Evidence map›Paper›PMID 20801880›Full record

ReviewThe Journal of biological chemistry2010

Molecular basis of phosphatidyl-myo-inositol mannoside biosynthesis and regulation in mycobacteria.

Marcelo E Guerin, Jana Korduláková, Pedro M Alzari, Patrick J Brennan, Mary Jackson

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

63 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Drug-TolerantInternational journal of molecular sciences · 2023
    Article
  9. Article
  10. Structure of mycobacterial respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Supramolecular organization and dynamics of mannosylated phosphatidylinositol lipids in the mycobacterial plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Bacterial glycosylation, it's complicated.Frontiers in molecular biosciences · 2022
    Review
  17. Article
  18. Review
  19. The Phosphatidyl-Journal of bacteriology · 2021
    Article
  20. Article

3 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 4 institutions in 4 countries.

Marcelo E GuerinUnidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea, Leioa, Bizkaia 48940, Spain. mrcguerin@gmail.com
Jana Korduláková
Pedro M Alzari
Patrick J Brennan
Mary Jackson
Colorado State University · USCentre National de la Recherche Scientifique · FRComenius University Bratislava · SKUniversity of the Basque Country · ES

Funding

Biogenesis of Lipoarabinomannan in MycobacteriaR01AI064798 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI JACKSON, MARY · 2005 to 2019
$5.4M
SURFACE ANTIGENS OF M LEPRAE AND OTHER MYCOBACTERIAR37AI018357 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI BRENNAN, PATRICK JOSEPH · 1988 to 2007
$2.7M
NIAID NIH HHS R01 AI064798NIAID NIH HHS R37 AI018357
6 · The paper itself

Abstract

Phosphatidyl-myo-inositol mannosides (PIMs) are unique glycolipids found in abundant quantities in the inner and outer membranes of the cell envelope of all Mycobacterium species. They are based on a phosphatidyl-myo-inositol lipid anchor carrying one to six mannose residues and up to four acyl chains. PIMs are considered not only essential structural components of the cell envelope but also the structural basis of the lipoglycans (lipomannan and lipoarabinomannan), all important molecules implicated in host-pathogen interactions in the course of tuberculosis and leprosy. Although the chemical structure of PIMs is now well established, knowledge of the enzymes and sequential events leading to their biosynthesis and regulation is still incomplete. Recent advances in the identification of key proteins involved in PIM biogenesis and the determination of the three-dimensional structures of the essential phosphatidyl-myo-inositol mannosyltransferase PimA and the lipoprotein LpqW have led to important insights into the molecular basis of this pathway.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsCell MembraneGlycerophospholipidsLipidsLipopolysaccharidesMannosidesMannosyltransferasesModels, BiologicalMycobacteriumMycobacterium tuberculosisPhosphatidylinositolsProtein ConformationBacterial ProteinsGlycerophospholipidsLipidslipoarabinomannanlipomannanLipopolysaccharidesMannosidesMannosyltransferasesPhosphatidylinositolsphosphatidyl-myo-inositol mannosyltransferase PimA, Mycobacterium smegmatis

Identifiers

PMID20801880
PMCPMC2962455
OpenAlexW2008554986

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.