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Volumn 119, Issue 5, 2004, Pages 629-640

Molecular mechanism of AHSP-mediated stabilization of α-hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA HEMOGLOBIN; ALPHA HEMOGLOBIN STABILIZING PROTEIN; HEME; HEMOGLOBIN; HISTIDINE; IRON; PROTEIN; UNCLASSIFIED DRUG;

EID: 8844285199     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2004.11.025     Document Type: Article
Times cited : (144)

References (38)
  • 1
    • 0031277482 scopus 로고    scopus 로고
    • Rice hemoglobins. Gene cloning, analysis, and O2-binding kinetics of a recombinant protein synthesized in Escherichia coli
    • Arredondo-Peter R., Hargrove M.S., Sarath G., Moran J.F., Lohrman J., Olson J.S., Klucas R.V. Rice hemoglobins. Gene cloning, analysis, and O2-binding kinetics of a recombinant protein synthesized in Escherichia coli. Plant Physiol. 115:1997;1259-1266
    • (1997) Plant Physiol. , vol.115 , pp. 1259-1266
    • Arredondo-Peter, R.1    Hargrove, M.S.2    Sarath, G.3    Moran, J.F.4    Lohrman, J.5    Olson, J.S.6    Klucas, R.V.7
  • 2
    • 0014366036 scopus 로고
    • Chromosomal and cytoplasmic regulation of haemoglobin synthesis
    • Baglioni C. Chromosomal and cytoplasmic regulation of haemoglobin synthesis. Bibl. Haematol. 29:1966;1056-1063
    • (1966) Bibl. Haematol. , vol.29 , pp. 1056-1063
    • Baglioni, C.1
  • 3
    • 0014150224 scopus 로고
    • Alpha-chain and globin: Intermediates in the synthesis of rabbit hemoglobin
    • Baglioni C., Campana T. Alpha-chain and globin. intermediates in the synthesis of rabbit hemoglobin Eur. J. Biochem. 2:1967;480-492
    • (1967) Eur. J. Biochem. , vol.2 , pp. 480-492
    • Baglioni, C.1    Campana, T.2
  • 5
    • 0023103593 scopus 로고
    • Subunit assembly of hemoglobin: An important determinant of hematologic phenotype
    • Bunn H.F. Subunit assembly of hemoglobin. an important determinant of hematologic phenotype Blood. 69:1987;1-6
    • (1987) Blood , vol.69 , pp. 1-6
    • Bunn, H.F.1
  • 6
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4) the CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project, Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y. Crystal structure of a procaspase-7 zymogen. mechanisms of activation and substrate binding Cell. 107:2001;399-407
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 8
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 9
    • 0035996732 scopus 로고    scopus 로고
    • 1H, 15N, and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex
    • Deane J.E., Visvader J.E., Mackay J.P., Matthew J.M. 1H, 15N, and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex. J. Biomol. NMR. 23:2002;165-166
    • (2002) J. Biomol. NMR , vol.23 , pp. 165-166
    • Deane, J.E.1    Visvader, J.E.2    MacKay, J.P.3    Matthew, J.M.4
  • 13
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., Williams K.R. Determination of molecular masses of proteins in solution. implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory J. Biomol. Tech. 10:1999;51-63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2
  • 14
    • 0037175053 scopus 로고    scopus 로고
    • Biophysical characterization of the α-globin binding protein α-hemoglobin stabilizing protein
    • Gell D., Kong Y., Eaton S.A., Weiss M.J., Mackay J.P. Biophysical characterization of the α-globin binding protein α-hemoglobin stabilizing protein. J. Biol. Chem. 277:2002;40602-40609
    • (2002) J. Biol. Chem. , vol.277 , pp. 40602-40609
    • Gell, D.1    Kong, Y.2    Eaton, S.A.3    Weiss, M.J.4    MacKay, J.P.5
  • 16
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:1997;283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J., Lu M., Bracken C. A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR. 20:2001;71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 21
    • 0035916246 scopus 로고    scopus 로고
    • Determination of the hemoglobin surface domains that react with cytochrome b5
    • Naito N.R., Hui H.L., Noble R.W., Hoffman B.M. Determination of the hemoglobin surface domains that react with cytochrome b5. Biochemistry. 40:2001;2060-2065
    • (2001) Biochemistry , vol.40 , pp. 2060-2065
    • Naito, N.R.1    Hui, H.L.2    Noble, R.W.3    Hoffman, B.M.4
  • 22
    • 0013974622 scopus 로고
    • Thalassemia: The consequences of unbalanced hemoglobin synthesis
    • Nathan D.G., Gunn R.B. Thalassemia. the consequences of unbalanced hemoglobin synthesis Am. J. Med. 41:1966;815-830
    • (1966) Am. J. Med. , vol.41 , pp. 815-830
    • Nathan, D.G.1    Gunn, R.B.2
  • 23
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling
    • Neri D., Szyperski T., Otting G., Senn H., Wuthrich K. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry. 28:1989;7510-7516
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wuthrich, K.5
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296
    • (1991) Proteins. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 2142773321 scopus 로고    scopus 로고
    • Pathophysiology of β thalassemia
    • M.H. Steinberg, B.G. Forget, D.R. Higgs, & R.L. Nagel. Cambridge: Cambridge University Press
    • Rachmilewitz E.A., Schrier S.L. Pathophysiology of β thalassemia. Steinberg M.H., Forget B.G., Higgs D.R., Nagel R.L. Disorders of Hemoglobin. 2001;233-251 Cambridge University Press, Cambridge
    • (2001) Disorders of Hemoglobin , pp. 233-251
    • Rachmilewitz, E.A.1    Schrier, S.L.2
  • 29
    • 0042324524 scopus 로고    scopus 로고
    • A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin
    • Robinson V.L., Smith B.B., Arnone A. A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin. Biochemistry. 42:2003;10113-10125
    • (2003) Biochemistry , vol.42 , pp. 10113-10125
    • Robinson, V.L.1    Smith, B.B.2    Arnone, A.3
  • 31
    • 0036814981 scopus 로고    scopus 로고
    • A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics
    • Schubert M., Labudde D., Oschkinat H., Schmieder P. A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics. J. Biomol. NMR. 24:2002;149-154
    • (2002) J. Biomol. NMR , vol.24 , pp. 149-154
    • Schubert, M.1    Labudde, D.2    Oschkinat, H.3    Schmieder, P.4
  • 33
    • 0016998013 scopus 로고
    • Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues
    • Spiro T.G., Burke J.M. Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. J. Am. Chem. Soc. 98:1976;5482-5489
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 5482-5489
    • Spiro, T.G.1    Burke, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.