Evidence map›Paper›PMID 22944696›Full record

ArticleBiological chemistry2012

Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes.

Maryta Sztukowska, Florian Veillard, Barbara Potempa, Matthew Bogyo, Jan J Enghild, Ida B Thogersen, Ky-Anh Nguyen, Jan Potempa

Abstract read
In one paragraph

Article in Biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Discovery of Gingipains andFoods (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Meprin β induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
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

8 authors.

Maryta SztukowskaOral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY 40202, USA.
Florian Veillard
Barbara Potempa
Matthew Bogyo
Jan J Enghild
Ida B Thogersen
Ky-Anh Nguyen
Jan Potempa

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
Small Molecule Imaging of Protease ActivityR01EB005011 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2005 to 2013
$3.0M
NIBIB NIH HHS R01 EB005011NIDCR NIH HHS R01 DE009761NIDCR NIH HHS R01 DE 09761
6 · The paper itself

Abstract

RgpA and Kgp gingipains are non-covalent complexes of endoprotease catalytic and hemagglutinin-adhesin domains on the surface of Porphyromonas gingivalis. A motif conserved in each domain has been suggested to function as an oligomerization motif. We tested this hypothesis by mutating motif residues to hexahistidine or insertion of hexahistidine tag to disrupt the motif within the Kgp catalytic domain. All modifications led to the secretion of entire Kgp activity into the growth media, predominantly in a form without functional His-tag. This confirmed the role of the conserved motif in correct posttranslational proteolytic processing and assembly of the multidomain complexes.

Indexed as

Adhesins, BacterialAmino Acid SequenceBase SequenceCysteine EndopeptidasesGingipain Cysteine EndopeptidasesMolecular Sequence DataAdhesins, BacterialCysteine EndopeptidasesGingipain Cysteine Endopeptidases

Identifiers

PMID22944696
PMCPMC3488288

What OpenQuestion holds

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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.