PLoS Computational Biology - Journal - Bridge of Knowledge

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PLoS Computational Biology

ISSN:

1553-7358

eISSN:

1553-734X

Publisher:

PLoS

Disciplines
(Field of Science):

  • Information and communication technology (Engineering and Technology)
  • 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 )
  • Family studies (Family studies)
  • Agriculture and horticulture (Agricultural sciences)
  • Biotechnology (Natural sciences)
  • Computer and information sciences (Natural sciences)
  • Biological sciences (Natural sciences)
  • Chemical sciences (Natural sciences)

Ministry points: Help

Ministry points - current year
Year Points List
Year 2024 140 Ministry scored journals list 2024
Ministry points - previous years
Year Points List
2024 140 Ministry scored journals list 2024
2023 140 Ministry Scored Journals List
2022 140 Ministry Scored Journals List 2019-2022
2021 140 Ministry Scored Journals List 2019-2022
2020 140 Ministry Scored Journals List 2019-2022
2019 140 Ministry Scored Journals List 2019-2022
2014 45 A
2013 45 A
2010 32 A

Model:

Open Access

Points CiteScore:

Points CiteScore - current year
Year Points
Year 2022 7.1
Points CiteScore - previous years
Year Points
2022 7.1
2021 6.6
2020 7.3
2019 7.3
2018 7.2
2017 7.8
2016 7.9
2015 7.9
2014 7.8
2013 8
2012 8.6
2011 8.1

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total: 5

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Catalog Journals

Year 2023
Year 2021
Year 2020
  • Two-step mechanism of J-domain action in driving Hsp70 function
    Publication
    • B. Tomiczek
    • W. Delewski
    • Ł. Nierzwicki
    • M. Stolarska
    • I. Grochowina
    • B. Schilke
    • R. Dutkiewicz
    • M. A. Uzarska
    • S. Ciesielski
    • J. Czub... and 2 others

    - PLoS Computational Biology - Year 2020

    J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with substrate polypeptides upon hydrolysis of its bound ATP. Although a recent crystal structure revealed the physical mode of interaction between a J-domain and an Hsp70, the structural and dynamic consequences of J-domain action once bound and how Hsp70s...

    Full text available to download

Year 2019
Year 2012

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