Evidence map›Paper›PMID 9294424›Full record

ArticleJournal of bacteriology1997

In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase.

E H Manting, C van der Does, A J Driessen

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. 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.

E H MantingDepartment of Microbiology, University of Groningen, Haren, The Netherlands.
C van der Does
A J Driessen
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Precursor protein translocation across the Escherichia coli inner membrane is mediated by the translocase, which is composed of a heterotrimeric integral membrane protein complex with SecY, SecE, and SecG as subunits and peripherally bound SecA. Cross-linking experiments were conducted to study which proteins are associated with SecA in vivo. Formaldehyde treatment of intact cells results in the specific cross-linking of SecA to SecY. Concurrently with the increased membrane association of SecA, an elevated amount of cross-linked product was obtained in cells harboring overproduced SecYEG complex. Cross-linked SecA copurified with hexahistidine-tagged SecY and not with SecE. The data indicate that SecA and SecY coexist as a stable complex in the cytoplasmic membrane in vivo.

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsBiological TransportCell MembraneCross-Linking ReagentsEscherichia coliMolecular WeightRecombinant ProteinsSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCross-Linking ReagentsEscherichia coli ProteinsMembrane Transport ProteinsRecombinant ProteinsSecA ProteinsSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID9294424
PMCPMC179456
OpenAlexW1910636673

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.