Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Paul N. Goudreau"'
Publikováno v:
Annual Review of Biochemistry. 69:183-215
▪ Abstract Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase and a response regulator protein. The histidine protein kinase, which i
Publikováno v:
Biochemistry. 37:14575-14584
The central signaling pathway in many bacterial regulatory systems involves phosphotransfer between two conserved proteins, a histidine protein kinase, and a response regulator. The occurrence of two-component signaling systems in thermophilic bacter
Publikováno v:
Biochemistry. 37:14038-14047
The response regulator CheB functions within the bacterial chemotaxis system together with the methyltransferase CheR to control the level of chemoreceptor methylation, influencing the signaling activities of the receptors. CheB catalyzes demethylati
Autor:
Paul N. Goudreau, Ann M. Stock
Publikováno v:
Current Opinion in Microbiology. 1:160-169
In bacteria, adaptive responses to changing environmental conditions are mediated by signal transduction systems that involve modular protein domains. Despite great diversity in the integration of domains into different systems, studies of individual
Publikováno v:
Proceedings of the National Academy of Sciences. 95:1381-1386
We report the x-ray crystal structure of the methylesterase CheB, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Methylesterase CheB and methyltransferase CheR modulate signaling
Autor:
Paul N. Goudreau, Martin P. Horvath, Michael R. Hobaugh, William T. Morgan, Suzanne J. Admiraal, James A. Fee, Tateo Yamanaka, Masao Ikeda-Saito, Jason S. Felsch, Taketomo Fujiwara, Susan Gursky, Yoshihiro Fukumori, Robert A. Copeland
Publikováno v:
Protein Science. 3:2097-2103
Second derivative absorption spectra are reported for the aa3-cytochrome c oxidase from bovine cardiac mitochondria, the aa3-600 ubiquinol oxidase from Bacillus subtilis, the ba3-cytochrome c oxidase from Thermus thermophilis, and the aco-cytochrome
Autor:
Amy Chang, Kenji Ohwaki, Erica Stec, Jeffrey P Varnerin, Toshimitsu Takagi, Berta Strulovici, Peter Hodder, Jun Kusunoki, Jonathan Schneeweis, Marc Ferrer, Oleg Kornienko, Paul N. Goudreau, Michael R. Tota, James Inglese, Christine C. Chung, Jason Cassaday, Lihu Yang, Takeru Yamakawa
Publikováno v:
Assay and drug development technologies. 6(3)
Here we report the development and miniaturization of a cell-free enzyme assay for ultra-high-throughput screening (uHTS) for inhibitors of two potential drug targets for obesity and cancer: fatty acid synthase (FAS) and acetyl-coenzyme A (CoA) carbo
Autor:
Alexey Rivkin, Yoona R. Kim, Mark T. Goulet, Nicole Ginanni, Jeffrey P Varnerin, Amy Chang, Nathan Bays, Michael R. Tota, Peter Strack, Stefan Krauss, Nancy E. Kohl, Armetta D. Hill, Christine C. Chung, Benito Munoz, Ilona Kariv, Paul N. Goudreau
Publikováno v:
Bioorganicmedicinal chemistry letters. 16(17)
A series of 3-aryl-4-hydroxyquinolin-2(1H)-ones with fatty acid synthase inhibitory activity was prepared. Starting from a derivative with an IC(50) = 1.4 microM, SAR studies led to compounds with more than 70-fold increase in potency (IC(50) < 20 nM
Publikováno v:
Protein science : a publication of the Protein Society. 9(5)
Enhancement of methylesterase activity of the response regulator CheB is dependent upon phosphorylation of the N-terminal regulatory domain of the enzyme. This domain plays a dual role in the regulation of methylesterase activity with an inhibitory e
Autor:
Richard D. Smith, Amy C. Harms, Xueheng Cheng, Paul N. Goudreau, Steven A. Hofstadler, James E. Bruce, Thomas C. Terwilliger, Ruidan Chen
Publisher Summary This chapter describes the feasibility of mass spectrometric analysis of structurally specific noncovalent biomolecular complexes and highlights the advantages of electrospray ionization (ESI)-Fourier transform ion cyclotron resonan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f27b906b46cbd267255d6df54971c64
https://doi.org/10.1016/s1080-8914(96)80005-6
https://doi.org/10.1016/s1080-8914(96)80005-6