Evidence map›Paper›PMID 35981415›Full record

ReviewCurrent opinion in structural biology2022

Structure and mechanism of the bacterial lipid ABC transporter, MlaFEDB.

Damian C Ekiert, Nicolas Coudray, Gira Bhabha

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Membrane-Focused Strategies AgainstAntibiotics (Basel, Switzerland) · 2026
    Review
  3. Article
  4. Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Following phospholipid transfer through the OmpFProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Coordinated subdomain movements of MlaC regulate ligand binding and transport.Computational and structural biotechnology journal · 2025
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. ABC Transporters in Bacterial Nanomachineries.International journal of molecular sciences · 2023
    Review
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 1 institution in 1 country.

Damian C EkiertDepartment of Cell Biology, New York University School of Medicine, New York, NY, USA; Department of Microbiology, New York University School of Medicine, New York, NY, USA. Electronic address: damian.ekiert@ekiertlab.org.
Nicolas CoudrayDepartment of Cell Biology, New York University School of Medicine, New York, NY, USA.
Gira BhabhaDepartment of Cell Biology, New York University School of Medicine, New York, NY, USA.
New York University · US

Funding

Unravelling lipid trafficking for the bacterial outer membraneR35GM128777 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Damian Ekiert · 2018 to 2026
$4.1M
NIGMS NIH HHS R35 GM128777
6 · The paper itself

Abstract

The cell envelope of Gram-negative bacteria is composed of an inner membrane, outer membane, and an intervening periplasmic space. How the outer membrane lipids are trafficked and assembled there, and how the asymmetry of the outer membrane is maintained is an area of intense research. The Mla system has been implicated in the maintenance of lipid asymmetry in the outer membrane, and is generally thought to drive the removal of mislocalized phospholipids from the outer membrane and their retrograde transport to the inner membrane. At the heart of the Mla pathway is a structurally unique ABC transporter complex in the inner membrane, called MlaFEDB. Recently, an explosion of cryo-EM studies has begun to shed light on the structure and lipid translocation mechanism of MlaFEDB, with many parallels to other ABC transporter families, including human ABCA and ABCG, as well as bacterial lipopolysaccharide and O-antigen transporters. Here we synthesize information from all available structures, and propose a model for lipid trafficking across the cell envelope by MlaFEDB.

Indexed as

ATP-Binding Cassette TransportersEscherichia coli ProteinsBacteriaBiological TransportCell MembraneHumansLipopolysaccharidesMembrane LipidsO AntigensPhospholipidsATP-Binding Cassette TransportersEscherichia coli ProteinsLipopolysaccharidesMembrane LipidsO AntigensPhospholipids

Identifiers

PMID35981415
PMCPMC9509461
OpenAlexW4291340400

What OpenQuestion holds

Textmetadata
LicenceTDM
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.