Evidence map›Paper›PMID 7670368›Full record

ReviewProtein science : a publication of the Protein Society1995

The astacin family of metalloendopeptidases.

J S Bond, R J Beynon

Open access · greenAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

115 citing papers in PubMed, 403 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Meprin β Modulates Brevican Proteolysis Impairing Neural Plasticity and Memory Formation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Isolation and evaluation of aFrontiers in bioengineering and biotechnology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Emerging role of BMPs/BMPR2 signaling pathway in treatment for pulmonary fibrosis.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2024
    Review
  10. Article
  11. Article
  12. Role ofFrontiers in microbiology · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

55 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

J S BondDepartment of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey 17033, USA.
R J Beynon
University of Manchester · GB

Funding

MEPRINS-METALLOPROTEINSASES OF THE KIDNEY AND INTESTINER01DK019691 · NIDDK · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI BOND, JUDITH S · 1986 to 2010
$3.1M
MEPRINS - METALLOPROTEINASES OF THE KIDNEY AND INTESTINER56DK019691 · NIDDK · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI BOND, JUDITH S · 2005 to 2005
$73k
INTRACELLULAR PROTEIN CATABOLISM IN DIABETES MELLITUSR37DK019691 · NIDDK · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI BOND, JUDITH S · 1989 to 1996
–
NIDDK NIH HHS DK 19691Wellcome Trust
6 · The paper itself

Abstract

The astacin family of metalloendopeptidases was recognized as a novel family of proteases in the 1990s. The crayfish enzyme astacin was the first characterized and is one of the smallest members of the family. More than 20 members of the family have now been identified. They have been detected in species ranging from hydra to humans, in mature and in developmental systems. Proposed functions of these proteases include activation of growth factors, degradation of polypeptides, and processing of extracellular proteins. Astacin family proteases are synthesized with NH2-terminal signal and proenzyme sequences, and many (such as meprins, BMP-1, tolloid) contain multiple domains COOH-terminal to the protease domain. They are either secreted from cells or are plasma membrane-associated enzymes. They have some distinguishing features in addition to the signature sequence in the protease domain: HEXXHXXGFXHEXXRXDR. They have a unique type of zinc binding, with pentacoordination, and a protease domain tertiary structure that contains common attributes with serralysins, matrix metalloendopeptidases, and snake venom proteases; they cleave peptide bonds in polypeptides such as insulin B chain and bradykinin and in proteins such as casein and gelatin; and they have arylamidase activity. Meprins are unique proteases in the astacin family, and indeed in the animal kingdom, in their oligomeric structure; they are dimers of disulfide-linked dimers and are highly glycosylated, type I integral membrane proteins that have many attributes of receptors or integrins with adhesion, epidermal growth factor-like, and transmembrane domains. The alpha and beta subunits are differentially expressed and processed to yield latent and active proteases as well as membrane-associated and secreted forms. Meprins represent excellent models of hetero- and homo-oligomeric enzymes that are regulated at the transcriptional and posttranslational levels.

Indexed as

MetalloendopeptidasesAmino Acid SequenceBinding SitesMacromolecular SubstancesModels, MolecularMolecular Sequence DataProtein Structure, TertiaryZincastacinMacromolecular SubstancesMetalloendopeptidasesZinc

Identifiers

PMID7670368
PMCPMC2143163
OpenAlexW2122266747

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.