Evidence map›Paper›PMID 17416658›Full record

ArticleJournal of bacteriology2007

Purification and characterization of mycobacterial phospholipase A: an activity associated with mycobacterial cutinase.

Sarah K Parker, Kathryn M Curtin, Michael L Vasil

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 52 citations in OpenAlex.

  1. Antimicrobial agents and chemotherapy · 2021
    Article
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  6. Biochemical Characterization of Isoniazid-resistantMolecular & cellular proteomics : MCP · 2018
    Article
  7. Article
  8. Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016
    Review
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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

3 authors at 2 institutions in 1 country.

Sarah K ParkerDepartment of Pediatrics, University of Colorado Health Sciences Center, Aurora, CO 80045, USA. sarah.parker@uchsc.edu
Kathryn M Curtin
Michael L Vasil
University of Colorado Anschutz Medical Campus · USUniversity of Colorado Health · US

Funding

NOVEL CLASS OF PHOSPHOLIPASES--MOLECULAR PATHOGENESISR01HL062608 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI VASIL, MICHAEL L. · 1998 to 2007
$3.2M
TUBERCULOSIS RESEARCH MATERIALS AND VACINE TESTINGN01AI075320 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · 1997 to 2004
$980k
Phospholipases in the Pathogenesis of M. tuberculosisK08AI050646 · NIAID · UNIVERSITY OF COLORADO DENVER · PI PARKER, SARAH KATHARINE · 2002 to 2006
$605k
NHLBI NIH HHS HL62608NHLBI NIH HHS R01 HL062608NIAID NIH HHS K08 AI050646NIAID NIH HHS N01 AI75320
6 · The paper itself

Abstract

We describe mycobacterial phospholipase A activity (MPLA) and, using reverse genetics, have associated this activity with putative mycobacterial cutinase. PLAs, which hydrolyze fatty acids on phospholipids, play a significant role in human inflammatory states and disease pathogenesis. In prokaryotes, the recognition of their role in virulence is more recent. Cutinases are serine esterases whose primary substrate is cutin, the waxy exterior layer of plants. Mycobacterium tuberculosis has maintained seven putative cutinases, though it should not encounter cutin; we demonstrate that known cutinases and MPLA cleave phospholipids in a PLA-type manner and also hydrolyze Tween. We analyzed cutinase motifs in mycobacteria and found the motif very prevalent. All mycobacteria tested had MPLA activity. These studies suggest an alternative use for putative cutinases by the M. tuberculosis group that is likely related to MPLA activity and lipid metabolism.

Indexed as

Amino Acid SequenceCarboxylic Ester HydrolasesChromatography, Thin LayerHydrolysisKineticsMembrane LipidsMolecular Sequence DataMycobacteriumMycobacterium tuberculosisNitrobenzenesPhospholipases APolysorbatesSequence Homology, Amino Acid4-nitrophenethyl bromideCarboxylic Ester HydrolasescutincutinaseMembrane LipidsNitrobenzenesPhospholipases APolysorbates

Identifiers

PMID17416658
PMCPMC1913378
OpenAlexW2110531064

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.