Evidence map›Paper›PMID 10893256›Full record

ArticleThe Journal of cell biology2000

Role of the cytoplasmic segments of Sec61alpha in the ribosome-binding and translocation-promoting activities of the Sec61 complex.

D Raden, W Song, R Gilmore

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

27 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein translocation across the rough endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013
    Review
  9. Article
  10. Article
  11. SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

3 authors at 1 institution in 1 country.

D RadenDepartment of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655-0103, USA.
W Song
R Gilmore
University of Massachusetts Chan Medical School · US

Funding

PROTEIN TRANSLOCATION ACROSS THE ENDOPLASMIC RETICULUMR01GM035687 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1985 to 2019
$5.9M
NIGMS NIH HHS GM 35687NIGMS NIH HHS R01 GM035687
6 · The paper itself

Abstract

The Sec61 complex performs a dual function in protein translocation across the RER, serving as both the high affinity ribosome receptor and the translocation channel. To define regions of the Sec61 complex that are involved in ribosome binding and translocation promotion, ribosome-stripped microsomes were subjected to limited digestions using proteases with different cleavage specificities. Protein immunoblot analysis using antibodies specific for the NH(2) and COOH terminus of Sec61alpha was used to map the location of proteolysis cleavage sites. We observed a striking correlation between the loss of binding activity for nontranslating ribosomes and the digestion of the COOH- terminal tail or cytoplasmic loop 8 of Sec61alpha. The proteolyzed microsomes were assayed for SRP-independent translocation activity to determine whether high affinity binding of the ribosome to the Sec61 complex is a prerequisite for nascent chain transport. Microsomes that do not bind nontranslating ribosomes at physiological ionic strength remain active in SRP-independent translocation, indicating that the ribosome binding and translocation promotion activities of the Sec61 complex do not strictly correlate. Translocation-promoting activity was most severely inhibited by cleavage of cytosolic loop 6, indicating that this segment is a critical determinant for this function of the Sec61 complex.

Indexed as

AnimalsBinding SitesBiological TransportCytoplasmDogsMacromolecular SubstancesMembrane ProteinsMicrosomesPancreasPeptide Chain Initiation, TranslationalPeptide HydrolasesProtein BindingProtein Structure, TertiaryRibosomesSEC Translocation ChannelsSeedsMacromolecular SubstancesMembrane ProteinsPeptide HydrolasesSEC Translocation ChannelsSignal Recognition ParticleThermolysin

Identifiers

PMID10893256
PMCPMC2185549
OpenAlexW2105596373

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.