Evidence map›Paper›PMID 17950636›Full record

ReviewSeminars in cell & developmental biology2007

Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation.

Zlatka Kostova, Yien Che Tsai, Allan M Weissman

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
–field-weighted citation impact
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

93 citing papers in PubMed.

  1. Review
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  17. Review
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  19. Article
  20. EBS7 is a plant-specific component of a highly conserved endoplasmic reticulum-associated degradation system in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article

33 more citing papers are in PubMed but not listed here.

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.

Zlatka KostovaLaboratory of Protein Dynamics and Signaling, Building 560 Room 22-103, Center for Cancer Research, National Cancer Institute at Frederick, National Institutes of Health, MD 21702, United States.
Yien Che Tsai
Allan M Weissman

Funding

REGULATION OF THE T CELL ANTIGEN RECEPTORZ01BC009392 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WEISSMAN, ALLAN M · 1996 to 2008
$1.8M
Intramural NIH HHS Z01 BC009392
6 · The paper itself

Abstract

Endoplasmic reticulum-associated degradation (ERAD) represents the primary means of quality control within the secretory pathway. Critical to this process are ubiquitin protein ligases (E3s) which, together with ubiquitin conjugating enzymes (E2s), mediate the ubiquitylation of proteins targeted for degradation from the ER. In this chapter we review our knowledge of both Saccharomyces cerevisiae and mammalian ERAD ubiquitin ligases. We focus on recent insights into these E3s, their associated proteins and potential mechanisms of action.

Indexed as

AnimalsEndoplasmic ReticulumHumansMammalsProteinsSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID17950636
PMCPMC2200800

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.