Evidence map›Paper›PMID 23539602›Full record

ArticleScience (New York, N.Y.)2013

Structure of the integral membrane protein CAAX protease Ste24p.

Edward E Pryor, Peter S Horanyi, Kathleen M Clark, Nadia Fedoriw, Sara M Connelly, Mary Koszelak-Rosenblum, Guangyu Zhu, Michael G Malkowski, Michael C Wiener, Mark E Dumont

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Improvement of silage characteristics ofFrontiers in microbiology · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. OMA1-An integral membrane protease?Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  13. Article
  14. Reversible autoinhibitory regulation ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Overview ofIndian journal of microbiology · 2020
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Edward E PryorMembrane Protein Structural Biology Consortium, USA.
Peter S Horanyi
Kathleen M Clark
Nadia Fedoriw
Sara M Connelly
Mary Koszelak-Rosenblum
Guangyu Zhu
Michael G Malkowski
Michael C Wiener
Mark E Dumont
University at Buffalo, State University of New York · USUniversity of Rochester · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
Multi-Level Optimization of Membrane Proteins for CrystallographyU54GM094611 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI DUMONT, MARK E. · 2010 to 2014
$6.3M
NCI NIH HHS P30 CA044579NIGMS NIH HHS U54 GM094611
6 · The paper itself

Abstract

Posttranslational lipidation provides critical modulation of the functions of some proteins. Isoprenoids (i.e., farnesyl or geranylgeranyl groups) are attached to cysteine residues in proteins containing C-terminal CAAX sequence motifs (where A is an aliphatic residue and X is any residue). Isoprenylation is followed by cleavage of the AAX amino acid residues and, in some cases, by additional proteolytic cuts. We determined the crystal structure of the CAAX protease Ste24p, a zinc metalloprotease catalyzing two proteolytic steps in the maturation of yeast mating pheromone a-factor. The Ste24p core structure is a ring of seven transmembrane helices enclosing a voluminous cavity containing the active site and substrate-binding groove. The cavity is accessible to the external milieu by means of gaps between splayed transmembrane helices. We hypothesize that cleavage proceeds by means of a processive mechanism of substrate insertion, translocation, and ejection.

Indexed as

Amino Acid SequenceCatalytic DomainCell MembraneCrystallography, X-RayMembrane ProteinsMetalloendopeptidasesMolecular Sequence DataProtein Structure, SecondarySaccharomyces cerevisiae ProteinsSubstrate SpecificityMembrane ProteinsMetalloendopeptidasesSaccharomyces cerevisiae ProteinsSTE24 protein, S cerevisiae

Identifiers

PMID23539602
PMCPMC4136949
OpenAlexW1977374839

What OpenQuestion holds

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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.