Evidence map›Paper›PMID 10781078›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery.

H Tian, D Boyd, J Beckwith

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 85 citations in OpenAlex.

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  15. Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  16. Review
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  20. A channel connecting the mother cell and forespore during bacterial endospore formation.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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 1 institution in 1 country.

H TianDepartment of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
D Boyd
J Beckwith
Harvard University · US

Funding

MEMBRANE PROTEINS INVOLVED IN CELL DIVISION IN E.COLIR01GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN · 1987 to 2005
$2.1M
INSERTION AND TOPOLOGY OF MEMBRANE PROTEINSR37GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN R · 1987 to 1996
–
NIGMS NIH HHS GM38922NIGMS NIH HHS R01 GM038922
6 · The paper itself

Abstract

We describe an Escherichia coli genetic screen that yields mutations affecting two different cellular processes: disulfide bond formation and membrane protein assembly. The mutants defective in disulfide bond formation include additional classes of dsbA and dsbB mutations. The membrane protein assembly defective mutants contain a mutation in the secA operon and three mutations in the ffs gene, which encodes 4.5S RNA. These latter mutations are the only ones to be isolated in a gene encoding a component of the bacterial signal recognition particle by screening in vivo for defects in membrane protein insertion. A sensitive method for examining membrane protein localization shows that the ffs and secA locus mutations affect membrane assembly of the polytopic membrane protein, MalF. The ffs mutations also affect the membrane insertion of the FtsQ and the AcrB proteins. Although both the ffs and the secA locus mutations interfere with membrane protein assembly, only the latter also reduces export of a protein containing a cleavable signal sequence.

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsMutationAdenosine TriphosphatasesBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsEscherichia coliMembrane ProteinsModels, MolecularOperonPlasmidsProtein ConformationProtein Disulfide-IsomerasesRecombinant Fusion ProteinsSecA ProteinsAdenosine TriphosphatasesBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsDsbB protein, BacteriaEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsOMPA outer membrane proteinsProtein Disulfide-IsomerasesRecombinant Fusion ProteinsSecA ProteinsSEC Translocation ChannelsSignal Recognition Particle

Identifiers

PMID10781078
PMCPMC18301
OpenAlexW2023486256

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.