Evidence map›Paper›PMID 21832066›Full record

ArticleThe Journal of biological chemistry2011

Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes.

Neil David Rawlings, Alan John Barrett, Alex Bateman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.

  1. Pooled it
  2. Incorporation of Multiple βACS central science · 2024
    Article
  3. Article
  4. Review
  5. Eosinophilic Chronic Rhinosinusitis and Pathogenic Role of Protease.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Approaches to Avoid Proteolysis During Protein Expression and Purification.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. How to use the MEROPS database and website to help understand peptidase specificity.Protein science : a publication of the Protein Society · 2021
    Article
  15. Article
  16. Article
  17. Origins of peptidases.Biochimie · 2019
    Article
  18. Article
  19. Article
  20. Review
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 at 1 institution in 1 country.

Neil David RawlingsWellcome Trust Genome Campus, The Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, United Kingdom. Electronic address: ndr@sanger.ac.uk.
Alan John BarrettWellcome Trust Genome Campus, The Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, United Kingdom.
Alex BatemanWellcome Trust Genome Campus, The Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, United Kingdom.
Wellcome Sanger Institute · GB

Funding

Wellcome TrustWellcome Trust WT077044/Z/05/Z
6 · The paper itself

Abstract

The terms "proteolytic enzyme" and "peptidase" have been treated as synonymous, and all proteolytic enzymes have been considered to be hydrolases (EC 3.4). However, the recent discovery of proteins that cleave themselves at asparagine residues indicates that not all peptide bond cleavage occurs by hydrolysis. These self-cleaving proteins include the Tsh protein precursor of Escherichia coli, in which the large C-terminal propeptide acts as an autotransporter; certain viral coat proteins; and proteins containing inteins. Proteolysis is the action of an amidine lyase (EC 4.3.2). These proteolytic enzymes are also the first in which the nucleophile is an asparagine, defining the seventh proteolytic catalytic type and the first to be discovered since 2004. We have assembled ten families based on sequence similarity in which cleavage is thought to be catalyzed by an asparagine.

Indexed as

Amino Acid MotifsAsparagineBiological TransportCatalysisEscherichia coliLyasesModels, MolecularMultigene FamilyPeptide HydrolasesPeptidesProtein ConformationProtein Processing, Post-TranslationalProtein Structure, TertiaryAsparagineLyasesPeptide HydrolasesPeptides

Identifiers

PMID21832066
PMCPMC3207474
OpenAlexW2020306031

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.