| Year |
Citation |
Score |
| 2016 |
Kim JJ, Lorenz R, Arold ST, Reger AS, Sankaran B, Casteel DE, Herberg FW, Kim C. Crystal Structure of PKG I:cGMP Complex Reveals a cGMP-Mediated Dimeric Interface that Facilitates cGMP-Induced Activation. Structure (London, England : 1993). PMID 27066748 DOI: 10.1016/J.Str.2016.03.009 |
0.465 |
|
| 2016 |
Campbell JC, Kim JJ, Li KY, Huang GY, Reger AS, Matsuda S, Sankaran B, Link TM, Yuasa K, Ladbury JE, Casteel DE, Kim C. Structural Basis of Cyclic Nucleotide Selectivity in cGMP-Dependent Protein Kinase II. The Journal of Biological Chemistry. PMID 26769964 DOI: 10.1186/2050-6511-16-S1-A15 |
0.459 |
|
| 2015 |
Qin L, Reger AS, Guo E, Yang MP, Zwart P, Casteel DE, Kim C. Structures of cGMP-Dependent Protein Kinase (PKG) Iα Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability. Biochemistry. 54: 4419-22. PMID 26132214 DOI: 10.1021/Acs.Biochem.5B00572 |
0.406 |
|
| 2014 |
Reger AS, Yang MP, Koide-Yoshida S, Guo E, Mehta S, Yuasa K, Liu A, Casteel DE, Kim C. Crystal structure of the cGMP-dependent protein kinase II leucine zipper and Rab11b protein complex reveals molecular details of G-kinase-specific interactions. The Journal of Biological Chemistry. 289: 25393-403. PMID 25070890 DOI: 10.1074/Jbc.M114.575894 |
0.406 |
|
| 2014 |
Huang GY, Kim JJ, Reger AS, Lorenz R, Moon EW, Zhao C, Casteel DE, Bertinetti D, Vanschouwen B, Selvaratnam R, Pflugrath JW, Sankaran B, Melacini G, Herberg FW, Kim C. Structural basis for cyclic-nucleotide selectivity and cGMP-selective activation of PKG i Structure. 22: 116-124. PMID 24239458 DOI: 10.1016/J.Str.2013.09.021 |
0.502 |
|
| 2014 |
Campbell J, Huang G, Reger A, Link T, Ladbury J, Kim C. Insights into the Cyclic Nucleotide Selectivity Mechanism of Cyclic GMP Dependent Protein Kinase II Biophysical Journal. 106: 658a. DOI: 10.1016/J.Bpj.2013.11.3644 |
0.394 |
|
| 2013 |
Lorenz R, Moon E, Huang GY, Reger AS, Kim JJ, Franz E, Bertinetti D, Kim C, Herberg FW. Transforming PKA into PKG – a structure-function approach to understand cyclic nucleotide selectivity Bmc Pharmacology and Toxicology. 14. DOI: 10.1186/2050-6511-14-S1-P41 |
0.448 |
|
| 2013 |
Huang GY, Kim JJ, Reger AS, Lorenz R, Moon E, Zhao C, Casteel DE, Bertinetti D, VanSchouwen B, Selvaratnam R, Pflugrath JW, Sankaran B, Melacini G, Herberg FW, Kim C. Structures of human PKG reveal cGMP-selectived activation mechanisms Bmc Pharmacology and Toxicology. 14. DOI: 10.1186/2050-6511-14-S1-O16 |
0.379 |
|
| 2009 |
Wu R, Reger AS, Lu X, Gulick AM, Dunaway-Mariano D. The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase. Biochemistry. 48: 4115-25. PMID 19320426 DOI: 10.1021/Bi9002327 |
0.693 |
|
| 2008 |
Wu R, Cao J, Lu X, Reger AS, Gulick AM, Dunaway-Mariano D. Mechanism of 4-chlorobenzoate:coenzyme a ligase catalysis. Biochemistry. 47: 8026-39. PMID 18620421 DOI: 10.1021/Bi800698M |
0.673 |
|
| 2008 |
Reger AS, Wu R, Dunaway-Mariano D, Gulick AM. Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase. Biochemistry. 47: 8016-25. PMID 18620418 DOI: 10.1021/Bi800696Y |
0.727 |
|
| 2007 |
Wu R, Reger AS, Cao J, Gulick AM, Dunaway-Mariano D. Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range. Biochemistry. 46: 14487-99. PMID 18027984 DOI: 10.1021/Bi701609W |
0.686 |
|
| 2007 |
Reger AS, Carney JM, Gulick AM. Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase. Biochemistry. 46: 6536-46. PMID 17497934 DOI: 10.1021/Bi6026506 |
0.682 |
|
| 2006 |
Sundlov JA, Garringer JA, Carney JM, Reger AS, Drake EJ, Duax WL, Gulick AM. Determination of the crystal structure of EntA, a 2,3-dihydro-2,3-dihydroxybenzoic acid dehydrogenase from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 62: 734-40. PMID 16790929 DOI: 10.1107/S0907444906015824 |
0.57 |
|
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