Zobrazeno 1 - 10
of 19
pro vyhledávání: '"35"'
Autor:
R. Adam Kinney, Bo Zhang, Rebecca L. McNaughton, Russ Hille, Muralidharan Shanmugam, Brian M. Hoffman
Publikováno v:
Journal of the American Chemical Society. 132:14015-14017
The formaldehyde-inhibited Mo(V) state of xanthine oxidase (I) has been studied for four decades, yet it has not proven possible to distinguish unequivocally among the several structures proposed for this form. The uniquely large isotropic hyperfine
Autor:
Aneel K. Aggarwal, Nicolas Bolik-Coulon, Fabien Ferrage, Ludovic Carlier, Philippe Pelupessy, Guillaume Bouvignies, Cyril Charlier, Sandrine Sagan, Rodrigue Marquant, Mikhail Kozlov, Astrid Walrant, Pablo De Ioannes, Patricia Cortes
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (35), pp.12219-12227. ⟨10.1021/jacs.7b05823⟩
International audience; Many intrinsically disordered proteins (IDPs) and protein regions (IDRs) engage in transient, yet specific, interactions with a variety of protein partners. Often, if not always, interactions with a protein partner lead to par
Autor:
Petra Hänzelmann, Sowmya Subramanian, Michael K. Johnson, Brian M. Hoffman, Heather L. Hernandez, Hermann Schindelin, Nicholas S. Lees
Publikováno v:
Journal of the American Chemical Society. 131:9184-9185
The S-adenosylmethionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guanosine 5'-triphosphate (5'-GTP) into precursor Z. A published X-ray crystal structure of MoaA wit
Publikováno v:
Journal of the American Chemical Society. 141:10821-10829
High fidelity human mitochondrial DNA polymerase (Pol γ) contains two active sites, a DNA polymerization site (pol) and a 3′−5′ exonuclease site (exo) for proofreading. Although separated by 35 Å, coordination between the pol and exo sites is
Publikováno v:
Journal of the American Chemical Society. 140:15744-15752
Class Ia ribonucleotide reductase (RNR) of Escherichia coli contains an unusually stable tyrosyl radical cofactor in the β2 subunit (Y122•) necessary for nucleotide reductase activity. Upon binding the cognate α2 subunit, loaded with nucleoside d
Autor:
Brandon Q. Mercado, Scott J. Miller, Nadia C. Abascal, Eric K. Paulson, Anthony J. Metrano, Anna E. Hurtley
Publikováno v:
Journal of the American Chemical Society
X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides that were previously assessed for catalytic activity in an atroposelective bromination reaction. Common to the series is a central Pro-Xaa sequence, where
Publikováno v:
Journal of the American Chemical Society, vol 137, iss 35
Optical modulation of proteins provides superior spatiotemporal resolution for understanding biological processes, and photoswitches built on light-sensitive proteins have been significantly advancing neuronal and cellular studies. Small molecule pho
Autor:
Elodie Point, Karine Moncoq, Marina Casiraghi, Ewen Lescop, Jean-Louis Banères, Marjorie Damian, Daniel Lévy, Eric Guittet, Nelly Morellet, Laurent Catoire, Jacky Marie
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2016, 138 (35), pp.11170-11175. ⟨10.1021/jacs.6b04432⟩
Journal of the American Chemical Society, American Chemical Society, 2016, 138 (35), pp.11170-11175. ⟨10.1021/jacs.6b04432⟩
International audience; Mapping the conformational landscape of G protein-coupled receptors (GPCRs), and in particular how this landscape is modulated by the membrane environment, is required to gain a clear picture of how signaling proceeds. To this
Publikováno v:
Journal of the American Chemical Society. 133:19807-19815
S-adenosylhomocysteine hydrolase (SAHH), a cellular enzyme that plays a key role in methylation reactions including those required for maturation of viral mRNA, is an important drug target in the discovery of antiviral agents. While targeting the act
Autor:
Mohammad R. Seyedsayamdost, Tomislav Argirević, JoAnne Stubbe, Ellen Catherine Minnihan, Marina Bennati
Publikováno v:
Journal of the American Chemical Society
E. coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, a process that requires long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a cysteine residue (C(439))