Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Maria Rutkiewicz"'
Autor:
Sebastian Proft, Janna Leiz, Udo Heinemann, Dominik Seelow, Kai M. Schmidt-Ott, Maria Rutkiewicz
Publikováno v:
BMC Genomics, Vol 24, Iss 1, Pp 1-11 (2023)
Abstract Background Transcription factors regulate gene expression by binding to transcription factor binding sites (TFBSs). Most models for predicting TFBSs are based on position weight matrices (PWMs), which require a specific motif to be present i
Externí odkaz:
https://doaj.org/article/28fe24eb9a574b1bb3d2d16dfad99c28
Autor:
Anna Bujacz, Jedrzej Rum, Maria Rutkiewicz, Agnieszka J. Pietrzyk-Brzezinska, Grzegorz Bujacz
Publikováno v:
Materials, Vol 14, Iss 12, p 3351 (2021)
Aromatic amino acid aminotransferases present a special potential in the production of drugs and synthons, thanks to their ability to accommodate a wider range of substrates in their active site, in contrast to aliphatic amino acid aminotransferases.
Externí odkaz:
https://doaj.org/article/b38fa1bd7e3742ff8aae08fa86491392
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 15, p 5354 (2020)
β-Galactosidase from Arthrobacter sp. 32cB (ArthβDG) is a cold-adapted enzyme able to catalyze hydrolysis of β-d-galactosides and transglycosylation reaction, where galactosyl moiety is being transferred onto an acceptor larger than a water molecu
Externí odkaz:
https://doaj.org/article/57f0fcb2bd394e70be29fad82875539b
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4301 (2019)
ArthβDG is a dimeric, cold-adapted β-d-galactosidase that exhibits high hydrolytic and transglycosylation activity. A series of crystal structures of its wild form, as well as its ArthβDG_E441Q mutein complexes with ligands were obtained in order
Externí odkaz:
https://doaj.org/article/8b1379d5a8dc441eb0b4d25e42a15a07
Autor:
Maria Rutkiewicz, Isabel Nogues, Wojciech Witek, Sebastiana Angelaccio, Roberto Contestabile, Milosz Ruszkowski
Publikováno v:
Plant physiology and biochemistry 196, 759-773 (2023). doi:10.1016/j.plaphy.2023.02.017
Plant physiology and biochemistry 196, 759 - 773 (2023). doi:10.1016/j.plaphy.2023.02.017
Histidinol-phosphate aminotransferase is the sixth protein (hence HISN6) in the histidine biosynthetic pathway in plants. HISN6 is a pyridoxal 5′-phospha
Histidinol-phosphate aminotransferase is the sixth protein (hence HISN6) in the histidine biosynthetic pathway in plants. HISN6 is a pyridoxal 5′-phospha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bdac2f01dc8979d04ebb352961f1e36
https://bib-pubdb1.desy.de/record/585103
https://bib-pubdb1.desy.de/record/585103
Autor:
Kai Schmidt-Ott, Maria Rutkiewicz, Dominik Seelow, Janna Leiz, Sebastian Proft, Udo Heinemann
Transcription factors regulate gene expression by binding to transcription factor binding sites (TFBSs). Most models for predicting TFBSs are based on position weight matrices (PWMs), which require a specific motif to be present in the DNA sequence a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::426c178867c597093024305fdf6e97e7
https://doi.org/10.1101/2022.06.28.497553
https://doi.org/10.1101/2022.06.28.497553
Publikováno v:
Medizinische Genetik. 33:147-155
Transcription factors (TFs) bind DNA in a sequence-specific manner and thereby regulate target gene expression. TF binding and its regulatory activity is highly context dependent, and is not only determined by specific cell types or differentiation s
Autor:
Grzegorz Bujacz, Maria Rutkiewicz, Anna Bujacz, Agnieszka J. Pietrzyk-Brzezinska, Jedrzej Rum
Publikováno v:
Materials, Vol 14, Iss 3351, p 3351 (2021)
Materials
Volume 14
Issue 12
Materials
Volume 14
Issue 12
Aromatic amino acid aminotransferases present a special potential in the production of drugs and synthons, thanks to their ability to accommodate a wider range of substrates in their active site, in contrast to aliphatic amino acid aminotransferases.
Prolidase catalyzes the cleavage of dipeptides containing proline on their C terminus. The reduction in prolidase activity is the cause of a rare disease named 'Prolidase Deficiency'. Local structural disorder was indicated as one of the causes for d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2086d57a8ceb63b9170ea2a1db05ebb
https://ruj.uj.edu.pl/xmlui/handle/item/270539
https://ruj.uj.edu.pl/xmlui/handle/item/270539
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1867(9)
Crystal structures of cold-adapted β-d-galactosidase (EC 3.2.1.23) from the Antarctic bacterium Arthrobacter sp. 32cB (ArthβDG) have been determined in an unliganded form resulting from diffraction experiments conducted at 100 K (at resolution 1.8