Evidence map›Paper›PMID 21570408›Full record

ArticleJournal of molecular biology2011

Expansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1.

Jimin Pei, Douglas A Mitchell, Jack E Dixon, Nick V Grishin

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
  2. Article
  3. Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026
    Article
  4. SpbR controls lipoteichoic acid length by directly inhibiting signal peptidase SpsB inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Journal of bacteriology · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. The Role of SilX in Bacteriocin Production ofFrontiers in microbiology · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Frontiers in cellular and infection microbiology · 2021
    Article
  19. LipoproteinmBio · 2020
    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

4 authors.

Jimin PeiHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390-9050, USA. jpei@chop.swmed.edu
Douglas A Mitchell
Jack E Dixon
Nick V Grishin

Funding

UCSD Cancer Center Training Program in Drug DevelopmentT32CA121938 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Michael Bouvet, Dwayne G. Stupack · 2006 to 2026
$10.3M
Computational methods for structural-functional studies of proteinsR01GM094575 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2010 to 2017
$2.4M
Fic-mediated AdenylylationR01GM090328 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIXON, JACK E, WORBY, CAROLYN ANN · 2010 to 2013
$1.3M
Howard Hughes Medical InstituteNCI NIH HHS T32 CA121938NIGMS NIH HHS 1R01GM094575-01NIGMS NIH HHS 2R01GM090328-06A1NIGMS NIH HHS R01 GM090328NIGMS NIH HHS R01 GM094575
6 · The paper itself

Abstract

Intramembrane proteases are responsible for a number of regulated proteolysis events occurring within or near the plasma and intracellular membranes. Members of one large and diverse family of putative intramembrane metalloproteases are widely distributed in all domains of life, including the type II CAAX prenyl proteases and their prokaryotic homologs with putative bacteriocin-related functions. We used sensitive sequence similarity searches to expand this large CPBP (CAAX proteases and bacteriocin-processing enzymes) family to include more than 5800 members and infer its homologous relationships to several other protein families, including the PrsW proteases, the DUF2324 (DUF, domain of unknown function) family and the γ-secretase subunit APH-1 proteins. They share four predicted core transmembrane segments and possess similar yet distinct sets of sequence motifs. Remote similarity between APH-1 and membrane proteases sheds light on APH-1's evolutionary origin and raises the possibility that APH-1 may possess proteolytic activity in the current or ancestral form of γ-secretase.

Indexed as

Evolution, MolecularMultigene FamilyAmino Acid SequenceAmyloid Precursor Protein SecretasesEndopeptidasesMembrane ProteinsMolecular Sequence DataPeptide HydrolasesProtein SubunitsSequence Homology, Amino AcidAmyloid Precursor Protein SecretasesEndopeptidasesMembrane ProteinsPeptide HydrolasesProtein Subunits

Identifiers

PMID21570408
PMCPMC3155266

What OpenQuestion holds

Textmetadata
LicenceTDM
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.