Evidence map›Paper›PMID 9303299›Full record

ArticleThe EMBO journal1997

Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.

B M Wilkinson, Y Esnault, R A Craven, F Skiba, J Fieschi, F K'epès, C J Stirling

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 57 citations in OpenAlex.

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  10. Sss1p is required to complete protein translocon activation.The Journal of biological chemistry · 2010
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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

7 authors at 1 institution in 1 country.

B M WilkinsonSchool of Biological Sciences, University of Manchester, UK.
Y Esnault
R A Craven
F Skiba
J Fieschi
F K'epès
C J Stirling
University of Manchester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The heterotrimeric Sec61p complex is a key component of the protein translocation apparatus of the endoplasmic reticulum membrane. The complex characterized from yeast includes Sec61p, a 10-transmembrane-domain membrane protein which has a direct interaction with Sss1p, a small C-terminal anchor protein. In order to gain some insight into the architecture of this complex we have functionally expressed Sec61p as complementary N- and C-terminal fragments. Chemical crosslinking of Sss1p to specific Sec61p fragments in these functional combinations and suppression of sec61 mutants by over-expression of Sss1p have led to identification of the region which includes transmembrane domains TM6, TM7 and TM8 (amino acid residues L232-R406) of Sec61p as a major site of interaction with Sss1p.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceBiological Transport, ActiveCross-Linking ReagentsDNA PrimersEndoplasmic ReticulumEscherichia coliFungal ProteinsMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataMutationPeptide FragmentsProtein ConformationSaccharomyces cerevisiaeCross-Linking ReagentsDNA PrimersFungal ProteinsMembrane ProteinsMembrane Transport ProteinsPeptide FragmentsSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation ChannelsSSS1 protein, S cerevisiae

Identifiers

PMID9303299
PMCPMC1170081
OpenAlexW2015320294

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.