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)

Ministry points: Help

Ministry points - current year
Year Points List
Year 2024 70 Ministry scored journals list 2024
Ministry points - previous years
Year Points List
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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total: 3

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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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