Zobrazeno 31 - 40
of 86
pro vyhledávání: '"35"'
Autor:
Travis Hoppe, Zhan-Guo Gao, Steven M. Moss, Khai Phan, Daniel H. Appella, Silvia Paoletta, Andrew V. Dix, Stewart R. Durell, Kenneth A. Jacobson, Eszter Kozma
Publikováno v:
Journal of the American Chemical Society
A programmable ligand display system can be used to dissect the multivalent effects of ligand binding to a membrane receptor. An antagonist of the A2A adenosine receptor, a G-protein-coupled receptor that is a drug target for neurodegenerative condit
Autor:
Aurélien Laguerre, Manuel Larrouy, Marc Pirrotta, David Genest, David Monchaud, Loic Stefan, Jana Novotna
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2014, 136 (35), pp.12406-12414. ⟨10.1021/ja506331x⟩
Journal of the American Chemical Society, American Chemical Society, 2014, 136 (35), pp.12406-12414. ⟨10.1021/ja506331x⟩
Recent and unambiguous evidences of the formation of DNA and RNA G-quadruplexes in cells has provided solid support for these structures to be considered as valuable targets in oncology. Beyond this, they have lent further credence to the anticancer
Autor:
Jeremy M. Smith, Brian M. Hoffman, Martin L. Kirk, Benjamin W. Stein, Deepak Subedi, George E. Cutsail
Publikováno v:
Journal of the American Chemical Society
The recently synthesized and isolated low-coordinate Fe(V) nitride complex has numerous implications as a model for high-oxidation states in biological and industrial systems. The trigonal [PhB((t)BuIm)3Fe(V)≡N](+) (where (PhB((t)BuIm)3(-) = phenyl
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
Autor:
Michal Avital-Shmilovici, Kalyaneswar Mandal, Nelson B. Phillips, Michael A. Weiss, Zachary P. Gates, Stephen B. H. Kent
Publikováno v:
Journal of the American Chemical Society. 135:3173-3185
Efficient total synthesis of insulin is important to enable the application of medicinal chemistry to the optimization of the properties of this important protein molecule. Recently we described "ester insulin"--a novel form of insulin in which the f
Autor:
Alireza Abi, Elena E. Ferapontova
Publikováno v:
Abi, A & Ferapontova, E 2012, ' Unmediated by DNA electron transfer in redox-labeled DNA duplexes end-tethered to gold electrodes ', Journal of American Chemical Society, vol. 134, no. 35, pp. 14499-14507 . https://doi.org/10.1021/ja304864w
Electron transfer (ET) between gold electrodes and redox-labeled DNA duplexes, immobilized onto the electrodes through the alkanethiol linker at the 3'-end and having internal either methylene blue (MB) or anthraquinone (AQ) redox labels, was shown t
Autor:
Ariella Oppenheim, Adam Zlotnick, Stanislav Kler, Uri Raviv, Daniel Harries, Chenglei Li, Avi Ginsburg, Roi Asor
Publikováno v:
Journal of the American Chemical Society. 134:8823-8830
Remarkably, uniform virus-like particles self-assemble in a process that appears to follow a rapid kinetic mechanism. The mechanisms by which spherical viruses assemble from hundreds of capsid proteins around nucleic acid, however, are yet unresolved
Publikováno v:
Journal of the American Chemical Society. 134:2520-2523
The reaction of a class I ribonucleotide reductase (RNR) begins when a cofactor in the β subunit oxidizes a cysteine residue ~35 Å away in the α subunit, generating a thiyl radical. In the class Ic enzyme from Chlamydia trachomatis (Ct), the cyste
Publikováno v:
Journal of the American Chemical Society. 133:18420-18432
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides using a diferric tyrosyl radical (Y(122)(•)) cofactor in β2 to initiate catalysis in α2. Each turnover requires revers
Autor:
Brian M. Hoffman, Joshua Telser, Brett M. Barney, Peter E. Doan, Lance C. Seefeldt, Robert Y. Igarashi, Dennis R. Dean
Publikováno v:
Journal of the American Chemical Society. 133:17329-17340
N(2) binds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has accumulated three or four electrons/protons (E(3) or E(4) states), with the E(4) state