Year |
Citation |
Score |
2011 |
Thévenin AF, Zony CL, Bahnson BJ, Colman RF. GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2. Protein Science : a Publication of the Protein Society. 20: 834-48. PMID 21384452 DOI: 10.1002/Pro.609 |
0.814 |
|
2011 |
De Zoysa Ariyananda L, Antonopoulos C, Currier J, Colman RF. In vitro hybridization and separation of hybrids of human adenylosuccinate lyase from wild-type and disease-associated mutant enzymes. Biochemistry. 50: 1336-46. PMID 21210713 DOI: 10.1021/Bi101734Q |
0.796 |
|
2011 |
Thévenin AF, Zony CL, Bahnson BJ, Colman RF. Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts. Protein Expression and Purification. 75: 138-46. PMID 20709173 DOI: 10.1016/J.Pep.2010.08.002 |
0.778 |
|
2010 |
Dange M, Colman RF. Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function. The Journal of Biological Chemistry. 285: 20520-5. PMID 20435888 DOI: 10.1074/Jbc.M110.115386 |
0.834 |
|
2009 |
Ariyananda Lde Z, Lee P, Antonopoulos C, Colman RF. Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants. Biochemistry. 48: 5291-302. PMID 19405474 DOI: 10.1021/Bi802321M |
0.559 |
|
2008 |
Hartong DT, Dange M, McGee TL, Berson EL, Dryja TP, Colman RF. Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle. Nature Genetics. 40: 1230-4. PMID 18806796 DOI: 10.1038/Ng.223 |
0.779 |
|
2008 |
Huang YC, Misquitta S, Blond SY, Adams E, Colman RF. Catalytically active monomer of glutathione S-transferase pi and key residues involved in the electrostatic interaction between subunits. The Journal of Biological Chemistry. 283: 32880-8. PMID 18796433 DOI: 10.1074/Jbc.M805484200 |
0.612 |
|
2008 |
Sivendran S, Colman RF. Effect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiens. Protein Science : a Publication of the Protein Society. 17: 1162-74. PMID 18469177 DOI: 10.1110/Ps.034777.108 |
0.817 |
|
2008 |
Hung SH, Liu AH, Pixley RA, Francis P, Williams LD, Matsko CM, Barnes KD, Sivendran S, Colman RF, Colman RW. A new nonhydrolyzable reactive cGMP analogue, (Rp)-guanosine-3',5'-cyclic-S-(4-bromo-2,3-dioxobutyl)monophosphorothioate, which targets the cGMP binding site of human platelet PDE3A. Bioorganic Chemistry. 36: 141-7. PMID 18394675 DOI: 10.1016/J.Bioorg.2008.02.006 |
0.778 |
|
2008 |
Ralat LA, Misquitta SA, Manevich Y, Fisher AB, Colman RF. Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin. Archives of Biochemistry and Biophysics. 474: 109-18. PMID 18358825 DOI: 10.1016/J.Abb.2008.02.043 |
0.814 |
|
2008 |
De Zoysa Ariyananda L, Colman RF. Evaluation of types of interactions in subunit association in Bacillus subtilis adenylosuccinate lyase. Biochemistry. 47: 2923-34. PMID 18237141 DOI: 10.1021/Bi701400C |
0.808 |
|
2007 |
Sivendran S, Segall ML, Rancy PC, Colman RF. Effect of Asp69 and Arg310 on the pK of His68, a key catalytic residue of adenylosuccinate lyase. Protein Science : a Publication of the Protein Society. 16: 1700-7. PMID 17600142 DOI: 10.1110/Ps.072927207 |
0.811 |
|
2007 |
Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL. Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism. Journal of Molecular Biology. 370: 541-54. PMID 17531264 DOI: 10.1016/J.Jmb.2007.04.052 |
0.514 |
|
2007 |
Bzymek KP, Colman RF. Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase. Biochemistry. 46: 5391-7. PMID 17432878 DOI: 10.1021/Bi700061T |
0.491 |
|
2007 |
Segall ML, Cashman MA, Colman RF. Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase. Protein Science : a Publication of the Protein Society. 16: 441-8. PMID 17322529 DOI: 10.1110/Ps.062650007 |
0.48 |
|
2007 |
Lee P, Colman RF. Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase. Protein Expression and Purification. 51: 227-34. PMID 16973378 DOI: 10.1016/J.Pep.2006.07.023 |
0.457 |
|
2007 |
Ralat LA, Misquitta SA, Zony CL, Manevich Y, Fisher AB, Colman RF. Evidence Supporting Model of Glutathione S‐Transferase pi/1‐Cysteine Peroxiredoxin Complex The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A644-A |
0.759 |
|
2007 |
Ariyananda LDZ, Colman R. Evaluation of Types of Interactions in Subunit Association in Bacillus subtilis Adenylosuccinate Lyase (ASL) The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A641-A |
0.336 |
|
2006 |
Ralat LA, Colman RF. Identification of tyrosine 79 in the tocopherol binding site of glutathione S-transferase pi. Biochemistry. 45: 12491-9. PMID 17029404 DOI: 10.1021/Bi061330K |
0.858 |
|
2006 |
Hung SH, Zhang W, Pixley RA, Jameson BA, Huang YC, Colman RF, Colman RW. New insights from the structure-function analysis of the catalytic region of human platelet phosphodiesterase 3A: a role for the unique 44-amino acid insert. The Journal of Biological Chemistry. 281: 29236-44. PMID 16873361 DOI: 10.1074/Jbc.M606558200 |
0.471 |
|
2006 |
Spiegel EK, Colman RF, Patterson D. Adenylosuccinate lyase deficiency. Molecular Genetics and Metabolism. 89: 19-31. PMID 16839792 DOI: 10.1016/J.Ymgme.2006.04.018 |
0.313 |
|
2006 |
Soundar S, O'hagan M, Fomulu KS, Colman RF. Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 281: 21073-81. PMID 16737955 DOI: 10.1074/Jbc.M602956200 |
0.398 |
|
2006 |
Lee P, Colman RF. Thr373, Asp375, and Lys260 are in the coenzyme site of porcine NADP-dependent isocitrate dehydrogenase. Archives of Biochemistry and Biophysics. 450: 183-90. PMID 16712772 DOI: 10.1016/J.Abb.2006.04.001 |
0.562 |
|
2006 |
Hearne JL, Colman RF. Catalytically active monomer of class mu glutathione transferase from rat. Biochemistry. 45: 5974-84. PMID 16681369 DOI: 10.1021/Bi060249E |
0.83 |
|
2006 |
Hearne JL, Colman RF. Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1. Protein Science : a Publication of the Protein Society. 15: 1277-89. PMID 16672236 DOI: 10.1110/Ps.062129506 |
0.84 |
|
2006 |
O'Sullivan SM, McCarthy RM, Vargo MA, Colman RF, Sheehan D. Chemical modification at subunit 1 of rat kidney Alpha class glutathione transferase with 2,3,5,6-tetrachloro-1,4-benzoquinone: close structural connectivity between glutathione conjugation activity and non-substrate ligand binding. Biochemical Pharmacology. 71: 1629-36. PMID 16620786 DOI: 10.1016/J.Bcp.2006.03.002 |
0.803 |
|
2006 |
Ralat LA, Manevich Y, Fisher AB, Colman RF. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry. 45: 360-72. PMID 16401067 DOI: 10.1021/Bi0520737 |
0.835 |
|
2006 |
Colman RF. Insights from affinity labeling into nucleotide- and coenzyme-dependent enzyme catalysis and regulation Letters in Drug Design and Discovery. 3: 462-480. DOI: 10.2174/157018006778194853 |
0.518 |
|
2005 |
Hearne JL, Colman RF. Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1. Protein Science : a Publication of the Protein Society. 14: 2526-36. PMID 16195544 DOI: 10.1110/Ps.051651905 |
0.84 |
|
2005 |
Huang YC, Colman RF. Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 280: 30349-53. PMID 15975917 DOI: 10.1074/Jbc.M505828200 |
0.557 |
|
2005 |
Misquitta SA, Colman RF. Communication between the two active sites of glutathione S-transferase A1-1, probed using wild-type-mutant heterodimers. Biochemistry. 44: 8608-19. PMID 15952767 DOI: 10.1021/Bi050449A |
0.557 |
|
2005 |
Lee P, Colman RF. Adenosine 2'-monophosphate, 5'-O-[S-(4-succinimidylbenzophenone)-thiophosphate]: a new photoaffinity label for the coenzyme site of porcine NADP-specific isocitrate dehydrogenase. Bioconjugate Chemistry. 16: 650-9. PMID 15898734 DOI: 10.1021/Bc049722W |
0.538 |
|
2005 |
Kim TK, Colman RF. Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate dehydrogenase. Protein Science : a Publication of the Protein Society. 14: 140-7. PMID 15576556 DOI: 10.1110/Ps.041091805 |
0.565 |
|
2005 |
Hung S, Zhang W, Tao J, Kim C, Noone R, Ezon D, Colman RF, Colman RW. New Insights from the Structure Function of the Catalytic Region of Human Platelet PDE3A: The Role of the Unique 44 Amino Acid Insert. Blood. 106: 3937-3937. DOI: 10.1182/Blood.V106.11.3937.3937 |
0.412 |
|
2004 |
Sivendran S, Patterson D, Spiegel E, McGown I, Cowley D, Colman RF. Two novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL. The Journal of Biological Chemistry. 279: 53789-97. PMID 15471876 DOI: 10.1074/Jbc.M409974200 |
0.766 |
|
2004 |
Ralat LA, Colman RF. Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site. The Journal of Biological Chemistry. 279: 50204-13. PMID 15347687 DOI: 10.1074/Jbc.M407445200 |
0.849 |
|
2004 |
Segall ML, Colman RF. Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis. Biochemistry. 43: 7391-402. PMID 15182182 DOI: 10.1021/Bi0494774 |
0.59 |
|
2004 |
Vargo MA, Colman RF. Heterodimers of wild-type and subunit interface mutant enzymes of glutathione S-transferase A1-1: interactive or independent active sites? Protein Science : a Publication of the Protein Society. 13: 1586-93. PMID 15152091 DOI: 10.1110/Ps.04694004 |
0.807 |
|
2004 |
Vargo MA, Nguyen L, Colman RF. Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium. Biochemistry. 43: 3327-35. PMID 15035604 DOI: 10.1021/Bi030245Z |
0.821 |
|
2004 |
Huang YC, Grodsky NB, Kim TK, Colman RF. Ligands of the Mn2+ bound to porcine mitochondrial NADP-dependent isocitrate dehydrogenase, as assessed by mutagenesis. Biochemistry. 43: 2821-8. PMID 15005617 DOI: 10.1021/Bi030253F |
0.505 |
|
2003 |
Ralat LA, Colman RF. Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi. Protein Science : a Publication of the Protein Society. 12: 2575-87. PMID 14573868 DOI: 10.1110/Ps.03249303 |
0.848 |
|
2003 |
Soundar S, Park JH, Huh TL, Colman RF. Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 278: 52146-53. PMID 14555658 DOI: 10.1074/Jbc.M306178200 |
0.481 |
|
2003 |
Kim TK, Lee P, Colman RF. Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 278: 49323-31. PMID 14512428 DOI: 10.1074/Jbc.M303781200 |
0.534 |
|
2003 |
Palenchar JB, Crocco JM, Colman RF. The characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase deficiencies. Protein Science : a Publication of the Protein Society. 12: 1694-705. PMID 12876319 DOI: 10.1110/Ps.0303903 |
0.846 |
|
2003 |
Palenchar JB, Colman RF. Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role. Biochemistry. 42: 1831-41. PMID 12590570 DOI: 10.1021/Bi020640+ |
0.841 |
|
2002 |
Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ. Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism. The Journal of Biological Chemistry. 277: 43454-62. PMID 12207025 DOI: 10.1074/Jbc.M207306200 |
0.503 |
|
2002 |
Lee P, Colman RF. Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial NADP-dependent isocitrate dehydrogenase. Archives of Biochemistry and Biophysics. 401: 81-90. PMID 12054490 DOI: 10.1016/S0003-9861(02)00041-3 |
0.58 |
|
2002 |
Huang YC, Colman RF. Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase. Biochemistry. 41: 5637-43. PMID 11969425 DOI: 10.1021/Bi0200716 |
0.555 |
|
2002 |
Hung SH, Madhusoodanan KS, Beres JA, Boyd RL, Baldwin JL, Zhang W, Colman RW, Colman RF. A new nonhydrolyzable reactive cAMP analog, (Sp)-adenosine-3',5'-cyclic-S-(4-bromo-2,3-dioxobutyl)monophosphorothioate irreversibly inactivates human platelet cGMP-inhibited cAMP phosphodiesterase. Bioorganic Chemistry. 30: 16-31. PMID 11955000 DOI: 10.1006/Bioo.2001.1226 |
0.338 |
|
2002 |
Hung SH, Madhusoodanan KS, Boyd RL, Baldwin JL, Colman RF, Colman RW. A nonhydrolyzable reactive cAMP analogue, (S(p))-8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3',5'-cyclic S-(methyl)monophosphorothioate, irreversibly inactivates human platelet cGMP-inhibited cAMP phosphodiesterase at micromolar concentrations. Biochemistry. 41: 2962-9. PMID 11863434 DOI: 10.1021/Bi0119823 |
0.41 |
|
2002 |
Brosius JL, Colman RF. Three subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are required. Biochemistry. 41: 2217-26. PMID 11841213 DOI: 10.1021/Bi011998T |
0.621 |
|
2001 |
Pettigrew NE, Colman RF. Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu. Archives of Biochemistry and Biophysics. 396: 225-30. PMID 11747301 DOI: 10.1006/Abbi.2001.2629 |
0.505 |
|
2001 |
Pettigrew NE, Brush EJ, Colman RF. 3-Methyleneoxindole: an affinity label of glutathione S-transferase pi which targets tryptophan 38. Biochemistry. 40: 7549-58. PMID 11412109 DOI: 10.1021/Bi002840W |
0.535 |
|
2001 |
Madhusoodanan KS, Colman RF. Adenosine 5'-0-[S-(4-succinimidyl-benzophenone)thiophosphate]: a new photoaffinity label of the allosteric ADP site of bovine liver glutamate dehydrogenase. Biochemistry. 40: 1577-86. PMID 11327816 DOI: 10.1021/Bi002336R |
0.585 |
|
2001 |
Vargo MA, Colman RF. Affinity labeling of rat glutathione S-transferase isozyme 1-1 by 17beta -iodoacetoxy-estradiol-3-sulfate. The Journal of Biological Chemistry. 276: 2031-6. PMID 11031273 DOI: 10.1074/Jbc.M008212200 |
0.829 |
|
2001 |
Colman RF, Barycki JJ, Vargo MA, Wang J. Probing subunit interactions in glutathione S-transferases using affinity labeling Chemico-Biological Interactions. 133: 159-162. |
0.795 |
|
2000 |
Brosius JL, Colman RF. A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis. Biochemistry. 39: 13336-43. PMID 11063569 DOI: 10.1021/Bi001488J |
0.561 |
|
2000 |
Mseeh F, Colman RF, Colman RW. Inactivation of platelet PDE2 by an affinity label: 8-[(4-bromo-2, 3-dioxobutyl)thio]cAMP. Thrombosis Research. 98: 395-401. PMID 10828479 DOI: 10.1016/S0049-3848(00)00195-X |
0.518 |
|
2000 |
Huang YC, Soundar S, Colman RF. Affinity cleavage at the divalent metal site of porcine NAD-specific isocitrate dehydrogenase. Protein Science : a Publication of the Protein Society. 9: 104-11. PMID 10739252 DOI: 10.1110/Ps.9.1.104 |
0.485 |
|
2000 |
Grodsky NB, Soundar S, Colman RF. Evaluation by site-directed mutagenesis of aspartic acid residues in the metal site of pig heart NADP-dependent isocitrate dehydrogenase. Biochemistry. 39: 2193-200. PMID 10694384 DOI: 10.1021/Bi9919753 |
0.53 |
|
2000 |
Soundar S, Danek BL, Colman RF. Identification by mutagenesis of arginines in the substrate binding site of the porcine NADP-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 275: 5606-12. PMID 10681542 DOI: 10.1074/Jbc.275.8.5606 |
0.567 |
|
2000 |
Wang J, Bauman S, Colman RF. Probing subunit interactions in alpha class rat liver glutathione S-transferase with the photoaffinity label glutathionyl S-[4-(succinimidyl)benzophenone]. The Journal of Biological Chemistry. 275: 5493-503. PMID 10681528 DOI: 10.1074/Jbc.275.8.5493 |
0.814 |
|
1999 |
Lee P, Gorrell A, Fromm HJ, Colman RF. 8-(4-Bromo-2,3-dioxobutylthio)guanosine 5'-triphosphate: a new affinity label for purine nucleotide sites in proteins. Archives of Biochemistry and Biophysics. 372: 205-13. PMID 10562435 DOI: 10.1006/Abbi.1999.1488 |
0.55 |
|
1999 |
Lee P, Gorrell A, Fromm HJ, Colman RF. Implication of arginine-131 and arginine-303 in the substrate site of adenylosuccinate synthetase of Escherichia coli by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate. Biochemistry. 38: 5754-63. PMID 10231526 DOI: 10.1021/Bi982779J |
0.586 |
|
1999 |
Pettigrew NE, Moyer-Myers M, Colman RF. Affinity labeling of pig lung glutathione S-transferase pi by 4-(fluorosulfonyl)benzoic acid. Archives of Biochemistry and Biophysics. 364: 107-14. PMID 10087171 DOI: 10.1006/Abbi.1999.1126 |
0.575 |
|
1999 |
Lee TT, Worby C, Bao ZQ, Dixon JE, Colman RF. His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis. Biochemistry. 38: 22-32. PMID 9890879 DOI: 10.1021/Bi982299S |
0.587 |
|
1999 |
Colman RF, Barycki JJ. Affinity labeling of rat GST A1-1 by 3β-(iodoacetoxy)dehydroisoandrosterone Clinical Chemistry and Enzymology Communications. 8: 255-259. |
0.641 |
|
1998 |
Wang J, Bauman S, Colman RF. Photoaffinity labeling of rat liver glutathione S-transferase, 4-4, by glutathionyl S-[4-(succinimidyl)-benzophenone]. Biochemistry. 37: 15671-9. PMID 9843371 DOI: 10.1021/Bi981381K |
0.795 |
|
1998 |
Lee TT, Worby C, Bao ZQ, Dixon JE, Colman RF. Implication of His68 in the substrate site of Bacillus subtilis adenylosuccinate lyase by mutagenesis and affinity labeling with 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-monophosphate. Biochemistry. 37: 8481-9. PMID 9622500 DOI: 10.1021/Bi9805339 |
0.62 |
|
1998 |
Chen H, Huang YC, Colman RF. Identification of the subunit and important target peptides of pig heart NAD-dependent isocitrate dehydrogenase modified by the affinity label adenosine 5'-O-[S-(4-bromo-2, 3-dioxobutyl)thiophosphate]. Biochemistry. 37: 6541-51. PMID 9572872 DOI: 10.1021/Bi973032G |
0.531 |
|
1997 |
Huang YC, Kumar A, Colman RF. Identification of the subunits and target peptides of pig heart NAD-specific isocitrate dehydrogenase modified by the affinity label 8-(4-bromo-2,3-dioxobutylthio)NAD. Archives of Biochemistry and Biophysics. 348: 207-18. PMID 9390193 DOI: 10.1006/Abbi.1997.0392 |
0.54 |
|
1997 |
Barycki JJ, Colman RF. Identification of the nonsubstrate steroid binding site of rat liver glutathione S-transferase, isozyme 1-1, by the steroid affinity label, 3beta-(iodoacetoxy)dehydroisoandrosterone. Archives of Biochemistry and Biophysics. 345: 16-31. PMID 9281307 DOI: 10.1006/Abbi.1997.0244 |
0.812 |
|
1997 |
Colman RF. Affinity labels for NAD(P)-specific sites. Methods in Enzymology. 280: 186-203. PMID 9211314 DOI: 10.1016/S0076-6879(97)80110-3 |
0.519 |
|
1997 |
Colman RF. Chemical arrows for enzymatic targets. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 11: 217-26. PMID 9068610 DOI: 10.1096/Fasebj.11.4.9068610 |
0.481 |
|
1997 |
Hu L, Colman RF. Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111. Biochemistry. 36: 1635-45. PMID 9048547 DOI: 10.1021/Bi962119J |
0.675 |
|
1997 |
Omburo GA, Torphy TJ, Scott G, Jacobitz S, Colman RF, Colman RW. Inactivation of recombinant monocyte cAMP-specific phosphodiesterase by cAMP analog, 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3',5'-cyclic monophosphate. Blood. 89: 1019-26. PMID 9028334 DOI: 10.1182/Blood.V89.3.1019 |
0.496 |
|
1997 |
Hu L, Borleske BL, Colman RF. Probing the active site of alpha-class rat liver glutathione S-transferases using affinity labeling by monobromobimane. Protein Science : a Publication of the Protein Society. 6: 43-52. PMID 9007975 DOI: 10.1002/Pro.5560060105 |
0.659 |
|
1997 |
Lee TT, Worby C, Dixon JE, Colman RF. Identification of His141 in the active site of Bacillus subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate. The Journal of Biological Chemistry. 272: 458-65. PMID 8995283 DOI: 10.1074/Jbc.272.1.458 |
0.586 |
|
1997 |
Lee TT, Worhv C, Dixon JE, Colman RF. Probing the substrate binding site of b. subtilis adenylosuccinate lyase by affinity labeling with 2-[(4-bromo2,3-dioxobutyl)thio] adenosine 5'-monophosphate Faseb Journal. 11: A898. |
0.305 |
|
1996 |
Soundar S, Jennings GT, McAlister-Henn L, Colman RF. Expression of pig heart mitochondrial NADP-dependent isocitrate dehydrogenase in Escherichia coli. Protein Expression and Purification. 8: 305-12. PMID 8936592 DOI: 10.1006/Prep.1996.0105 |
0.517 |
|
1996 |
Wang J, Barycki JJ, Colman RF. Tyrosine 8 contributes to catalysis but is not required for activity of rat liver glutathione S-transferase, 1-1. Protein Science : a Publication of the Protein Society. 5: 1032-42. PMID 8762135 DOI: 10.1002/Pro.5560050606 |
0.858 |
|
1996 |
Moe OA, Baker-Malcolm JF, Wang W, Kang C, Fromm HJ, Colman RF. Involvement of arginine 143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from Escherichia coli. Biochemistry. 35: 9024-33. PMID 8703905 DOI: 10.1021/Bi960426J |
0.574 |
|
1996 |
Puri RN, Colman RF, Colman RW. Platelet activation by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-diphosphate is mediated by its binding to a putative ADP receptor, aggregin. European Journal of Biochemistry / Febs. 236: 862-70. PMID 8665907 DOI: 10.1111/J.1432-1033.1996.00862.X |
0.32 |
|
1996 |
Gite SU, Colman RF. Affinity Labeling of the active site of rabbit muscle adenylosuccinate lyase by 2-[(4-bromo-2.3-dioxobutyl)thio] adenosine 5'-monophosphate. Biochemistry. 35: 2658-67. PMID 8611571 DOI: 10.1021/Bi952640Y |
0.532 |
|
1995 |
Colman RF. Affinity labeling and related approaches to targeting specific enzyme sites. Sub-Cellular Biochemistry. 24: 177-205. PMID 7900176 DOI: 10.1007/978-1-4899-1727-0_7 |
0.578 |
|
1995 |
Huang YC, Haselbeck RJ, McAlister-Henn L, Colman RF. N-ethylmaleimide profiling of yeast NADP-dependent isocitrate dehydrogenase. Archives of Biochemistry and Biophysics. 316: 485-92. PMID 7840654 DOI: 10.1006/Abbi.1995.1064 |
0.447 |
|
1995 |
Ehrlich RS, Colman RF. Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart. Biochimica Et Biophysica Acta. 1246: 135-41. PMID 7819280 DOI: 10.1016/0167-4838(94)00192-J |
0.399 |
|
1995 |
Hu L, Colman RF. Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3. The Journal of Biological Chemistry. 270: 21875-83. PMID 7665611 DOI: 10.1074/Jbc.270.37.21875 |
0.719 |
|
1994 |
Vollmer SH, Walner MB, Tarbell KV, Colman RF. Guanosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate and adenosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate. New nucleotide affinity labels which react with rabbit muscle pyruvate kinase. The Journal of Biological Chemistry. 269: 8082-90. PMID 8132533 |
0.316 |
|
1994 |
Kumar A, Colman RF. 8-(4-Bromo-2,3-dioxobutylthio)NAD: a new affinity label for NAD-specific isocitrate dehydrogenase. Archives of Biochemistry and Biophysics. 308: 357-66. PMID 8109965 DOI: 10.1006/Abbi.1994.1051 |
0.584 |
|
1994 |
Wrzeszczynski KO, Colman RF. Activation of bovine liver glutamate dehydrogenase by covalent reaction of adenosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)thiophosphate] with arginine-459 at an ADP regulatory site. Biochemistry. 33: 11544-53. PMID 7918368 DOI: 10.1021/Bi00204A017 |
0.572 |
|
1994 |
Colman RF. Targeting enzyme sites in pyruvate kinase, glutamate dehydrogenase and glutathione S-transferase Pure and Applied Chemistry. 66: 15-26. DOI: 10.1351/Pac199466010015 |
0.528 |
|
1993 |
Park I, Ozturk DH, Soundar S, Colman RF. Nicotinamide ribose 5'-O-[S-(3-bromo-2-oxopropyl)]thiophosphate: a new affinity label for NMN sites in enzymes. Archives of Biochemistry and Biophysics. 303: 483-8. PMID 8512330 DOI: 10.1006/Abbi.1993.1312 |
0.454 |
|
1993 |
Soundar S, Colman RF. Identification of metal-isocitrate binding site of pig heart NADP-specific isocitrate dehydrogenase by affinity cleavage of the enzyme by Fe(2+)-isocitrate. The Journal of Biological Chemistry. 268: 5264-71. PMID 8444900 |
0.314 |
|
1993 |
Barycki JJ, Colman RF. Affinity labeling of glutathione S-transferase, isozyme 4-4, by 4-(fluorosulfonyl)benzoic acid reveals Tyr115 to be an important determinant of xenobiotic substrate specificity. Biochemistry. 32: 13002-11. PMID 8241154 DOI: 10.1021/Bi00211A008 |
0.82 |
|
1993 |
Zhou G, Charbonneau H, Colman RF, Zalkin H. Identification of sites for feedback regulation of glutamine 5-phosphoribosylpyrophosphate amidotransferase by nucleotides and relationship to residues important for catalysis. The Journal of Biological Chemistry. 268: 10471-81. PMID 7683680 |
0.495 |
|
1992 |
Haselbeck RJ, Colman RF, McAlister-Henn L. Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase. Biochemistry. 31: 6219-23. PMID 1627563 DOI: 10.1021/Bi00142A007 |
0.451 |
|
1992 |
Dombrowski KE, Huang YC, Colman RF. Identification of amino acids modified by the bifunctional affinity label 5'-(p-(fluorosulfonyl)benzoyl)-8-azidoadenosine in the reduced coenzyme regulatory site of bovine liver glutamate dehydrogenase. Biochemistry. 31: 3785-93. PMID 1567833 DOI: 10.1021/Bi00130A008 |
0.512 |
|
1992 |
Mills DC, Puri R, Hu CJ, Minniti C, Grana G, Freedman MD, Colman RF, Colman RW. Clopidogrel inhibits the binding of ADP analogues to the receptor mediating inhibition of platelet adenylate cyclase. Arteriosclerosis and Thrombosis : a Journal of Vascular Biology / American Heart Association. 12: 430-6. PMID 1558834 DOI: 10.1161/01.Atv.12.4.430 |
0.321 |
|
1992 |
Smyth GE, Colman RF. Inactivation of pig heart NADP-specific isocitrate dehydrogenase by two affinity reagents is due to reaction with a cysteine not essential for function. Archives of Biochemistry and Biophysics. 293: 356-61. PMID 1536572 DOI: 10.1016/0003-9861(92)90406-M |
0.567 |
|
1992 |
Haeffner-Gormley L, Chen Z, Zalkin H, Colman RF. Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium. Biochemistry. 31: 7807-14. PMID 1510967 DOI: 10.1021/Bi00149A010 |
0.505 |
|
1992 |
Ehrlich RS, Colman RF. Selectivity in the binding of NAD(P)+ analogues to NAD- and NADP-dependent pig heart isocitrate dehydrogenases. A nuclear magnetic resonance study. Biochemistry. 31: 12524-31. PMID 1463739 DOI: 10.1021/Bi00164A032 |
0.501 |
|
1992 |
Katusz RM, Bono B, Colman RF. Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3. Archives of Biochemistry and Biophysics. 298: 667-77. PMID 1416995 DOI: 10.1016/0003-9861(92)90464-8 |
0.475 |
|
1992 |
Katusz RM, Bono B, Colman RF. Affinity labeling of Cys111 of glutathione S-transferase, isoenzyme 1-1, by S-(4-bromo-2,3-dioxobutyl)glutathione. Biochemistry. 31: 8984-90. PMID 1390685 DOI: 10.1021/Bi00152A040 |
0.498 |
|
1992 |
Ozturk DH, Park I, Colman RF. Guanosine 5'-O-[S-(3-bromo-2-oxopropyl)]thiophosphate: a new reactive purine nucleotide analog labeling Met-169 and Tyr-262 in bovine liver glutamate dehydrogenase. Biochemistry. 31: 10544-55. PMID 1329952 DOI: 10.1021/Bi00158A018 |
0.542 |
|
1992 |
Grant PG, DeCamp DL, Bailey JM, Colman RF, Colman RW. Low-Km cyclic AMP phosphodiesterase from human platelets. Stimulation of activity by phosphorylation of the enzyme and affinity labeling of the active site. Advances in Second Messenger and Phosphoprotein Research. 25: 73-85. PMID 1313273 |
0.36 |
|
1992 |
Haeffner-Gormley L, Chen ZD, Zalkin H, Colman RF. Reaction of the nucleotide analogue 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 2',5'-bisphosphate at the coenzyme site of wild-type and mutant NADP(+)-specific glutamate dehydrogenases from Salmonella typhimurium. Archives of Biochemistry and Biophysics. 292: 179-89. PMID 1309291 DOI: 10.1016/0003-9861(92)90066-6 |
0.52 |
|
1992 |
Vollmer SH, Colman RF. Cysteinyl peptides labeled by dibromobutanedione in reaction with rabbit muscle pyruvate kinase. Protein Science : a Publication of the Protein Society. 1: 678-87. PMID 1304366 DOI: 10.1002/Pro.5560010513 |
0.451 |
|
1992 |
Ozturk DH, Park I, Colman RF. Guanosine 5′-O-[S-(3-bromo-2-oxopropyl)]thiophosphate: A new reactive purine nucleotide analog labeling Met-169 and Tyr-262 in bovine liver glutamate dehydrogenase Biochemistry. 31: 10544-10555. |
0.446 |
|
1991 |
Katusz RM, Colman RF. S-(4-Bromo-2,3-dioxobutyl)glutathione: a new affinity label for the 4-4 isoenzyme of rat liver glutathione S-transferase. Biochemistry. 30: 11230-8. PMID 1958660 DOI: 10.1021/Bi00111A006 |
0.459 |
|
1991 |
Smyth GE, Colman RF. Cysteinyl peptides of pig heart NADP-dependent isocitrate dehydrogenase that are modified upon inactivation by N-ethylmaleimide. The Journal of Biological Chemistry. 266: 14918-25. PMID 1869531 |
0.346 |
|
1991 |
Ozturk DH, Colman RF. Identification of cysteine-319 as the target amino acid of 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-triphosphate in bovine liver glutamate dehydrogenase. Biochemistry. 30: 7126-34. PMID 1854724 DOI: 10.1021/Bi00243A013 |
0.54 |
|
1991 |
Haeffner-Gormley L, Chen ZD, Zalkin H, Colman RF. Evaluation of cysteine 283 and glutamic acid 284 in the coenzyme binding site of Salmonella typhimurium glutamate dehydrogenase by site-directed mutagenesis and reaction with the nucleotide analogue 2-[4-bromo-2,3-dioxobutyl)thio)-1,N6-ethenoadenosine 2',5'-bisphosphate. The Journal of Biological Chemistry. 266: 5388-94. PMID 1672312 |
0.468 |
|
1990 |
Ehrlich RS, Colman RF. Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart. Biochemistry. 29: 5179-87. PMID 2378874 DOI: 10.1021/Bi00473A026 |
0.431 |
|
1990 |
Vollmer SH, Colman RF. Cysteinyl peptides of rabbit muscle pyruvate kinase labeled by the affinity label 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-triphosphate. Biochemistry. 29: 2495-501. PMID 2334678 DOI: 10.1021/Bi00462A009 |
0.414 |
|
1990 |
Lark RH, Colman RF. Distance between the substrate and regulatory reduced coenzyme binding sites of bovine liver glutamate dehydrogenase by resonance energy transfer. European Journal of Biochemistry / Febs. 188: 377-83. PMID 2318212 DOI: 10.1111/J.1432-1033.1990.Tb15414.X |
0.57 |
|
1990 |
Colman RF, Bailey JM, DeCamp DL, Huang YC, Vollmer SH. Affinity labeling of adenine nucleotide sites in enzymes. Annals of the New York Academy of Sciences. 603: 417-26. PMID 2291535 DOI: 10.1111/J.1749-6632.1990.Tb37690.X |
0.531 |
|
1990 |
Huang YC, Colman RF. Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase. Biochemistry. 29: 8266-73. PMID 2252888 DOI: 10.1021/Bi00488A010 |
0.417 |
|
1990 |
Ozturk DH, Safer D, Colman RF. Affinity labeling of bovine liver glutamate dehydrogenase with 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-diphosphate and 5'-triphosphate. Biochemistry. 29: 7112-8. PMID 2223765 DOI: 10.1021/Bi00482A024 |
0.573 |
|
1990 |
Grant PG, DeCamp DL, Bailey JM, Colman RW, Colman RF. Three new potential cAMP affinity labels. Inactivation of human platelet low Km cAMP phosphodiesterase by 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3',5'-cyclic monophosphate. Biochemistry. 29: 887-94. PMID 2160272 DOI: 10.1021/Bi00456A006 |
0.49 |
|
1990 |
Colman RF. Affinity labeling of nucleotide binding sites of enzymes and platelets. Advances in Experimental Medicine and Biology. 281: 257-63. PMID 1966353 DOI: 10.1007/978-1-4615-3806-6_26 |
0.587 |
|
1990 |
Colman RF. 6 Site-Specific Modification of Enzyme Sites Enzymes. 19: 283-321. DOI: 10.1016/S1874-6047(08)60199-7 |
0.565 |
|
1989 |
Batra SP, Lark RH, Colman RF. Identification of histidyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5′-monophosphate in an ADP regulatory site of glutamate dehydrogenase Archives of Biochemistry and Biophysics. 270: 277-285. PMID 2930190 DOI: 10.1016/0003-9861(89)90029-5 |
0.476 |
|
1989 |
Dombrowski KE, Colman RF. 5'-p-fluorosulfonyl)benzoyl-8-azidoadenosine: a new bifunctional affinity label for nucleotide binding sites in proteins. Archives of Biochemistry and Biophysics. 275: 302-8. PMID 2817902 DOI: 10.1016/0003-9861(89)90377-9 |
0.549 |
|
1989 |
Colman RF. Affinity labels and spectroscopic probes of porcine heart NADP-dependent isocitrate dehydrogenase Biochemical Society Transactions. 17: 307-311. PMID 2753210 DOI: 10.1042/Bst0170307 |
0.334 |
|
1989 |
Huang YC, Colman RF. Aspartyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-diphosphate in the allosteric ADP site of pig heart NAD+-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 264: 12208-14. PMID 2745437 |
0.395 |
|
1989 |
Bansal A, Dayton MA, Zalkin H, Colman RF. Affinity labeling of a glutamyl peptide in the coenzyme binding site of NADP+-specific glutamate dehydrogenase of Salmonella typhimurium by 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate. The Journal of Biological Chemistry. 264: 9827-35. PMID 2656714 |
0.448 |
|
1989 |
Saha A, Huang YC, Colman RF. Cysteinyl peptide labeled by 3-bromo-2-ketoglutarate in the active site of pig heart NAD+-dependent isocitrate dehydrogenase. Biochemistry. 28: 8425-31. PMID 2605193 DOI: 10.1021/Bi00447A023 |
0.466 |
|
1989 |
Ehrlich RS, Colman RF. Multinuclear NMR studies of the divalent metal binding site of NADP-dependent isocitrate dehydrogenase from pig heart Biochemistry. 28: 2058-2065. PMID 2541772 DOI: 10.1021/Bi00431A014 |
0.425 |
|
1989 |
DeCamp DL, Colman RF. 2-[(4-Bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 5'-diphosphate. A new fluorescent affinity label of a tyrosyl residue in the active site of rabbit muscle pyruvate kinase. The Journal of Biological Chemistry. 264: 8430-41. PMID 2489027 |
0.453 |
|
1988 |
Saha A, Colman RF. Modification of NAD-dependent isocitrate dehydrogenase by the 2′,3′-dialdehyde derivatives of NAD, NADH, NADP, and NADPH Archives of Biochemistry and Biophysics. 264: 665-677. PMID 3401017 DOI: 10.1016/0003-9861(88)90333-5 |
0.576 |
|
1988 |
DeCamp DL, Lim S, Colman RF. Reaction of pyruvate kinase with the new nucleotide affinity labels 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-diphosphate and 5′-triphosphate Biochemistry. 27: 7651-7658. PMID 3207694 DOI: 10.1021/Bi00420A012 |
0.499 |
|
1987 |
Colman RF. Distances among coenzyme and metal Sites of NADP+-dependent isocitrate dehydrogenase using resonance energy transfer Biochemistry®. 26: 4893-4900. PMID 3663631 DOI: 10.1021/Bi00389A042 |
0.489 |
|
1987 |
Ehrlich RS, Colman RF. Ionization of isocitrate bound to pig heart NADP+-dependent isocitrate dehydrogenase: 13C NMR study of substrate binding Biochemistry. 26: 3461-3466. PMID 3651391 DOI: 10.1021/Bi00386A032 |
0.416 |
|
1987 |
Ehrlich RS, Colman RF. Characterization of an active site peptide modified by the substrate analogue 3-bromo-2-ketoglutarate on a single chain of dimeric NADP+-dependent isocitrate dehydrogenase Journal of Biological Chemistry. 262: 12614-12619. PMID 3624273 |
0.53 |
|
1987 |
Bailey JM, Colman RF. 2-[(4-Bromo-2,3-dioxobutyl)thio]- and 2-[(3-bromo-2-oxopropyl)thio]adenosine 2′,5′-bisphosphate: New nucleotide analogues that act as affinity labels of nicotinamide adenine dinucleotide phosphate specific isocitrate dehydrogenase Biochemistry. 26: 6858-6869. PMID 3427047 DOI: 10.1021/Bi00395A041 |
0.471 |
|
1987 |
Bailey JM, Colman RF. Isolation of the glutamyl peptide labeled by the nucleotide analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N(6)-ethenoadenosine 2',5'-biphosphate in the active site of NADP+-specific isocitrate dehydrogenase Journal of Biological Chemistry. 262: 12620-12626. PMID 2887570 |
0.429 |
|
1986 |
Batra SP, Colman RF. Affinity labeling of an allosteric ADP site of glutamate dehydrogenase by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-monophosphate Journal of Biological Chemistry. 261: 15565-15571. PMID 3782079 |
0.511 |
|
1986 |
Huang YC, Bailey JM, Colman RF. Inactivation of NAD-dependent isocitrate dehydrogenase by affinity labeling of the allosteric ADP site by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-diphosphate Journal of Biological Chemistry. 261: 14100-14107. PMID 3771526 |
0.448 |
|
1986 |
Lark RH, Colman RF. Reaction of the 2',3'-dialdehyde derivative of NADPH at a nucleotide site of bovine glutamate dehydrogenase Journal of Biological Chemistry. 261: 10659-10666. PMID 3733724 |
0.471 |
|
1986 |
Batra SP, Colman RF. Isolation and identification of cysteinyl peptide labeled by 6-[(4-bromo-2,3-dioxobutyl)thio]-6-deaminoadenosine 5′-diphosphate in the reduced diphosphopyridine nucleotide inhibitory site of glutamate dehydrogenase Biochemistry. 25: 3508-3515. PMID 3718940 DOI: 10.1021/Bi00360A005 |
0.497 |
|
1986 |
DeCamp DL, Colman RF. Identification of tyrosine and lysine peptides labeled by 5'-p-fluorosulfonylbenzoyl adenosine in the active site of pyruvate kinase The Journal of Biological Chemistry. 261: 4499-4503. PMID 3082867 |
0.383 |
|
1985 |
Kapetanovic E, Bailey JM, Colman RF. 2-[(4-Bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate, a new nucleotide analogue that acts as an affinity label of pyruvate kinase Biochemistry. 24: 7586-7593. PMID 4092026 DOI: 10.1021/Bi00347A013 |
0.524 |
|
1985 |
Ehrlich RS, Colman RF. 1H nuclear magnetic resonance studies of the conformation and environment of nucleotides bound to pig heart NADP+-dependent isocitrate dehydrogenase Biochemistry. 24: 5378-5387. PMID 4074702 DOI: 10.1021/Bi00341A016 |
0.458 |
|
1985 |
Bailey JM, Colman RF. Affinity labeling of NADP+-specific isocitrate dehydrogenase by a new fluorescent nucleotide analogue, 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2′,5′-bisphosphate Biochemistry. 24: 5367-5377. PMID 4074701 DOI: 10.1021/Bi00341A015 |
0.516 |
|
1985 |
Tomich JM, Colman RF. Reaction of 5′-p-fluorosulfonylbenzoyl-1,N6-ethenoadenosine with histidine and cysteine residues in the active site of rabbit muscle pyruvate kinase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 827: 344-357. PMID 3970942 DOI: 10.1016/0167-4838(85)90219-5 |
0.691 |
|
1985 |
Mas MT, Colman RF. Spectroscopic studies of the interactions of coenzymes and coenzyme fragments with pig heart, oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase Biochemistry. 24: 1634-1646. PMID 3843532 DOI: 10.1021/Bi00328A011 |
0.505 |
|
1985 |
Colman RF. New developments in affinity labeling of purine nucleotide sites in enzymes Federation Proceedings. 44: No. 7916. |
0.401 |
|
1984 |
Mas MT, Colman RF. Phosphorus-31 nuclear magnetic resonance studies of the binding of nucleotides to NADP+-specific isocitrate dehydrogenase Biochemistry. 23: 1675-1683. PMID 6722120 DOI: 10.1021/Bi00303A015 |
0.492 |
|
1984 |
Jacobson MA, Colman RF. Evaluation of the intramolecular stacking of the fluorosulfonylbenzoyl derivatives of 1-N6-ethenoadenosine, adenosine, and guanosine Journal of Biological Chemistry. 259: 1454-1460. PMID 6693416 |
0.635 |
|
1984 |
Huang YC, Colman RF. Affinity labeling of the allosteric ADP activation site of NAD-dependent isocitrate dehydrogenase by 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-diphosphate Journal of Biological Chemistry. 259: 12481-12488. PMID 6548473 |
0.449 |
|
1984 |
Jacobson MA, Colman RF. Isolation and identification of a tyrosyl peptide labeled by 5′-[p-(fluorosulfonyl)benzoyl]-1,N6-ethenoadenosine at a GTP site of glutamate dehydrogenase Biochemistry. 23: 6377-6382. PMID 6529553 DOI: 10.1021/Bi00321A014 |
0.738 |
|
1984 |
Batra SP, Colman RF. Affinity labeling of the reduced diphosphopyridine nucleotide inhibitory site of glutamate dehydrogenase by 6-[(4-bromo-2,3-dioxobutyl)thio]-6-deaminoadenosine 5′-diphosphate Biochemistry. 23: 4940-4946. PMID 6498169 DOI: 10.1021/Bi00316A018 |
0.574 |
|
1984 |
Jacobson MA, Colman RF. Distance relationships between the catalytic site labeled with 4-(iodoacetamido)salicylic acid and regulatory sites of glutamate dehydrogenase Biochemistry. 23: 3789-3798. PMID 6487574 DOI: 10.1021/Bi00312A001 |
0.761 |
|
1984 |
Ehrlich RS, Colman RF. The role of dissimilar subunits of NAD-specific isocitrate dehydrogenase from pig heart. Evaluation using affinity labeling Journal of Biological Chemistry. 259: 11936-11942. PMID 6480590 |
0.368 |
|
1984 |
Colman RF, Huang YC, King MM, Erb M. 6-[(4-bromo-2,3-dioxobutyl)thio]-6-deaminoadenosine 5'-monophosphate and 5'-diphosphate: new affinity labels for purine nucleotide sites in proteins Biochemistry. 23: 3281-3286. PMID 6466641 DOI: 10.1021/Bi00309A025 |
0.531 |
|
1984 |
Schmidt JA, Colman RF. Identification of the lysine and tyrosine peptides labeled by 5'-p-fluorosulfonylbenzoyladenosine in the NADH inhibitory site of glutamate dehydrogenase. The Journal of Biological Chemistry. 259: 14515-9. PMID 6438099 |
0.406 |
|
1984 |
Batra SP, Colman RF. Affinity labeling of the NADH inhibitory site of glutamate dehydrogenase by 6-(4-bromo-2,3-dioxobutyl)-thioadenosine 5'- diphosphate Federation Proceedings. 43: no. 2199. |
0.305 |
|
1984 |
Yu-chu Huang, Colman RF. Affinity labelling of the allosteric ADP activation site of NAD+ dependent isocitrate dehydrogenase by 6-(4-bromo-2,3- dioxobutyl)-thioadenosine 5'-diphosphate Federation Proceedings. 43: no. 1683. |
0.392 |
|
1984 |
Schmidt JA, Colman RF. Identification of LYS and TYR residues in the NADH inhibitory site of glutamate dehydrogenase Federation Proceedings. 43: no. 739. |
0.321 |
|
1983 |
Mas MT, Colman RF. Modification of TPN-dependent isocitrate dehydrogenase by the 2', 3'-dialdehyde derivatives of TPNH and TPN Journal of Biological Chemistry. 258: 9332-9338. PMID 6874692 |
0.475 |
|
1983 |
King MM, Colman RF. Affinity labeling of nicotinamide adenine dinucleotide dependent isocitrate dehydrogenase by the 2',3'-dialdehyde derivative of adenosine 5'-diphosphate. Evidence for the formation of an unusual reaction product Biochemistry. 22: 1656-1665. PMID 6849874 DOI: 10.1021/Bi00276A021 |
0.358 |
|
1983 |
Jacobson MA, Colman RF. Resonance energy transfer between the adenosine 5prime;-diphosphate site of glutamate dehydrogenase and a guanosine 5′-triphosphate site containing a tyrosine labeled with 5′-[p-(Fluorosulfonyl)benzoyl]-1,N6-ethenoadenosine Biochemistry. 22: 4247-4257. PMID 6414507 DOI: 10.1021/Bi00287A014 |
0.764 |
|
1983 |
Reimann JE, Grant PG, Colman RW, Colman RF. Synthesis and characterization of iodopropyl derivatives of adenosine 3′,5′-cyclic-monophosphate: Potential affinity labels of cAMP binding sites in enzymes Journal of Protein Chemistry. 2: 113-129. DOI: 10.1007/Bf01025376 |
0.389 |
|
1982 |
Annamalai AE, Tomich JM, Mas MT, Colman RF. Evidence for distinguishable sites of attack in the reactions of 5′-p-fluorosulfonylbenzoyl adenosine and 5′-p-fluorosulfonylbenzoyl guanosine with rabbit muscle pyruvate kinase Archives of Biochemistry and Biophysics. 219: 47-57. PMID 7181514 DOI: 10.1016/0003-9861(82)90132-1 |
0.626 |
|
1982 |
Hayman S, Colman RF. Activity associated with individual subunits of pig heart NAD-specific isocitrate dehydrogenase Archives of Biochemistry and Biophysics. 218: 492-501. PMID 7159097 DOI: 10.1016/0003-9861(82)90373-3 |
0.375 |
|
1982 |
Bednar RA, Colman RF. Chemical modification A probe of the structure and function of the subunits of DPN-dependent isocitrate dehydrogenase. The Journal of Biological Chemistry. 257: 11734-9. PMID 7118908 |
0.747 |
|
1982 |
Bednar RA, Hartman FC, Colman RF. 3,4-Didehydro-2-ketoglutarate: an affinity label for diphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 21: 3690-7. PMID 7115695 DOI: 10.1021/Bi00258A026 |
0.698 |
|
1982 |
Bednar RA, Hartman FC, Colman RF. 3-Bromo-2-ketoglutarate: a substrate and affinity label for diphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 21: 3681-9. PMID 7115694 DOI: 10.1021/Bi00258A025 |
0.73 |
|
1982 |
Jacobson MA, Colman RF. Affinity labeling of a guanosine 5′-triphosphate site of glutamate dehydrogenase by a fluorescent nucleotide analogue, 5′-[p-(fluorosulfonyl)benzoyl]-1,N6-ethenoadenosine Biochemistry. 21: 2177-2186. PMID 7093238 DOI: 10.1021/Bi00538A029 |
0.735 |
|
1982 |
Ehrlich RS, Colman RF. Interrelationships among nucleotide binding sites of pig heart NAD-dependent isocitrate dehydrogenase Journal of Biological Chemistry. 257: 4769-4774. PMID 7068663 |
0.331 |
|
1982 |
Jadus M, Hanson RW, Colman RF. Inactivation of phosphoenolpyruvate carboxykinase by the guanosine nucleotide analogue, 5'-p-fluorosulfonylbenzoyl guanosine. Biochemical and Biophysical Research Communications. 101: 884-92. PMID 6458292 DOI: 10.1016/0006-291X(81)91832-5 |
0.358 |
|
1982 |
Bednar RA, Colman RF. Synthesis, characterization, and reactions of 2′-, 3′-, and 5′-(2-bromoethyl)-AMP: Potential affinity labels for nucleotide binding sites in enzymes Journal of Protein Chemistry. 1: 203-224. DOI: 10.1007/Bf01025000 |
0.722 |
|
1981 |
Bacon CR, Bednar RA, Colman RF. The reaction of 4-iodoacetamidosalicylic acid with TPN-dependent isocitrate dehydrogenase from pig heart. The Journal of Biological Chemistry. 256: 6593-9. PMID 7240232 |
0.616 |
|
1981 |
Johanson RA, Colman RF. Cysteine in the manganous-isocitrate binding site of pig heart TPN-specific isocitrate dehydrogenase. I. Kinetics of chemical modification and properties of thiocyano enzyme. Archives of Biochemistry and Biophysics. 207: 9-20. PMID 7235724 DOI: 10.1016/0003-9861(81)90002-3 |
0.562 |
|
1981 |
Johanson RA, Colman RF. Cysteine in the manganous-isocitrate binding site of pig heart TPN-specific isocitrate dehydrogenase. II. Identification of a critical cysteine-containing tryptic peptide derived from the thiocyano enzyme. Archives of Biochemistry and Biophysics. 207: 21-31. PMID 7235719 DOI: 10.1016/0003-9861(81)90003-5 |
0.471 |
|
1981 |
Likos JJ, Colman RF. Affinity labeling of rabbit muscle pyruvate kinase by a new fluorescent nucleotide alkylating agent 5′-[p-(fluorosulfonyl)benzoyl]-1 ,N6-ethenoadenosine Biochemistry. 20: 491-499. PMID 7213592 DOI: 10.1021/Bi00506A008 |
0.553 |
|
1981 |
Saradambal KV, Bednar RA, Colman RF. Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase. The Journal of Biological Chemistry. 256: 11866-72. PMID 6795194 |
0.662 |
|
1981 |
Tomich JM, Marti C, Colman RF. Modification of two essential cysteines in rabbit muscle pyruvate kinase by the guanine nucleotide analogue 5′-[p-(fluorosulfonyl)benzoyl]guanosine Biochemistry. 20: 6711-6720. DOI: 10.1021/Bi00526A029 |
0.717 |
|
1980 |
Stevens E, Colman RF. Chemical modification of enzymes: critical evaluation of the graphical correlation between residual enzyme activity and number of groups modified. Bulletin of Mathematical Biology. 42: 239-55. PMID 7370445 DOI: 10.1007/bf02464640 |
0.404 |
|
1980 |
Roy S, Colman RF. Affinity labeling of a lysine residue in the coenzyme binding site of pig heart mitochondrial malate dehydrogenase. Biochemistry. 18: 4683-90. PMID 497160 DOI: 10.1021/Bi00588A032 |
0.393 |
|
1980 |
STEVENS E, COLMAN R. Chemical modification of enzymes: Critical evaluation of the graphical correlation between residual enzyme activity and number of groups modified Bulletin of Mathematical Biology. 42: 239-255. DOI: 10.1016/S0092-8240(80)80042-5 |
0.478 |
|
1979 |
Pal PK, Colman RF. Affinity labeling of an allosteric GTP site of bovine liver glutamate dehydrogenase by 5'-p-fluorosulfonylbenzoylguanosine. Biochemistry. 18: 838-45. PMID 570414 DOI: 10.1021/Bi00572A016 |
0.383 |
|
1979 |
Hayman S, Colman RF. Effect of arginine modification on the catalytic activity and allosteric activation by adenosine diphosphate of the diphosphopyridine nucleotide specific isocitrate dehydrogenase of pig heart. Biochemistry. 17: 4161-8. PMID 213104 DOI: 10.1021/Bi00613A009 |
0.416 |
|
1979 |
Ehrlich RS, Colman RF. Histidine in the nucleotide-binding site of NADP-linked isocitrate dehydrogenase from pig heart. European Journal of Biochemistry. 89: 575-87. PMID 30632 DOI: 10.1111/J.1432-1033.1978.Tb12562.X |
0.542 |
|
1978 |
Ramachandran N, Colman RF. Evidence for the presence of two nonidentical subunits in NAD-dependent isocitrate dehydrogenase of pig heart. Proceedings of the National Academy of Sciences of the United States of America. 75: 252-5. PMID 203934 DOI: 10.1073/pnas.75.1.252 |
0.397 |
|
1978 |
Seelig GF, Colman RF. Characterization of the physicochemical and catalytic properties of human heart NADP-dependent isocitrate dehydrogenase. Archives of Biochemistry and Biophysics. 188: 394-409. PMID 28091 DOI: 10.1016/S0003-9861(78)80024-1 |
0.526 |
|
1977 |
Colman RF, Pal PK, Wyatt JL. Adenosine derivatives for dehydrogenases and kinases. Methods in Enzymology. 46: 240-9. PMID 909414 DOI: 10.1016/S0076-6879(77)46027-0 |
0.46 |
|
1977 |
Hayman S, Colman RF. Reaction of essential lysyl residues of pig heart diphosphyridine nucleotide dependent isocitrate dehydrogenase with 2,4-pentanedione. Biochemistry. 16: 998-1005. PMID 191059 DOI: 10.1021/Bi00624A030 |
0.576 |
|
1977 |
Ehrlich RS, Colman RF. The role of arginine in the triphosphopyridine nucleotide dependent isocitrate dehydrogenase of pig heart. Biochemistry. 16: 3378-83. PMID 19048 DOI: 10.1021/Bi00634A014 |
0.304 |
|
1977 |
Ramachandran N, Colman RF. Evidence for a critical glutamyl and an aspartyl residue in the function of pig heart diphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 16: 1564-73. PMID 15585 DOI: 10.1021/Bi00627A006 |
0.549 |
|
1977 |
Wyatt JL, Colman RF. Affinity labeling of rabbit muscle pyruvate kinase by 5'-p-fluorosulfonylbenzoyladenosine. Biochemistry. 16: 1333-42. PMID 14678 DOI: 10.1021/Bi00626A015 |
0.51 |
|
1976 |
Ehrlich RS, Colman RF. Coenzyme binding by native and chemically modified pig heart triphosphopyridine nucleotide dependent isocitrate dehydrogenase. Biochemistry. 14: 5008-16. PMID 241396 DOI: 10.1021/Bi00693A035 |
0.513 |
|
1976 |
Pal PK, Colman RF. The importance of arginine residues in the catalytic and regulatory functions of bovine-liver glutamate dehydrogenase. European Journal of Biochemistry. 68: 437-43. PMID 185052 DOI: 10.1111/J.1432-1033.1976.Tb10831.X |
0.565 |
|
1976 |
Ehrlich RS, Colman RF. Influence of substrates and coenzymes on the role of manganous ion in reactions catalyzed by pig heart triphosphopyridine nucleotide-dependent isocitrate dehydrogenase. Biochemistry. 15: 4034-41. PMID 9128 DOI: 10.1021/Bi00663A018 |
0.351 |
|
1976 |
Mauck L, Colman RF. Alkylation of cysteinyl residues of pig heart NAD-specific isocitrate dehydrogenase by iodoacetate. Biochimica Et Biophysica Acta. 429: 301-15. PMID 4125 DOI: 10.1016/0005-2744(76)90278-3 |
0.593 |
|
1976 |
Colman RF. Mechanisms for the oxidative decarboxylation of isocitrate: implications for control. Advances in Enzyme Regulation. 13: 413-33. PMID 1977 DOI: 10.1016/0065-2571(75)90028-X |
0.544 |
|
1975 |
Cohen PF, Colman RF. Role of manganous ion in the kinetics of pig-heart NAD-specific isocitrate dehydrogenase. European Journal of Biochemistry. 47: 35-45. PMID 4373239 DOI: 10.1111/J.1432-1033.1974.Tb03665.X |
0.485 |
|
1975 |
Pal PK, Wechter WJ, Colman RF. Affinity labeling of a regulatory site of bovine liver glutamate dehydrogenase. Biochemistry. 14: 707-15. PMID 1167788 DOI: 10.1021/Bi00675A010 |
0.587 |
|
1975 |
Ramachandran N, Durbano M, Colman RF. CorrigendumKinetic isotope effects in the NAD- and NADP-specific isocitrate dehydrogenases of pig heart Febs Letters. 52. DOI: 10.1016/0014-5793(75)80664-8 |
0.311 |
|
1974 |
Villafranca JJ, Colman RF. Frequency and temperature dependence of the proton relaxation rates of solvent and substrate interaction with isocitrate dehydrogenase bound Mn(II). Biochemistry. 13: 1152-60. PMID 4360780 DOI: 10.1021/Bi00703A016 |
0.319 |
|
1974 |
Ramachandran N, Durbano M, Colman RF. Kinetic isotope effects in the NAD- and NADP-specific isocitrate dehydrogenases of pig heart. Febs Letters. 49: 129-33. PMID 4155374 DOI: 10.1016/0014-5793(74)80648-4 |
0.337 |
|
1972 |
Cohen PF, Colman RF. Diphosphopyridine nucleotide dependent isocitrate dehydrogenase from pig heart. Charactgerization of the active substrate and modes of regulation. Biochemistry. 11: 1501-8. PMID 4336621 DOI: 10.1021/Bi00758A027 |
0.347 |
|
1971 |
Colman RF. [202] Glutathione reductase (Yeast)☆ Methods in Enzymology. 17: 500-503. DOI: 10.1016/0076-6879(71)17088-7 |
0.509 |
|
1970 |
Colman RF. Binding of substrates by native and chemically modified isocitrate dehydrogenase. Biochimica Et Biophysica Acta. 191: 469-72. PMID 4390952 DOI: 10.1016/0005-2744(69)90267-8 |
0.34 |
|
1969 |
Colman RF. The role of sulfhydryl groups in the catalytic function of isocitrate dehydrogenase. I. Reaction with 5,5'-dithiobis(2-nitrobenzoic acid). Biochemistry. 8: 888-98. PMID 4388636 DOI: 10.1021/Bi00831A019 |
0.331 |
|
1967 |
Colman RF. Evidence for a methionyl residue in the active site of isocitrate dehydrogenase. Biochemical and Biophysical Research Communications. 28: 222-8. PMID 6035498 DOI: 10.1016/0006-291X(67)90433-0 |
0.357 |
|
1967 |
Frieden C, Colman RF. Glutamate dehydrogenase concentration as a determinant in the effect of purine nucleotides on enzymatic activity. The Journal of Biological Chemistry. 242: 1705-15. PMID 4381598 |
0.535 |
|
1966 |
Colman RF, Frieden C. On the role of amino groups in the structure and function of glutamate dehydrogenase. II. Effect of acetylation on molecular properties. The Journal of Biological Chemistry. 241: 3661-70. PMID 4288133 |
0.487 |
|
1966 |
Colman RF, Frieden C. On the role of amino groups in the structure and function of glutamate dehydrogenase. I. Effect of acetylation on catalytic and regulatory properties. The Journal of Biological Chemistry. 241: 3652-60. PMID 4288132 |
0.516 |
|
1966 |
Colman RF, Frieden C. Cooperative interaction between the GTP binding sites of glutamate dehydrogenase. Biochemical and Biophysical Research Communications. 22: 100-5. PMID 4287088 DOI: 10.1016/0006-291X(66)90609-7 |
0.562 |
|
1965 |
COLMAN RF, BLACK S. ON THE ROLE OF FLAVIN ADENINE DINUCLEOTIDE AND THIOL GROUPS IN THE CATALYTIC MECHANISM OF YEAST GLUTATHIONE REDUCTASE. The Journal of Biological Chemistry. 240: 1796-803. PMID 14285527 |
0.537 |
|
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