Evidence map›Paper›PMID 11406580›Full record

ArticleThe EMBO journal2001

Molecular markers of serine protease evolution.

M M Krem, E Di Cera

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Homology-based identification and structural analysis ofComputational and structural biotechnology journal · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Thrombin has dual trypsin-like and chymotrypsin-like specificity.Journal of thrombosis and haemostasis : JTH · 2024
    Article
  10. Article
  11. Comparative sequence analysis of vitamin K-dependent coagulation factors.Journal of thrombosis and haemostasis : JTH · 2022
    Article
  12. Article
  13. Subtilisin ofCurrent issues in molecular biology · 2022
    Article
  14. The active site region plays a critical role in NaThe Journal of biological chemistry · 2022
    Article
  15. Biomaterials-Mediated Tumor Infarction Therapy.Frontiers in bioengineering and biotechnology · 2022
    Review
  16. Article
  17. Article
  18. Review
  19. 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.

M M KremDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St Louis, MO 63110-1093, USA.
E Di Cera

Funding

STUDIES ON THROMBIN ALLOSTERYR01HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI Enrico Di Cera · 2000 to 2026
$9.6M
Studies on Na+ binding to thrombinR01HL058141 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 1997 to 2010
$4.7M
BIOPHYSICAL STUDIES OF THROMBINR29HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 1995 to 1999
–
NHLBI NIH HHS HL49413NHLBI NIH HHS HL58141NHLBI NIH HHS R01 HL049413NHLBI NIH HHS R01 HL058141NHLBI NIH HHS R29 HL049413
6 · The paper itself

Abstract

The evolutionary history of serine proteases can be accounted for by highly conserved amino acids that form crucial structural and chemical elements of the catalytic apparatus. These residues display non- random dichotomies in either amino acid choice or serine codon usage and serve as discrete markers for tracking changes in the active site environment and supporting structures. These markers categorize serine proteases of the chymotrypsin-like, subtilisin-like and alpha/beta-hydrolase fold clans according to phylogenetic lineages, and indicate the relative ages and order of appearance of those lineages. A common theme among these three unrelated clans of serine proteases is the development or maintenance of a catalytic tetrad, the fourth member of which is a Ser or Cys whose side chain helps stabilize other residues of the standard catalytic triad. A genetic mechanism for mutation of conserved markers, domain duplication followed by gene splitting, is suggested by analysis of evolutionary markers from newly sequenced genes with multiple protease domains.

Indexed as

Evolution, MolecularChymotrypsinHydrolasesPhylogenySerine EndopeptidasesSubtilisinChymotrypsinHydrolasesSerine EndopeptidasesSubtilisin

Identifiers

PMID11406580
PMCPMC150214

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.