Evidence map›Paper›PMID 33493965›Full record

ReviewCurrent opinion in structural biology2021

Outer membrane protein evolution.

Rik Dhar, Joanna Sg Slusky

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection againstInternational journal of environmental research and public health · 2021
    Article
  12. Membrane Barrels Are Taller, Fatter, Inside-Out Soluble Barrels.The journal of physical chemistry. B · 2021
    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

2 authors.

Rik DharDepartment of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Ave., Lawrence KS 66045-3101, United States.
Joanna Sg SluskyDepartment of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Ave., Lawrence KS 66045-3101, United States; Center for Computational Biology, The University of Kansas, 2030 Becker Dr., Lawrence, KS 66045-7534, United States. Electronic address: slusky@ku.edu.

Funding

DESIGNED BETA-STRANDS FOR INHIBITING EFFLUX PUMPS AND DISABLING ANTIBIOTIC RESISTANCEDP2GM128201 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SLUSKY, JOANNA SG · 2017 to 2017
$2.3M
NIGMS NIH HHS DP2 GM128201
6 · The paper itself

Abstract

Outer membrane proteins have remarkably homogeneous structure. They are all up down β-barrels. Up down barrels themselves are composed of repeated sets of β-hairpins. The consistency of the usage of the β-hairpin throughout the outer membrane milieu allows for interrogation of the evolution of these repetitive structures. Here we describe recent investigations of outer membrane protein evolution and how evolutionary precepts have been used for novel outer membrane protein design.

Indexed as

Bacterial Outer Membrane ProteinsBacterial Outer Membrane Proteins

Identifiers

PMID33493965
PMCPMC8222147

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.