Evidence map›Paper›PMID 22027825›Full record

ReviewThe Journal of biological chemistry2011

Metalloproteinases in Drosophila to humans that are central players in developmental processes.

Alison Muir, Daniel S Greenspan

Open access · hybridAbstract readReview
In one paragraph

Review 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. PCPE1 and PCPE2: When Sequence Similarity Masks Functional Diversity.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  2. BMP Signaling: Lighting up the Way for Embryonic Dorsoventral Patterning.Frontiers in cell and developmental biology · 2021
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. BMP1-like proteinases are essential to the structure and wound healing of skin.Matrix biology : journal of the International Society for Matrix Biology · 2016
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Production and crystallization of the C-propeptide trimer from human procollagen III.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  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 at 1 institution in 1 country.

Alison MuirDepartment of Cell and Regenerative Biology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53792.
Daniel S GreenspanDepartment of Cell and Regenerative Biology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53792. Electronic address: dsgreens@wisc.edu.
University of Wisconsin–Madison · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007133 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PERNA, NICOLE T · 1985 to 2023
$16.5M
Molecular Biology Of Collagen Type VR01AR047746 · NIAMS · UNIVERSITY OF WISCONSIN-MADISON · PI GREENSPAN, DANIEL S · 2001 to 2013
$3.0M
PROCOLLAGEN C-PROTEINASE ENHANCERS: IN VIVO ROLESR01AR053815 · NIAMS · UNIVERSITY OF WISCONSIN-MADISON · PI GREENSPAN, DANIEL S · 2006 to 2010
$1.9M
NIAMS NIH HHS AR53815NIAMS NIH HHS R01 AR047746NIAMS NIH HHS R01 AR053815NIGMS NIH HHS T32 GM007133
6 · The paper itself

Abstract

Many secreted proteins are synthesized as precursors with propeptides that must be cleaved to yield the mature functional form of the molecule. In addition, various growth factors occur in extracellular latent complexes with protein antagonists and are activated upon cleavage of such antagonists. Research in the separate fields of embryonic patterning and extracellular matrix formation has identified members of the BMP1/Tolloid-like family of metalloproteinases as key players in these types of biosynthetic processing events in species ranging from Drosophila to humans.

Indexed as

Gene Expression Regulation, DevelopmentalAnimalsBone Morphogenetic Protein 1CollagenDrosophila melanogasterExtracellular MatrixHumansInsulin-Like Growth Factor IIntercellular Signaling Peptides and ProteinsMetalloproteasesProtein Structure, TertiaryTransforming Growth Factor betaXenopus laevisASTL protein, humanBone Morphogenetic Protein 1CollagenInsulin-Like Growth Factor IIntercellular Signaling Peptides and ProteinsMetalloproteasesTransforming Growth Factor beta

Identifiers

PMID22027825
PMCPMC3234945
OpenAlexW1977165921

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.