Evidence map›Paper›PMID 10535938›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif.

H Ton-That, G Liu, S K Mazmanian, K F Faull, O Schneewind

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers.

0numbers the graph read from it
0cells of the map it votes in
248citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

248 citing papers in PubMed, 564 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Global Transcriptional Differences inAntibiotics (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Functional Characterization of a Putative Sortase FA1364 inInternational journal of molecular sciences · 2026
    Article
  7. Article
  8. Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026
    Article
  9. A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Development of aApplied and environmental microbiology · 2024
    Article
  18. Article
  19. Article
  20. Article

188 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

H Ton-ThatDepartment of Microbiology, Department of Psychiatry, University of California, Los Angeles School of Medicine, USA.
G Liu
S K Mazmanian
K F Faull
O Schneewind
University of California, Los Angeles · US

Funding

MULTIDISCIPLINARY TRAINING IN MICROBIAL PATHOGENESIST32AI007323 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Peter John Bradley · 1988 to 2026
$8.6M
PREDOCTORAL TRAINING PROGRAM IN GENETIC MECHANISMS AT UCT32GM007104 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GOBER, JAMES W · 1985 to 2011
$3.6M
NIAID NIH HHS AI07323NIAID NIH HHS AI33987NIAID NIH HHS T32 AI007323NIGMS NIH HHS T32 GM007104NIGMS NIH HHS T32GM07104
6 · The paper itself

Abstract

Surface proteins of Staphylococcus aureus are linked to the bacterial cell wall by sortase, an enzyme that cleaves polypeptides at the threonine of the LPXTG motif. Surface proteins can be released from staphylococci by treatment with hydroxylamine, resulting in the formation of threonine hydroxamate. Staphylococcal extracts, as well as purified sortase, catalyze the hydroxylaminolysis of peptides bearing an LPXTG motif, a reaction that can be inhibited with sulfhydryl-modifying reagents. Replacement of the single conserved cysteine at position 184 of sortase with alanine abolishes enzyme activity. Thus, sortase appears to catalyze surface-protein anchoring by means of a transpeptidation reaction that captures cleaved polypeptides as thioester enzyme intermediates.

Indexed as

Amino Acid MotifsAmino Acid SequenceAminoacyltransferasesBacterial ProteinsBase SequenceCatalysisCysteineCysteine EndopeptidasesDNA PrimersHydrolysisHydroxylamineMembrane ProteinsMolecular Sequence DataSequence Homology, Amino AcidStaphylococcus aureusAminoacyltransferasesBacterial ProteinsCysteineCysteine EndopeptidasesDNA PrimersHydroxylamineMembrane Proteinssortase A

Identifiers

PMID10535938
PMCPMC22937
OpenAlexW1988872938

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.