PEPTIDES - Journal - Bridge of Knowledge

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PEPTIDES

ISSN:

0196-9781

eISSN:

1873-5169

Disciplines
(Field of Science):

  • biomedical engineering (Engineering and Technology)
  • medical biology (Medical and Health Sciences )
  • pharmacology and pharmacy (Medical and Health Sciences )
  • medical sciences (Medical and Health Sciences )
  • health sciences (Medical and Health Sciences )
  • agriculture and horticulture (Agricultural sciences)
  • food and nutrition technology (Agricultural sciences)
  • animal science and fisheries (Agricultural sciences)
  • biotechnology (Natural sciences)
  • biological sciences (Natural sciences)
  • chemical sciences (Natural sciences)

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Ministry points - current year
Year Points List
Year 2025 70 Ministry scored journals list 2024
Ministry points - previous years
Year Points List
2025 70 Ministry scored journals list 2024
2024 70 Ministry scored journals list 2024
2023 100 Ministry Scored Journals List
2022 70 Ministry Scored Journals List 2019-2022
2021 70 Ministry Scored Journals List 2019-2022
2020 70 Ministry Scored Journals List 2019-2022
2019 70 Ministry Scored Journals List 2019-2022
2018 25 A
2017 25 A
2016 25 A
2015 25 A
2014 25 A
2013 25 A
2012 25 A
2011 25 A
2010 27 A

Model:

Hybrid

Points CiteScore:

Points CiteScore - current year
Year Points
Year 2023 6.4
Points CiteScore - previous years
Year Points
2023 6.4
2022 6.2
2021 6.4
2020 5.6
2019 5.1
2018 5
2017 6.1
2016 5.7
2015 5.4
2014 5.2
2013 5.1
2012 4.7
2011 4.5

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Catalog Journals

Year 2019
Year 2017
Year 2012
  • Inhibitory and antimicrobial activities of OGTI and HV-BBI peptides, fragments and analogs derived from amphibian skin
    Publication
    • D. Dębowski
    • R. Łukajtis
    • A. Łęgowska
    • N. Karna
    • M. Pikuła
    • M. Wysocka
    • I. Maliszewska
    • M. Sieńczyk
    • A. Lesner
    • K. Rolka

    - PEPTIDES - Year 2012

    A series of linear and cyclic fragments and analogs of two peptides (OGTI and HV-BBI) isolated from skin secretions of frogs were synthesized by the solid-phase method. Their inhibitory activity against several serine proteinases: bovine beta-trypsin, bovine alpha-chymotypsin, human leukocyte elastase and cathepsin G from human neutrophils, was investigated together with evaluation of their antimicrobial activities against Gram-negative...

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