Evidence map›Paper›PMID 31016177›Full record

ReviewAdvanced biomedical research2019

Reteplase: Structure, Function, and Production.

Elmira Mohammadi, Hooria Seyedhosseini-Ghaheh, Karim Mahnam, Ali Jahanian-Najafabadi, Hamid Mir Mohammad Sadeghi

Open access · goldAbstract readReview
In one paragraph

Review in Advanced biomedical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 28% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Core determinant of theFrontiers in pharmacology · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Thrombolytic Agents: Nanocarriers in Targeted Release.Molecules (Basel, Switzerland) · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. [Transient expression of bioactive recombinant human plasminogen activator in tobacco leaf].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2019
    Article
  15. Article
  16. 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

5 authors at 3 institutions in 1 country.

Elmira MohammadiDepartment of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran.
Hooria Seyedhosseini-GhahehYoung Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Karim MahnamDepartment of Biology, Faculty of Science, Shahrekord University, Shahr-e Kord, Iran.
Ali Jahanian-NajafabadiDepartment of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran.
Hamid Mir Mohammad SadeghiDepartment of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran.
Isfahan University of Medical Sciences · IRIslamic Azad University, Science and Research Branch · IRShahrekord University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thrombolytic drugs activate plasminogen which creates a cleaved form called plasmin, a proteolytic enzyme that breaks the crosslinks between fibrin molecules. The crosslinks create blood clots, so reteplase dissolves blood clots. Tissue plasminogen activator (tPA) is a well-known thrombolytic drug and is fibrin specific. Reteplase is a modified nonglycosylated recombinant form of tPA used to dissolve intracoronary emboli, lysis of acute pulmonary emboli, and handling of myocardial infarction. This protein contains kringle-2 and serine protease domains. The lack of glycosylation means that a prokaryotic system can be used to express reteplase. Therefore, the production of reteplase is more affordable than that of tPA. Different methods have been proposed to improve the production of reteplase. This article reviews the structure and function of reteplase as well as the methods used to produce it.

Indexed as

Bacterial expressionfibrin specificityreteplasethrombolytic drug

Identifiers

PMID31016177
PMCPMC6446582
OpenAlexW2923723616

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.