Evidence map›Paper›PMID 23585568›Full record

ReviewThe Journal of biological chemistry2013

Structural biology of presenilins and signal peptide peptidases.

Taisuke Tomita, Takeshi Iwatsubo

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.6field-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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Conformational Changes in Transmembrane Domain 4 of Presenilin 1 Are Associated with Altered Amyloid-β 42 Production.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  12. Review
  13. Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Structural biology of presenilin 1 complexes.Molecular neurodegeneration · 2014
    Review
  18. Article
  19. Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

2 authors at 2 institutions in 1 country.

Taisuke TomitaDepartment of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan. taisuke@mol.f.utokyo.ac.jp
Takeshi Iwatsubo
Kumamoto University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Presenilin and signal peptide peptidase are multispanning intramembrane-cleaving proteases with a conserved catalytic GxGD motif. Presenilin comprises the catalytic subunit of γ-secretase, a protease responsible for the generation of amyloid-β peptides causative of Alzheimer disease. Signal peptide peptidase proteins are implicated in the regulation of the immune system. Both protease family proteins have been recognized as druggable targets for several human diseases, but their detailed structure still remains unknown. Recently, the x-ray structures of some archaeal GxGD proteases have been determined. We review the recent progress in biochemical and biophysical probing of the structure of these atypical proteases.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsArchaeaArchaeal ProteinsCatalytic DomainHumansMembrane ProteinsPresenilinsProtein Structure, TertiarySerine EndopeptidasesStructure-Activity RelationshipAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesArchaeal ProteinsMembrane ProteinsPresenilinsSerine Endopeptidasestype I signal peptidaseIntramembrane ProteolysisMembrane ProteinsPresenilinProteolytic EnzymesSecretases

Identifiers

PMID23585568
PMCPMC3663492
OpenAlexW1980666220

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.