semantic proximity Read ↗

Lysine-based structure in the proregion of procathepsin L is the recognition site for mannose phosphorylation.Semantic proximity Read ↗

Compensatory expression of human N-acetylglucosaminyl-1-phosphotransferase subunits in mucolipidosis type III gamma.Semantic proximity Read ↗

Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.Semantic proximity Read ↗

Glycosylation and phosphorylation of lysosomal glycosylasparaginase.Semantic proximity Read ↗

An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.Semantic proximity Read ↗

Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine.Semantic proximity Read ↗

Purifying selection of the lysosomal enzymes arylsulfatase A and beta-galactocerebrosidase and their evolutionary impact on myelin integrity.Semantic proximity Read ↗

Misfolded endoplasmic reticulum retained subunits cause degradation of wild-type subunits of arylsulfatase A heteromers.Semantic proximity Read ↗

Effects of glycosylation and pH conditions in the dynamics of human arylsulfatase A.Semantic proximity Read ↗

Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1.Semantic proximity Read ↗

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