Evidence map›Paper›PMID 19401470›Full record

ReviewThe Journal of biological chemistry2009

Exosite determinants of serpin specificity.

Peter G W Gettins, Steven T Olson

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

49 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. A reactive center loop-based prediction platform to enhance the design of therapeutic SERPINs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Heparin - Messias or Verschlimmbesserung?Journal of thrombosis and haemostasis : JTH · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. SERPINs-From Trap to Treatment.Frontiers in medicine · 2019
    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

2 authors at 2 institutions in 1 country.

Peter G W GettinsDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60612, USA. pgettins@uic.edu
Steven T Olson
Centers for New Horizons · USUniversity of Illinois Chicago · US

Funding

Molecular Basis of Blood Coagulation RegulationR37HL039888 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI OLSON, STEVEN T. · 2010 to 2019
$3.9M
MOLECULAR BASIS OF BLOOD COAGULATION REGULATIONR01HL039888 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI OLSON, STEVEN T. · 1993 to 2009
$3.8M
FUNCTION AND DYSFUNCTION IN HUMAN ANTITHROMBINSR37HL049234 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GETTINS, PETER G.W. · 1998 to 2007
$2.8M
Structural Basis of Serpin Function and RegulationR01HL078827 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI OLSON, STEVEN T. · 2005 to 2009
$1.9M
Structural examination of serpin-protein interactionsR01HL079430 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GETTINS, PETER G.W. · 2005 to 2009
$1.9M
MOLECULAR BASIS OF BLOOD COAGULATION REGULATIONR29HL039888 · NHLBI · HENRY FORD HOSPITAL · PI OLSON, STEVEN T. · 1988 to 1992
–
DYSFUNCTION OF VARIANT HUMAN ANTITHROMBINSR01HL049234 · NHLBI · VANDERBILT UNIVERSITY · PI GETTINS, PETER G.W. · 1993 to 1997
–
NHLBI NIH HHS HL39888NHLBI NIH HHS HL49234NHLBI NIH HHS HL78827NHLBI NIH HHS HL79430NHLBI NIH HHS R01 HL039888NHLBI NIH HHS R01 HL078827NHLBI NIH HHS R01 HL079430NHLBI NIH HHS R37 HL039888NHLBI NIH HHS R37 HL049234
6 · The paper itself

Abstract

Serpins form an enormous superfamily of 40-60-kDa proteins found in almost all types of organisms, including humans. Most are one-use suicide substrate serine and cysteine proteinase inhibitors that have evolved to finely regulate complex proteolytic pathways, such as blood coagulation, fibrinolysis, and inflammation. Despite distinct functions for each serpin, there is much redundancy in the primary specificity-determining residues. However, many serpins exploit additional exosites to generate the exquisite specificity that makes a given serpin effective only when certain other criteria, such as the presence of specific cofactors, are met. With a focus on human serpins, this minireview examines use of exosites by nine serpins in the initial complex-forming phase to modulate primary specificity in either binary serpin-proteinase complexes or ternary complexes that additionally employ a protein or other cofactor. A frequent theme is down-regulation of inhibitory activity unless the exosite(s) are engaged. In addition, the use of exosites by maspin and plasminogen activator inhibitor-1 to indirectly affect proteolytic processes is considered.

Indexed as

Catalytic DomainAnimalsHumansProtease InhibitorsProtein BindingSerpinsSignal TransductionSubstrate SpecificityProtease InhibitorsSerpins

Identifiers

PMID19401470
PMCPMC2742806
OpenAlexW2024273754

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.