Evidence map›Paper›PMID 29555747›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Monoclonal antibody targeting the β-barrel assembly machine of

Kelly M Storek, Marcy R Auerbach, Handuo Shi, Natalie K Garcia, Dawei Sun, Nicholas N Nickerson, Rajesh Vij, Zhonghua Lin, Nancy Chiang, Kellen Schneider and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed, 1 pooled it
16.0field-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

122 citing papers in PubMed, 1 synthesis or guideline pooled it, 179 citations in OpenAlex.

  1. Pooled it
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  7. A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026
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62 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors.

Kelly M StorekDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080.
Marcy R AuerbachDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080.
Handuo ShiDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080.
Natalie K GarciaDepartment of Protein Analytical Chemistry, Genentech Inc., South San Francisco, CA 94080.
Dawei SunDepartment of Structural Biology, Genentech Inc., South San Francisco, CA 94080.
Nicholas N NickersonDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080.
Rajesh VijDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Zhonghua LinDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Nancy ChiangDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Kellen SchneiderDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Aaron T WeckslerDepartment of Protein Analytical Chemistry, Genentech Inc., South San Francisco, CA 94080.
Elizabeth SkippingtonDepartment of Bioinformatics and Computational Biology, Genentech Inc., South San Francisco, CA 94080.
Gerald NakamuraDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Dhaya SeshasayeeDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
James T KoerberDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080.
Jian PayandehDepartment of Structural Biology, Genentech Inc., South San Francisco, CA 94080.
Peter A SmithDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080.
Steven T RutherfordDepartment of Infectious Diseases, Genentech Inc., South San Francisco, CA 94080; rutherford.steven@gene.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The folding and insertion of integral β-barrel membrane proteins into the outer membrane of Gram-negative bacteria is required for viability and bacterial pathogenesis. Unfortunately, the lack of selective and potent modulators to dissect β-barrel folding in vivo has hampered our understanding of this fundamental biological process. Here, we characterize a monoclonal antibody that selectively inhibits an essential component of the

Indexed as

Anti-Bacterial AgentsAntibodies, BacterialAntibodies, MonoclonalBacterial Outer Membrane ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsMembrane FluidityModels, MolecularProtein ConformationProtein FoldingAnti-Bacterial AgentsAntibodies, BacterialAntibodies, MonoclonalBacterial Outer Membrane ProteinsBamA protein, E coliEscherichia coli ProteinsBamAGram-negative bacteriaLPSmembrane protein foldingβ-barrel protein

Identifiers

PMID29555747
PMCPMC5889671
OpenAlexW2793159453

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.