Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jarosław Zimny"'
Autor:
Yulia Yu. Stroylova, Hieronim Jakubowski, Vladimir I. Muronetz, Thomas Haertlé, Jean-Marc Chobert, Reza Yousefi, Jarosław Zimny
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814:1234-1245
Elevated homocysteine levels are resulting in N-homocysteinylation of lysyl residues in proteins and they correlate with a number of human pathologies. However, the role of homocysteinylation of lysyl residues is still poorly known. In order to study
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::149a026bd21d9374b77f17a513ce0c00
https://doi.org/10.1016/j.bbapap.2011.05.017
https://doi.org/10.1016/j.bbapap.2011.05.017
Autor:
Jacek Jemielity, Andrzej Guranowski, Jarosław Zimny, Anna Maria Wojdyła, Paweł Bieganowski, Richard E. Davis, Anna Wypijewska, Joanna Kowalska
Publikováno v:
FEBS Letters. 584:93-98
Histidine triad (HIT)-family proteins interact with different mono- and dinucleotides and catalyze their hydrolysis. During a study of the substrate specificity of seven HIT-family proteins, we have shown that each can act as a sulfohydrolase, cataly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65c9a5f385cac5c39e726a5d54d8d64d
https://doi.org/10.1016/j.febslet.2009.11.003
https://doi.org/10.1016/j.febslet.2009.11.003
Autor:
Jarosław Zimny, Adam Kraszewski, Paweł Bieganowski, Andrzej Guranowski, Anna Maria Wojdyla-Mamon, Jacek Stawinski, Joanna Romanowska
Publikováno v:
The Biochemical journal. 468(2)
Fragile histidine triad (HIT) proteins (Fhits) occur in all eukaryotes but their function is largely unknown. Human Fhit is presumed to function as a tumour suppressor. Previously, we demonstrated that Fhits catalyse hydrolysis of not only dinucleosi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dea0d6cd78d35a40aa55a7685530e46f
https://pubmed.ncbi.nlm.nih.gov/25826698
https://pubmed.ncbi.nlm.nih.gov/25826698
Publikováno v:
Journal of Biological Chemistry. 281:22485-22492
Homocysteine (Hcy) editing by methionyl-tRNA synthetase results in the formation of Hcy-thiolactone and initiates a pathway that has been implicated in human disease. In addition to being cleared from the circulation by urinary excretion, Hcy-thiolac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e42a9280dfabf867e39f9a9a93e725c7
https://doi.org/10.1074/jbc.m603656200
https://doi.org/10.1074/jbc.m603656200
Autor:
Ewa Bretes, Jarosław Zimny
Publikováno v:
Scopus-Elsevier
The formation of homocysteine thiolactone (HcyTl) from homocysteine occurs in all examined so far organisms including bacteria, yeast, and humans. Protein N-homocysteinylation at the ε-amino group of lysine is an adverse result of HcyTl accumulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eaea629e2d578626255b7b3c3078c62
https://pubmed.ncbi.nlm.nih.gov/24051443
https://pubmed.ncbi.nlm.nih.gov/24051443
Autor:
Jarosław, Zimny
Publikováno v:
Postepy biochemii. 54(1)
Elevated concentrations of homocysteine (Hcy) in human tissues have been correlated with some diseases, such as cardio-vascular, neurodegenerative, and kidney disorders. Hcy occurs in human blood in several forms. The most reactive is homocysteine th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f7bba65b8ca6047862800cccdfbdf9a0
https://pubmed.ncbi.nlm.nih.gov/18610586
https://pubmed.ncbi.nlm.nih.gov/18610586
Autor:
Paweł Bieganowski, Maciej Łukaszewicz, Andrzej Guranowski, Anna Wypijewska, Agata Jagiełło, Anna Maria Wojdyła, Joanna Kowalska, Edward Darzynkiewicz, Jacek Jemielity, Jarosław Zimny
Publikováno v:
New Journal of Chemistry. 34:888
Proteins that have a histidine triad in their active sites belong to the HIT-protein superfamily. They are ubiquitous, are involved in the metabolism of different nucleotides and catalyze their hydrolysis and/or phosphorolysis liberating either the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b241e8c317f2d0ae75d89aee2f5a162
https://doi.org/10.1039/b9nj00660e
https://doi.org/10.1039/b9nj00660e