Evidence map›Paper›PMID 35335974›Full record

ReviewPharmaceutics2022

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions.

Marina V Pokrovskaya, Vadim S Pokrovsky, Svetlana S Aleksandrova, Nikolay N Sokolov, Dmitry D Zhdanov

Open access · goldAbstract readReview
In one paragraph

Review in Pharmaceutics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

14 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Enhancing the Catalytic Activity of Thermo-Asparaginase fromInternational journal of molecular sciences · 2023
    Article
  9. In Silico Design of a Chimeric Humanized L-asparaginase.International journal of molecular sciences · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. 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 2 institutions in 1 country.

Marina V PokrovskayaInstitute of Biomedical Chemistry, Pogodinskaya Str. 10/8, 119121 Moscow, Russia.
Vadim S PokrovskyDepartment of Biochemistry, Peoples' Friendship University of Russia (RUDN University), Miklukho-Maklaya Str. 6, 117198 Moscow, Russia.ORCID 0000-0003-4006-9320
Svetlana S AleksandrovaInstitute of Biomedical Chemistry, Pogodinskaya Str. 10/8, 119121 Moscow, Russia.ORCID 0000-0002-4248-765X
Nikolay N SokolovInstitute of Biomedical Chemistry, Pogodinskaya Str. 10/8, 119121 Moscow, Russia.
Dmitry D ZhdanovInstitute of Biomedical Chemistry, Pogodinskaya Str. 10/8, 119121 Moscow, Russia.ORCID 0000-0003-4753-7588
Institute of Biomedical Chemistry · RUPeoples' Friendship University of Russia · RU

Funding

The Ministry of Education and Science of the Russian Federation RF00121X0004
6 · The paper itself

Abstract

L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and ammonia. These proteins with different biochemical, physicochemical and pharmacological properties are found in many organisms, including bacteria, fungi, algae, plants and mammals. To date, asparaginases from

Indexed as

acute lymphoblastic leukemiaimmunogenicityL-asparaginaseprotein engineeringsite-directed mutagenesissubstrate specificity

Identifiers

PMID35335974
PMCPMC8948990
OpenAlexW4220709638

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.