Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Joshua F Alfaro"'
Autor:
Jessica L Martin, Phillip A Yates, Radika Soysa, Joshua F Alfaro, Feng Yang, Kristin E Burnum-Johnson, Vladislav A Petyuk, Karl K Weitz, David G Camp, Richard D Smith, Phillip A Wilmarth, Larry L David, Gowthaman Ramasamy, Peter J Myler, Nicola S Carter
Publikováno v:
PLoS Pathogens, Vol 10, Iss 2, p e1003938 (2014)
The ability of Leishmania to survive in their insect or mammalian host is dependent upon an ability to sense and adapt to changes in the microenvironment. However, little is known about the molecular mechanisms underlying the parasite response to env
Externí odkaz:
https://doaj.org/article/36e8f0994aaf4437ba1879260ecffd0a
Autor:
Suresh Gupta, Joshua F. Alfaro, Elijah M. Bolotin, Anita M. Leporati, Alexei A. Bogdanov, Marina Gottikh, Gerardo M. Castillo
Publikováno v:
Pharmaceutical research. 36(5)
PURPOSE. Developing and testing of microbicides for pre-exposure prophylaxis and post-exposure protection from HIV are on the list of major HIV/AIDS research priorities. To improve solubility and bioavailability of highly potent anti-retroviral drugs
Autor:
Joshua F. Alfaro, Wenyun Ouyang, Joseph Nichols, Jeffrey P. Jones, Gregory J. Crouch, Carolyn A. Joswig-Jones
Publikováno v:
Drug Metabolism and Disposition. 37:2393-2398
Human aldehyde oxidase 1 (AOX1) has been subcloned into a vector suitable for expression in Escherichia coli, and the protein has been expressed. The resulting protein is active, with sulfur being incorporated in the molybdopterin cofactor. Expressio
Autor:
Jeffrey P. Jones, Joshua F. Alfaro
Publikováno v:
The Journal of Organic Chemistry. 73:9469-9472
DFT calculations support a concerted mechanism for xanthine oxidase and aldehyde oxidase hydride displacement from the sp(2) carbon of 6-substituted 4-quinazolinones. The variations in transition state structure show that C-O bond formation is nearly
Autor:
Tianzhu Zang, Joshua J. Klaene, Shujia Dai, Zhaohui Sunny Zhou, Joshua F. Alfaro, Steven Clarke, He G. Sun, Barry L. Karger, Jonathan D. Lowenson, Laura A. Gillies, Byung Ju Kim
Publikováno v:
Analytical Chemistry. 80:3882-3889
Isoaspartate formation is a ubiquitous post-translation modification arising from spontaneous asparagine deamidation or aspartate isomerization. The formation of isoaspartate inserts a methylene group into the protein backbone, generating a "kink", a
Autor:
Kathleen M. Dorgan, Erin L. Karschner, DonRaphael P. Wynn, Zhaohui Sunny Zhou, Yinqiu Cui, Joan M. Hevel, Joshua F. Alfaro, Whitney L. Wooderchak
Publikováno v:
Analytical Biochemistry. 350:249-255
Modification of small molecules and proteins by methyltransferases affects a wide range of biological processes. Here, we report an enzyme-coupled continuous spectrophotometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)
Publikováno v:
Pharmaceutical Research. 21:2095-2104
This study aims to evaluate a cytochrome P450-based tamoxifen-isoflavone interaction and to determine the mechanisms responsible for inhibitory effects of isoflavones (e.g., genistein) on the formation of alpha-hydroxytamoxifen.Metabolism studies wer
Publikováno v:
Organic Letters. 6:3043-3046
[reaction: see text] Quorum sensing is a process by which bacteria sense cell density. This cell-cell communication process is mediated by autoinducers. A cross-species messenger, autoinducer-2 (AI-2) is produced from S-ribosyl-L-homocysteine by the
Autor:
Shahrzad Mansouri, Zhaohui Sunny Zhou, Joshua F. Alfaro, Kenneth A. Cornell, Wei Wan, Bonnie L. Bassler, Gang Zhao
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 13:3897-3900
Bacterial quorum sensing is mediated by autoinducers, small signaling molecules generated by bacteria. It has been proposed that the LuxS enzyme converts S-ribosyl-L-homocysteine to 4,5-dihydroxy-2,3-pentanedione, the precursor of autoinducer 2 (AI-2
Publikováno v:
Journal of pharmaceutical sciences. 103(10)
The formation of aspartyl succinimide is a common post-translational modification of protein pharmaceuticals under acidic conditions. We present a method to detect and quantitate succinimide in intact protein via hydrazine trapping and chemical deriv