Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Maria Bucholc"'
Publikováno v:
Frontiers in Plant Science, Vol 14 (2023)
In nature, all living organisms must continuously sense their surroundings and react to the occurring changes. In the cell, the information about these changes is transmitted to all cellular compartments, including the nucleus, by multiple phosphoryl
Externí odkaz:
https://doaj.org/article/1d36f94b708445ca84a83553c21696cd
Autor:
Paulina Stachula, Katarzyna Kapela, Ewelina Malecka, Kamila Jaronczyk, Jacek Patryn, Nina Siwirykow, Maria Bucholc, Malgorzata Marczak, Maciej Kotlinski, Rafal Archacki
Publikováno v:
International Journal of Molecular Sciences
Volume 24
Issue 4
Pages: 3917
Volume 24
Issue 4
Pages: 3917
ATP-dependent SWI/SNF chromatin remodelling complexes are conserved multi-subunit assemblies that control genome activity. Functions of SWI/SNF complexes in plant development and growth have been well established, but the architecture of particular a
Autor:
Justyna Maszkowska, Grażyna Goch, Maria Bucholc, Ewa Krzywińska, Maria Klimecka, Małgorzata Lichocka, Grażyna Dobrowolska, Jadwiga Szczegielniak
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 4984, p 4984 (2020)
International Journal of Molecular Sciences; Volume 21; Issue 14; Pages: 4984
International Journal of Molecular Sciences
International Journal of Molecular Sciences; Volume 21; Issue 14; Pages: 4984
International Journal of Molecular Sciences
Phosphatidic acid (PA) is involved in the regulation of plant growth and development, as well as responses to various environmental stimuli. Several PA targets in plant cells were identified, including two SNF1-related protein kinases 2 (SnRK2s), SnR
Autor:
Justyna Maszkowska, Kris Gevaert, Geert De Jaeger, Ahmed Abd-El-Haliem, Maria Bucholc, Henk L. Dekker, Michel A. Haring, Grażyna Dobrowolska, A. Jessica Meyer, Robert C. Schuurink, Eveline Van De Slijke, Christa Testerink, Dorota Kawa
Publikováno v:
Plant Physiology
Plant Physiology 182 (2020) 1
Plant Physiology, 182(1)
Plant Physiology, 182(1), 361-377. American Society of Plant Biologists
Plant Physiology 182 (2020) 1
Plant Physiology, 182(1)
Plant Physiology, 182(1), 361-377. American Society of Plant Biologists
SNF1-RELATED PROTEIN KINASES 2 (SnRK2) are important components of early osmotic and salt stress signaling pathways in plants. The Arabidopsis (Arabidopsis thaliana) SnRK2 family comprises the abscisic acid (ABA)-activated protein kinases SnRK2.2, Sn
Autor:
Nina Siwirykow, Maria Bucholc, Piotr Pupel, Rafal Archacki, Paulina Stachula, Roksana Iwanicka-Nowicka, Katarzyna Sosnowska, Marta Koblowska, Kamila Jarończyk, Andrzej Jerzmanowski, Adam Zaborowski, Ewelina Małecka
Publikováno v:
Plant Communications
SWI/SNF chromatin remodelers are evolutionarily conserved multiprotein complexes that use the energy of ATP hydrolysis to change chromatin structure. A characteristic feature of SWI/SNF remodelers is the occurrence in both the catalytic ATPase subuni
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
Autor:
Olga Sztatelman, Justyna Maszkowska, Maria Bucholc, Grażyna Dobrowolska, Małgorzata Lichocka, Anna Kulik, Janusz Debski, Michał Kistowski, Maria Klimecka, Michal Dadlez, Katarzyna Patrycja Szymańska
Publikováno v:
Plant, cellenvironment. 42(3)
SNF1-related protein kinases 2 (SnRK2s) regulate the plant responses to abiotic stresses, especially water deficits. They are activated in plants subjected to osmotic stress, and some of them are additionally activated in response to enhanced concent
Autor:
Pedro L. Rodriguez, Maria A. Fernandez, Maria Bucholc, Ewa Krzywińska, Grażyna Dobrowolska, Anna Kulik
Publikováno v:
Plant Signaling & Behavior
RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname
RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname
[EN] Protein phosphatases 2C (PP2Cs) are important regulators of plant responses to abiotic stress. It is established that clade A PP2Cs inhibit ABA-activated SNF1-related protein kinases 2 (SnRK2s). Our recently published results show that ABI1, a m
Autor:
Agnieszka Ludwików, Janusz Debski, Pedro L. Rodriguez, Arkadiusz Ciesielski, Ewa Krzywińska, Małgorzata Lichocka, Anna Kulik, Grażyna Dobrowolska, Michal Dadlez, Maria Bucholc
Publikováno v:
RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname
BMC Plant Biology
instname
BMC Plant Biology
Background: SNF1-related protein kinases 2 (SnRK2s) are key regulators of the plant response to osmotic stress. They are transiently activated in response to drought and salinity. Based on a phylogenetic analysis SnRK2s are divided into three groups.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3764597644d2029b6359a5d366795728
https://doi.org/10.1186/s12870-016-0817-1
https://doi.org/10.1186/s12870-016-0817-1