Evidence map›Paper›PMID 12192075›Full record

ArticleProtein science : a publication of the Protein Society2002

The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes.

Yufeng Zhai, Milton H Saier

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 110 citations in OpenAlex.

  1. General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  2. Article
  3. Article
  4. Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021
    Review
  5. Review
  6. Review
  7. Article
  8. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    Review
  9. Article
  10. Article
  11. Charge asymmetry in the proteins of the outer membrane.Bioinformatics (Oxford, England) · 2013
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Isolation of improved free fatty acid overproducing strains ofEnvironmental progress & sustainable energy · 2012
    Article
  17. Article
  18. Article
  19. Article
  20. 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 at 1 institution in 1 country.

Yufeng ZhaiDepartment of Biology, University of California at San Diego, La Jolla, California 92093-0116, USA.
Milton H Saier
University of California, San Diego · US

Funding

ENCYCLOPEDIA OF E COLI GENES AND METABOLISMR01RR007861 · NCRR · SRI INTERNATIONAL · PI KARP, PETER D · 1992 to 2005
$4.0M
Mechanism of Carbohydrate Transport in BacteriaR01GM064368 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 2001 to 2004
$1.4M
NCRR NIH HHS R01 RR007861NCRR NIH HHS RR07861NIGMS NIH HHS GM64368NIGMS NIH HHS R01 GM064368
6 · The paper itself

Abstract

Many outer membrane proteins (OMPs) in Gram-negative bacteria possess known beta-barrel three-dimensional (3D) structures. These proteins, including channel-forming transmembrane porins, are diverse in sequence but exhibit common structural features. We here report computational analyses of six outer membrane proteins of known 3D structures with respect to (1) secondary structure, (2) hydropathy, and (3) amphipathicity. Using these characteristics, as well as the presence of an N-terminal targeting sequence, a program was developed allowing prediction of integral membrane beta-barrel proteins encoded within any completely sequenced prokaryotic genome. This program, termed the beta-barrel finder (BBF) program, was used to analyze the proteins encoded within the Escherichia coli genome. Out of 4290 sequences examined, 118 (2.8%) were retrieved. Of these, almost all known outer membrane proteins with established beta-barrel structures as well as many probable outer membrane proteins were identified. This program should be useful for predicting the occurrence of outer membrane proteins in bacteria with completely sequenced genomes.

Indexed as

Protein Structure, SecondarySoftwareBacterial Outer Membrane ProteinsDatabases, ProteinEscherichia coliGenomeProtein Sorting SignalsSequence Homology, Amino AcidBacterial Outer Membrane ProteinsProtein Sorting Signals

Identifiers

PMID12192075
PMCPMC2373602
OpenAlexW2128298966

What OpenQuestion holds

Textmetadata
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.