Year |
Citation |
Score |
2012 |
Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Uncensored exchange of scientific results (Proceedings of the National Academy of Sciences (2003) 100, 4, (1464) DOI: 10.1073/pnas.0630491100) Proceedings of the National Academy of Sciences of the United States of America. 109: 8352. DOI: 10.1073/Pnas.1206993109 |
0.481 |
|
2011 |
Hammes GG, Benkovic SJ, Hammes-Schiffer S. Flexibility, diversity, and cooperativity: pillars of enzyme catalysis. Biochemistry. 50: 10422-30. PMID 22029278 DOI: 10.1021/Bi201486F |
0.399 |
|
2011 |
Alberty RA, Cornish-Bowden A, Goldberg RN, Hammes GG, Tipton K, Westerhoff HV. Recommendations for terminology and databases for biochemical thermodynamics. Biophysical Chemistry. 155: 89-103. PMID 21501921 DOI: 10.1016/J.Bpc.2011.03.007 |
0.53 |
|
2008 |
Hammes GG. How do enzymes really work? The Journal of Biological Chemistry. 283: 22337-46. PMID 18477561 DOI: 10.1074/Jbc.X800005200 |
0.333 |
|
2008 |
Benkovic SJ, Hammes GG, Hammes-Schiffer S. Free-energy landscape of enzyme catalysis. Biochemistry. 47: 3317-21. PMID 18298083 DOI: 10.1021/Bi800049Z |
0.336 |
|
2007 |
Smiley RD, Collins TR, Hammes GG, Hsieh TS. Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II. Proceedings of the National Academy of Sciences of the United States of America. 104: 4840-5. PMID 17360343 DOI: 10.1073/Pnas.0700342104 |
0.318 |
|
2007 |
Hammes GG. SINGLE MOLECULE STUDIES OF ENZYME DYNAMICS AND MECHANISMS The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A90-B |
0.319 |
|
2006 |
Smiley RD, Hammes GG. Single molecule studies of enzyme mechanisms. Chemical Reviews. 106: 3080-94. PMID 16895319 DOI: 10.1021/Cr0502955 |
0.33 |
|
2005 |
Antikainen NM, Smiley RD, Benkovic SJ, Hammes GG. Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase. Biochemistry. 44: 16835-43. PMID 16363797 DOI: 10.1021/Bi051378I |
0.388 |
|
2004 |
Zhang Z, Rajagopalan PT, Selzer T, Benkovic SJ, Hammes GG. Single-molecule and transient kinetics investigation of the interaction of dihydrofolate reductase with NADPH and dihydrofolate. Proceedings of the National Academy of Sciences of the United States of America. 101: 2764-9. PMID 14978269 DOI: 10.1073/Pnas.0400091101 |
0.4 |
|
2003 |
Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Statement on scientific publication and security. Science (New York, N.Y.). 299: 1149. PMID 12595658 DOI: 10.1126/Science.299.5610.1149 |
0.461 |
|
2003 |
Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Statement on the consideration of biodefence and biosecurity. Nature. 421: 771. PMID 12594463 DOI: 10.1038/Nature01479 |
0.472 |
|
2003 |
Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Uncensored exchange of scientific results. Proceedings of the National Academy of Sciences of the United States of America. 100: 1464. PMID 12590129 DOI: 10.1073/pnas.0630491100 |
0.438 |
|
2002 |
Rajagopalan PT, Zhang Z, McCourt L, Dwyer M, Benkovic SJ, Hammes GG. Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics. Proceedings of the National Academy of Sciences of the United States of America. 99: 13481-6. PMID 12359872 DOI: 10.1073/Pnas.172501499 |
0.389 |
|
2002 |
Hammes GG. Multiple conformational changes in enzyme catalysis. Biochemistry. 41: 8221-8. PMID 12081470 DOI: 10.1021/Bi0260839 |
0.383 |
|
1998 |
FASELLA P, HAMMES GG, VALLEE BL. Concerning the role of metals in enzymic transamination. Biochimica Et Biophysica Acta. 65: 142-3. PMID 13944491 DOI: 10.1016/0006-3002(62)90158-0 |
0.402 |
|
1998 |
FASELLA P, HAMMES GG. Studies of the enzyme hexokinase. IV. The role of sulfhydryl groups. Archives of Biochemistry and Biophysics. 100: 295-7. PMID 13944490 DOI: 10.1016/0003-9861(63)90075-4 |
0.318 |
|
1998 |
Hammes GG. A golden era for understanding enzyme mechanisms. Protein Science : a Publication of the Protein Society. 7: 799-802. PMID 9541414 DOI: 10.1002/Pro.5560070331 |
0.34 |
|
1995 |
Fierke CA, Hammes GG. Transient kinetic approaches to enzyme mechanisms. Methods in Enzymology. 249: 3-37. PMID 7791616 DOI: 10.1016/0076-6879(95)49029-9 |
0.392 |
|
1990 |
Musier-Forsyth KM, Hammes GG. Rotational dynamics of chloroplast ATP synthase in phospholipid vesicles. Biochemistry. 29: 3236-41. PMID 2159333 DOI: 10.1021/Bi00465A014 |
0.663 |
|
1990 |
Chang SI, Hammes GG. Structure and mechanism of action of a multifunctional enzyme: Fatty acid synthase Accounts of Chemical Research. 23: 363-369. DOI: 10.1021/Ar00179A003 |
0.526 |
|
1989 |
Chang SI, Hammes GG. Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase. Biochemistry. 28: 3781-8. PMID 2751995 DOI: 10.1021/Bi00435A023 |
0.557 |
|
1989 |
Holzer KP, Liu W, Hammes GG. Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA. Proceedings of the National Academy of Sciences of the United States of America. 86: 4387-91. PMID 2734291 DOI: 10.1073/Pnas.86.12.4387 |
0.307 |
|
1989 |
Chang SI, Hammes GG. Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast. Proceedings of the National Academy of Sciences of the United States of America. 86: 8373-6. PMID 2682649 DOI: 10.1073/Pnas.86.21.8373 |
0.546 |
|
1989 |
Mitra B, Hammes GG. Structural map of the dicyclohexylcarbodiimide site of chloroplast coupling factor determined by resonance energy transfer. Biochemistry. 28: 3063-9. PMID 2525921 DOI: 10.1021/Bi00433A049 |
0.345 |
|
1988 |
Kashem MA, Hammes GG. Correlation of enzymatic activities and aggregation state in chicken liver fatty acid synthase. Biochimica Et Biophysica Acta. 956: 39-48. PMID 3408738 DOI: 10.1016/0167-4838(88)90295-6 |
0.365 |
|
1988 |
Chang SI, Hammes GG. Amino acid sequences of substrate-binding sites in chicken liver fatty acid synthase. Biochemistry. 27: 4753-60. PMID 3167014 DOI: 10.1021/Bi00413A026 |
0.534 |
|
1988 |
Musier KM, Hammes GG. Assessment of the number of nucleotide binding sites on chloroplast coupling factor 1 by the continuous variation method. Biochemistry. 27: 7015-20. PMID 2904277 DOI: 10.1021/Bi00418A052 |
0.345 |
|
1988 |
Leckband D, Hammes GG. Function of tightly bound nucleotides on membrane-bound chloroplast coupling factor. Biochemistry. 27: 3629-33. PMID 2900652 DOI: 10.1021/Bi00410A016 |
0.59 |
|
1988 |
Mitra B, Hammes GG. Characterization of three-subunit chloroplast coupling factor. Biochemistry. 27: 245-50. PMID 2894846 DOI: 10.1021/Bi00401A037 |
0.371 |
|
1987 |
Musier KM, Hammes GG. Rotation of nucleotide sites is not required for the enzymatic activity of chloroplast coupling factor 1. Biochemistry. 26: 5982-8. PMID 2891373 DOI: 10.1021/Bi00393A006 |
0.303 |
|
1987 |
Leckband D, Hammes GG. Interactions between nucleotide binding sites on chloroplast coupling factor during ATP hydrolysis. Biochemistry. 26: 2306-12. PMID 2887200 DOI: 10.1021/Bi00382A035 |
0.623 |
|
1987 |
Admon A, Hammes GG. Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1. Biochemistry. 26: 3193-7. PMID 2886150 DOI: 10.1021/Bi00385A038 |
0.352 |
|
1987 |
McCarty RE, Hammes GG. Molecular architecture of chloroplast coupling factor 1 Trends in Biochemical Sciences. 12: 234-237. DOI: 10.1016/0968-0004(87)90116-2 |
0.332 |
|
1986 |
Leanz GF, Hammes GG. Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase. Biochemistry. 25: 5617-24. PMID 3535882 DOI: 10.1021/Bi00367A041 |
0.395 |
|
1986 |
Chang SI, Hammes GG. Interaction of spin-labeled nicotinamide adenine dinucleotide phosphate with chicken liver fatty acid synthase. Biochemistry. 25: 4661-8. PMID 3021196 DOI: 10.1021/Bi00364A031 |
0.566 |
|
1986 |
Schinkel JE, Hammes GG. Chloroplast coupling factor 1: dependence of rotational correlation time on polypeptide composition. Biochemistry. 25: 4066-71. PMID 2874828 DOI: 10.1021/Bi00362A012 |
0.358 |
|
1986 |
Krupinski J, Hammes GG. Steady-state ATP synthesis by bacteriorhodopsin and chloroplast coupling factor co-reconstituted into asolectin vesicles. Proceedings of the National Academy of Sciences of the United States of America. 83: 4233-7. PMID 2872676 DOI: 10.1073/Pnas.83.12.4233 |
0.306 |
|
1985 |
Krupinski J, Hammes GG. Phase-lifetime spectrophotometry of deoxycholate-purified bacteriorhodopsin reconstituted into asolectin vesicles. Biochemistry. 24: 6963-72. PMID 4074733 DOI: 10.1021/Bi00345A032 |
0.307 |
|
1985 |
Yuan ZY, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. Acylation of specific binding sites. The Journal of Biological Chemistry. 260: 13532-8. PMID 4055747 |
0.312 |
|
1985 |
Anderson VE, Hammes GG. Distribution of reaction intermediates on chicken liver fatty acid synthase. Biochemistry. 24: 2147-54. PMID 3995008 DOI: 10.1021/Bi00330A007 |
0.566 |
|
1985 |
Cognet JA, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: beta-ketoacyl reductase and enoyl reductase. Biochemistry. 24: 290-7. PMID 3978075 DOI: 10.1021/Bi00323A008 |
0.415 |
|
1985 |
Kambouris NG, Hammes GG. Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate. Proceedings of the National Academy of Sciences of the United States of America. 82: 1950-3. PMID 3856872 DOI: 10.1073/Pnas.82.7.1950 |
0.341 |
|
1985 |
Richter ML, Snyder B, McCarty RE, Hammes GG. Binding stoichiometry and structural mapping of the epsilon polypeptide of chloroplast coupling factor 1. Biochemistry. 24: 5755-63. PMID 2867774 DOI: 10.1021/Bi00342A011 |
0.406 |
|
1985 |
Snyder B, Hammes GG. Structural organization of chloroplast coupling factor. Biochemistry. 24: 2324-31. PMID 2859887 DOI: 10.1021/Bi00330A030 |
0.337 |
|
1984 |
Anderson VE, Hammes GG. Stereochemistry of the reactions catalyzed by chicken liver fatty acid synthase. Biochemistry. 23: 2088-94. PMID 6722137 DOI: 10.1021/Bi00304A033 |
0.561 |
|
1984 |
Waskiewicz DE, Hammes GG. Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation. Biochemistry. 23: 3136-43. PMID 6380583 DOI: 10.1021/Bi00309A005 |
0.344 |
|
1984 |
Snyder B, Hammes GG. Structural mapping of chloroplast coupling factor. Biochemistry. 23: 5787-95. PMID 6240988 DOI: 10.1021/Bi00319A018 |
0.334 |
|
1983 |
Cognet JA, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: acetylation-deacetylation. Biochemistry. 22: 3002-7. PMID 6871181 DOI: 10.1021/Bi00281A033 |
0.4 |
|
1983 |
Anderson VE, Hammes GG. Fluorescent properties of pyrene bound at specific acylation sites of chicken liver fatty acid synthase. Biochemistry. 22: 2995-3001. PMID 6871180 DOI: 10.1021/Bi00281A032 |
0.624 |
|
1983 |
Cox BG, Hammes GG. Steady-state kinetic study of fatty acid synthase from chicken liver. Proceedings of the National Academy of Sciences of the United States of America. 80: 4233-7. PMID 6576333 DOI: 10.1073/Pnas.80.14.4233 |
0.365 |
|
1983 |
Cognet JA, Cox BG, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: reduced nicotinamide adenine dinucleotide phosphate binding and formation and reduction of acetoacetyl-enzyme. Biochemistry. 22: 6281-7. PMID 6362722 DOI: 10.1021/Bi00295A037 |
0.431 |
|
1983 |
Cerione RA, McCarty RE, Hammes GG. Spatial relationships between specific sites on reconstituted chloroplast proton adenosinetriphosphatase and the phospholipid vesicle surface. Biochemistry. 22: 769-76. PMID 6220736 DOI: 10.1021/Bi00273A010 |
0.475 |
|
1983 |
Hammes GG. Mechanism of ATP synthesis and coupled proton transport: studies with purified chloroplast coupling factor Trends in Biochemical Sciences. 8: 131-134. DOI: 10.1016/0968-0004(83)90236-0 |
0.327 |
|
1982 |
Cardon JW, Hammes GG. Investigation of reduced nicotinamide adenine dinucleotide phosphate and acyl-binding sites on avian fatty acid synthase. Biochemistry. 21: 2863-70. PMID 7104298 DOI: 10.1021/Bi00541A009 |
0.419 |
|
1982 |
Waskiewicz DE, Hammes GG. Fluorescence polarization study of the alpha-ketoglutarate dehydrogenase complex from Escherichia coli. Biochemistry. 21: 6489-96. PMID 6758846 DOI: 10.1021/Bi00268A026 |
0.35 |
|
1982 |
Cerione RA, Hammes GG. Structural mapping of nucleotide binding sites on chloroplast coupling factor. Biochemistry. 21: 745-52. PMID 6462173 DOI: 10.1021/Bi00533A026 |
0.546 |
|
1982 |
Hammes GG. Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis. Proceedings of the National Academy of Sciences of the United States of America. 79: 6881-4. PMID 6129623 DOI: 10.1073/Pnas.79.22.6881 |
0.367 |
|
1981 |
Akiyama SK, Hammes GG. Elementary steps in the reaction mechanism of pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of flavin reduction. Biochemistry. 20: 1491-7. PMID 7013795 DOI: 10.1021/Bi00509A013 |
0.327 |
|
1981 |
Bruist MF, Hammes GG. Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry. 20: 6298-305. PMID 6458326 DOI: 10.1021/Bi00525A003 |
0.367 |
|
1981 |
Cerione RA, Hammes GG. Nucleotide interactions with the dicyclohexylcarbodiimide-sensitive adenosinetriphosphatase from spinach chloroplasts. Biochemistry. 20: 3359-65. PMID 6455155 DOI: 10.1021/Bi00515A008 |
0.594 |
|
1980 |
Akiyama SK, Hammes GG. Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation. Biochemistry. 19: 4208-13. PMID 6998493 DOI: 10.1021/Bi00559A011 |
0.398 |
|
1980 |
Craig DW, Hammes GG. Structural mapping of rabbit muscle phosphofructokinase. Distance between the adenosine cyclic 3',5'-phosphate binding site and a reactive sulfhydryl group. Biochemistry. 19: 330-4. PMID 6243478 DOI: 10.1021/Bi00543A013 |
0.364 |
|
1979 |
Baird BA, Hammes GG. Structure of oxidative- and photo-phosphorylation coupling factor complexes. Biochimica Et Biophysica Acta. 549: 31-53. PMID 157776 DOI: 10.1016/0304-4173(79)90017-X |
0.506 |
|
1979 |
Carlier MF, Holowka DA, Hammes GG. Interaction of photoreactive and fluorescent nucleotides with chloroplast coupling factor 1. Biochemistry. 18: 3452-7. PMID 157773 |
0.491 |
|
1979 |
Baird BA, Pick U, Hammes GG. Structural investigation of reconstituted chloroplast ATPase with fluorescence measurements. The Journal of Biological Chemistry. 254: 3818-25. PMID 155694 |
0.469 |
|
1978 |
Hahn LH, Hammes GG. Structural mapping of aspartate transcarbamoylase by fluorescence energy-transfer measurements: determination of the distance between catalytic sites of different subunits. Biochemistry. 17: 2423-9. PMID 678521 DOI: 10.1021/Bi00605A027 |
0.306 |
|
1978 |
Angelides KJ, Hammes GG. Mechanism of action of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 75: 4877-80. PMID 368802 DOI: 10.1073/Pnas.75.10.4877 |
0.349 |
|
1977 |
Baird BA, Hammes GG. Chemical cross-linking studies of beef heart mitochondrial coupling factor 1. The Journal of Biological Chemistry. 252: 4743-8. PMID 873913 |
0.439 |
|
1977 |
Shepherd GB, Hammes GG. Fluorescence energy transfer measurements in the pyruvate dehydrogenase multienzyme complex from Escherichia coli with chemically modified lipoic acid. Biochemistry. 16: 5234-41. PMID 336083 DOI: 10.1021/Bi00643A012 |
0.31 |
|
1977 |
Papadakis N, Hammes GG. Fluorescent derivatives of the pyruvate dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex. Biochemistry. 16: 1890-6. PMID 192277 DOI: 10.1021/Bi00628A020 |
0.418 |
|
1977 |
Holowka DA, Hammes GG. Chemical modification and fluorescence studies of chloroplast coupling factor. Biochemistry. 16: 5538-45. PMID 144521 DOI: 10.1021/Bi00644A023 |
0.538 |
|
1976 |
Cantley LC, Hammes GG. Investigation of quercetin binding sites on chloroplast coupling factor 1. Biochemistry. 15: 1-8. PMID 1247500 DOI: 10.1021/Bi00646A001 |
0.501 |
|
1976 |
Shepherd GB, Hammes GG. Fluorescence energy transfer measurements between ligand binding sites of the pyruvate dehydrogenase multienzyme complex. Biochemistry. 15: 311-7. PMID 764864 DOI: 10.1021/Bi00647A011 |
0.415 |
|
1976 |
Baird BA, Hammes GG. Chemical cross-linking studies of chloroplast coupling factor 1. The Journal of Biological Chemistry. 251: 6953-62. PMID 136444 |
0.465 |
|
1976 |
Parr GR, Hammes GG. A kinetic study of the subunit dissociation and reassembly of rabbit muscle phosphofructokinase. Biochemistry. 15: 857-62. PMID 129154 DOI: 10.1021/Bi00649A020 |
0.377 |
|
1976 |
Cantley LC, Hammes GG. Characterization of sulfhydryl groups on chloroplast coupling factor 1 exposed by heat activation. Biochemistry. 15: 9-14. PMID 129152 DOI: 10.1021/Bi00646A002 |
0.5 |
|
1976 |
Hammes GG, Rodbell M. Simple model for hormone-activated adenylate cyclase systems. Proceedings of the National Academy of Sciences of the United States of America. 73: 1189-92. PMID 4796 DOI: 10.1073/Pnas.73.4.1189 |
0.332 |
|
1975 |
Cantley LC, Hammes GG. Fluorescence energy transfer between ligand binding sites on chloroplast coupling factor 1. Biochemistry. 14: 2976-81. PMID 1148188 DOI: 10.1021/Bi00684A028 |
0.492 |
|
1975 |
Cantley LC, Hammes GG. Characterization of nucleotide binding sites on chloroplast coupling factor 1. Biochemistry. 14: 2968-75. PMID 1148187 DOI: 10.1021/Bi00684A027 |
0.521 |
|
1975 |
Matsumoto S, Hammes GG. Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase Biochemistry. 14: 214-224. PMID 1091284 DOI: 10.1021/Bi00673A004 |
0.356 |
|
1975 |
Fan S, Harrison LW, Hammes GG. Nuclear magnetic resonance study of ligand binding to Mn-aspartate transcarbamylase. Biochemistry. 14: 2219-24. PMID 807235 DOI: 10.1021/Bi00681A027 |
0.393 |
|
1975 |
Koren R, Hammes GG. Interaction of reduced nicotinamide adenine dinucleotide with beef heart s-malate dehydrogenase Biochemistry. 14: 1021-1025. PMID 164884 DOI: 10.1021/Bi00676A021 |
0.411 |
|
1975 |
Parr GR, Hammes GG. Subunit dissociation and unfolding of rabbit muscle phosphofructokinase by guanidine hydrochloride Biochemistry. 14: 1600-1605. PMID 123759 DOI: 10.1021/Bi00679A009 |
0.346 |
|
1975 |
Hill DE, Hammes GG. An equilibrium binding study of the interaction of fructose 6-phosphate and fructose 1,6-bisphosphate with rabbit muscle phosphofructokinase Biochemistry. 14: 203-213. PMID 123467 DOI: 10.1021/Bi00673A003 |
0.383 |
|
1974 |
Moe OA, Hammes GG. A study of the binding of thiamine diphosphate and thiochrome diphosphate to the pyruvate dehydrogenase multienzyme complex Biochemistry. 13: 2547-2552. PMID 4598732 DOI: 10.1021/Bi00709A011 |
0.334 |
|
1974 |
Hammes GG, Wu CW. Kinetics of allosteric enzymes Annual Review of Biophysics and Bioengineering. 3: 1-33. PMID 4371650 |
0.542 |
|
1974 |
Grover AK, Hammes GG. Affinity chromatography of β-hydroxybutyrate dehydrogenase on NAD and hydrophobic chain derivatives of sepharose Bba - Biomembranes. 356: 309-318. PMID 4367726 DOI: 10.1016/0005-2736(74)90271-5 |
0.332 |
|
1974 |
Moe OA, Lerner DA, Hammes GG. Fluorescence energy transfer between the thiamine diphosphate and flavine adenine dinucleotide binding sites on the pyruvate dehydrogenase multienzyme complex Biochemistry. 13: 2552-2557. PMID 4364834 DOI: 10.1021/Bi00709A012 |
0.342 |
|
1974 |
Hammes GG. Elementary steps in enzyme catalysis and regulation Pure and Applied Chemistry. 40: 525-548. DOI: 10.1351/Pac197440040525 |
0.417 |
|
1973 |
Wu CW, Hammes GG. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5′-triphosphate analog Biochemistry. 12: 1400-1408. PMID 4572360 DOI: 10.1021/Bi00731A021 |
0.628 |
|
1973 |
Harrison LW, Hammes GG. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5′-triphosphate Biochemistry. 12: 1395-1400. PMID 4572359 DOI: 10.1021/Bi00731A020 |
0.426 |
|
1973 |
Matsumoto S, Hammes GG. An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate. Biochemistry. 12: 1388-94. PMID 4572358 DOI: 10.1021/Bi00731A019 |
0.312 |
|
1973 |
Cantley LC, Hammes GG. Activation of beef heart mitochondrial adenosine triphosphatase by 2,4-dinitrophenol. Biochemistry. 12: 4900-4. PMID 4271561 DOI: 10.1021/Bi00748A014 |
0.395 |
|
1973 |
Tondre C, Hammes GG. A kinetic study of the binding of an ADP fluorescent analog to mitochondrial ATPase. Biochimica Et Biophysica Acta. 314: 245-9. PMID 4270537 DOI: 10.1016/0005-2728(73)90139-4 |
0.376 |
|
1972 |
Hammes GG, Hilborn DA. Steady state kinetics of soluble and membrane-bound mitochondrial ATPase. Biochimica Et Biophysica Acta. 233: 580-90. PMID 4255902 DOI: 10.1016/0005-2736(71)90156-8 |
0.372 |
|
1971 |
Hammes GG, Tallman DE. A nuclear magnetic resonance study of the interaction of l-epinephrine with phospholipid vesicles Bba - Biomembranes. 233: 17-25. PMID 5103878 DOI: 10.1016/0005-2736(71)90353-1 |
0.54 |
|
1971 |
Hammes GG, Wu CW. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate Biochemistry. 10: 2150-2156. PMID 4935107 DOI: 10.1021/Bi00787A030 |
0.601 |
|
1971 |
Hammes GG, Wu CW. Regulation of enzyme activity Science. 172: 1205-1211. PMID 4930512 DOI: 10.1126/Science.172.3989.1205 |
0.562 |
|
1971 |
Hammes GG, Wu CW. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs Biochemistry. 10: 1051-1057. PMID 4927804 DOI: 10.1021/Bi00782A018 |
0.604 |
|
1971 |
Hammes GG, Porter RW, Stark GR. Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate. Biochemistry. 10: 1046-50. PMID 4927803 DOI: 10.1021/Bi00782A017 |
0.305 |
|
1970 |
Hammes GG, Porter RW, Wu CW. Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase. Biochemistry. 9: 2992-4. PMID 5474800 DOI: 10.1021/Bi00817A009 |
0.532 |
|
1970 |
Hammes GG, Tallman DE. Application of the temperature-jump technique to the study of phospholipid dispersions Journal of the American Chemical Society. 92: 6042-6046. PMID 5460540 DOI: 10.1021/Ja00723A038 |
0.562 |
|
1970 |
Hammes GG, Simplicio J. Relaxation spectra of pyruvate kinase. Biochimica Et Biophysica Acta. 212: 428-33. PMID 5456993 DOI: 10.1016/0005-2744(70)90248-2 |
0.389 |
|
1970 |
Eckfeldt J, Hammes GG, Mohr SC, Wu CW. Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit Biochemistry. 9: 3353-3362. PMID 4941833 DOI: 10.1021/Bi00819A010 |
0.621 |
|
1970 |
Faeder EJ, Hammes GG. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit. Biochemistry. 9: 4043-9. PMID 4917898 DOI: 10.1021/Bi00823A003 |
0.308 |
|
1970 |
Hammes GG, Schimmel PR. 2 Rapid Reactions and Transient States The Enzymes. 2: 67-114. DOI: 10.1016/S1874-6047(08)60181-X |
0.33 |
|
1969 |
Hammes GG, Hurst JK. Relaxation spectra of adenosine triphosphate-creatine phosphotransferase. Biochemistry. 8: 1083-94. PMID 5813732 DOI: 10.1021/Bi00831A040 |
0.567 |
|
1968 |
Hammes GG, Pace CN. Ultrasonic absorption measurements in aqueous solutions of glycine, diglycine, and triglycine. The Journal of Physical Chemistry. 72: 2227-30. PMID 5650147 DOI: 10.1021/j100852a060 |
0.422 |
|
1968 |
Anderson DG, Hammes GG, Walz FG. Binding of phosphate ligands to ribonuclease A Biochemistry. 7: 1637-1645. PMID 4297049 DOI: 10.1021/Bi00845A004 |
0.32 |
|
1967 |
Hammes GG, Schimmel PR. Relaxation spectra of enzymatic reactions. The Journal of Physical Chemistry. 71: 917-23. PMID 6045206 DOI: 10.1021/J100863A023 |
0.599 |
|
1966 |
Erman JE, Hammes GG. Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3′:5′-cytidine Journal of the American Chemical Society. 88: 5614-5617. PMID 5980178 DOI: 10.1021/Ja00975A047 |
0.377 |
|
1966 |
Erman JE, Hammes GG. Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2′:3′-cyclic phosphate Journal of the American Chemical Society. 88: 5607-5614. PMID 5980177 DOI: 10.1021/Ja00975A046 |
0.401 |
|
1965 |
Fasella P, Hammes GG, Schimmel PR. A Sephadex dialysis method of determining small molecule-macromolecule binding constants. Biochimica Et Biophysica Acta. 103: 708-10. PMID 5859855 DOI: 10.1016/0005-2787(65)90094-8 |
0.588 |
|
1965 |
Hammes GG, Schimmel PR. Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease. Journal of the American Chemical Society. 87: 4665-9. PMID 5844451 DOI: 10.1021/Ja00949A001 |
0.602 |
|
1965 |
Cathou RE, Hammes GG, Schimmel PR. Optical rotatory dispersion of ribonuclease and ribonuclease--nucleotide complexes. Biochemistry. 4: 2687-90. PMID 4286548 DOI: 10.1021/Bi00888A018 |
0.557 |
|
1964 |
Hammes GG. Mechanism of Enzyme Catalysis Nature. 204: 342-343. PMID 14228866 DOI: 10.1038/204342A0 |
0.354 |
|
1964 |
Cathou RE, Hammes GG. Relaxation Spectra of Ribonuclease. I. The Interaction of Ribonuclease with Cytidine 3′-Phosphate Journal of the American Chemical Society. 86: 3240-3245. DOI: 10.1021/Ja01070A008 |
0.398 |
|
1963 |
EIGEN M, HAMMES GG. ELEMENTARY STEPS IN ENZYME REACTIONS (AS STUDIED BY RELAXATION SPECTROMETRY). Advances in Enzymology and Related Areas of Molecular Biology. 25: 1-38. PMID 14149678 |
0.553 |
|
1962 |
Hammes GG, Kochavi D. Studies of the Enzyme Hexokinase. II. Kinetic Inhibition by Products Journal of the American Chemical Society. 84: 2073-2076. DOI: 10.1021/Ja00870A013 |
0.314 |
|
1962 |
Hammes GG, Kochavi D. Studies of the Enzyme Hexokinase. I. Steady State Kinetics at pH 8 Journal of the American Chemical Society. 84: 2069-2073. DOI: 10.1021/Ja00870A012 |
0.325 |
|
1961 |
Eigen M, Hammes GG. Kinetic Studies of ADP Reactions with the Temperature Jump Method—Corrections Journal of the American Chemical Society. 83: 2786-2786. DOI: 10.1021/Ja01473A056 |
0.543 |
|
1960 |
DIEBLER H, EIGEN M, HAMMES GG. [Relaxation spectrometric studies of fast reactions of ATP in aqueous solution]. Zeitschrift FüR Naturforschung. Teil B: Chemie, Biochemie, Biophysik, Biologie. 15: 554-60. PMID 13722730 DOI: 10.1515/Znb-1960-0903 |
0.55 |
|
1960 |
Diebler H, Eigen M, Hammes GG. Relaxations-spektrometrische Untersuchungen schneller Reaktionen von ATP in wässeriger Lösung Zeitschrift Fur Naturforschung - Section B Journal of Chemical Sciences. 15: 554-560. DOI: 10.1515/znb-1960-0903 |
0.506 |
|
1960 |
Eigen M, Hammes GG. KINETIC STUDIES OF ADP REACTIONS WITH THE TEMPERATURE JUMP METHOD Journal of the American Chemical Society. 82: 5951-5952. DOI: 10.1021/Ja01507A041 |
0.542 |
|
1960 |
Figen M, Hammes GG, Kustin K. FAST REACTIONS OF IMIDAZOLE STUDIED WITH RELAXATION SPECTROMETRY Journal of the American Chemical Society. 82: 3482-3483. DOI: 10.1021/Ja01498A063 |
0.518 |
|
1960 |
Hammes GG, Alberty RA. The Relaxation Spectra of Simple Enzymatic Mechanisms1,2 Journal of the American Chemical Society. 82: 1564-1569. DOI: 10.1021/Ja01492A012 |
0.521 |
|
1959 |
Hammes GG, Alberty RA. The influence of the net protein charge on the rate of formation of enzyme-substrate complexes Journal of Physical Chemistry. 63: 274-279. DOI: 10.1021/J150572A034 |
0.55 |
|
1958 |
Alberty RA, Hammes GG. Application of the theory of diffusion-controlled reactions to enzyme kinetics Journal of Physical Chemistry. 62: 154-159. DOI: 10.1021/J150560A005 |
0.54 |
|
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