Evidence map›Paper›PMID 28811933›Full record

ReviewCell death discovery2017

Nuclear matrix metalloproteinases: functions resemble the evolution from the intracellular to the extracellular compartment.

Yingqiu Xie, Aidana Mustafa, Adina Yerzhan, Dalmira Merzhakupova, Perizat Yerlan, Askarbek N Orakov, Xiao Wang, Yi Huang, Lixia Miao

Open access · goldAbstract readReview
In one paragraph

Review in Cell death discovery, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. IL-17 Class Inhibitors and Plaque Psoriasis: Not All Biologics Relapse Equally.The Journal of clinical and aesthetic dermatology · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Oncogenic Functions of Alternatively SplicedInternational journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. Importance of Metalloproteinase 8 (MMP-8) in the Diagnosis of Periodontitis.International journal of molecular sciences · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
    Review
  19. Article
  20. 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

9 authors at 4 institutions in 2 countries.

Yingqiu XieDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Aidana MustafaDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Adina YerzhanDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Dalmira MerzhakupovaDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Perizat YerlanDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Askarbek N OrakovDepartment of Biology, School of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Xiao WangShandong Analysis and Test Center, Shandong Academy of Sciences, 19 Keyuan Street, Jinan 250014, China.
Yi HuangDepartment of Urology, Shenzhen University Luohu Hospital, Shenzhen Following Precision Medical Research Institute, Luohu Hospital Group, Shenzhen 51800, China.
Lixia MiaoCollege of Basic Medicine, Wuhan University, Wuhan 430071, China.
Nazarbayev University · KZShandong Academy of Sciences · CNShenzhen Luohu People's Hospital · CNWuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteinase (MMP) is defined as an endopeptidase in the extracellular matrix (ECM), which plays essential roles in physiological processes such as organogenesis, wound healing, angiogenesis, apoptosis and motility. MMPs are produced and assembled in the cytoplasm as proenzymes with a cytoplasmic domain and require extracellular activation. MMPs can degrade receptors, extracellular matrix proteins, PARPs and release apoptotic substances. MMPs have been found in the cytosol, organelles and extracellular compartments and recently many types of MMPs have been found in the nucleus. However, the mechanisms and roles of MMPs inside the cell nucleus are still poorly understood. Here we summarized the nuclear localization mechanisms of MMPs and their functions in the nucleus such as apoptosis, tissue remodeling upon injury and cancer progression. Most importantly, we found that nuclear MMPs have evolved to translocate to membrane and target ECM possibly through evolution of nuclear localization signal (NLS), natural selection and anti-apoptotic survival. Thus, the knowledge about the evolution and regulation of nuclear MMPs appears to be essential in understanding a variety of cellular processes along with the development of MMP-targeted therapeutic drugs against the progression of certain diseases.

Identifiers

PMID28811933
PMCPMC5554797
OpenAlexW2746421487

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.