Zobrazeno 1 - 10
of 89
pro vyhledávání: '"Daniel M. Quinn"'
Publikováno v:
Molecules, Vol 22, Iss 9, p 1464 (2017)
Organophosphorus agents are potent inhibitors of acetylcholinesterase. Inhibition involves successive chemical events. The first is phosphylation of the active site serine to produce a neutral adduct, which is a close structural analog of the acylati
Externí odkaz:
https://doaj.org/article/6c380cdf88f54fc88ef697e72c302536
Autor:
Qi Guo, Christopher M. Cheatum, Andrew L. Lee, Chethya Ranasinghe, Paul J. Sapienza, Amnon Kohen, Daniel M. Quinn
Publikováno v:
Journal of the American Chemical Society. 139:17405-17413
Isotopically labeled enzymes (denoted as "heavy" or "Born-Oppenheimer" enzymes) have been used to test the role of protein dynamics in catalysis. The original idea was that the protein's higher mass would reduce the frequency of its normal-modes with
Publikováno v:
Archives of Biochemistry and Biophysics. 632:11-19
Thymidylate is synthesized de novo in all living organisms for replication of genomes. The chemical transformation is reductive methylation of deoxyuridylate at C5 to form deoxythymidylate. All eukaryotes including humans complete this well-understoo
Autor:
Joseph J. Topczewski, Daniel M. Quinn, Jason A. Morrill, Nilanthi Yasapala, Alexander M. Lodge
Publikováno v:
Journal of Molecular Graphics and Modelling. 62:181-189
Among the most toxic substances known are the organophosphorus (OP) compounds used as pesticides and chemical warfare agents. Owing to their high toxicity there is a number of efforts underway to develop effective therapies for OP agent exposure. To
Publikováno v:
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
Molecules, Vol 22, Iss 9, p 1464 (2017)
Molecules, Vol 22, Iss 9, p 1464 (2017)
Organophosphorus agents are potent inhibitors of acetylcholinesterase. Inhibition involves successive chemical events. The first is phosphylation of the active site serine to produce a neutral adduct, which is a close structural analog of the acylati
Autor:
Daniel M. Quinn
Publikováno v:
Journal of Medicinal Chemistry. 61:7032-7033
Organophosphorus agents such as sarin and soman that phosphylate the active site serine of the enzyme acetylcholinesterase are notorious and pernicious, not only because they have been used by tyrants to effect mass murder of their own populations bu
Autor:
Pedrom M. Keshavarzi, Joseph J. Topczewski, Sumana N. Yasapala, Maurice K. Payne, Alexander M. Lodge, Daniel M. Quinn
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 23:5786-5789
The irreversible inhibition of acetylcholinesterase (AChE) by organophosphorous chemical warfare agents necessitates that antidotes be administered for effective treatment. Currently no antidote is known that resurrects the phosphyl-AChE complex once
Autor:
Daniel M. Quinn, Markus Wohlgenannt, Adam B. Brummett, Ned B. Bowden, Jun Yoo, Tyler A. Graf, Ran Lin
Publikováno v:
Macromolecules. 45:8193-8200
The synthesis and some of the physical properties of the first poly(disulfidediamines) are reported. The disulfidediamine functional group (R2NSSNR2) possesses a disulfide bond in a unique environment that leads to a low bond dissociation energy (cal
Publikováno v:
Chemico-Biological Interactions. 187:124-127
beta-Secondary deuterium isotope effects have been measured for equine serum butyrylcholinesterase-catalyzed hydrolysis of acetyl-L(3)-thiocholine (L=H or (2)H). The dependencies of initial rates on isotopic substrate concentrations show close adhere
The Fifth International Meeting on Cholinesterases convened in Madras, India, in September of 1994. The long and rich history and culture of India provided an excellent setting for the meeting. More than 120 delegates from Asia, Australia, Europe and