Zobrazeno 1 - 10
of 33
pro vyhledávání: '"James N. Blaza"'
Autor:
Rhianna J. Rowland, Svitlana Korolchuk, Marco Salamina, Natalie J. Tatum, James R. Ault, Sam Hart, Johan P. Turkenburg, James N. Blaza, Martin E. M. Noble, Jane A. Endicott
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The cell division cycle 25 phosphatases CDC25A, B and C regulate cell cycle transitions by dephosphorylating residues in the conserved glycine-rich loop of CDKs to activate their activity. Here, we present the cryo-EM structure of CDK2-cycli
Externí odkaz:
https://doaj.org/article/7f9036edb0fb4c63978dfd51fe5e5873
Autor:
Rhianna J. Rowland, Richard Heath, Daniel Maskell, Rebecca F. Thompson, Neil A. Ranson, James N. Blaza, Jane A. Endicott, Martin E. M. Noble, Marco Salamina
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-11 (2023)
Abstract p27KIP1 (cyclin-dependent kinase inhibitor 1B, p27) is a member of the CIP/KIP family of CDK (cyclin dependent kinase) regulators that inhibit cell cycle CDKs. p27 phosphorylation by CDK1/2, signals its recruitment to the SCFSKP2 (S-phase ki
Externí odkaz:
https://doaj.org/article/255a782ee4174ccbb388f8fffc48d107
Autor:
Richard W. Meek, James N. Blaza, Jil A. Busmann, Matthew G. Alteen, David J. Vocadlo, Gideon J. Davies
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
The modification of proteins with O-linked β-N-acetylglucosamine (OGlcNAc) plays roles in regulation of numerous cellular functions while incorrect O-GlcNAcylation patterns are linked to disease. Here, the authors report a cryo-EM structure of full-
Externí odkaz:
https://doaj.org/article/b53d14eee722429eb6788dd3501e0e16
Autor:
Hannah R. Bridges, Justin G. Fedor, James N. Blaza, Andrea Di Luca, Alexander Jussupow, Owen D. Jarman, John J. Wright, Ahmed-Noor A. Agip, Ana P. Gamiz-Hernandez, Maxie M. Roessler, Ville R. I. Kaila, Judy Hirst
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
The respiratory complex I (NADH:ubiquinone oxidoreductase) is a large redox-driven proton pump that initiates respiration in mitochondria. Here, the authors present the 3.0 Å cryo-EM structure of complex I from mouse heart mitochondria with the ubiq
Externí odkaz:
https://doaj.org/article/c67a68fb52d54db99aeb5805317cf695
Publikováno v:
Open Biology, Vol 8, Iss 1 (2018)
In oxidative phosphorylation, ATP synthases interconvert two forms of free energy: they are driven by the proton-motive force across an energy-transducing membrane to synthesize ATP and displace the ADP/ATP ratio from equilibrium. For thermodynamical
Externí odkaz:
https://doaj.org/article/2a454bad7e8940ce9a81bfacce8ab196
Autor:
Jinling Li, Mahima Sharma, Richard Meek, Amani Alhifthi, Zachary Armstrong, Niccolay Madiedo Soler, Ethan D. Goddard-Borger, James N. Blaza, Gideon J. Davies, Spencer J. Williams
Sulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turns derives from sulfoglycolysis of the sulfosugar sulfoquinovose, or thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c43d6837048411697bd909da64fa1e51
https://doi.org/10.1101/2023.03.13.532361
https://doi.org/10.1101/2023.03.13.532361
Autor:
Solomon L. D. Wrathall, Barbara Procacci, Marius Horch, Emily Saxton, Chris Furlan, Julia Walton, Yvonne Rippers, James N. Blaza, Gregory M. Greetham, Michael Towrie, Anthony W. Parker, Jason Lynam, Alison Parkin, Neil T. Hunt
Publikováno v:
Physical Chemistry Chemical Physics. 24:24767-24783
Ultrafast two-dimensional infrared (2D-IR) spectroscopy of Escherichia coli Hyd-1 (EcHyd-1) reveals the structural and dynamic influence of the protein scaffold on the Fe(CO)(CN)2 unit of the active site. Measurements on as-isolated EcHyd-1 probed a
Autor:
Karla Helena-Bueno, Chinenye L. Ekemezie, Charlotte R. Brown, Arnaud Baslé, James N. Blaza, Chris H. Hill, Sergey V. Melnikov
During starvation and stress, virtually all organisms arrest protein synthesis to conserve energy. Inactive ribosomes are converted into a dormant state, in which they are protected from damage by hibernation factor proteins. In bacteria, two major f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76956aa9af2776805a7123a319d10d27
https://doi.org/10.1101/2022.11.24.517861
https://doi.org/10.1101/2022.11.24.517861
Cryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis
Publikováno v:
Structure, 30(10), 1443-1451.e5
Enzymatic hydrolysis of α-L-fucose from fucosylated glycoconjugates is consequential in bacterial infections and the neurodegenerative lysosomal storage disorder fucosidosis. Understanding human α-L-fucosidase catalysis, in an effort toward drug de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13ad1fef0f71711b67c53713589cea88
https://doi.org/10.1016/j.str.2022.07.001
https://doi.org/10.1016/j.str.2022.07.001