Evidence map›Paper›PMID 27026255›Full record

ReviewNature reviews. Microbiology2016

Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model.

Suguru Okuda, David J Sherman, Thomas J Silhavy, Natividad Ruiz, Daniel Kahne

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
212citing papers in PubMed, 1 pooled it
41.4field-weighted citation impact, top 1% 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

212 citing papers in PubMed, 1 synthesis or guideline pooled it, 392 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. 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
  8. Article
  9. Article
  10. Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Molecular Basis for the Activation ofJournal of the American Chemical Society · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

152 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 2 countries.

Suguru OkudaDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
David J ShermanDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Thomas J SilhavyDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Natividad RuizDepartment of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA.
Daniel KahneDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Harvard University · USOsaka University · JPPrinceton University · USThe Ohio State University · US

Funding

Outer Membrane Biogenesis: New Antibiotic TargetsR01AI081059 · NIAID · HARVARD UNIVERSITY · PI Daniel Kahne · 2009 to 2026
$9.5M
Biogenesis and maintenance of the outer membrane of Gram-negative bacteriaR35GM118024 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 2016 to 2025
$8.1M
GENETIC ANALYSIS OF PROTEIN EXPORTR37GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1999 to 2008
$4.9M
GENETIC ANALYSIS OF PROTEIN EXPORTR01GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1985 to 2015
$4.7M
Envelope Biogenesis in Gram-negative BacteriaR01GM100951 · NIGMS · OHIO STATE UNIVERSITY · PI RUIZ, NATIVIDAD · 2012 to 2023
$3.7M
NIAID NIH HHS R01 AI081059NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R01 GM100951NIGMS NIH HHS R35 GM118024NIGMS NIH HHS R37 GM034821
6 · The paper itself

Abstract

Gram-negative bacteria have a double-membrane cellular envelope that enables them to colonize harsh environments and prevents the entry of many clinically available antibiotics. A main component of most outer membranes is lipopolysaccharide (LPS), a glycolipid containing several fatty acyl chains and up to hundreds of sugars that is synthesized in the cytoplasm. In the past two decades, the proteins that are responsible for transporting LPS across the cellular envelope and assembling it at the cell surface in Escherichia coli have been identified, but it remains unclear how they function. In this Review, we discuss recent advances in this area and present a model that explains how energy from the cytoplasm is used to power LPS transport across the cellular envelope to the cell surface.

Indexed as

Models, BiologicalBacterial Outer Membrane ProteinsBiological TransportCell MembraneEscherichia coliEscherichia coli ProteinsLipopolysaccharidesMetabolic Networks and PathwaysBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipopolysaccharides

Identifiers

PMID27026255
PMCPMC4937791
OpenAlexW2314285321

What OpenQuestion holds

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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.