Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Larry P. Solomonson"'
Publikováno v:
Biochemical and Biophysical Research Communications. 377:1042-1046
Argininosuccinate synthase (AS) is essential for endothelial nitric oxide (NO) production and its regulation in this capacity has been studied primarily at the transcriptional level. The dynamics of vascular function suggest that an acute regulation
Publikováno v:
Photosynthesis Research. 83:11-16
Publikováno v:
Journal of Biological Chemistry. 277:25363-25369
Based on the integral role that argininosuccinate synthase (AS) plays in the production of nitric oxide in vascular endothelial cells and urea in liver, an analysis was carried out to determine whether signals reside in the AS mRNA to account for tis
Autor:
Brenda R. Flam, Melissa Harrell-Booth, Larry P. Solomonson, Paul J. Hartmann, Duane C. Eichler
Publikováno v:
Nitric Oxide. 5:187-197
Although normal intracellular levels of arginine are well above the K(m), and should be sufficient to saturate nitric oxide synthase in vascular endothelial cells, nitric oxide production can, nonetheless, be stimulated by exogenous arginine. This ph
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1382:129-136
A water soluble truncated heme domain (a tetramer of MW = 45 kDa) of the tetrameric nitrate reductase complex from the green alga Chlorella vulgaris has been overexpressed and purified. This truncated heme domain with four identical subunits has a hi
Autor:
Gary Hellermann, Larry P. Solomonson
Publikováno v:
Journal of Biological Chemistry. 272:12030-12034
The active form of endothelial nitric-oxide synthase (eNOS) is a homodimer. The activity of the enzyme is regulated in vivo by calcium signaling involving the binding of calmodulin (CAM), which triggers the activation of eNOS. We have examined the po
Publikováno v:
Gene. 171:139-145
The reduction of nitrate to nitrite catalyzed by nitrate reductase (NR) is considered to be the rate-limiting and regulated step of nitrate assimilation, a major metabolic pathway occurring in a wide range of organisms which in turn supply the nutrit
Autor:
Eugene M. Barnes, Patricia A. Calkin, Satoshi Kuroda, Shigemi Norioka, Masanori Mitta, Ikunoshin Kato, Fumio Sakiyama, Heinz Nika, David T. Chow, Daniel Hess, Edward J. Bures, Hamish D. Morrison, Ruedi Aebersold, G. Marius Clore, Angela M. Gronenborn, Bengt Persson, Patrick Argos, Peter James, Andrew C. Cannons, Larry P. Solomonson, Kenneth E. Dombrowski, William E. Moddeman, Stephen E. Wright, Winona C. Barker, David G. George, Subhendra N. Mattagajasingh, Hara P. Misra, Shuan Shian Huang, Jung San Huang, Y. C. Lee, Wolfgang H. Fischer, A. Grey Craig, Philip N. McFadden, Jonathan A. Lind-quist, M. Bartlet-Jones, W. Jeffery, H. F. Hansen, D. J. C. Pappin, Tomas Bergman, Lars Hjelmqvist, Mats Estonius, Hans Jörnvall, Donna S. Dorow, H. Tschesche, V. Knäuper, T. Kleine, P. Reinemer, S. Schnierer, F. Grams, W. Bode, Christopher Southan, Kenneth Fantom, Patric Lavery, J. B. C. Findlay, D. Akrigg, T. K. Attwood, M. J. Beck, A. J. Bleasby, A. C. T. North, D. J. Parry-Smith, D. N. Perkins, A. Aitken, Y. Patel, H. Martin, D. Jones, K. Robinson, J. Madrazo, S. Howell, Tom Yungwirth, Michael Affolter, Lawrence Amankwa, Harold A. Scheraga, Chao -Yuh Yang, Natalia V. Valentinova, Manlan Yang, Zi -Wei Gu, Antonio M. Gotto, Norman J. Dovichi, Karen C. Waldron, Min Chen, Ian Ireland, Akira Omori, Sachiyo Yoshida, Johann Schaller, Stephan Lengweiler, Egon E. Rickli, José Bubis, Julio O. Ortiz, Carolina Möller, Enrique J. Millán, Victoria L. Boyd, MeriLisa Bozzini, Jindong Zhao, Robert J. DeFranco, Pau -Miau Yuan, G. Marc Loudon, Duy Nguyen, Masaharu Kamo, Takao Kawakami, Norifumi Miyatake, Akira Tsugita, Keiji Takamoto, Kazuo Satake, Oliver Bischof, Mirko Hechenberger, Bernd Thiede, Volker Kruft, Brigitte Wittmann-Liebold, Albrecht Otto, Rainer Benndorf, Peter Jungblut, Monika Ühlein, Henning Urlaub, Rita Berhardt, Regine Kraft, Heike Uhlmann, Vita Beckert, Toshifumi Akizawa, Takaaki Ayabe, Motomi Matsukawa, Michiyasu Itoh, Masatoshi Nishi, Hiroshi Sato, Motoharu Seiki, Masanori Yoshioka, Michal Lebl, Viktor Krchňák, Nikolai F. Sepetov, Petr Kočiš, Marcel Pátek, Zuzana Flegelová, Ronald Ferguson, Kit S. Lam, Robert L. Moritz, James Eddes, Hong Ji, Gavin E. Reid, Richard J. Simpson, William Seffens, C. Dale Poulter, Julia M. Dolence, Pamela D. Bond, Kiyoshi Nokihara, Kazuo Ikegaya, Naoki Morita, Takao Ohmura, S. I. Salikhov, N. J. Sagdiev, A. S. Korneev, Behzod Z. Dolimbek, M. Zhouhair Atassi, J. S. Rosenberg, Z. Yun, P. R. Wyde, M. Z. Atassi, Simon J. Gaskell, Kalyan Rao Anumula, David P. Goldenberg, Ettore Appella, Michelle Fiscella, Nicola Zambrano, Stephen J. Ullrich, Kazuyasu Sakaguchi, Hiroshi Sakamoto, Marc S. Lewis, David Lin, W. Edward Mercer, Carl W. Anderson, Marjorie A. Connelly, Hong Zhang, John D. Sipley, Susan P. Lees-Miller, Stephen P. Jackson, Yong-hong Xie, Jun A. Quion, Chao-yuh Yang, W. F. Brandt, H. Alk, R. Bhaskaran, Chin Yu, C. C. Yang, Agnes H. Henschen, Keith Ashman, Matthias Mann, Juan Guevara, Hung Michael Nguyen, Daniel B. Davison, Joel D. Morrisett, Richard N. Perham, Donald A. Marvin, Martyn F. Symmons, Tamsin D. Terry, Z. H. Beg, J. A. Stonik, J. M. Hoeg, H. B. Brewer, Boris M. Gorovits, C. S. Raman, Paul M. Horowtiz
Publikováno v:
Journal of Protein Chemistry. 13:431-512
Publikováno v:
Plant Physiology. 101:415-419
The major proteinase in maize (Zea mays) roots behaves as a serine endopeptidase. A possible physiological role of this enzyme could be in the turnover of nitrate reductase (NR) and, as such, it could be of great importance in regulating the assimila
Publikováno v:
Journal of Biological Chemistry. 268:3268-3271
A recombinant protein corresponding to the putative heme-binding domain of assimilatory NADH:nitrate reductase from Chlorella vulgaris has been expressed and purified from transformed Escherichia coli BL21 cells. The recombinant protein, exhibited a