Evidence map›Paper›PMID 25341963›Full record

ArticleNature communications2014

Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes.

Hsin-Hui Shen, Denisse L Leyton, Takuya Shiota, Matthew J Belousoff, Nicholas Noinaj, Jingxiong Lu, Stephen A Holt, Khershing Tan, Joel Selkrig, Chaille T Webb and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  4. Polydextrose reduces the infection ofMicrobiology spectrum · 2025
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  8. POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

13 authors at 3 institutions in 2 countries.

Hsin-Hui ShenDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Denisse L Leyton *Department of Microbiology, Monash University, Melbourne 3800, Australia.
Takuya Shiota *Department of Microbiology, Monash University, Melbourne 3800, Australia.
Matthew J BelousoffDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Nicholas NoinajNIDDK, NIH, Bethesda 20892, United States of America.
Jingxiong LuDepartment of Chemical Engineering, Monash University, Melbourne 3800.
Stephen A HoltThe Bragg Institute, Australian Nuclear Science and Technology Organization (ANSTO), Lucas Heights 2234, Australia.
Khershing TanDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Joel SelkrigDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Chaille T WebbDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Susan K BuchananNIDDK, NIH, Bethesda 20892, United States of America.
Lisandra L MartinSchool of Chemistry, Monash University, Melbourne 3800, Australia.
Trevor LithgowDepartment of Microbiology, Monash University, Melbourne 3800, Australia.
Monash University · AUNational Institutes of Health · USAustralian Nuclear Science and Technology Organisation · AU

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
Intramural NIH HHS ZIA DK036139
6 · The paper itself

Abstract

In biological membranes, various protein secretion devices function as nanomachines, and measuring the internal movements of their component parts is a major technological challenge. The translocation and assembly module (TAM) is a nanomachine required for virulence of bacterial pathogens. We have reconstituted a membrane containing the TAM onto a gold surface for characterization by quartz crystal microbalance with dissipation (QCM-D) and magnetic contrast neutron reflectrometry (MCNR). The MCNR studies provided structural resolution down to 1 Å, enabling accurate measurement of protein domains projecting from the membrane layer. Here we show that dynamic movements within the TamA component of the TAM are initiated in the presence of a substrate protein, Ag43, and that these movements recapitulate an initial stage in membrane protein assembly. The reconstituted system provides a powerful new means to study molecular movements in biological membranes, and the technology is widely applicable to studying the dynamics of diverse cellular nanomachines.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneEscherichia coli ProteinsLipid BilayersModels, MolecularMutagenesis, InsertionalNanoparticlesProtein Structure, SecondaryQuartz Crystal Microbalance TechniquesSubstrate SpecificityBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipid Bilayers

Identifiers

PMID25341963
PMCPMC4633281
OpenAlexW1967764488

What OpenQuestion holds

Textmetadata
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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.