Evidence map›Paper›PMID 11023840›Full record

ArticleThe Biochemical journal2000

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.

C P Ponting

Abstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
  8. Article
  9. The cholangiocyte primary cilium in health and disease.Biochimica et biophysica acta. Molecular basis of disease · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
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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

1 author.

C P PontingMRC Functional Genetics Unit, Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, UK. Chris.Ponting@anat.ox.ac.uk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sequence database searches, using iterative-profile and Hidden-Markov-model approaches, were used to detect hitherto-undetected homologues of proteins that regulate the endoplasmic reticulum (ER)-associated degradation pathway. The translocon-associated subunit Sec63p (Sec=secretory) was shown to contain a domain of unknown function found twice in several Brr2p-like RNA helicases (Brr2=bad response to refrigeration 2). Additionally, Cue1p (Cue=coupling of ubiquitin conjugation to ER degradation), a yeast protein that recruits the ubiquitin-conjugating (UBC) enzyme Ubc7p to an ER-associated complex, was found to be one of a large family of putative scaffolding-domain-containing proteins that include the autocrine motility factor receptor and fungal Vps9p (Vps=vacuolar protein sorting). Two other yeast translocon-associated molecules, Sec72p and Hrd3p (Hrd=3-hydroxy-3-methylglutaryl-CoA reductase degradation), were shown to contain multiple tetratricopeptide-repeat-like sequences. From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein). Finally, the luminal portion of Ire1p (Ire=high inositol-requiring), thought to convey the sensing function of this transmembrane kinase and endoribonuclease, was shown to contain repeats similar to those in beta-propeller proteins. This finding hints at the mechanism by which Ire1p may sense extended unfolded proteins at the expense of compact folded molecules.

Indexed as

Heat-Shock ProteinsMembrane Transport ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsAmino Acid SequenceCarrier ProteinsDatabases, FactualEndoplasmic ReticulumFungal ProteinsMarkov ChainsMembrane GlycoproteinsMembrane ProteinsModels, BiologicalMolecular Sequence DataProtein FoldingProtein Structure, TertiaryBRR2 protein, S cerevisiaeCarrier ProteinsCUE1 protein, S cerevisiaeFungal ProteinsHeat-Shock ProteinsHRD3 protein, S cerevisiaeIRE1 protein, S cerevisiaeMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsProtein Serine-Threonine KinasesRepressor ProteinsRNA HelicasesSaccharomyces cerevisiae ProteinsSEC63 protein, S cerevisiaeSEC72 protein, S cerevisiae

Identifiers

PMID11023840
PMCPMC1221390

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.