Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Marcin Pierechod"'
Autor:
Ole Jakob Hegelund, Alistair Everett, Ted Cheeseman, Penelope Wagner, Nick Hughes, Marcin Pierechod, Ken Southerland, Philip Robinson, Jennifer Hutchings, Åshild Kiærbech, Joakim Lillehaug Pedersen
The Ice Watch program coordinates routine visual observations of sea-ice including icebergs and meteorological parameters. The development and use of the Arctic Shipborne Sea Ice Standardization Tool (ASSIST) software has enabled the program to colle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::52e3e568c7440a8818f85fc6c751244e
https://doi.org/10.5194/egusphere-egu2020-7126
https://doi.org/10.5194/egusphere-egu2020-7126
Autor:
Grażyna Goch, Maria Bucholc, Michal Dadlez, Jarosław Poznański, Halina Fedak, Grażyna Dobrowolska, Marcin Pierechod, Arkadiusz Ciesielski, Maria Klimecka, Małgorzata Lichocka, Anna Kulik, Krzysztof Tarnowski, Richard A. Engh
SNF1-related protein kinases 2 (SnRK2s) are key signaling elements that regulate abscisic acid (ABA)-dependent plant development and responses to environmental stresses. Our previous data showed that the SnRK2-interacting Calcium Sensor (SCS) is an i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f35518cb9a1a34c32fec57cfe327bf3e
Autor:
Grażyna Goch, Małgorzata Lichocka, Krzysztof Tarnowski, Richard A. Engh, Maria Bucholc, Halina Fedak, Grażyna Dobrowolska, Marcin Pierechod, Maria Klimecka, Anna Kulik, Arkadiusz Ciesielski, Jarosław Poznański, Michal Dadlez
Publikováno v:
Plant Physiol
SNF1-related protein kinases 2 (SnRK2s) are key signaling elements regulating abscisic acid-dependent plant development and responses to environmental stresses. Our previous data showed that the SnRK2-interacting Calcium Sensor (SCS) inhibits SnRK2 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::638eb801bd4d0c0f47bb01fa74468e08
https://hdl.handle.net/10037/21003
https://hdl.handle.net/10037/21003
Publikováno v:
Nucleic Acids Research
DNA replication initiation proteins (Reps) are subjected to degradation by cellular proteases. We investigated how the formation of nucleoprotein complex, involving Rep and a protease, affects Rep degradation. All known Escherichia coli AAA+ cytosoli
Autor:
Gro Elin Kjæreng Bjerga, Bjørn Altermark, Adele Kim Williamson, Arne O. Smalås, Marcin Pierechod, Erik Hjerde, Nils Peder Willassen
Publikováno v:
Genome Announcements
The cold-adapted Rhodococcus sp. strain AW25M09 was isolated from an Atlantic hagfish caught off the shore of northern Norway as part of an ongoing bioprospecting project that aims to identify novel bacteria with biotechnological potential. Here, we
Publikováno v:
Nucleic Acids Research
Transcription proceeding downstream of the λ phage replication origin was previously shown to support initial steps of the λ primosome assembly in vitro and to regulate frequency and directionality of λ DNA replication in vivo. In this report, the
Autor:
Igor Konieczny, Marcin Pierechod, Janusz M. Bujnicki, Anna Saari, Elzbieta Purta, Agnieszka Nowak
Publikováno v:
Protein science : a publication of the Protein Society. 18(3)
Proteins from the Rep family of DNA replication initiators exist mainly as dimers, but only monomers can initiate DNA replication by interaction with the replication origin (ori). In this study, we investigated both the activation (monomerization) an
Publikováno v:
Microbiology (Reading, England). 154(Pt 9)
It has been demonstrated that plasmids are not randomly distributed but are located symmetrically in mid-cell, or (1/4), (3/4) positions in bacterial cells. In this work we compared the localization of broad-host-range plasmid RK2 mini-replicons, whi
Publikováno v:
The Biochemical journal. 366(Pt 3)
Bacillus subtilis is a Gram-positive bacterium with a relatively large number of protein phosphatases. Previous studies have shown that some Ser/Thr phosphatases play an important role in the life cycle of this bacterium [Losick and Stragier (1992) N
Autor:
Nils Peder Willassen, Marcin Pierechod, Donatella de Pascale, Bjørn Altermark, Luca Ambrosino, Concetta De Santi
Publikováno v:
BMC biochemistry (Online) (2016). doi:10.1186/s12858-016-0057-x
info:cnr-pdr/source/autori:De Santi C.; Altermark B.; Pierechod M.M.; Ambrosino L.; de Pascale D.; Willassen N.-P./titolo:Characterization of a cold-active and salt tolerant esterase identified by functional screening of Arctic metagenomic libraries/doi:10.1186%2Fs12858-016-0057-x/rivista:BMC biochemistry (Online)/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume
BMC Biochemistry
info:cnr-pdr/source/autori:De Santi C.; Altermark B.; Pierechod M.M.; Ambrosino L.; de Pascale D.; Willassen N.-P./titolo:Characterization of a cold-active and salt tolerant esterase identified by functional screening of Arctic metagenomic libraries/doi:10.1186%2Fs12858-016-0057-x/rivista:BMC biochemistry (Online)/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume
BMC Biochemistry
Background The use of metagenomics in enzyme discovery constitutes a powerful approach to access to genomes of unculturable community of microorganisms and isolate novel valuable biocatalysts for use in a wide range of biotechnological and pharmaceut