Evidence map›Paper›PMID 10930451›Full record

ArticleMolecular biology of the cell2000

Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum.

L Roy, J J Bergeron, C Lavoie, R Hendriks, J Gushue, A Fazel, A Pelletier, D J Morré, V N Subramaniam, W Hong and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Review
  7. Article
  8. Review
  9. UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer.International journal of molecular sciences · 2016
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. AAA ATPase p97/VCP: cellular functions, disease and therapeutic potential.Journal of cellular and molecular medicine · 2008
    Article
  17. Article
  18. Review
  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

11 authors at 6 institutions in 5 countries.

L RoyDépartement de Pathologie et Biologie Cellulaire, Faculté de Médecine, Université de Montréal, Québec, Canada.
J J Bergeron
C Lavoie
R Hendriks
J Gushue
A Fazel
A Pelletier
D J Morré
V N Subramaniam
W Hong
J Paiement
Université de Montréal · CAMcGill University · CAHeidelberg University · DEInstitute of Molecular and Cell Biology · SGPurdue University West Lafayette · USQIMR Berghofer Medical Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transitional endoplasmic reticulum (tER) consists of confluent rough and smooth endoplasmic reticulum (ER) domains. In a cell-free incubation system, low-density microsomes (1.17 g cc(-1)) isolated from rat liver homogenates reconstitute tER by Mg(2+)GTP- and Mg(2+)ATP-hydrolysis-dependent membrane fusion. The ATPases associated with different cellular activities protein p97 has been identified as the relevant ATPase. The ATP depletion by hexokinase or treatment with either N-ethylmaleimide or anti-p97 prevented assembly of the smooth ER domain of tER. High-salt washing of low-density microsomes inhibited assembly of the smooth ER domain of tER, whereas the readdition of purified p97 with associated p47 promoted reconstitution. The t-SNARE syntaxin 5 was observed within the smooth ER domain of tER, and antisyntaxin 5 abrogated formation of this same membrane compartment. Thus, p97 and syntaxin 5 regulate assembly of the smooth ER domain of tER and hence one of the earliest membrane differentiated components of the secretory pathway.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsAntibodiesCell-Free SystemEndoplasmic Reticulum, RoughEndoplasmic Reticulum, SmoothEnzyme InhibitorsEthylmaleimideGuanosine TriphosphateHexokinaseIntracellular MembranesMembrane FusionMembrane ProteinsMicroscopy, ElectronMicrosomes, LiverAdenosine TriphosphatasesAdenosine TriphosphateAntibodiesEnzyme InhibitorsEthylmaleimideGuanosine TriphosphateHexokinaseMembrane ProteinsNuclear Proteinsp97 ATPaseQa-SNARE Proteins

Identifiers

PMID10930451
PMCPMC14937
OpenAlexW2113324555

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.