Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Nathan M. Gallup"'
Autor:
Tomas Base, Adem Yavuz, Han Guo, Erin Avery, Michal Dušek, Jan Macháček, Mehmet Fatih Danışman, Monika Kučeráková, Anastassia N. Alexandrova, Václav Šícha, Nathan M. Gallup, K. N. Houk, Brian J. Levandowski, Zdenek Bastl, Saliha Gün, Jan Stanek, John C. Thomas, Paul S. Weiss, Dominic P. Goronzy, Ersen Mete
Publikováno v:
Chemistry of Materials. 32:6800-6809
The structure and function of self-assembled monolayers (SAMs) at the nanoscale are determined by the steric and electronic effects of their building blocks. Carboranethiol molecules form pristine ...
Publikováno v:
The Journal of organic chemistry, vol 83, iss 5
We report a DFT computational study (M06-2X) of π-facial selectivity in the Diels-Alder reactions of thiophene 1-oxide. The preference for the syn cycloaddition arises because the ground state geometry of thiophene 1-oxide is predistorted into an en
Autor:
Nathan M. Gallup, Anastassia N. Alexandrova, Mark E. Eberhart, Michael R. Nechay, Amanda Morgenstern, Quentin A. Smith
Publikováno v:
The Journal of Physical Chemistry B. 120:5884-5895
Histone deacetylases (HDACs) are responsible for the removal of acetyl groups from histones, resulting in gene silencing. Overexpression of HDACs is associated with cancer, and their inhibitors are of particular interest as chemotherapeutics. However
Autor:
Jennifer L. DuBois, Rodrigo L. Silveira, Kendall N. Houk, Michael F. Crowley, Gregg T. Beckham, Marc Garcia-Borràs, Mark D. Allen, Christopher W. Johnson, Ellen L. Neidle, Nathan M. Gallup, Munir S. Skaf, Melodie M. Machovina, John McGeehan, Sam J. B. Mallinson
Publikováno v:
Mallinson, S J B, Machovina, M M, Silveira, R L, Garcia-Borràs, M, Gallup, N, Johnson, C W, Allen, M D, Skaf, M S, Crowley, M F, Neidle, E L, Houk, K N, Beckham, G T, DuBois, J L & McGeehan, J 2018, ' A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion ', Nature Communications, vol. 9, no. 1, 2487 . https://doi.org/10.1038/s41467-018-04878-2
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Nature Communications
Nature communications, vol 9, iss 1
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Nature Communications
Nature communications, vol 9, iss 1
Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-deri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e3dce9dc097d5dbc1fe9f30b49a6f61
https://researchportal.port.ac.uk/ws/files/10761985/A_promiscuous_cytochrome_P450.pdf
https://researchportal.port.ac.uk/ws/files/10761985/A_promiscuous_cytochrome_P450.pdf
Publikováno v:
Chemical Physics Letters. 604:77-82
Acireductone dioxygenase (ARD) oxidizes 1,2-dihydroxy-3-keto-5-(methylthio)pentene to either formate and an α-keto acid, or formate, methylthiopropionate and CO, depending on the nature of the catalytic metal, Fe 2+ or Ni 2+ . We recently showed tha
Autor:
Michael R. Nechay, Nathan M. Gallup
Publikováno v:
Biophysical Journal. 110(3)
Histone Deacetylases (HDACs) are responsible for the removal of acetyl groups from histones resulting in gene silencing. Overexpression of HDACs is associated with cancer, and HDAC inhibitors are of particular interest as chemotherapeutics. The best
Autor:
Nathan M. Gallup, A N Alexandrova
Enzymes are complex biomolecules capable of performing unique catalysis under physiological conditions at neutral temperature and pH. However, the architecture of enzymatic catalysis is often a combination of the quantum influence of the immediate ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49d794c60108bb014c172ab4bd44f3cc
https://doi.org/10.1016/bs.mie.2016.05.018
https://doi.org/10.1016/bs.mie.2016.05.018
Autor:
Alvan C. Hengge, Sean J. Johnson, Gwendolyn Moise, Nathan M. Gallup, Anastassia N. Alexandrova
Publikováno v:
Moise, G; Gallup, NM; Alexandrova, AN; Hengge, AC; & Johnson, SJ. (2015). Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites. Biochemistry, 54(42), 6490-6500. doi: 10.1021/acs.biochem.5b00496. UCLA: Retrieved from: http://www.escholarship.org/uc/item/8wg4n0pm
Biochemistry, vol 54, iss 42
Biochemistry, vol 54, iss 42
© 2015 American Chemical Society. Catalysis in protein tyrosine phosphatases (PTPs) involves movement of a protein loop called the WPD loop that brings a conserved aspartic acid into the active site to function as a general acid. Mutation of the try
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30d6bf09212c34dc56c2769c5f81db69
https://europepmc.org/articles/PMC4887194/
https://europepmc.org/articles/PMC4887194/