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(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 )
- agriculture and horticulture (Agricultural sciences)
- food and nutrition technology (Agricultural sciences)
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(Field of Science)
Ministry points: Help
Year | Points | List |
---|---|---|
Year 2024 | 100 | Ministry scored journals list 2024 |
Year | Points | List |
---|---|---|
2024 | 100 | Ministry scored journals list 2024 |
2023 | 140 | Ministry Scored Journals List |
2022 | 100 | Ministry Scored Journals List 2019-2022 |
2021 | 100 | Ministry Scored Journals List 2019-2022 |
2020 | 100 | Ministry Scored Journals List 2019-2022 |
2019 | 100 | Ministry Scored Journals List 2019-2022 |
2018 | 30 | A |
2017 | 30 | A |
2016 | 30 | A |
2015 | 25 | A |
2014 | 30 | A |
2013 | 30 | A |
2012 | 25 | A |
2011 | 25 | A |
2010 | 27 | A |
Model:
Points CiteScore:
Year | Points |
---|---|
Year 2023 | 7.4 |
Year | Points |
---|---|
2023 | 7.4 |
2022 | 7.5 |
2021 | 6.7 |
2020 | 5.8 |
2019 | 6.3 |
2018 | 6.1 |
2017 | 6.4 |
2016 | 5.1 |
2015 | 5.7 |
2014 | 5.4 |
2013 | 6.7 |
2012 | 5.5 |
2011 | 5.7 |
Impact Factor:
Sherpa Romeo:
Papers published in journal
Filters
total: 3
Catalog Journals
Year 2018
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Plasma lipidomic profile signature of rheumatoid arthritis versus Lyme arthritis patients
Publication -
The structurally similar TRFH domain of TRF1 and TRF2 dimers shows distinct behaviour towards TIN2
PublicationThe telomere repeat binding-factor 1 and 2 (TRF1 and TRF2) proteins of the shelterin complex bind to duplex telomeric DNA as homodimers, and the homodimerization is mediated by their TRFH (TRF-homology) domains. We performed molecular dynamic (MD) simulations of the dimer forms of TRF1TRFH and TRF2TRFH in the presence/absence of the TIN2TBM (TIN2, TRF-interacting nuclear protein 2, TBM, TRF-binding motif) peptide. The MD results...
Year 2006
-
Structural analogues of reactive intermediates as inhibitors of glucosamine-6-phosphate synthase and phosphoglucose isomerase
PublicationCentra aktywne izomerazy fosfoglukozowej (PGI) oraz domeny izomerazowej (HPI) syntazy glukozamino-6-fosforanu (GlcN-6-P), wykazują podobieństwo ułożenia przestrzennego kluczowych reszt aminokwasowych, z wyjątkiem reszty Arg272 PGI i reszt Lys603 i Lys485 HPI. Dziesięć pochodnych D-heksitolo-6-P, kwasu 5-fosfoarabonowego i kwasu 6-fosfoglukonowego, strukturalnych analogów cis-enolaminy lub cis-enolanu, przypuszczalnych stanów przejściowych...
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