Evidence map›Paper›PMID 27862971›Full record

ReviewThe FEBS journal2017

Structural snapshots of the β-barrel assembly machinery.

Jeremy Bakelar, Susan K Buchanan, Nicholas Noinaj

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020
    Review
  6. Article
  7. Article
  8. 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

3 authors at 2 institutions in 1 country.

Jeremy BakelarDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University, West Lafayette, IN, USA.
Susan K BuchananNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
Nicholas NoinajDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University, West Lafayette, IN, USA.
Purdue University West Lafayette · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

structural characterization of bacterial secretion channelsZIADK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.3M
The role of BamA in the biogenesis of beta-barrel membrane proteinsK22AI113078 · NIAID · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2015 to 2016
$267k
Intramural NIH HHS ZIA DK036139NIAID NIH HHS K22 AI113078
6 · The paper itself

Abstract

The β-barrel assembly machinery (BAM) is a multicomponent complex responsible for the biogenesis of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria, with conserved systems in both mitochondria and chloroplasts. Given its importance in the integrity of the outer membrane and in the assembly of surface exposed virulence factors, BAM is an attractive therapeutic target against pathogenic bacteria, particularly multidrug-resistant strains. While the mechanism for how BAM functions remains elusive, previous structural studies have described each of the individual components of BAM, offering only a few clues to how the complex functions. Recently, a number of structures have been reported of complexes, including that of fully assembled BAM in differing conformational states. These studies have provided the molecular blueprint detailing the atomic interactions between the components and have revealed new details about BAM, which suggest a dynamic mechanism that may use conformational changes to assist in the biogenesis of new OMPs.

Indexed as

Bacterial Outer Membrane ProteinsGram-Negative BacteriaProtein Structure, SecondaryStructure-Activity RelationshipBacterial Outer Membrane ProteinsBAM complexlateral gateMD simulationsmembrane biogenesismembrane proteinouter membrane proteinprotein foldingX-ray crystallographyβ-barrel assembly machineryβ-barrel membrane proteins

Identifiers

PMID27862971
PMCPMC5429997
OpenAlexW2554980636

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.