Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Yashwanth Ashok"'
Publikováno v:
PLoS ONE, Vol 15, Iss 2, p e0223870 (2020)
Lactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in biol
Externí odkaz:
https://doaj.org/article/d6bff684775d40468d3bd47bfcf7a10d
DTX3L and USP28 fine-tune DNA double strand repair through mutual regulation of their protein levels
Autor:
Yashwanth Ashok, Daniela Mennerich, Carlos Vela-Rodríguez, Heli I. Alanen, Melanie Rall-Scharpf, Lisa Wiesmüller, Renata Prunskaite-Hyyryläinen, Lari Lehtiö, Thomas Kietzmann
The DNA damage response involves a complex protein network with members mediating different post-translational modifications such as ubiquitination and deubiquitination. Thereby the E3 ubiquitin ligase DTX3L as well as the deubiquitinase USP28 are re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d009846c2fe6abd4155517a3392094fd
https://doi.org/10.1101/2023.01.30.526213
https://doi.org/10.1101/2023.01.30.526213
Autor:
Sudarshan, Murthy, Maria Giulia, Nizi, Mirko M, Maksimainen, Serena, Massari, Juho, Alaviuhkola, Barbara E, Lippok, Chiara, Vagaggini, Sven T, Sowa, Albert, Galera-Prat, Yashwanth, Ashok, Harikanth, Venkannagari, Renata, Prunskaite-Hyyryläinen, Elena, Dreassi, Bernhard, Lüscher, Patricia, Korn, Oriana, Tabarrini, Lari, Lehtiö
Publikováno v:
Journal of medicinal chemistry.
We report [1,2,4]triazolo[3,4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b7842b39c06010b4651f7dd439c1106f
https://pubmed.ncbi.nlm.nih.gov/36598465
https://pubmed.ncbi.nlm.nih.gov/36598465
Autor:
Sudarshan Murthy, Maria Giulia Nizi, Mirko M. Maksimainen, Serena Massari, Juho Alaviuhkola, Barbara E. Lippok, Chiara Vagaggini, Sven T. Sowa, Albert Galera-Prat, Yashwanth Ashok, Harikanth Venkannagari, Renata Prunskaite-Hyyryläinen, Elena Dreassi, Bernhard Lüscher, Patricia Korn, Oriana Tabarrini, Lari Lehtiö
Publikováno v:
Journal of medicinal chemistry 66(2), 1301-1320 (2023). doi:10.1021/acs.jmedchem.2c01460
Journal of medicinal chemistry 66(2), 1301-1320 (2023). doi:10.1021/acs.jmedchem.2c01460
Published by American Chemical Society, Washington, DC
Published by American Chemical Society, Washington, DC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d02c78b88c3e04c15acc5405940609a1
http://urn.fi/urn:nbn:fi-fe2023032232837
http://urn.fi/urn:nbn:fi-fe2023032232837
Autor:
Yashwanth Ashok, Carlos Vela-Rodríguez, Chunsong Yang, Heli I. Alanen, Fan Liu, Bryce M. Paschal, Lari Lehtiö
Publikováno v:
The Biochemical journal. 479(3)
Ubiquitination and ADP-ribosylation are post-translational modifications that play major roles in pathways including the DNA damage response and viral infection. The enzymes responsible for these modifications are therefore potential targets for ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3a88869bbd971d656303112211baa60
https://pubmed.ncbi.nlm.nih.gov/35037691
https://pubmed.ncbi.nlm.nih.gov/35037691
Autor:
Liu F, Chun-Song Yang, Yashwanth Ashok, Lari Lehtiö, Vela-Rodríguez C, Heli I. Alanen, Bryce M. Paschal
In a reaction that requires processing by E1 and E2 enzymes, the E3 ligase complex DTX3L-PARP9 ADP-ribosylates the carboxyl terminus of Ubiquitin and prevents its conjugation to substrate protein. This provides an NAD+-sensitive mechanism for regulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfddc846f06c6d043442b76cbf167878
https://doi.org/10.1101/2021.06.14.448324
https://doi.org/10.1101/2021.06.14.448324
Autor:
Arto T. Pulliainen, Lari Lehtiö, Michael O. Hottiger, Yashwanth Ashok, Avlokita Tiwari, Moona Miettinen, Mark S. Johnson, Mahlet Z. Tamirat, Danilo Kimio Hirabae de Oliveira, Katja Näreoja
Publikováno v:
ACS infectious diseases. 6(4)
Targeted pathogen-selective approach to antibiotic development holds promise to minimize collateral damage to the beneficial microbiome. The AB5-topology pertussis toxin (PtxS1-S5, 1:1:1:2:1) is a major virulence factor ofBordetella pertussis, the ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69c6356e4142a88c33c4d5eabe5758f5
https://pubmed.ncbi.nlm.nih.gov/31899865
https://pubmed.ncbi.nlm.nih.gov/31899865
Publikováno v:
PLoS ONE
'PloS One ', vol: 15, pages: e0223870-1-e0223870-16 (2020)
PLoS ONE, Vol 15, Iss 2, p e0223870 (2020)
'PloS One ', vol: 15, pages: e0223870-1-e0223870-16 (2020)
PLoS ONE, Vol 15, Iss 2, p e0223870 (2020)
Lactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in biol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8a948767ac69d2dbf3eedd9876bbda0
http://urn.fi/urn:nbn:fi-fe2020040310324
http://urn.fi/urn:nbn:fi-fe2020040310324
Autor:
Yashwanth Ashok, Veli-Pekka Jaakola
Publikováno v:
MethodsX
Graphical abstract
Membrane proteins are generally unstable in detergents. Therefore, biochemical and biophysical studies of membrane proteins in lipidic environments provides a near native-like environment suitable for membrane proteins. Howeve
Membrane proteins are generally unstable in detergents. Therefore, biochemical and biophysical studies of membrane proteins in lipidic environments provides a near native-like environment suitable for membrane proteins. Howeve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a722e044d73fa84e55760b6b6d67b26e
https://doi.org/10.1016/j.mex.2016.03.009
https://doi.org/10.1016/j.mex.2016.03.009
Publikováno v:
Biochemical Pharmacology. 98:681-689
Many nucleoside transport inhibitors are in clinical use as anti-cancer, vasodilator and cardioprotective drugs. However, little is known about the binding energetics of these inhibitors to nucleoside transporters (NTs) due to their low endogenous ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e250300b772a946f29aa3e1586ad9c3c
https://doi.org/10.1016/j.bcp.2015.09.019
https://doi.org/10.1016/j.bcp.2015.09.019