Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Michael Strickler"'
Autor:
Barry M. Goldstein, Donald S. Matteson, Jeffrey P. Jones, Kathleen Maxfield, Michael Strickler, Gyung‐Youn Kim, Laura Shireman
Publikováno v:
Biochemistry. 42:11943-11950
Crystallographic and spectroscopic studies have been undertaken to characterize the binding behavior of the non-native substrate nicotine in the active site of the monooxygenase hemoprotein cytochrome P450cam. Despite the existence of a theoretical m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e5f3e222bbb782188561466debadcb4
https://doi.org/10.1021/bi034833o
https://doi.org/10.1021/bi034833o
Publikováno v:
Radiation Research, 154, 163-170. Radiation Research Society
The aim of this project was to gain an improved understanding of how the efficiency of hole and electron transfer from the solvation layer to DNA decreases as a function of distance from DNA. The packing of DNA in crystals of known structure makes it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc52daeadc464d7c27aad85290154fab
https://doi.org/10.1667/0033-7587(2000)154[0163:oteoha]2.0.co
https://doi.org/10.1667/0033-7587(2000)154[0163:oteoha]2.0.co
Autor:
Barry M. Goldstein, Kristen Vanderveen, Thomas D. Colby, Michael Strickler, George D. Markham
Publikováno v:
Proceedings of the National Academy of Sciences. 96:3531-3536
Inosine monophosphate dehydrogenase (IMPDH) controls a key metabolic step in the regulation of cell growth and differentiation. This step is the NAD-dependent oxidation of inosine 5′ monophosphate (IMP) to xanthosine 5′ monophosphate, the rate-li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::656e29ed803e12aef5158d1191cbbbf8
https://doi.org/10.1073/pnas.96.7.3531
https://doi.org/10.1073/pnas.96.7.3531
Autor:
Barry M. Goldstein, Christopher Ceccarelli, Michael Strickler, Judith P. Klinman, Zhao-Xun Liang, Brian J. Bahnson, Gerd Prehna
Publikováno v:
Biochemistry. 43(18)
The crystal structure of NAD + -dependent alcohol dehydrogenase from Bacillus stearother- mophilus strain LLD-R (htADH) was determined using X-ray diffraction data at a resolution of 2.35 A. The structure of homotetrameric htADH is highly homologous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::811222e662271687731b625ad1407401
https://pubmed.ncbi.nlm.nih.gov/15122892
https://pubmed.ncbi.nlm.nih.gov/15122892
Autor:
Krzysztof W. Pankiewicz, Barry M. Goldstein, George Weber, Yutaka Natsumeda, James L. Sherley, Jing Jin Gu, Sander Stegmann, Beverly S. Mitchell, Dongjiu Ye, Jeniece Nott, Sherry F. Queener, Dipesh Risal, Michael Strickler, George D. Markham, Lizbeth Hedstrom, Jennifer A. Digits, Victor E. Marquez, P. Franchetti, L. Cappellacci, M. Grifantini, H. N. Jayaram, B. M. Goldstein, Hiremagalur N. Jayaram, Joel A. Yalowitz, Georg Krupitza, Thomas Szekeres, Karsten Krohn, Steven Patterson, Frank R. Collart, Eliezer Huberman, Hiroaki Ishikawa, Masahiko Tsuchiya, Hiromichi Itoh
