Evidence map›Paper›PMID 39161580›Full record

ArticleBiochemistry and biophysics reports2024

Unconventional localization of PAI-1 in PML bodies: A possible link with cellular growth of endothelial cells.

Pragya Gehlot, Daniela Brünnert, Vibha Kaushik, Arpana Yadav, Saloni Bage, Kritika Gaur, Mahesh Saini, Jens Ehrhardt, Gowrang Kasaba Manjunath, Abhishek Kumar and 4 more

Abstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

14 authors.

Pragya GehlotDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Daniela BrünnertUniversity Hospital of Würzburg, Department of Obstetrics and Gynecology, Josef-Schneider-Str. 4, D-97080, Würzburg, Germany.
Vibha KaushikDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Arpana YadavDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Saloni BageDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Kritika GaurDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Mahesh SainiDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.
Jens EhrhardtDepartment of Obstetrics and Gynecology, University of Greifswald, Ferdinand-Sauerbruchstrasse, D-17489, Greifswald, Germany.
Gowrang Kasaba ManjunathManipal Academy of Higher Education (MAHE), Manipal, 576104, Karnataka, India.
Abhishek KumarManipal Academy of Higher Education (MAHE), Manipal, 576104, Karnataka, India.
Neena KasliwalDepartment of Pathology, J.L.N. Medical College, Ajmer, 305001, Rajasthan, India.
Ajay Kumar SharmaDepartment of Obstetrics and Gynecology, J.L.N. Medical College, Ajmer, 305001, Rajasthan, India.
Marek ZygmuntDepartment of Obstetrics and Gynecology, University of Greifswald, Ferdinand-Sauerbruchstrasse, D-17489, Greifswald, Germany.
Pankaj GoyalDepartment of Biotechnology, School of Life Sciences, Central University of Rajasthan, Bandarsindri, Kishangarh, 305 817, Rajasthan, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasminogen activator inhibitor-1 (PAI-1/Serpin E1) is classically known for its antifibrinolytic activity via inhibiting uPA and tPA of the fibrinolytic pathway. PAI-1 has a paradoxical role in tumor progression, and its molecular functions are poorly understood. PAI-1 is a widely accepted secretory protease inhibitor, however, a study suggested the localization of PAI-1 in the cytoplasm and the nucleus. Besides the plethora of its biological functions as a secretory protein, intracellular localization, and functions of PAI-1 remain unexplored at the molecular level. In this study, using various

Indexed as

CRM1Endothelial cellsPAI-1PMLSenescenceSerpin E1

Identifiers

PMID39161580
PMCPMC11332193

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