ISSN:
eISSN:
Disciplines
(Field of Science):
- biomedical engineering (Engineering and Technology)
- chemical engineering (Engineering and Technology)
- materials engineering (Engineering and Technology)
- environmental engineering, mining and energy (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 )
- forestry (Agricultural 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)
(Field of Science)
Ministry points: Help
Year | Points | List |
---|---|---|
Year 2024 | 70 | Ministry scored journals list 2024 |
Year | Points | List |
---|---|---|
2024 | 70 | Ministry scored journals list 2024 |
2023 | 70 | 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 | 35 | A |
2017 | 35 | A |
2016 | 30 | A |
2015 | 30 | A |
2014 | 30 | A |
2013 | 35 | A |
2012 | 30 | A |
2011 | 30 | A |
2010 | 27 | A |
Model:
Points CiteScore:
Year | Points |
---|---|
Year 2023 | 8.9 |
Year | Points |
---|---|
2023 | 8.9 |
2022 | 6.8 |
2021 | 6 |
2020 | 6.6 |
2019 | 6.2 |
2018 | 5.4 |
2017 | 4.8 |
2016 | 4.7 |
2015 | 4.9 |
2014 | 4.7 |
2013 | 5.2 |
2012 | 5.2 |
2011 | 4.7 |
Impact Factor:
Sherpa Romeo:
Papers published in journal
Filters
total: 6
Catalog Journals
Year 2017
-
In vitro affinity of Deinococcus radiodurans MutS towards mismatched DNA exceeds that of its orthologues from Escherichia coli and Thermus thermophilus
PublicationThe mismatch binding protein MutS is responsible for the recognition of mispaired and unpaired bases, which is the initial step in DNA repair. Among the MutS proteins most extensively studied in vitro are those derived from Thermus thermophilus, Thermus aquaticus and Escherichia coli. Here, we present the first report on the in vitro examination of DNA mismatch binding activity of MutS protein from Deinococcus radiodurans and confront...
Year 2014
Year 2009
-
A cryptic ribosome binding site, false signals in reporter systems and avoidance of protein translation chaos
PublicationThe expression of reporter gene may be induced by activation of cryptic signalling sequences, as we found while constructing the mutS-lacZ fusion gene. We cloned the Escherichia coli lacZ gene encoding beta-galactosidase into a plasmid vector carrying the Thermus thermophilus mutS gene. The clones expected to produce beta-galactosidase as the C-terminal fusion were selected for the complementation of beta-galactosidase activity...
Year 2007
-
A bifunctional chimeric protein consisting of MutS and beta-galactoside
PublicationPraca pokazuje konstrukcję DNA plazmidowego kodującego bifunkcjonalne białko chimeryczne złożone z MutS Thermus thermophilus i beta-galaktozydazy E.coli, optymalizację jego ekspresji i oczyszczania. Białko to testowano w metodzie wykrywania mutacji punktowych, wykorzystując kolorymetryczne mierzenie aktywności domeny reporterowej beta galaktozydazy.
-
Bacterial SSB-like proteins of family Deinococcaceae - indentification, isolation, obtaining, purification and molecular characteristic
PublicationWiększość poznanych białek SSB jest aktywna w formie homotetramerycznej. Od 2002 roku znane są białka organizmów ekstremofilnych. Scharakteryzowano białka mikroorganizmów rodziny Deinococaceae. Uzyskane termostabilne białka stanowią atrakcyjną alternatywę w stosunku do znanych białek SSB w metodach diagnostyki molekularnej, technikach biologii molekularnej i analityce.
Year 2006
-
The construction of bifunctional fusion proteins consisting of MutS and GFP
PublicationSkonstruowano białka chimeryczne zawierające białko MutS z Thermus thermophilus i białko zielonej fluoresceiny GFP z Aequorea victoria, posiadające dla łatwiejszego oczyszczania domeny oligo-histydynowe na N- lub C-końcu. Fuzyjne białka rozpoznawały niekomplementarności w DNA podobnie do MutS T. thermophilus. Fluorescencyjne białka rozpoznające niekomplementarne DNA mogą być użyteczne w wykrywaniu jednonukleotydowych polimorfizmów...
seen 801 times