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Volumn 9, Issue 10, 2014, Pages 2318-2325

Identification of a small molecule that increases hemoglobin oxygen affinity and reduces SS erythrocyte sickling

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; 5 HYDROXYMETHYLFURFURAL; ANTISICKLING AGENT; CARBOXYHEMOGLOBIN; DI[5 (2,3 DIHYDRO 1,4 BENZODIOXIN 2 YL) 4H 1,2,4 TRIAZOL 3 YL]DISULFIDE; HEMOGLOBIN; HEMOGLOBIN S; N ETHYLMALEIMIDE; OXYGEN; TETRAMER; UNCLASSIFIED DRUG; BIS(5-(2,3-DIHYDRO-1,4-BENZODIOXIN-2-YL)-4H-1,2,4-TRIAZOL-3-YL)DISULFIDE; DISULFIDE; MOLECULAR LIBRARY; TRIAZOLE DERIVATIVE;

EID: 84908037773     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500230b     Document Type: Article
Times cited : (48)

References (48)
  • 1
    • 84908026231 scopus 로고    scopus 로고
    • accessed Dec 7, 2013
    • http://www.nhlbi.nih.gov/health/health-topics/topics/sca/atrisk.html (accessed Dec 7, 2013).
  • 2
    • 0025276708 scopus 로고
    • Sickle cell hemoglobin polymerization
    • Eaton, W. A., and Hofrichter, J. (1990) Sickle cell hemoglobin polymerization. Adv. Protein Chem. 40, 63-279.
    • (1990) Adv. Protein Chem. , vol.40 , pp. 63-279
    • Eaton, W.A.1    Hofrichter, J.2
  • 3
    • 0030853711 scopus 로고    scopus 로고
    • Pathogenesis and treatment of sickle cell disease
    • Bunn, H. F. (1997) Pathogenesis and treatment of sickle cell disease. N. Engl. J. Med. 337, 762-769.
    • (1997) N. Engl. J. Med. , vol.337 , pp. 762-769
    • Bunn, H.F.1
  • 5
    • 0018199125 scopus 로고
    • Requirement for therapeutic inhibition of sickle haemoglobin gelation
    • Sunshine, H. R., Hofrichter, J., and Eaton, W. A. (1978) Requirement for therapeutic inhibition of sickle haemoglobin gelation. Nature 275, 238-240.
    • (1978) Nature , vol.275 , pp. 238-240
    • Sunshine, H.R.1    Hofrichter, J.2    Eaton, W.A.3
  • 6
    • 0035283074 scopus 로고    scopus 로고
    • Treatment with NS3623, a novel Cl-conductance blocker, ameliorates erythrocyte dehydration in transgenic SAD mice: A possible new therapeutic approach for sickle cell disease
    • Bennekou, P., de Franceschi, L., Pedersen, O., Lian, L., Asakura, T., Evans, G., Brugnara, C., and Christophersen, P. (2001) Treatment with NS3623, a novel Cl-conductance blocker, ameliorates erythrocyte dehydration in transgenic SAD mice: A possible new therapeutic approach for sickle cell disease. Blood 97, 1451-1457.
    • (2001) Blood , vol.97 , pp. 1451-1457
    • Bennekou, P.1    De Franceschi, L.2    Pedersen, O.3    Lian, L.4    Asakura, T.5    Evans, G.6    Brugnara, C.7    Christophersen, P.8
  • 8
    • 84896734559 scopus 로고    scopus 로고
    • Therapeutic strategies to alter the oxygen affinity of sickle hemoglobin
    • Safo, M. K., and Kato, G. J. (2014) Therapeutic strategies to alter the oxygen affinity of sickle hemoglobin. Hematol. Oncol. Clin. North Am. 28, 217-231.
    • (2014) Hematol. Oncol. Clin. North Am. , vol.28 , pp. 217-231
    • Safo, M.K.1    Kato, G.J.2
  • 13
    • 0015621521 scopus 로고
    • Acetylation of Sickle Cell Hemoglobin by Aspirin
    • Klotz, I. M., and Tam, J. W. O. (1973) Acetylation of Sickle Cell Hemoglobin by Aspirin. Proc. Natl. Acad. Sci. U.S.A. 70, 1313-1315.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 1313-1315
    • Klotz, I.M.1    Tam, J.W.O.2
  • 14
    • 0019198649 scopus 로고
    • Development of antisickling compounds that chemically modify hemoglobin S specifically within the 2,3-diphosphoglycerate binding site
    • Walder, J. A., Walder, R. Y., and Arnone, A. (1980) Development of antisickling compounds that chemically modify hemoglobin S specifically within the 2,3-diphosphoglycerate binding site. J. Mol. Biol. 141, 195-216.
    • (1980) J. Mol. Biol. , vol.141 , pp. 195-216
    • Walder, J.A.1    Walder, R.Y.2    Arnone, A.3
  • 15
    • 0026690528 scopus 로고
    • Effects of methyl acetyl phosphate, a covalent antisickling agent, on the density profiles of sickle erythrocytes
    • Ueno, H., Yatco, E., Benjamin, L. J., and Manning, J. M. (1992) Effects of methyl acetyl phosphate, a covalent antisickling agent, on the density profiles of sickle erythrocytes. J. Clin. Lab. Med. 120, 152-158.
    • (1992) J. Clin. Lab. Med. , vol.120 , pp. 152-158
    • Ueno, H.1    Yatco, E.2    Benjamin, L.J.3    Manning, J.M.4
  • 17
    • 0001317733 scopus 로고
    • Chemistry of Bohr effect 1. Reaction of N-ethyl maleimide with oxygen-linked acid groups of hemoglobin
    • Benesch, R., and Benesch, R. (1961) Chemistry of Bohr effect 1. Reaction of N-ethyl maleimide with oxygen-linked acid groups of hemoglobin. J. Biol. Chem. 236, 405-410.
    • (1961) J. Biol. Chem. , vol.236 , pp. 405-410
    • Benesch, R.1    Benesch, R.2
  • 18
    • 79955842879 scopus 로고    scopus 로고
    • Hemoglobin-ligand binding: Understanding Hb function and allostery on atomic level
    • Safo, M. K., Ahmed, M. H., Ghatge, M. S., and Boyiri, T. (2011) Hemoglobin-ligand binding: Understanding Hb function and allostery on atomic level. Biochim. Biophys. Acta 1814, 797-809.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 797-809
    • Safo, M.K.1    Ahmed, M.H.2    Ghatge, M.S.3    Boyiri, T.4
  • 21
    • 84884629488 scopus 로고    scopus 로고
    • How does hemoglobin generate such diverse functionality of physiological relevance?
    • Yonetani, T., and Kanaori, K. (2013) How does hemoglobin generate such diverse functionality of physiological relevance? Biochim. Biophys. Acta 1834, 1873-1884.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1873-1884
    • Yonetani, T.1    Kanaori, K.2
  • 23
    • 84857911980 scopus 로고    scopus 로고
    • Unbiased binding assays for discovering small-molecule probes and drugs
    • Kemp, M. M., Weiwer, M., and Koehler, A. N. (2012) Unbiased binding assays for discovering small-molecule probes and drugs. Bioorg. Med. Chem. 20, 1979-1989.
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 1979-1989
    • Kemp, M.M.1    Weiwer, M.2    Koehler, A.N.3
  • 24
    • 82355188164 scopus 로고    scopus 로고
    • Ligand discovery using small-molecule microarrays
    • Casalena, D. E., Wassaf, D., and Koehler, A. N. (2012) Ligand discovery using small-molecule microarrays. Methods Mol. Biol. 803, 249-263.
    • (2012) Methods Mol. Biol. , vol.803 , pp. 249-263
    • Casalena, D.E.1    Wassaf, D.2    Koehler, A.N.3
  • 25
    • 0014214428 scopus 로고
    • Effect of organic phosphates from human erythrocyte on allosteric properties of hemoglobin
    • Benesch, R., and Benesch, R. (1967) Effect of organic phosphates from human erythrocyte on allosteric properties of hemoglobin. Biochem. Biophys. Res. Commun. 26, 162-167.
    • (1967) Biochem. Biophys. Res. Commun. , vol.26 , pp. 162-167
    • Benesch, R.1    Benesch, R.2
  • 26
    • 47049094619 scopus 로고    scopus 로고
    • Oxygen binding to heme proteins in solution, encapsulated in silica gels, and in the crystalline state
    • Ronda, L., Bruno, S., Faggiano, S., Bettati, S., and Mozzarelli, A. (2008) Oxygen binding to heme proteins in solution, encapsulated in silica gels, and in the crystalline state. Methods Enzymol. 437, 311-328.
    • (2008) Methods Enzymol. , vol.437 , pp. 311-328
    • Ronda, L.1    Bruno, S.2    Faggiano, S.3    Bettati, S.4    Mozzarelli, A.5
  • 28
    • 0014250343 scopus 로고
    • Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin
    • Benesch, R., Benesch, R. E., and Yu, C. I. (1968) Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 59, 526-532.
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 526-532
    • Benesch, R.1    Benesch, R.E.2    Yu, C.I.3
  • 29
    • 0039505434 scopus 로고
    • The nature and significance of the Bohr effect in mammalian hemoglobins
    • Riggs, A. (1960) The nature and significance of the Bohr effect in mammalian hemoglobins. J. Gen. Physiol. 43, 737-752.
    • (1960) J. Gen. Physiol. , vol.43 , pp. 737-752
    • Riggs, A.1
  • 30
    • 20444417111 scopus 로고    scopus 로고
    • The enigma of the liganded hemoglobin end state: A novel quaternary structure of human carbonmonoxy hemoglobin
    • Safo, M. K., and Abraham, D. J. (2005) The enigma of the liganded hemoglobin end state: A novel quaternary structure of human carbonmonoxy hemoglobin. Biochemistry 44, 8347-8359.
    • (2005) Biochemistry , vol.44 , pp. 8347-8359
    • Safo, M.K.1    Abraham, D.J.2
  • 31
    • 0023806752 scopus 로고
    • Reactivity of aromatic and heterocyclic disulphides with thiol group of bovine serum albumin
    • Gosselet, M., Mahieu, J.-P., and Sebille, B. (1988) Reactivity of aromatic and heterocyclic disulphides with thiol group of bovine serum albumin. Int. J.Biol. Macromol. 10, 241-247.
    • (1988) Int. J.Biol. Macromol. , vol.10 , pp. 241-247
    • Gosselet, M.1    Mahieu, J.-P.2    Sebille, B.3
  • 32
    • 0027219952 scopus 로고
    • Reactivity of 42 disulfides with thiol group of human haemoglobin and human serum albumin
    • Mahieu, J. P., Gosselet, N. M., Sebille, B., Garel, M. C., and Beuzard, Y. (1993) Reactivity of 42 disulfides with thiol group of human haemoglobin and human serum albumin. Int. J. Biol. Macromol. 15, 233-240.
    • (1993) Int. J. Biol. Macromol. , vol.15 , pp. 233-240
    • Mahieu, J.P.1    Gosselet, N.M.2    Sebille, B.3    Garel, M.C.4    Beuzard, Y.5
  • 33
    • 33947312669 scopus 로고    scopus 로고
    • The role of β93 Cys in the inhibition of Hb S fiber formation
    • Knee, K. M., Roden, C. K., Flory, M. R., and Mukerji, I. (2007) The role of β93 Cys in the inhibition of Hb S fiber formation. Biophys. Chem. 127, 181-193.
    • (2007) Biophys. Chem. , vol.127 , pp. 181-193
    • Knee, K.M.1    Roden, C.K.2    Flory, M.R.3    Mukerji, I.4
  • 35
    • 0014962564 scopus 로고
    • Kinetics of the reaction of the "masked" and "free" sulfhydryl groups of human hemoglobin with p-mercuribenzoate
    • Chiancone, E., Currell, D. L., Vecchini, P., Antonini, E., and Wyman, J. (1970) Kinetics of the reaction of the "masked" and "free" sulfhydryl groups of human hemoglobin with p-mercuribenzoate. J. Biol. Chem. 245, 4105-4111.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4105-4111
    • Chiancone, E.1    Currell, D.L.2    Vecchini, P.3    Antonini, E.4    Wyman, J.5
  • 36
    • 84883407801 scopus 로고    scopus 로고
    • Subunit disassembly pathway of human hemoglobin revealing the site-specific role of its cysteine residues
    • Kan, H. I., Chen, I. Y., Zulfajri, M., and Wang, C. C. (2013) Subunit disassembly pathway of human hemoglobin revealing the site-specific role of its cysteine residues. J. Phys. Chem. B 117, 9831-9839.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 9831-9839
    • Kan, H.I.1    Chen, I.Y.2    Zulfajri, M.3    Wang, C.C.4
  • 37
    • 0030452492 scopus 로고    scopus 로고
    • Structural characterization by mass spectrometry of hemoglobin adducts formed after in vivo exposure to methyl bromide
    • Ferranti, P., Sannolo, N., Mamone, G., Fiume, I., Carbone, V., Tornqvist, M., Bergman, A., and Malorni, A. (1996) Structural characterization by mass spectrometry of hemoglobin adducts formed after in vivo exposure to methyl bromide. Carcinogenesis 17, 2661-2671.
    • (1996) Carcinogenesis , vol.17 , pp. 2661-2671
    • Ferranti, P.1    Sannolo, N.2    Mamone, G.3    Fiume, I.4    Carbone, V.5    Tornqvist, M.6    Bergman, A.7    Malorni, A.8
  • 38
    • 0025801633 scopus 로고
    • Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli, A., Rivetti, C., Rossi, G. L., Henry, E. R., and Eaton, W. A. (1991) Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature 351, 416-419.
    • (1991) Nature , vol.351 , pp. 416-419
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Henry, E.R.4    Eaton, W.A.5
  • 41
    • 0015515865 scopus 로고
    • X-ray diffraction study of binding 2,3-diphosphoglycerate to human deoxyhemoglobin
    • Arnone, A. (1972) X-ray diffraction study of binding 2,3-diphosphoglycerate to human deoxyhemoglobin. Nature 237, 146-149.
    • (1972) Nature , vol.237 , pp. 146-149
    • Arnone, A.1
  • 42
    • 0142228328 scopus 로고    scopus 로고
    • X-ray crystallography of hemoglobins
    • Safo, M. K., and Abraham, D. J. (2003) X-ray crystallography of hemoglobins. Methods Mol. Med. 82, 1-19.
    • (2003) Methods Mol. Med. , vol.82 , pp. 1-19
    • Safo, M.K.1    Abraham, D.J.2
  • 48
    • 0025845073 scopus 로고
    • Morphology of sickle cells produced in solutions of varying osmolarities
    • Hijiya, N., Horiuchi, K., and Asakura, T. (1991) Morphology of sickle cells produced in solutions of varying osmolarities. J. Clin. Lab. Med. 117, 60-66.
    • (1991) J. Clin. Lab. Med. , vol.117 , pp. 60-66
    • Hijiya, N.1    Horiuchi, K.2    Asakura, T.3


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