| Year |
Citation |
Score |
| 2017 |
Pierce E, Mansoorabadi SO, Can M, Reed GH, Ragsdale SW. Properties of intermediates in the catalytic cycle of oxalate oxidoreductase and its suicide inactivation by pyruvate. Biochemistry. PMID 28514140 DOI: 10.1021/Acs.Biochem.7B00222 |
0.756 |
|
| 2012 |
Reed GH, Ragsdale SW, Mansoorabadi SO. Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases. Biochimica Et Biophysica Acta. 1824: 1291-8. PMID 22178227 DOI: 10.1016/J.Bbapap.2011.11.010 |
0.765 |
|
| 2011 |
Frey PA, Reed GH. Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases. Biochimica Et Biophysica Acta. 1814: 1548-57. PMID 21435400 DOI: 10.1016/J.Bbapap.2011.03.005 |
0.517 |
|
| 2009 |
Tang KH, Mansoorabadi SO, Reed GH, Frey PA. Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase. Biochemistry. 48: 8151-60. PMID 19634897 DOI: 10.1021/Bi900828F |
0.755 |
|
| 2009 |
Martinez-Gomez NC, Poyner RR, Mansoorabadi SO, Reed GH, Downs DM. Reaction of AdoMet with ThiC generates a backbone free radical. Biochemistry. 48: 217-9. PMID 19113839 DOI: 10.1021/Bi802154J |
0.76 |
|
| 2008 |
Bender G, Poyner RR, Reed GH. Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase. Biochemistry. 47: 11360-6. PMID 18826329 DOI: 10.1021/Bi801316V |
0.708 |
|
| 2007 |
Schwartz PA, Lobrutto R, Reed GH, Frey PA. Probing interactions from solvent-exchangeable protons and monovalent cations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase. Protein Science : a Publication of the Protein Society. 16: 1157-64. PMID 17525464 DOI: 10.1110/Ps.072768007 |
0.505 |
|
| 2007 |
Carmieli R, Larsen TM, Reed GH, Zein S, Neese F, Goldfarb D. The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations. Journal of the American Chemical Society. 129: 4240-52. PMID 17367133 DOI: 10.1021/Ja066124E |
0.356 |
|
| 2006 |
Mansoorabadi SO, Magnusson OT, Poyner RR, Frey PA, Reed GH. Analysis of the Cob(II)alamin-5'-deoxy-3',4'-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase. Biochemistry. 45: 14362-70. PMID 17128975 DOI: 10.1021/Bi061586Q |
0.751 |
|
| 2006 |
Behshad E, Ruzicka FJ, Mansoorabadi SO, Chen D, Reed GH, Frey PA. Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases. Biochemistry. 45: 12639-46. PMID 17042480 DOI: 10.1021/bi061328t |
0.738 |
|
| 2006 |
Yoon M, Patwardhan A, Qiao C, Mansoorabadi SO, Menefee AL, Reed GH, Marsh EN. Reaction of adenosylcobalamin-dependent glutamate mutase with 2-thiolglutarate. Biochemistry. 45: 11650-7. PMID 16981724 DOI: 10.1021/Bi061067N |
0.785 |
|
| 2006 |
Frey PA, Hegeman AD, Reed GH. Free radical mechanisms in enzymology. Chemical Reviews. 106: 3302-16. PMID 16895329 DOI: 10.1021/Cr050292S |
0.41 |
|
| 2006 |
Mansoorabadi SO, Seravalli J, Furdui C, Krymov V, Gerfen GJ, Begley TP, Melnick J, Ragsdale SW, Reed GH. EPR spectroscopic and computational characterization of the hydroxyethylidene-thiamine pyrophosphate radical intermediate of pyruvate:ferredoxin oxidoreductase. Biochemistry. 45: 7122-31. PMID 16752902 DOI: 10.1021/Bi0602516 |
0.76 |
|
| 2006 |
Poyner RR, Anderson MA, Bandarian V, Cleland WW, Reed GH. Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Journal of the American Chemical Society. 128: 7120-1. PMID 16734439 DOI: 10.1021/Ja060710Q |
0.678 |
|
| 2006 |
Astashkin AV, Seravalli J, Mansoorabadi SO, Reed GH, Ragsdale SW. Pulsed electron paramagnetic resonance experiments identify the paramagnetic intermediates in the pyruvate ferredoxin oxidoreductase catalytic cycle. Journal of the American Chemical Society. 128: 3888-9. PMID 16551078 DOI: 10.1021/Ja0585275 |
0.728 |
|
| 2006 |
Sims PA, Menefee AL, Larsen TM, Mansoorabadi SO, Reed GH. Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit. Journal of Molecular Biology. 355: 422-31. PMID 16309698 DOI: 10.1016/J.Jmb.2005.10.050 |
0.731 |
|
| 2005 |
Mansoorabadi SO, Padmakumar R, Fazliddinova N, Vlasie M, Banerjee R, Reed GH. Characterization of a succinyl-CoA radical-cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase. Biochemistry. 44: 3153-8. PMID 15736925 DOI: 10.1021/Bi0482102 |
0.78 |
|
| 2004 |
Reed GH. Radical mechanisms in adenosylcobalamin-dependent enzymes. Current Opinion in Chemical Biology. 8: 477-83. PMID 15450489 DOI: 10.1016/J.Cbpa.2004.08.008 |
0.477 |
|
| 2004 |
Mansoorabadi SO, Reed GH. Effects of Electron Spin Delocalization and Non-Collinearity of Interaction Terms in EPR Triplet Powder Patterns Cheminform. 35. DOI: 10.1002/chin.200414295 |
0.692 |
|
| 2003 |
Reed GH, Mansoorabadi SO. The positions of radical intermediates in the active sites of adenosylcobalamin-dependent enzymes. Current Opinion in Structural Biology. 13: 716-21. PMID 14675550 DOI: 10.1016/J.Sbi.2003.10.011 |
0.768 |
|
| 2003 |
Sims PA, Larsen TM, Poyner RR, Cleland WW, Reed GH. Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry. 42: 8298-306. PMID 12846578 DOI: 10.1021/Bi0346345 |
0.406 |
|
| 2003 |
Schwart P, LoBrutto R, Reed GH, Frey PA. Suicide Inactivation of Dioldehydrase by 2-Chloroacetaldehyde: Formation of the 'cis-Ethanesemidione' Radical, and the Role of a Monovalent Cation Helvetica Chimica Acta. 86: 3764-3775. DOI: 10.1002/Hlca.200390318 |
0.488 |
|
| 2002 |
Frey PA, Chang CH, Ballinger MD, Reed GH. Kinetic characterization of transient free radical intermediates in reaction of lysine 2,3-aminomutase by EPR lineshape analysis. Methods in Enzymology. 354: 426-35. PMID 12418244 DOI: 10.1016/S0076-6879(02)54033-7 |
0.481 |
|
| 2002 |
Bandarian V, Reed GH. Analysis of the electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol. Biochemistry. 41: 8580-8. PMID 12093274 DOI: 10.1021/Bi0201217 |
0.727 |
|
| 2002 |
Poyner RR, Larsen TM, Wong SW, Reed GH. Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Archives of Biochemistry and Biophysics. 401: 155-63. PMID 12054465 DOI: 10.1016/S0003-9861(02)00024-3 |
0.373 |
|
| 2001 |
Poyner RR, Cleland WW, Reed GH. Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme. Biochemistry. 40: 8009-17. PMID 11434770 DOI: 10.1021/Bi0103922 |
0.327 |
|
| 2001 |
Magnusson OT, Reed GH, Frey PA. Characterization of an allylic analogue of the 5'-deoxyadenosyl radical: an intermediate in the reaction of lysine 2,3-aminomutase. Biochemistry. 40: 7773-82. PMID 11425303 DOI: 10.1021/Bi0104569 |
0.53 |
|
| 2001 |
Miller J, Bandarian V, Reed GH, Frey PA. Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate. Archives of Biochemistry and Biophysics. 387: 281-8. PMID 11370852 DOI: 10.1006/Abbi.2001.2261 |
0.7 |
|
| 2001 |
LoBrutto R, Bandarian V, Magnusson OT, Chen X, Schramm VL, Reed GH. 5'-Deoxyadenosine contacts the substrate radical intermediate in the active site of ethanolamine ammonia-lyase: 2H and 13C electron nuclear double resonance studies. Biochemistry. 40: 9-14. PMID 11141051 DOI: 10.1021/Bi001865S |
0.695 |
|
| 2000 |
Frey PA, Reed GH. Radical mechanisms in adenosylmethionine- and adenosylcobalamin-dependent enzymatic reactions. Archives of Biochemistry and Biophysics. 382: 6-14. PMID 11051091 DOI: 10.1006/Abbi.2000.2010 |
0.467 |
|
| 2000 |
Bandarian V, Reed GH. Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: Determination of the number of exchangeable hydrogens in the enzyme - Cofactor complex Biochemistry. 39: 12069-12075. PMID 11009622 DOI: 10.1021/Bi001014K |
0.671 |
|
| 2000 |
Wu W, Booker S, Lieder KW, Bandarian V, Reed GH, Frey PA. Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism. Biochemistry. 39: 9561-70. PMID 10924153 DOI: 10.1021/Bi000658P |
0.724 |
|
| 2000 |
Abend A, Bandarian V, Reed GH, Frey PA. Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase. Biochemistry. 39: 6250-7. PMID 10821701 DOI: 10.1021/Bi992963K |
0.744 |
|
| 2000 |
Chang CWT, Johnson DA, Bandarian V, Zhou H, LoBrutto R, Reed GH, Liu HW. Characterization of a unique coenzyme B6 radical in the ascarylose biosynthetic pathway [14] Journal of the American Chemical Society. 122: 4239-4240. DOI: 10.1021/Ja0000807 |
0.64 |
|
| 1999 |
Abend A, Bandarian V, Nitsche R, Stupperich E, Rétey J, Reed GH. Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B(12). Archives of Biochemistry and Biophysics. 370: 138-41. PMID 10496987 DOI: 10.1006/Abbi.1999.1382 |
0.642 |
|
| 1999 |
Bandarian V, Poyner RR, Reed GH. Hydrogen atom exchange between 5'-deoxyadenosine and hydroxyethylhydrazine during the single turnover inactivation of ethanolamine ammonia-lyase Biochemistry. 38: 12403-12407. PMID 10493808 DOI: 10.1021/Bi9906219 |
0.682 |
|
| 1999 |
Bandarian V, Reed GH. Hydrazine cation radical in the active site of ethanolamine ammonia- lyase: Mechanism-based inactivation by hydroxyethylhydrazine Biochemistry. 38: 12394-12402. PMID 10493807 DOI: 10.1021/Bi990620G |
0.698 |
|
| 1999 |
Magnusson OT, Reed GH, Frey PA. Spectroscopic evidence for the participation of an allylic analogue of the 5'-deoxyadenosyl radical in the reaction of lysine 2,3-aminomutase [22] Journal of the American Chemical Society. 121: 9764-9765. DOI: 10.1021/Ja9925507 |
0.398 |
|
| 1998 |
Frey PA, Ballinger MD, Reed GH. S-adenosylmethionine: a 'poor man's coenzyme B12' in the reaction of lysine 2,3-aminomutase. Biochemical Society Transactions. 26: 304-10. PMID 9765869 DOI: 10.1042/Bst0260304 |
0.305 |
|
| 1998 |
Larsen TM, Benning MM, Rayment I, Reed GH. Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel. Biochemistry. 37: 6247-55. PMID 9572839 DOI: 10.1021/Bi980243S |
0.345 |
|
| 1998 |
Lieder KW, Booker S, Ruzicka FJ, Beinert H, Reed GH, Frey PA. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Biochemistry. 37: 2578-85. PMID 9485408 DOI: 10.1021/Bi972417W |
0.416 |
|
| 1997 |
Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH. Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. Archives of Biochemistry and Biophysics. 345: 199-206. PMID 9308890 DOI: 10.1006/Abbi.1997.0257 |
0.331 |
|
| 1997 |
Bandarian V, Reed GH. Mechanistic studies on ethanolamine ammonia lyase Faseb Journal. 11. |
0.392 |
|
| 1996 |
Reed GH, Poyner RR, Larsen TM, Wedekind JE, Rayment I. Structural and mechanistic studies of enolase. Current Opinion in Structural Biology. 6: 736-43. PMID 8994873 DOI: 10.1016/S0959-440X(96)80002-9 |
0.393 |
|
| 1996 |
Babbitt PC, Hasson MS, Wedekind JE, Palmer DR, Barrett WC, Reed GH, Rayment I, Ringe D, Kenyon GL, Gerlt JA. The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry. 35: 16489-501. PMID 8987982 DOI: 10.1021/Bi9616413 |
0.411 |
|
| 1996 |
Johnson DA, Gassner GT, Bandarian V, Ruzicka FJ, Ballou DP, Reed GH, Liu HW. Kinetic characterization of an organic radical in the ascarylose biosynthetic pathway. Biochemistry. 35: 15846-56. PMID 8961949 DOI: 10.1021/Bi961370W |
0.716 |
|
| 1996 |
Chang CH, Ballinger MD, Reed GH, Frey PA. Lysine 2,3-aminomutase: rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate. Biochemistry. 35: 11081-4. PMID 8780510 DOI: 10.1021/Bi960850K |
0.491 |
|
| 1996 |
Xia B, Cheng H, Bandarian V, Reed GH, Markley JL. Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants. Biochemistry. 35: 9488-95. PMID 8755728 DOI: 10.1021/Bi960467F |
0.621 |
|
| 1996 |
Poyner RR, Laughlin LT, Sowa GA, Reed GH. Toward identification of acid/base catalysts in the active site of enolase: Comparison of the properties of K345A, E168Q, and E211Q variants Biochemistry. 35: 1692-1699. PMID 8634301 DOI: 10.1021/Bi952186Y |
0.366 |
|
| 1996 |
Larsen TM, Wedekind JE, Rayment I, Reed GH. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry. 35: 4349-58. PMID 8605183 DOI: 10.1021/Bi952859C |
0.399 |
|
| 1996 |
Reed GH. Getting in step with enolase Faseb Journal. 10. |
0.343 |
|
| 1995 |
Reed GH, Ballinger MD. Characterization of a radical intermediate in the lysine 2,3-aminomutase reaction Methods in Enzymology. 258: 362-379. PMID 8524161 DOI: 10.1016/0076-6879(95)58056-5 |
0.418 |
|
| 1995 |
Wedekind JE, Reed GH, Rayment I. Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII--enzyme complex from yeast at 1.9 A resolution. Biochemistry. 34: 4325-30. PMID 7703246 DOI: 10.1021/Bi00013A022 |
0.38 |
|
| 1995 |
Wu W, Lieder KW, Reed GH, Frey PA. Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: a radical centered on the beta-carbon of the alternative substrate, 4-thia-L-lysine. Biochemistry. 34: 10532-7. PMID 7654708 DOI: 10.1021/Bi00033A027 |
0.467 |
|
| 1995 |
Ballinger MD, Frey PA, Reed GH, LoBrutto R. Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement. Biochemistry. 34: 10086-93. PMID 7632680 DOI: 10.1021/Bi00031A033 |
0.473 |
|
| 1995 |
Frey P, Ballinger M, Reed G, LoBrutto R, Lieder K, Wu W. The role of iron-sulfur clusters, S-adenosylmethionine, and radicals in the reaction of lysine 2,3-aminomutase Journal of Inorganic Biochemistry. 59: 291. DOI: 10.1016/0162-0134(95)97392-4 |
0.337 |
|
| 1994 |
Larsen TM, Laughlin LT, Holden HM, Rayment I, Reed GH. Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Biochemistry. 33: 6301-9. PMID 8193145 DOI: 10.1021/Bi00186A033 |
0.364 |
|
| 1994 |
Cheng H, Xia B, Reed GH, Markley JL. Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin. Biochemistry. 33: 3155-64. PMID 8136349 DOI: 10.1021/Bi00177A003 |
0.327 |
|
| 1994 |
Wedekind JE, Poyner RR, Reed GH, Rayment I. Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution. Biochemistry. 33: 9333-42. PMID 8049235 DOI: 10.1021/Bi00197A038 |
0.367 |
|
| 1993 |
Buchbinder JL, Baraniak J, Frey PA, Reed GH. Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase. Biochemistry. 32: 14111-6. PMID 8260493 DOI: 10.1021/Bi00214A006 |
0.354 |
|
| 1992 |
Ballinger MD, Frey PA, Reed GH. Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase Biochemistry. 31: 10782-10789. PMID 1329955 DOI: 10.1021/Bi00159A020 |
0.506 |
|
| 1992 |
Petrovich RM, Ruzicka FJ, Reed GH, Frey PA. Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy Biochemistry. 31: 10774-10781. PMID 1329954 DOI: 10.1021/Bi00159A019 |
0.411 |
|
| 1992 |
Poyner RR, Reed GH. Structure of the bis divalent cation complex with phosphonoacetohydroxamate at the active site of enolase Biochemistry. 31: 7166-7173. PMID 1322695 DOI: 10.1021/Bi00146A020 |
0.383 |
|
| 1992 |
Latwesen DG, Poe M, Leigh JS, Reed GH. Electron paramagnetic resonance studies of a ras p21-MnIIGDP complex in solution. Biochemistry. 31: 4946-50. PMID 1318075 DOI: 10.1021/Bi00136A004 |
0.319 |
|
| 1992 |
Ballinger MD, Reed GH, Frey PA. An organic radical in the lysine 2,3-aminomutase reaction Biochemistry®. 31: 949-953. PMID 1310425 DOI: 10.1021/Bi00119A001 |
0.527 |
|
| 1991 |
Schmidt-Base K, Buchbinder JL, Reed GH, Rayment I. Crystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle Proteins: Structure, Function and Genetics. 11: 153-157. PMID 1658780 DOI: 10.1002/Prot.340110208 |
0.322 |
|
| 1990 |
Lord KA, Reed GH. Vanadyl(IV) complexes with pyruvate kinase: activation of the enzyme and electron paramagnetic resonance properties of ternary complexes with the protein. Archives of Biochemistry and Biophysics. 281: 124-31. PMID 2166476 DOI: 10.1016/0003-9861(90)90421-T |
0.427 |
|
| 1990 |
Smithers GW, Poe M, Latwesen DG, Reed GH. Electron paramagnetic resonance measurements of the hydration of Mn(II) in ternary complexes with GDP and ras p21 proteins Archives of Biochemistry and Biophysics. 280: 416-420. PMID 2164357 DOI: 10.1016/0003-9861(90)90351-X |
0.364 |
|
| 1990 |
Kofron JL, Reed GH. Synthesis of oxalyl phosphate and processing of the acyl phosphate by phosphoenolpyruvate-dependent enzymes Archives of Biochemistry and Biophysics. 280: 40-44. PMID 2162154 DOI: 10.1016/0003-9861(90)90515-Z |
0.399 |
|
| 1990 |
Buchbinder JL, Reed GH. Electron paramagnetic resonance studies of the coordination schemes and site selectivities for divalent metal ions in complexes with pyruvate kinase. Biochemistry. 29: 1799-806. PMID 2158815 DOI: 10.1021/Bi00459A019 |
0.345 |
|
| 1988 |
Kofron JL, Ash DE, Reed GH. Coordination of manganous ion at the active site of pyruvate,phosphate dikinase: The complex of oxalate with the phosphorylated enzyme Biochemistry. 27: 4781-4787. PMID 2844239 DOI: 10.1021/Bi00413A030 |
0.403 |
|
| 1987 |
Smithers GW, Jahansouz H, Kofron JL, Himes RH, Reed GH. Substrate activity of synthetic formyl phosphate in the reaction catalyzed by formyltetrahydrofolate synthetase. Biochemistry. 26: 3943-8. PMID 3651425 DOI: 10.1021/Bi00387A030 |
0.414 |
|
| 1987 |
Lodato DT, Reed GH. Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations Biochemistry. 26: 2243-2250. PMID 3040085 DOI: 10.1021/Bi00382A026 |
0.385 |
|
| 1986 |
LoBrutto R, Smithers GW, Reed GH, Orme-Johnson WH, Tan SL, Leigh JS. Observation of manganese(II)-ligand superhyperfine couplings in complexes with proteins by electron spin-echo spectroscopy. Biochemistry. 25: 5654-60. PMID 3022800 DOI: 10.1021/Bi00367A046 |
0.393 |
|
| 1985 |
Moore JM, Reed GH. Coordination scheme and stereochemical configuration of manganese(II) adenosine 5́-diphosphate at the active site of 3-phosphoglycerate kinase Biochemistry. 24: 5328-5333. PMID 3000431 DOI: 10.1021/Bi00341A009 |
0.364 |
|
| 1982 |
Cohn M, Reed GH. Magnetic resonance studies of active sites in enzymic complexes Annual Review of Biochemistry. 51: 365-394. PMID 6287918 DOI: 10.1146/Annurev.Bi.51.070182.002053 |
0.401 |
|
| 1977 |
Chapman BE, O'Sullivan WJ, Scopes RK, Reed GH. Magnetic resonance studies on manganese-nucleotide complexes of phosphoglycerate kinase Biochemistry. 16: 1005-1010. PMID 321006 DOI: 10.1021/Bi00624A031 |
0.393 |
|
| 1976 |
Hershberg RD, Reed GH, Slotboom AJ, DeHaas GH. Phospholipase A2 complexes with gadolinium(III) and interaction of the enzyme-metal ion complex with monomeric and micellar alkylphosphorylcholines. Water proton nuclear magnetic relaxation studies Biochemistry. 15: 2268-2274. PMID 945070 DOI: 10.1021/Bi00656A004 |
0.375 |
|
| 1976 |
Loscalzo J, Reed GH. Spectroscopic studies of actin-metal-nucleotide complexes Biochemistry. 15: 5407-5413. PMID 187216 DOI: 10.1021/Bi00669A030 |
0.336 |
|
| 1975 |
Loscalzo J, Reed GH, Weber A. Conformational change and cooperativity in actin filaments free of tropomyosin Proceedings of the National Academy of Sciences of the United States of America. 72: 3412-3415. PMID 1103145 DOI: 10.1073/Pnas.72.9.3412 |
0.34 |
|
| 1975 |
Michaels G, Milner Y, Reed GH. Magnetic resonance and kinetic studies of pyruvate, phosphate dikinase. Interaction of oxalate with the phosphorylated form of the enzyme. Biochemistry. 14: 3213-9. PMID 167819 DOI: 10.1021/Bi00685A028 |
0.454 |
|
| 1974 |
Reed GH, Morgan SD. Kinetic and magnetic resonance studies of the interaction of oxalate with pyruvate kinase Biochemistry. 13: 3537-3541. DOI: 10.1021/Bi00714A020 |
0.388 |
|
| 1973 |
Price NC, Reed GH, Cohn M. Magnetic resonance studies of substrate and inhibitor binding to porcine muscle adenylate kinase Biochemistry. 12: 3322-3327. PMID 4354608 DOI: 10.1021/Bi00741A026 |
0.387 |
|
| 1971 |
Reed GH, Ray WJ. Electron paramagnetic resonance studies of manganese (II) coordination in the phosphoglucomutase system Biochemistry. 10: 3190-3197. PMID 4330325 DOI: 10.1021/Bi00793A005 |
0.39 |
|
| 1971 |
Reed GH, Leigh JS, Pearson JE. Electron Paramagnetic Relaxation and EPR Line Shapes of Manganous Ion Complexes in Aqueous Solutions. Frequency and Ligand Dependence Journal of Chemical Physics. 55: 3311-3316. DOI: 10.1063/1.1676582 |
0.316 |
|
| 1971 |
Leigh JS, Reed GH. Electron paramagnetic resonance studies in frozen aqueous solutions. Elimination of freezing artifacts The Journal of Physical Chemistry. 75: 1202-1204. DOI: 10.1021/J100679A003 |
0.31 |
|
| 1971 |
Reed GH, Kula RJ. Nuclear magnetic resonance and infrared spectral studies of structural and kinetic properties of amino polycarboxylate chelates of divalent lead, zinc, cadmium, and mercury in acidic aqueous solutions Inorganic Chemistry. 10: 2050-2057. DOI: 10.1021/Ic50103A043 |
0.751 |
|
| 1965 |
Kula RJ, Rabenstein DL, Reed GH. Nuclear Magnetic Resonance Technique for Determining Hydration Numbers Analytical Chemistry. 37: 1783-1784. DOI: 10.1021/ac60232a045 |
0.451 |
|
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