Evidence map›Paper›PMID 27630193›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Distinct biological events generated by ECM proteolysis by two homologous collagenases.

Inna Solomonov, Eldar Zehorai, Dalit Talmi-Frank, Sharon G Wolf, Alla Shainskaya, Alina Zhuravlev, Elena Kartvelishvily, Robert Visse, Yishai Levin, Nir Kampf and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Matrix degradation enhances stress relaxation, regulating cell adhesion and spreading.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Degradability tunes ECM stress relaxation and cellular mechanics.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. [Research advances of collagen-based biomaterials in wound repair].Zhonghua shao shang yu chuang mian xiu fu za zhi · 2024
    Review
  11. Bidirectionally validatedFrontiers in bioengineering and biotechnology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Role of matrix metalloproteinase in wound healing.American journal of translational research · 2022
    Review
  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

15 authors at 2 institutions in 2 countries.

Inna SolomonovDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel;
Eldar ZehoraiDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel;
Dalit Talmi-FrankDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel; Department of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel;
Sharon G WolfDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 76100, Israel;ORCID 0000-0002-5337-5063
Alla ShainskayaNancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 76100, Israel;
Alina ZhuravlevDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel;
Elena KartvelishvilyDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 76100, Israel;
Robert VisseKennedy Institute of Rheumatology, Nuffield Department of Orthopaedics, Rheumatology, and Musculoskeletal Sciences, University of Oxford, Oxford, OX3 7FY, United Kingdom;
Yishai LevinNancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 76100, Israel;
Nir KampfDepartment of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
Diego Adhemar JaitinDepartment of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel;
Eyal DavidDepartment of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel;
Ido AmitDepartment of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel;
Hideaki NagaseKennedy Institute of Rheumatology, Nuffield Department of Orthopaedics, Rheumatology, and Musculoskeletal Sciences, University of Oxford, Oxford, OX3 7FY, United Kingdom;
Irit SagiDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel; Irit.sagi@weizmann.ac.il.
Weizmann Institute of Science · ILUniversity of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

It is well established that the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Although enzymatic redundancy might be inferred from their close similarity in structure, their in vivo activity can lead to extremely diverse tissue-remodeling outcomes. We observed that proteolysis of collagen-rich natural extracellular matrix (ECM), performed uniquely by individual homologous proteases, leads to distinct events that eventually affect overall ECM morphology, viscoelastic properties, and molecular composition. We revealed striking differences in the motility and signaling patterns, morphology, and gene-expression profiles of cells interacting with natural collagen-rich ECM degraded by different collagenases. Thus, in contrast to previous notions, matrix-remodeling systems are not redundant and give rise to precise ECM-cell crosstalk. Because ECM proteolysis is an abundant biochemical process that is critical for tissue homoeostasis, these results improve our fundamental understanding its complexity and its impact on cell behavior.

Indexed as

ProteolysisSequence Homology, Amino AcidAnimalsCell-Matrix JunctionsCollagenElasticityExtracellular MatrixFibroblastsHumansImaging, Three-DimensionalMatrix Metalloproteinase 1Matrix Metalloproteinase 13Principal Component AnalysisRatsRheologyViscosityCollagenMatrix Metalloproteinase 1Matrix Metalloproteinase 13ECMMMPproteolysis

Identifiers

PMID27630193
PMCPMC5047162
OpenAlexW2520582069

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.