Evidence map›Paper›PMID 28347746›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2017

Matrix metalloproteinases - From the cleavage data to the prediction tools and beyond.

Piotr Cieplak, Alex Y Strongin

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. IGF-II regulates lysyl oxidase propeptide and mediates its effects in part via basic helix-loop-helix E40.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Predicting Proteolysis in Complex Proteomes Using Deep Learning.International journal of molecular sciences · 2021
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  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.

Piotr CieplakCancer Research Center, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037, USA. Electronic address: pcieplak@sbpdiscovery.org.
Alex Y StronginCancer Research Center, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037, USA. Electronic address: strongin@sbpdiscovery.org.
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

Proteolysis of Myelin as a Source of Neuropathic PainR01DE022757 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHUBAYEV, VERONICA · 2012 to 2022
$7.3M
METALLOPROTEINASES IN TUMOR NEOVASCULARIZATIONR01CA083017 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2014
$3.8M
MT1-MMP pericellular proteolysis in malignancyR01CA077470 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2009
$3.1M
Proteolysis in silico: statistics, structural chemistry, and biologyR01GM098835 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI CIEPLAK, PIOTR · 2011 to 2014
$1.5M
NCI NIH HHS R01 CA077470NCI NIH HHS R01 CA083017NIDCR NIH HHS R01 DE022757NIGMS NIH HHS R01 GM098835
6 · The paper itself

Abstract

Understanding the physiological role of any protease requires identification of both its cleavage substrates and their relative cleavage efficacy as compared with other substrates and other proteinases. Our review manuscript is focused on the cleavage preferences of the individual matrix metalloproteinases (MMPs) and the cleavage similarity and distinction that exist in the human MMP family. The recent in-depth analysis of MMPs by us and many others greatly increased knowledge of the MMP biology and structural-functional relationships among this protease family members. A better knowledge of cleavage preferences of MMPs has led us to the development of the prediction tools that are now capable of the high throughput reliable prediction and ranking the MMP cleavage sites in the peptide sequences in silico. Our software unifies and consolidates volumes of the pre-existing data. Now this prediction-ranking in silico tool is ready to be used by others. The software we developed may facilitate both the identification of the novel proteolytic regulatory pathways and the discovery of the previously uncharacterized substrates of the individual MMPs. Because now the MMP research may be based on the mathematical probability parameters rather than on either random luck or common sense alone, the researchers armed with this novel in silico tool will be better equipped to fine-tune or, at least, to sharply focus their wet chemistry experiments. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman.

Indexed as

ProteolysisSequence Analysis, ProteinSoftwareAnimalsHumansMatrix MetalloproteinasesMatrix Metalloproteinasescleavage prediction toolsCleavPredictmatrix metalloproteinasesMMPssoftwaresubstrate cleavagesubstrate phage display

Identifiers

PMID28347746
PMCPMC5831720
OpenAlexW2599651054

What OpenQuestion holds

Textmetadata
LicenceTDM
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.