Search Results - "Poland, Bradley W."

Comparing 2-nt 3' overhangs against blunt-ended siRNAs: a systems biology based study by Ghosh, Preetam, Dullea, Robert, Fischer, James E, Turi, Tom G, Sarver, Ronald W, Zhang, Chaoyang, Basu, Kalyan, Das, Sajal K, Poland, Bradley W

“…In this study, we formulate a computational reaction model following a chemical kinetic theory approach to predict the binding rate constant for the siRNA-RISC…”
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Mechanistic Implications from Crystalline Complexes of Wild-Type and Mutant Adenylosuccinate Synthetases from Escherichia coli by Choe, Jun-Yong, Poland, Bradley W, Fromm, Herbert J, Honzatko, Richard B

“…Asp13 and His41 are essential residues of adenylosuccinate synthetase, putatively catalyzing the formation of adenylosuccinate from an intermediate of…”
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Structural Insights into the Protein Splicing Mechanism of PI-SceI by Poland, Bradley W., Xu, Ming-Qun, Quiocho, Florante A.

“…PI-SceI is a member of a class of proteins (inteins) that excise themselves from a precursor protein and in the process ligate the flanking protein sequences…”
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Common pathways and cellular processes as revealed by computational analysis of expression patterns from Tg4510 mice and human Alzheimer brains by Zagouras, Panayiotis, Poland, Bradley W, Naik, Snehal, Kawabe, Thomas T, Brown, Tracy M, Peitzsch, Robert M, Hicks, Carol D, Milici, Anthony J

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Role of a Dynamic Loop in Cation Activation and Allosteric Regulation of Recombinant Porcine Fructose-1,6-bisphosphatase by Choe, Jun-Yong, Poland, Bradley W, Fromm, Herbert J, Honzatko, Richard B

“…A disordered loop (loop 52−72, residues 52−72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated in regulatory and catalytic…”
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Entrapment of 6-Thiophosphoryl-IMP in the Active Site of Crystalline Adenylosuccinate Synthetase from Escherichia coli by Poland, Bradley W., Bruns, Christina, Fromm, Herbert J., Honzatko, Richard B.

“…Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with Mg2+, 6-thiophosphoryl-IMP, GDP, and hadacidin at 298 and 100 K have…”
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Refined Crystal Structures of Guanine Nucleotide Complexes of Adenylosuccinate Synthetase from Escherichia coli by Poland, B W, Hou, Z, Bruns, C, Fromm, H J, Honzatko, R B

“…Structures of adenylosuccinate synthetase from Escherichia coli complexed with guanosine-5′-(β,γ-imido) triphosphate and…”
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Residues Essential for Catalysis and Stability of the Active Site of Escherichia coli Adenylosuccinate Synthetase as Revealed by Directed Mutation and Kinetics by Kang, C, Sun, N, Poland, B W, Gorrell, A, Honzatko, R B, Fromm, H J

“…Examined here by directed mutation, circular dichroism spectroscopy, and kinetics are the relationships of five residues, Asp 13 , Glu 14 , Lys 16 , His 41 ,…”
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Refined Crystal Structures of Guanine Nucleotide Complexes of Adenylosuccinate Synthetase from by Poland, Bradley W., Hou, Zenglin, Bruns, Christina, Fromm, Herbert J., Honzatko, Richard B.

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Major Changes in the Kinetic Mechanism of AMP Inhibition and AMP Cooperativity Attend the Mutation of Arg49 in Fructose-1,6-bisphosphatase by Shyur, Lie-Fen, Poland, Bradley W., Honzatko, Richard B., Fromm, Herbert J.

“…The significance of subunit interface residues Arg49 and Lys50 in the function of porcine liver fructose-1,6-bisphosphatase was explored by site-directed…”
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Identification of Arginine Residues in the Putative L-Aspartate Binding Site of Escherichiacoli Adenylosuccinate Synthetase by Wang, Wenyan, Poland, Bradley W., Honzatko, Richard B., Fromm, Herbert J.

“…Three arginine residues in the putative aspartate binding site of Escherichia coli adenylosuccinate synthetase were changed to leucines by site-directed…”
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P1‐140: Common pathways and cellular processes as revealed by computational analysis of expression patterns from Tg4510 mice and human Alzheimer brains by Zagouras, Panayiotis, Poland, Bradley W., Naik, Snehal, Kawabe, Thomas T., Brown, Tracy M., Peitzsch, Robert M., Hicks, Carol D., Milici, Anthony J.

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Crystal structure of S-glutathiolated carbonic anhydrase III by Mallis, Robert J., Poland, Bradley W., Chatterjee, Tapan K., Fisher, Rory A., Darmawan, Steven, Honzatko, Richard B., Thomas, James A.

“…S-Glutathiolation of carbonic anhydrase III (CAIII) occurs rapidly in hepatocytes under oxidative stress. The crystal structure of the S-glutathiolated CAIII…”
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Crystal Structures of Adenylosuccinate Synthetase fromEscherichia coliComplexed with GDP, IMP Hadacidin, NO3–, and Mg2 by Poland, Bradley W., Fromm, Herbert J., Honzatko, Richard B.

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Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO42-, Mg2+, and Hadacidin by POLAND, Bradley W., LEE, Shy-Fuh, SUBRAMANIAN, Mani V., SIEHL, Daniel L., ANDERSON, Richard J., FROMM, Herbert J., HONZATKO, Richard B.

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Crystal Structures of Adenylosuccinate Synthetase from Escherichia coliComplexed with GDP, IMP Hadacidin, NO 3–, and Mg 2 by Poland, Bradley W., Fromm, Herbert J., Honzatko, Richard B.

“…Crystal structures of adenylosuccinate synthetase from Esherichia colicomplexed with Mg 2 +, IMP, GDP, NO 3 –and hadacidin at 298 and 100 K have been refined…”
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Refined Crystal Structures of Unligated Adenylosuccinate Synthetase from Escherichia coli by Silva, M.Mercedes, Poland, Bradley W., Hoffman, Chad R., Fromm, Herbert J., Honzatko, Richard B.

“…Crystal structures of unligated adenylosuccinate synthetase from Escherichia coliin space groups P2 1and P2 12 12 1have been refined to R-factors of 0.199 and…”
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Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains by Poland, B W, Silva, M M, Serra, M A, Cho, Y, Kim, K H, Harris, E M, Honzatko, R B

“…The structure of the P2(1) crystal form of adenylosuccinate synthetase from Escherichia coli has been determined to a resolution of 2.8 A. The refined model…”
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Refined Crystal Structures of Unligated Adenylosuccinate Synthetase fromEscherichia coli by Silva, M.Mercedes, Poland, Bradley W., Hoffman, Chad R., Fromm, Herbert J., Honzatko, Richard B.

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Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetase by Wang, W, Poland, B W, Honzatko, R B, Fromm, H J

“…Three arginine residues in the putative aspartate binding site of Escherichia coli adenylosuccinate synthetase were changed to leucines by site-directed…”
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