| Year |
Citation |
Score |
| 2016 |
Munro PD, Ackers GK, Shearwin KE. Aspects of protein-DNA interactions: a review of quantitative thermodynamic theory for modelling synthetic circuits utilising LacI and CI repressors, IPTG and the reporter gene lacZ. Biophysical Reviews. 8: 331-345. PMID 28510022 DOI: 10.1007/S12551-016-0231-9 |
0.43 |
|
| 2012 |
Holt JM, Ackers GK. Kinetic trapping of a key hemoglobin intermediate. Methods in Molecular Biology (Clifton, N.J.). 796: 19-29. PMID 22052483 DOI: 10.1007/978-1-61779-334-9_2 |
0.424 |
|
| 2009 |
Holt JM, Ackers GK. The Hill coefficient: inadequate resolution of cooperativity in human hemoglobin. Methods in Enzymology. 455: 193-212. PMID 19289207 DOI: 10.1016/S0076-6879(08)04207-9 |
0.425 |
|
| 2006 |
Ackers GK, Holt JM. Asymmetric cooperativity in a symmetric tetramer: human hemoglobin. The Journal of Biological Chemistry. 281: 11441-3. PMID 16423822 DOI: 10.1074/Jbc.R500019200 |
0.426 |
|
| 2005 |
Holt JM, Ackers GK. Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 2. Stepwise cooperative free energy. Biochemistry. 44: 11939-49. PMID 16142892 DOI: 10.1021/Bi050710N |
0.479 |
|
| 2005 |
Holt JM, Klinger AL, Yarian CS, Keelara V, Ackers GK. Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobin. Biochemistry. 44: 11925-38. PMID 16142891 DOI: 10.1021/Bi050709O |
0.463 |
|
| 2004 |
Goldbeck RA, Esquerra RM, Kliger DS, Holt JM, Ackers GK. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 2. Cooperative free energies of (αFeCOβFe)2 and (αFeβFeCO)2 T-state tetramers Biochemistry. 43: 12065-12080. PMID 15379546 DOI: 10.1021/Bi0493923 |
0.382 |
|
| 2004 |
Goldbeck RA, Esquerra RM, Holt JM, Ackers GK, Kliger DS. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations Biochemistry. 43: 12048-12064. PMID 15379545 DOI: 10.1021/Bi049393V |
0.389 |
|
| 2004 |
Ackers GK, Holt JM, Burgie ES, Yarian CS. Analyzing intermediate state cooperativity in hemoglobin. Methods in Enzymology. 379: 3-28. PMID 15051349 DOI: 10.1016/S0076-6879(04)79001-1 |
0.776 |
|
| 2002 |
Ackers GK, Dalessio PM, Lew GH, Daugherty MA, Holt JM. Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function. Proceedings of the National Academy of Sciences of the United States of America. 99: 9777-82. PMID 12119405 DOI: 10.1073/Pnas.152225999 |
0.413 |
|
| 2000 |
Ackers GK, Holt JM, Huang Y, Grinkova Y, Klinger AL, Denisov I. Confirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1)half-oxygenated intermediate supports the symmetry rule model of allosteric regulation. Proteins. 23-43. PMID 11013398 DOI: 10.1002/1097-0134(2000)41:4+<23::Aid-Prot30>3.0.Co;2-D |
0.423 |
|
| 2000 |
Darling PJ, Holt JM, Ackers GK. Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding II: cooperative interactions of cro dimers. Journal of Molecular Biology. 302: 625-38. PMID 10986123 DOI: 10.1006/Jmbi.2000.4050 |
0.464 |
|
| 2000 |
Darling PJ, Holt JM, Ackers GK. Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations. Biochemistry. 39: 11500-7. PMID 10985796 DOI: 10.1021/Bi000935S |
0.492 |
|
| 1999 |
Hui HL, Kavanaugh JS, Doyle ML, Wierzba A, Rogers PH, Arnone A, Holt JM, Ackers GK, Noble RW. Structural and functional properties of human hemoglobins reassembled after synthesis in Escherichia coli. Biochemistry. 38: 1040-9. PMID 9894000 DOI: 10.1021/Bi981986G |
0.365 |
|
| 1998 |
Pray TR, Burz DS, Ackers GK. Cooperative non-specific DNA binding by octamerizing lambda cI repressors: a site-specific thermodynamic analysis. Journal of Molecular Biology. 282: 947-58. PMID 9753546 DOI: 10.1006/Jmbi.1998.2056 |
0.5 |
|
| 1998 |
Klinger AL, Ackers GK. Analysis of spectra from multiwavelength oxygen-binding studies of mixed metal hybrid hemoglobins. Methods in Enzymology. 295: 190-207. PMID 9750220 DOI: 10.1016/S0076-6879(98)95041-8 |
0.415 |
|
| 1998 |
Bain DL, Ackers GK. A quantitative cryogenic gel-shift technique for analysis of protein-DNA binding. Analytical Biochemistry. 258: 240-5. PMID 9570836 DOI: 10.1006/Abio.1998.2626 |
0.486 |
|
| 1998 |
Kiger L, Klinger AL, Kwiatkowski LD, De Young A, Doyle ML, Holt JM, Noble RW, Ackers GK. Thermodynamic studies on the equilibrium properties of a series of recombinant betaW37 hemoglobin mutants. Biochemistry. 37: 4336-45. PMID 9521754 DOI: 10.1021/Bi970868A |
0.473 |
|
| 1997 |
Abraham DJ, Kellogg GE, Holt JM, Ackers GK. Hydropathic analysis of the non-covalent interactions between molecular subunits of structurally characterized hemoglobins. Journal of Molecular Biology. 272: 613-32. PMID 9325116 DOI: 10.1006/Jmbi.1997.1249 |
0.358 |
|
| 1997 |
Ackers GK, Perrella M, Holt JM, Denisov I, Huang Y. Thermodynamic stability of the asymmetric doubly-ligated hemoglobin tetramer (alpha+CNbeta+CN)(alphabeta): methodological and mechanistic issues. Biochemistry. 36: 10822-9. PMID 9312272 DOI: 10.1021/Bi971382X |
0.314 |
|
| 1997 |
Doyle ML, Holt JM, Ackers GK. Effects of NaCl on the linkages between O2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. Biophysical Chemistry. 64: 271-87. PMID 9127950 DOI: 10.1016/S0301-4622(96)02235-1 |
0.452 |
|
| 1997 |
Huang Y, Koestner ML, Ackers GK. Tertiary and quaternary chloride effects of the partially ligated (CN-met) hemoglobin intermediates. Biophysical Chemistry. 64: 157-73. PMID 9127944 DOI: 10.1016/S0301-4622(96)02236-3 |
0.426 |
|
| 1997 |
Huang Y, Koestner ML, Ackers GK. Heterotropic effects of chloride on the ligation microstates of hemoglobin at constant water activity. Biophysical Journal. 71: 2106-16. PMID 8889185 DOI: 10.1016/S0006-3495(96)79409-2 |
0.347 |
|
| 1996 |
ACKERS GK, THOMPSON TE. DETERMINATION OF STOICHIOMETRY AND EQUILIBRIUM CONSTANTS FOR REVERSIBLY ASSOCIATING SYSTEMS BY MOLECULAR SIEVE CHROMATOGRAPHY. Proceedings of the National Academy of Sciences of the United States of America. 53: 342-9. PMID 14294067 DOI: 10.1073/pnas.53.2.342 |
0.471 |
|
| 1996 |
Huang Y, Doyle ML, Ackers GK. The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids. Biophysical Journal. 71: 2094-105. PMID 8889184 DOI: 10.1016/S0006-3495(96)79408-0 |
0.359 |
|
| 1996 |
Burz DS, Ackers GK. Cooperativity mutants of bacteriophage lambda cI repressor: temperature dependence of self-assembly. Biochemistry. 35: 3341-50. PMID 8605172 DOI: 10.1021/Bi952055X |
0.377 |
|
| 1996 |
Huang Y, Ackers GK. Transformation of cooperative free energies between ligation systems of hemoglobin: resolution of the carbon monoxide binding intermediates. Biochemistry. 35: 704-18. PMID 8547251 DOI: 10.1021/Bi952400I |
0.442 |
|
| 1995 |
Bain DL, Ackers GK. Self-association and DNA binding of lambda cI repressor N-terminal domains reveal linkage between sequence-specific binding and the C-terminal cooperativity domain. Biochemistry. 33: 14679-89. PMID 7993896 DOI: 10.1021/Bi00253A005 |
0.447 |
|
| 1995 |
Holt JM, Ackers GK. The pathway of allosteric control as revealed by hemoglobin intermediate states. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 210-8. PMID 7781923 DOI: 10.1096/Fasebj.9.2.7781923 |
0.378 |
|
| 1995 |
Huang Y, Ackers GK. Enthalpic and entropic components of cooperativity for the partially ligated intermediates of hemoglobin support a "symmetry rule" mechanism. Biochemistry. 34: 6316-27. PMID 7756259 DOI: 10.1021/Bi00019A009 |
0.4 |
|
| 1995 |
Merabet E, Ackers GK. Calorimetric analysis of lambda cI repressor binding to DNA operator sites. Biochemistry. 34: 8554-63. PMID 7612597 DOI: 10.1021/Bi00027A005 |
0.503 |
|
| 1995 |
Holt JM, Ackers GK. [1] Pathway of allosteric control as revealed by intermediate states of hemoglobin☆ Methods in Enzymology. 259: 1-19. DOI: 10.1016/0076-6879(95)59037-4 |
0.473 |
|
| 1994 |
LiCata VJ, Dalessio PM, Ackers GK. Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. Proteins. 17: 279-96. PMID 8272426 DOI: 10.1002/Prot.340170306 |
0.42 |
|
| 1994 |
Ackers GK, Hazzard JH. Transduction of binding energy into hemoglobin cooperativity. Trends in Biochemical Sciences. 18: 385-90. PMID 8256288 DOI: 10.1016/0968-0004(93)90095-5 |
0.349 |
|
| 1994 |
Daugherty MA, Shea MA, Ackers GK. Bohr effects of the partially-ligated (CN-met) intermediates of hemoglobin as probed by quaternary assembly. Biochemistry. 33: 10345-57. PMID 8068671 DOI: 10.1021/Bi00200A015 |
0.645 |
|
| 1994 |
Burz DS, Ackers GK. Single-site mutations in the C-terminal domain of bacteriophage lambda cI repressor alter cooperative interactions between dimers adjacently bound to OR. Biochemistry. 33: 8406-16. PMID 8031776 DOI: 10.1021/Bi00194A004 |
0.437 |
|
| 1994 |
Burz DS, Beckett D, Benson N, Ackers GK. Self-assembly of bacteriophage lambda cI repressor: effects of single-site mutations on the monomer-dimer equilibrium. Biochemistry. 33: 8399-405. PMID 8031775 DOI: 10.1021/Bi00194A003 |
0.641 |
|
| 1993 |
Beckett D, Burz DS, Ackers GK, Sauer RT. Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry. 32: 9073-9. PMID 8369279 DOI: 10.1021/Bi00086A012 |
0.707 |
|
| 1992 |
Englander SW, Englander JJ, McKinnie RE, Ackers GK, Turner GJ, Westrick JA, Gill SJ. Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin. Science (New York, N.Y.). 256: 1684-7. PMID 1609279 DOI: 10.1126/Science.256.5064.1684 |
0.334 |
|
| 1992 |
Koblan KS, Bain DL, Beckett D, Shea MA, Ackers GK. Analysis of site-specific interaction parameters in protein-DNA complexes Methods in Enzymology. 210: 405-425. PMID 1584044 DOI: 10.1016/0076-6879(92)10021-5 |
0.733 |
|
| 1992 |
Ackers GK, Doyle ML, Myers D, Daugherty MA. Molecular code for cooperativity in hemoglobin. Science (New York, N.Y.). 255: 54-63. PMID 1553532 DOI: 10.1126/Science.1553532 |
0.461 |
|
| 1992 |
Koblan KS, Ackers GK. Site-specific enthalpic regulation of DNA transcription at bacteriophage lambda OR. Biochemistry. 31: 57-65. PMID 1531023 DOI: 10.1021/Bi00116A010 |
0.523 |
|
| 1992 |
Doyle ML, Ackers GK. Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Biochemistry. 31: 11182-95. PMID 1445857 DOI: 10.1021/Bi00160A032 |
0.372 |
|
| 1992 |
Doyle ML, Lew G, Turner GJ, Rucknagel D, Ackers GK. Regulation of oxygen affinity by quaternary enhancement: does hemoglobin Ypsilanti represent an allosteric intermediate? Proteins. 14: 351-62. PMID 1438174 DOI: 10.1002/Prot.340140304 |
0.428 |
|
| 1992 |
Turner GJ, Galacteros F, Doyle ML, Hedlund B, Pettigrew DW, Turner BW, Smith FR, Moo-Penn W, Rucknagel DL, Ackers GK. Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers. Proteins. 14: 333-50. PMID 1438173 DOI: 10.1002/Prot.340140303 |
0.515 |
|
| 1992 |
Doyle ML, Lew G, De Young A, Kwiatkowski L, Wierzba A, Noble RW, Ackers GK. Functional properties of human hemoglobins synthesized from recombinant mutant beta-globins. Biochemistry. 31: 8629-39. PMID 1390647 DOI: 10.1021/Bi00151A033 |
0.395 |
|
| 1991 |
Ackers GK. The energetics of ligand-linked subunit assembly in hemoglobin require a third allosteric structure. Biophysical Chemistry. 37: 371-82. PMID 2285798 DOI: 10.1016/0301-4622(90)88036-R |
0.428 |
|
| 1991 |
LiCata VJ, Speros PC, Rovida E, Ackers GK. Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids. Biochemistry. 29: 9771-83. PMID 2271615 DOI: 10.1021/Bi00494A003 |
0.396 |
|
| 1991 |
Daugherty MA, Shea MA, Johnson JA, LiCata VJ, Turner GJ, Ackers GK. Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching. Proceedings of the National Academy of Sciences of the United States of America. 88: 1110-4. PMID 1996311 DOI: 10.1073/Pnas.88.4.1110 |
0.668 |
|
| 1991 |
Beckett D, Koblan KS, Ackers GK. Quantitative study of protein association at picomolar concentrations: The λ phage cl repressor Analytical Biochemistry. 196: 69-75. PMID 1888038 DOI: 10.1016/0003-2697(91)90118-D |
0.588 |
|
| 1991 |
Doyle ML, Speros PC, LiCata VJ, Gingrich D, Hoffman BM, Ackers GK. Linkage between cooperative oxygenation and subunit assembly of cobaltous human hemoglobin. Biochemistry. 30: 7263-71. PMID 1854736 DOI: 10.1021/Bi00243A031 |
0.432 |
|
| 1991 |
Speros PC, LiCata VJ, Yonetani T, Ackers GK. Experimental resolution of cooperative free energies for the ten ligation species of cobalt(II)/iron(II)-CO hemoglobin. Biochemistry. 30: 7254-62. PMID 1854735 DOI: 10.1021/Bi00243A030 |
0.346 |
|
| 1991 |
Koblan KS, Ackers GK. Cooperative protein-DNA interactions: effects of KCl on lambda cI binding to OR. Biochemistry. 30: 7822-7. PMID 1831046 DOI: 10.1021/Bi00245A023 |
0.497 |
|
| 1991 |
Koblan KS, Ackers GK. Energetics of subunit dimerization in bacteriophage lambda cI repressor: linkage to protons, temperature, and KCl. Biochemistry. 30: 7817-21. PMID 1831045 DOI: 10.1021/Bi00245A022 |
0.409 |
|
| 1990 |
Perrella M, Benazzi L, Shea MA, Ackers GK. Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states. Biophysical Chemistry. 35: 97-103. PMID 2328279 DOI: 10.1016/0301-4622(90)80064-E |
0.668 |
|
| 1990 |
Ackers GK, Johnson ML. Analysis of hemoglobin oxygenation from combined equilibrium and kinetic data Is quaternary enhancement necessary? Biophysical Chemistry. 37: 265-279. PMID 2285788 DOI: 10.1016/0301-4622(90)88026-O |
0.48 |
|
| 1990 |
Senear DF, Ackers GK. Proton-linked contributions to site-specific interactions of lambda cI repressor and OR. Biochemistry. 29: 6568-77. PMID 2168735 DOI: 10.1021/Bi00480A004 |
0.486 |
|
| 1989 |
Brenowitz M, Senear DF, Ackers GK. Flanking DNA-sequences contribute to the specific binding of cI-repressor and OR1. Nucleic Acids Research. 17: 3747-55. PMID 2525252 DOI: 10.1093/nar/17.10.3747 |
0.354 |
|
| 1987 |
Smith FR, Gingrich D, Hoffman BM, Ackers GK. Three-state combinatorial switching in hemoglobin tetramers: comparison between functional energetics and molecular structures. Proceedings of the National Academy of Sciences of the United States of America. 84: 7089-93. PMID 3478682 DOI: 10.1073/Pnas.84.20.7089 |
0.39 |
|
| 1987 |
Senear DF, Brenowitz M, Shea MA, Ackers GK. Energetics of cooperative protein-DNA interactions: comparison between quantitative deoxyribonuclease footprint titration and filter binding. Biochemistry. 25: 7344-54. PMID 3026451 DOI: 10.1021/Bi00371A016 |
0.711 |
|
| 1986 |
Ackers GK, Smith FR. Resolving pathways of functional coupling within protein assemblies by site-specific structural perturbation. Biophysical Journal. 49: 155-65. PMID 3955167 DOI: 10.1016/S0006-3495(86)83631-1 |
0.372 |
|
| 1986 |
Brenowitz M, Senear DF, Shea MA, Ackers GK. Quantitative DNase footprint titration: a method for studying protein-DNA interactions. Methods in Enzymology. 130: 132-81. PMID 3773731 DOI: 10.1016/0076-6879(86)30011-9 |
0.709 |
|
| 1986 |
Brenowitz M, Senear DF, Shea MA, Ackers GK. "Footprint" titrations yield valid thermodynamic isotherms. Proceedings of the National Academy of Sciences of the United States of America. 83: 8462-6. PMID 3464963 DOI: 10.1073/Pnas.83.22.8462 |
0.725 |
|
| 1985 |
Smith FR, Ackers GK. Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 82: 5347-51. PMID 3860865 DOI: 10.1073/Pnas.82.16.5347 |
0.433 |
|
| 1985 |
Shea MA, Ackers GK. The OR control system of bacteriophage lambda. A physical-chemical model for gene regulation. Journal of Molecular Biology. 181: 211-30. PMID 3157005 DOI: 10.1016/0022-2836(85)90086-5 |
0.654 |
|
| 1985 |
Frankel AD, Ackers GK, Smith HO. Measurement of DNA-protein equilibria using gel chromatography: Application to the HinfI restriction endonuclease Biochemistry. 24: 3049-3054. PMID 2990540 DOI: 10.1021/Bi00333A037 |
0.728 |
|
| 1984 |
Johnson ML, Turner BW, Ackers GK. A quantitative model for the cooperative mechanism of human hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 81: 1093-7. PMID 6583698 DOI: 10.1073/Pnas.81.4.1093 |
0.449 |
|
| 1983 |
Ackers GK, Shea MA, Smith FR. Free energy coupling within macromolecules. The chemical work of ligand binding at the individual sites in co-operative systems. Journal of Molecular Biology. 170: 223-42. PMID 6631962 DOI: 10.1016/S0022-2836(83)80234-4 |
0.706 |
|
| 1982 |
Ackers GK, Benesch RE, Edalji R. Effects of inositol hexasulfate on the oxygen affinity of hemoglobin: verification of the integral function theory of thermodynamic linkage. Biochemistry. 21: 875-9. PMID 7074057 DOI: 10.1021/Bi00534A010 |
0.411 |
|
| 1982 |
Johnson ML, Ackers GK. Thermodynamic analysis of human hemoglobins in terms of the Perutz mechanism: extensions of the Szabo--Karplus model to include subunit assembly. Biochemistry. 21: 201-11. PMID 7074009 DOI: 10.1021/Bi00531A001 |
0.423 |
|
| 1982 |
Ackers GK, Johnson AD, Shea MA. Quantitative model for gene regulation by lambda phage repressor. Proceedings of the National Academy of Sciences of the United States of America. 79: 1129-33. PMID 6461856 DOI: 10.1073/Pnas.79.4.1129 |
0.675 |
|
| 1981 |
Flanagan MA, Ackers GK, Matthew JB, Hanania GIH, Gurd FRN. Electrostatic contributions to the energetics of dimer-tetramer assembly in human hemoglobin: pH dependence and effect of specifically bound chloride ions Biochemistry. 20: 7439-7449. PMID 7326236 DOI: 10.1021/Bi00529A018 |
0.394 |
|
| 1981 |
Ackers GK, Johnson ML. Linked functions in allosteric proteins. Extension of the concerted (MWC) model for ligand-linked subunit assembly and its application to human hemoglobins. Journal of Molecular Biology. 147: 559-82. PMID 7277501 DOI: 10.1016/0022-2836(81)90400-9 |
0.391 |
|
| 1981 |
Johnson AD, Poteete AR, Lauer G, Sauer RT, Ackers GK, Ptashne M. lambda Repressor and cro--components of an efficient molecular switch. Nature. 294: 217-23. PMID 6457992 DOI: 10.1038/294217A0 |
0.539 |
|
| 1981 |
Turner BW, Pettigrew DW, Ackers GK. [37] Measurement and analysis of ligand-linked subunit dissociation equilibria in human hemoglobins Methods in Enzymology. 76: 596-628. DOI: 10.1016/0076-6879(81)76147-0 |
0.399 |
|
| 1979 |
Ackers GK. Linked functions in allosteric proteins: an exact theory for the effect of organic phosphates on oxygen affinity of hemoglobin. Biochemistry. 18: 3372-80. PMID 465477 DOI: 10.1021/Bi00582A025 |
0.31 |
|
| 1979 |
Mills FC, Ackers GK. Quaternary enhancement in binding of oxygen by human hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 76: 273-7. PMID 284341 DOI: 10.1073/Pnas.76.1.273 |
0.422 |
|
| 1978 |
Valdes R, Vickers LP, Halvorson HR, Ackers GK. Reciprocal effects in human hemoglobin: direct measurement of the dimer-tetramer association constant at partial oxygen saturation. Proceedings of the National Academy of Sciences of the United States of America. 75: 5493-6. PMID 281698 DOI: 10.1073/Pnas.75.11.5493 |
0.373 |
|
| 1978 |
Valdes R, Ackers GK. Self-association of hemoglobin betaSH chains is linked to oxygenation. Proceedings of the National Academy of Sciences of the United States of America. 75: 311-4. PMID 24215 DOI: 10.1073/Pnas.75.1.311 |
0.326 |
|
| 1976 |
Ip SH, Johnson ML, Ackers GK. Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates. Biochemistry. 15: 654-60. PMID 1252417 DOI: 10.1021/Bi00648A032 |
0.419 |
|
| 1976 |
Johnson ML, Halvorson HR, Ackers GK. Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms. Biochemistry. 15: 5363-71. PMID 999812 DOI: 10.1021/Bi00669A024 |
0.384 |
|
| 1976 |
Mills FC, Johnson ML, Ackers GK. Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves. Biochemistry. 15: 5350-62. PMID 999811 DOI: 10.1021/Bi00669A023 |
0.476 |
|
| 1975 |
Ackers GK, Halvorson HR. The linkage between oxygenation and subunit dissociation in human hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 71: 4312-6. PMID 4530985 DOI: 10.1073/Pnas.71.11.4312 |
0.434 |
|
| 1975 |
Ackers GK, Johnson ML, Mills FC, Halvorson HR, Shapiro S. The linkage between oxygenation and subunit dissociation in human hemoglobin. Consequences for the analysis of oxygenation curves. Biochemistry. 14: 5128-34. PMID 1191632 DOI: 10.1021/Bi00694A017 |
0.393 |
|
| 1974 |
Ackers GK. Studies of protein ligand binding by gel permeation techniques. Methods in Enzymology. 27: 441-55. PMID 4773289 DOI: 10.1016/S0076-6879(73)27018-0 |
0.414 |
|
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