Evidence map›Paper›PMID 19582234›Full record

ReviewInternational journal of molecular sciences2009

Protease inhibitors from plants with antimicrobial activity.

Jin-Young Kim, Seong-Cheol Park, Indeok Hwang, Hyeonsook Cheong, Jae-Woon Nah, Kyung-Soo Hahm, Yoonkyung Park

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

75 citing papers in PubMed, 245 citations in OpenAlex.

  1. Article
  2. Article
  3. Journal of Taibah University Medical Sciences · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Complex of Defense Polypeptides of Wheatgrass (Plants (Basel, Switzerland) · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Frontiers in plant science · 2023
    Article
  15. Article
  16. The Role of ABA in the Interaction between Citrus Fruit andInternational journal of molecular sciences · 2022
    Article
  17. Article
  18. Article
  19. Review
  20. Article

15 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Jin-Young KimResearch Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Seong-Cheol ParkResearch Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Indeok HwangDepartment of Biotechnology and BK21 Research Team for Protein Activity Control, Chosun University, Gwangju 501-759, Korea.
Hyeonsook CheongDepartment of Biotechnology and BK21 Research Team for Protein Activity Control, Chosun University, Gwangju 501-759, Korea.
Jae-Woon NahDepartment of Polymer Science and Engineering, Sunchon National University, 315 Maegok, Suncheon, Korea.
Kyung-Soo HahmResearch Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Yoonkyung ParkResearch Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Chosun University · KRSunchon National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial proteins (peptides) are known to play important roles in the innate host defense mechanisms of most living organisms, including plants, insects, amphibians and mammals. They are also known to possess potent antibiotic activity against bacteria, fungi, and even certain viruses. Recently, the rapid emergence of microbial pathogens that are resistant to currently available antibiotics has triggered considerable interest in the isolation and investigation of the mode of action of antimicrobial proteins (peptides). Plants produce a variety of proteins (peptides) that are involved in the defense against pathogens and invading organisms, including ribosome-inactivating proteins, lectins, protease inhibitors and antifungal peptides (proteins). Specially, the protease inhibitors can inhibit aspartic, serine and cysteine proteinases. Increased levels of trypsin and chymotrypsin inhibitors correlated with the plants resistance to the pathogen. Usually, the purification of antimicrobial proteins (peptides) with protease inhibitor activity was accomplished by salt-extraction, ultrafiltration and C(18) reverse phase chromatography, successfully. We discuss the relation between antimicrobial and anti-protease activity in this review. Protease inhibitors from plants potently inhibited the growth of a variety of pathogenic bacterial and fungal strains and are therefore excellent candidates for use as the lead compounds for the development of novel antimicrobial agents.

Indexed as

Anti-Infective AgentsBacteriaCandida albicansFabaceaePeptidesPlantsProtease InhibitorsSolanum tuberosumAnti-Infective AgentsPeptidesProtease Inhibitorsantimicrobial peptidechromatographic columnsnovel antimicrobial agentspathogenic bacterial and fungal strainsplantsprotease inhibitors

Identifiers

PMID19582234
PMCPMC2705521
OpenAlexW2016661782

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.