Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution.

Citations

1. Donkor AK, Pagare PP, Mughram MHA, Safo MK. X-ray crystallography and sickle cell disease drug discovery-a tribute to Donald Abraham.. Front Mol Biosci 2023;10:1136970.
   doi: 10.3389/fmolb.2023.1136970pubmed: 37293554google scholar: lookup
2. Dimitrova YN, Gutierrez JA, Huard K. It's ok to be outnumbered - sub-stoichiometric modulation of homomeric protein complexes.. RSC Med Chem 2023 Jan 25;14(1):22-46.
   doi: 10.1039/d2md00212dpubmed: 36760737google scholar: lookup
3. Zhao X, Huang Y, Bian C, You X, Zhang X, Chen J, Wang M, Hu C, Xu Y, Xu J, Shi Q. Whole genome sequencing of the fast-swimming Southern bluefin tuna (Thunnus maccoyii).. Front Genet 2022;13:1020017.
   doi: 10.3389/fgene.2022.1020017pubmed: 36406129google scholar: lookup
4. Sawaya MR, Hughes MP, Rodriguez JA, Riek R, Eisenberg DS. The expanding amyloid family: Structure, stability, function, and pathogenesis.. Cell 2021 Sep 16;184(19):4857-4873.
   doi: 10.1016/j.cell.2021.08.013pubmed: 34534463google scholar: lookup
5. Shou K, Sarter M, de Souza NR, de Campo L, Whitten AE, Kuchel PW, Garvey CJ, Stadler AM. Effect of red blood cell shape changes on haemoglobin interactions and dynamics: a neutron scattering study.. R Soc Open Sci 2020 Oct;7(10):201507.
   doi: 10.1098/rsos.201507pubmed: 33204483google scholar: lookup
6. Mikkelsen JH, Runager K, Andersen CBF. The human protein haptoglobin inhibits IsdH-mediated heme-sequestering by Staphylococcus aureus.. J Biol Chem 2020 Feb 14;295(7):1781-1791.
   doi: 10.1074/jbc.RA119.011612pubmed: 31819010google scholar: lookup
7. Rapp O, Yifrach O. Using the MWC model to describe heterotropic interactions in hemoglobin.. PLoS One 2017;12(8):e0182871.
   doi: 10.1371/journal.pone.0182871pubmed: 28793329google scholar: lookup
8. Burley SK, Berman HM, Kleywegt GJ, Markley JL, Nakamura H, Velankar S. Protein Data Bank (PDB): The Single Global Macromolecular Structure Archive.. Methods Mol Biol 2017;1607:627-641.
   doi: 10.1007/978-1-4939-7000-1_26pubmed: 28573592google scholar: lookup
9. Berman HM, Burley SK, Kleywegt GJ, Markley JL, Nakamura H, Velankar S. The archiving and dissemination of biological structure data.. Curr Opin Struct Biol 2016 Oct;40:17-22.
   doi: 10.1016/j.sbi.2016.06.018pubmed: 27450113google scholar: lookup
10. Gevorkian SG, Allahverdyan AE, Gevorgyan DS, Hu CK. Thermal-induced force release in oxyhemoglobin.. Sci Rep 2015 Aug 17;5:13064.
    doi: 10.1038/srep13064pubmed: 26277901google scholar: lookup
11. Erman JE, Chinchilla D, Studer J, Vitello LB. Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L).. Biochim Biophys Acta 2015 Aug;1854(8):869-81.
    doi: 10.1016/j.bbapap.2015.04.013pubmed: 25907133google scholar: lookup
12. Jones CP, Ferré-D'Amaré AR. RNA quaternary structure and global symmetry.. Trends Biochem Sci 2015 Apr;40(4):211-20.
    doi: 10.1016/j.tibs.2015.02.004pubmed: 25778613google scholar: lookup
13. Wiederstein M, Gruber M, Frank K, Melo F, Sippl MJ. Structure-based characterization of multiprotein complexes.. Structure 2014 Jul 8;22(7):1063-70.
    doi: 10.1016/j.str.2014.05.005pubmed: 24954616google scholar: lookup
14. Kutsenko OK, Trusova VM, Gorbenko GP, Lipovaya AS, Slobozhanina EI, Lukyanenko LM, Deligeorgiev T, Vasilev A. Fluorescence study of the membrane effects of aggregated lysozyme.. J Fluoresc 2013 Nov;23(6):1229-37.
    doi: 10.1007/s10895-013-1254-2pubmed: 23807458google scholar: lookup
15. Orville AM, Buono R, Cowan M, Héroux A, Shea-McCarthy G, Schneider DK, Skinner JM, Skinner MJ, Stoner-Ma D, Sweet RM. Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C.. J Synchrotron Radiat 2011 May;18(Pt 3):358-66.
    doi: 10.1107/S0909049511006315pubmed: 21525643google scholar: lookup
16. Foshay MC, Vitello LB, Erman JE. Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: properties of CcP mutants H52D, H52E, H52N, and H52Q.. Biochim Biophys Acta 2011 May;1814(5):525-35.
    doi: 10.1016/j.bbapap.2011.02.009pubmed: 21354339google scholar: lookup
17. Nagel ZD, Klinman JP. Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.. Chem Rev 2010 Dec 8;110(12):PR41-67.
    doi: 10.1021/cr1001035pubmed: 21141912google scholar: lookup
18. Pagán M, Solá RJ, Griebenow K. On the role of protein structural dynamics in the catalytic activity and thermostability of serine protease subtilisin Carlsberg.. Biotechnol Bioeng 2009 May 1;103(1):77-84.
    doi: 10.1002/bit.22221pubmed: 19132746google scholar: lookup
19. Cozzini P, Kellogg GE, Spyrakis F, Abraham DJ, Costantino G, Emerson A, Fanelli F, Gohlke H, Kuhn LA, Morris GM, Orozco M, Pertinhez TA, Rizzi M, Sotriffer CA. Target flexibility: an emerging consideration in drug discovery and design.. J Med Chem 2008 Oct 23;51(20):6237-55.
    doi: 10.1021/jm800562dpubmed: 18785728google scholar: lookup
20. Michel D. An alternative theoretical formula for hemoglobin oxygenation.. Eur Biophys J 2008 Jul;37(6):823-7.
    doi: 10.1007/s00249-008-0283-2pubmed: 18286275google scholar: lookup
21. Yan A, Wu E, Lennarz WJ. Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.. Proc Natl Acad Sci U S A 2005 May 17;102(20):7121-6.
    doi: 10.1073/pnas.0502669102pubmed: 15886282google scholar: lookup
22. Safo MK, Abraham DJ. The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 A resoultion and its relationship to the quaternary structures of other hemoglobin crystal froms.. Protein Sci 2001 Jun;10(6):1091-9.
    doi: 10.1110/ps.48301pubmed: 11369847google scholar: lookup
23. Safo MK, Moure CM, Burnett JC, Joshi GS, Abraham DJ. High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector.. Protein Sci 2001 May;10(5):951-7.
    doi: 10.1110/ps.50601pubmed: 11316875google scholar: lookup
24. Antosiewicz J, Porschke D. Electrostatics of hemoglobins from measurements of the electric dichroism and computer simulations.. Biophys J 1995 Feb;68(2):655-64.
    doi: 10.1016/S0006-3495(95)80226-2pubmed: 7696517google scholar: lookup
25. Beddell CR, Goodford PJ, Kneen G, White RD, Wilkinson S, Wootton R. Substituted benzaldehydes designed to increase the oxygen affinity of human haemoglobin and inhibit the sickling of sickle erythrocytes.. Br J Pharmacol 1984 Jun;82(2):397-407.
    doi: 10.1111/j.1476-5381.1984.tb10775.xpubmed: 6733364google scholar: lookup
26. Kilmartin JV, Rossi-Bernardi L. The binding of carbon dioxide by horse haemoglobin.. Biochem J 1971 Aug;124(1):31-45.
    doi: 10.1042/bj1240031pubmed: 5166592google scholar: lookup
27. Boyer SH, Charache S, Fairbanks VF, Maldonado JE, Noyes A, Gayle EE. Hemoglobin Malmö Beta-97 (FG-4) histidine--glutamine: a cause of polycythemia.. J Clin Invest 1972 Mar;51(3):666-76.
    doi: 10.1172/JCI106855pubmed: 5011106google scholar: lookup
28. Kilmartin JV. The interaction of inositol hexaphosphate with methaemoglobin.. Biochem J 1973 Aug;133(4):725-33.
    doi: 10.1042/bj1330725pubmed: 4748831google scholar: lookup
29. Lokich JJ, Moloney WC, Bunn HF, Bruckheimer SM, Ranney HM. Hemoglobin brigham (alpha2Abeta2100 Pro--Leu). Hemoglobin variant associated with familial erythrocytosis.. J Clin Invest 1973 Aug;52(8):2060-7.
    doi: 10.1172/JCI107390pubmed: 4719677google scholar: lookup
30. Stamatoyannopoulos G, Nute PE, Adamson JW, Bellingham AJ, Funk D. Hemoglobin olympia ( 20 valine leads to methionine): an electrophoretically silent variant associated with high oxygen affinity and erythrocytosis.. J Clin Invest 1973 Feb;52(2):342-9.
    doi: 10.1172/JCI107190pubmed: 4683875google scholar: lookup
31. Pulsinelli PD, Perutz MF, Nagel RL. Structure of hemoglobin M Boston, a variant with a five-coordinated ferric heme.. Proc Natl Acad Sci U S A 1973 Dec;70(12):3870-4.
    doi: 10.1073/pnas.70.12.3870pubmed: 4521212google scholar: lookup
32. Hofrichter J, Hendricker DG, Eaton WA. Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes.. Proc Natl Acad Sci U S A 1973 Dec;70(12):3604-8.
    doi: 10.1073/pnas.70.12.3604pubmed: 4519649google scholar: lookup
33. Kilmartin JV, Breen JJ, Roberts GC, Ho C. Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin.. Proc Natl Acad Sci U S A 1973 Apr;70(4):1246-9.
    doi: 10.1073/pnas.70.4.1246pubmed: 4515623google scholar: lookup
34. Moon RB, Richards JH. Conformation studies of various hemoglobins by natural-abundance 13 C NMR spectroscopy.. Proc Natl Acad Sci U S A 1972 Aug;69(8):2193-7.
    doi: 10.1073/pnas.69.8.2193pubmed: 4506089google scholar: lookup
35. Hewitt JA, Kilmartin JV, Eyck LF, Perutz MF. Noncooperativity of the dimer in the reaction of hemoglobin with oxygen (human-dissociation-equilibrium-sulfhydryl-absorption-x-ray analysis).. Proc Natl Acad Sci U S A 1972 Jan;69(1):203-7.
    doi: 10.1073/pnas.69.1.203pubmed: 4500548google scholar: lookup
36. Kleihauer E. [Structure-function relationship in normal and abnormal hemoglobins (author's transl)].. Klin Wochenschr 1974 Nov 1;52(21):995-1002.
    doi: 10.1007/BF01494271pubmed: 4457729google scholar: lookup
37. Ogata RT, McConnell HM. Mechanism of cooperative oxygen binding to hemoglobin (spin-labeled triphosphate-concerted transition model-hemoglobin chesapeake).. Proc Natl Acad Sci U S A 1972 Feb;69(2):335-9.
    doi: 10.1073/pnas.69.2.335pubmed: 4333976google scholar: lookup
38. Merrett M, Stammers DK, White RD, Wootton R, Kneen G. Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.. Biochem J 1986 Oct 15;239(2):387-92.
    doi: 10.1042/bj2390387pubmed: 3814079google scholar: lookup
39. Fermi G, Perutz MF, Shulman RG. Iron distances in hemoglobin: comparison of x-ray crystallographic and extended x-ray absorption fine structure studies.. Proc Natl Acad Sci U S A 1987 Sep;84(17):6167-8.
    doi: 10.1073/pnas.84.17.6167pubmed: 3476938google scholar: lookup
40. Tibbitts TT, Caspar DL, Phillips WC, Goodenough DA. Diffraction diagnosis of protein folding in gap junction connexons.. Biophys J 1990 May;57(5):1025-36.
    doi: 10.1016/S0006-3495(90)82621-7pubmed: 2160297google scholar: lookup
41. Horimoto K, Suzuki H, Otsuka J. Discrimination between adaptive and neutral amino acid substitutions in vertebrate hemoglobins.. J Mol Evol 1990 Oct;31(4):302-24.
    doi: 10.1007/BF02101125pubmed: 2124278google scholar: lookup
42. Johnson MS, Sutcliffe MJ, Blundell TL. Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.. J Mol Evol 1990 Jan;30(1):43-59.
    doi: 10.1007/BF02102452pubmed: 2107323google scholar: lookup
43. Wireko FC, Abraham DJ. X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin.. Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2209-11.
    doi: 10.1073/pnas.88.6.2209pubmed: 2006159google scholar: lookup
44. Vuk Pavlović S. Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis.. J Mol Evol 1975 Nov 4;6(3):209-14.
    doi: 10.1007/BF01732357pubmed: 1206726google scholar: lookup
45. Levinthal C, Wodak SJ, Kahn P, Dadivanian AK. Hemoglobin interaction in sickle cell fibers. I: Theoretical approaches to the molecular contacts.. Proc Natl Acad Sci U S A 1975 Apr;72(4):1330-4.
    doi: 10.1073/pnas.72.4.1330pubmed: 1055409google scholar: lookup
46. Goodford PJ, St-Louis J, Wootton R. A quantitative analysis of the effects of 2,3-diphosphoglycerate, adenosine triphosphate and inositol hexaphosphate on the oxygen dissociation curve of human haemoglobin.. J Physiol 1978 Oct;283:397-407.
    doi: 10.1113/jphysiol.1978.sp012508pubmed: 722582google scholar: lookup
47. Goodford PJ, Norrington FE, Paterson RA, Wootton R. The effect of 2,3-diphosphoglycerate on the oxygen dissociation curve of human haemoglobin.. J Physiol 1977 Dec;273(3):631-45.
    doi: 10.1113/jphysiol.1977.sp012114pubmed: 604451google scholar: lookup
48. Beddell CR, Goodford PJ, Stammers DK, Wootton R. Species differences in the binding of compounds designed to fit a site of known structure in adult human haemoglobin.. Br J Pharmacol 1979 Mar;65(3):535-43.
    doi: 10.1111/j.1476-5381.1979.tb07862.xpubmed: 427327google scholar: lookup
49. Tucker PW, Phillips SE, Perutz MF, Houtchens R, Caughey WS. Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding.. Proc Natl Acad Sci U S A 1978 Mar;75(3):1076-80.
    doi: 10.1073/pnas.75.3.1076pubmed: 274697google scholar: lookup
50. Van Wart HE, Scheraga HA. Stable conformations of aliphatic disulfides: influence of 1,4 interactions involving sulfur atoms.. Proc Natl Acad Sci U S A 1977 Jan;74(1):13-7.
    doi: 10.1073/pnas.74.1.13pubmed: 264666google scholar: lookup
51. Valentine JS, Sheridan RP, Allen LC, Kahn PC. Coupling between oxidation state and hydrogen bond conformation in heme proteins.. Proc Natl Acad Sci U S A 1979 Mar;76(3):1009-13.
    doi: 10.1073/pnas.76.3.1009pubmed: 220604google scholar: lookup
52. Champion AB, Soderberg KL, Wilson AC. Immunological comparison of azurins of known amino acid sequence. Dependence of cross-reactivity upon sequence resemblance.. J Mol Evol 1975 Sep 8;5(4):291-305.
    doi: 10.1007/BF01732216pubmed: 53292google scholar: lookup