Secondary Structure of Subgenomic RNA M of SARS-CoV-2

Autor: Marta Soszynska-Jozwiak, Agnieszka Ruszkowska, Ryszard Kierzek, Collin A. O’Leary, Walter N. Moss, Elzbieta Kierzek

Publikováno v: Viruses, Vol 14, Iss 2, p 322 (2022)

SARS-CoV-2 belongs to the Coronavirinae family. Like other coronaviruses, SARS-CoV-2 is enveloped and possesses a positive-sense, single-stranded RNA genome of ~30 kb. Genomic RNA is used as the template for replication and transcription. During thes

Externí odkaz: https://doaj.org/article/9938f5610965473687afdd90a403215c

Chloroplastic Serine Hydroxymethyltransferase From Medicago truncatula: A Structural Characterization

Autor: Milosz Ruszkowski, Bartosz Sekula, Agnieszka Ruszkowska, Zbigniew Dauter

Publikováno v: Frontiers in Plant Science, Vol 9 (2018)

Serine hydroxymethyltransferase (SHMT, EC 2.1.2.1) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme which catalyzes the reversible serine-to-glycine conversion in either a tetrahydrofolate-dependent or -independent manner. The enzyme is also resp

Externí odkaz: https://doaj.org/article/9e5598df78944118a1bed48f82a6d317

New aspects of DNA recognition by group II WRKY transcription factor revealed by structural and functional study of AtWRKY18 DNA binding domain

Autor: Marta Grzechowiak, Agnieszka Ruszkowska, Joanna Sliwiak, Anna Urbanowicz, Mariusz Jaskolski, Milosz Ruszkowski

Publikováno v: International journal of biological macromolecules 213, 589-601 (2022). doi:10.1016/j.ijbiomac.2022.05.186

International journal of biological macromolecules 213, 589 - 601 (2022). doi:10.1016/j.ijbiomac.2022.05.186
WRKY transcription factors (TFs) constitute one of the largest families of plant TFs. Based on the organization of domains and motifs, W

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c877a7056957ae08a4d7847587c5ae28
https://doi.org/10.1016/j.ijbiomac.2022.05.186

Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models

Autor: Isabel Nogués, Andrzej Szczepaniak, Milosz Ruszkowski, Zbigniew Dauter, Sebastiana Angelaccio, Bartosz Sekula, Agnieszka Ruszkowska, Roberto Contestabile

Publikováno v: Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports
Scientific reports (Nature Publishing Group) 9 (2019). doi:10.1038/s41598-019-56043-4
info:cnr-pdr/source/autori:Ruszkowski, Milosz; Sekula, Bartosz; Ruszkowska, Agnieszka; Contestabile, Roberto; Nogues, Isabel; Angelaccio, Sebastiana; Szczepaniak, Andrzej; Dauter, Zbigniew/titolo:Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models/doi:10.1038%2Fs41598-019-56043-4/rivista:Scientific reports (Nature Publishing Group)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9

Serine hydroxymethyltransferases (SHMTs) reversibly transform serine into glycine in a reaction accompanied with conversion of tetrahydrofolate (THF) into 5,10-methylene-THF (5,10-meTHF). In vivo, 5,10-meTHF is the main carrier of one-carbon (1C) uni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6874a4607c8eec9f06c6261ded1a11a6
http://link.springer.com/article/10.1038/s41598-019-56043-4

METTL16, Methyltransferase-Like Protein 16: Current Insights into Structure and Function

Autor: Agnieszka Ruszkowska

Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 2176, p 2176 (2021)
International Journal of Molecular Sciences

Methyltransferase-like protein 16 (METTL16) is a human RNA methyltransferase that installs m6A marks on U6 small nuclear RNA (U6 snRNA) and S-adenosylmethionine (SAM) synthetase pre-mRNA. METTL16 also controls a significant portion of m6A epitranscri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::199f379843b2aa2a1418f2b22b7c1e5e
https://www.mdpi.com/1422-0067/22/4/2176