메뉴 건너뛰기




Volumn 21, Issue 11-12, 2002, Pages 813-823

Kinetic and molecular modeling of nucleoside and nucleotide inhibition of malate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CYCLIC AMP; MALATE DEHYDROGENASE; NUCLEOSIDE DERIVATIVE; NUCLEOTIDE DERIVATIVE;

EID: 0036913631     PISSN: 15257770     EISSN: None     Source Type: Journal    
DOI: 10.1081/NCN-120016483     Document Type: Article
Times cited : (3)

References (13)
  • 1
    • 0027302991 scopus 로고
    • Crystal structure of a ternary complex of escherichia coli malate dehydrogenase citrate and NAD at 1.9 Å resolution
    • Hall, M.D.; Banaszak, L.J. Crystal structure of a ternary complex of escherichia coli malate dehydrogenase citrate and NAD at 1.9 Å resolution. J. Mol. Biol. 1993, 232, 213-222.
    • (1993) J. Mol. Biol. , vol.232 , pp. 213-222
    • Hall, M.D.1    Banaszak, L.J.2
  • 2
    • 0024413884 scopus 로고
    • Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution
    • Birktoft, J.J.; Rhodes, G.; Banaszak, L.J. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5 Å resolution. Biochemistry 1989, 28, 6065-6081.
    • (1989) Biochemistry , vol.28 , pp. 6065-6081
    • Birktoft, J.J.1    Rhodes, G.2    Banaszak, L.J.3
  • 3
    • 0028331873 scopus 로고
    • Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases
    • Gleason, W.B.; Zhuji, F.; Birktoft, J.; Banaszak, L. Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. Biochemistry 1994, 33, 2078-2088.
    • (1994) Biochemistry , vol.33 , pp. 2078-2088
    • Gleason, W.B.1    Zhuji, F.2    Birktoft, J.3    Banaszak, L.4
  • 4
    • 0029922127 scopus 로고    scopus 로고
    • Dye-affinity labeling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site
    • Labrou, N.E.; Éliopoulos, E.; Clonis, Y.D. Dye-affinity labeling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site. Biochem. J. 1996, 315, 687-693.
    • (1996) Biochem. J. , vol.315 , pp. 687-693
    • Labrou, N.E.1    Éliopoulos, E.2    Clonis, Y.D.3
  • 5
    • 0030000366 scopus 로고    scopus 로고
    • Molecular modeling for the design of chimaeric biomimetic dye-ligands and their interaction with bovine heart mitochondrial malate dehydrogenase
    • Labrou, N.E.; Eliopoulos, E.; Clonis, Y.D. Molecular modeling for the design of chimaeric biomimetic dye-ligands and their interaction with bovine heart mitochondrial malate dehydrogenase. Biochem. J. 1996, 315, 695-703.
    • (1996) Biochem. J. , vol.315 , pp. 695-703
    • Labrou, N.E.1    Eliopoulos, E.2    Clonis, Y.D.3
  • 6
  • 7
    • 0015538963 scopus 로고
    • The effects of adenine nucleotides on NADH binding to mitochondrial malate dehydrogenase
    • Oza, N.B.; Shore, J.D. The effects of adenine nucleotides on NADH binding to mitochondrial malate dehydrogenase. Arch. Biochem. Biophys. 1973, 154, 360-365.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 360-365
    • Oza, N.B.1    Shore, J.D.2
  • 8
    • 84912167671 scopus 로고
    • Effect of cyclic 3′,5′-adenosine monophosphate on gonadal diphosphopyridine and triphosphopyridine nucleotide linked dehydrogenases
    • New York Hospital-Cornell Medical Center; Saxena, B.B., Beling, C.G., Gandy, H.M., Eds.; Wiley-Interscience: New York
    • Sulimovici, S.; Lunenfeld, B. Effect of cyclic 3′,5′-adenosine monophosphate on gonadal diphosphopyridine and triphosphopyridine nucleotide linked dehydrogenases. In Gonadotropins, International Symposium on Gonadotopins; New York Hospital-Cornell Medical Center, 1971; Saxena, B.B., Beling, C.G., Gandy, H.M., Eds.; Wiley-Interscience: New York, 1972; 287-300.
    • (1971) Gonadotropins, International Symposium on Gonadotopins , pp. 287-300
    • Sulimovici, S.1    Lunenfeld, B.2
  • 9
    • 0032567678 scopus 로고    scopus 로고
    • A computational study of the resistance of HIV-1 aspartic protease to the inhibitors ABT-538 and VX-478 and design of new analogues
    • Nair, A.C.; Miertus, S.; Tossi, A.; Romeo, D. A Computational study of the resistance of HIV-1 aspartic protease to the inhibitors ABT-538 and VX-478 and design of new analogues. Biochem. Biophys. Res. Commun. 1998, 242, 545-551.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 545-551
    • Nair, A.C.1    Miertus, S.2    Tossi, A.3    Romeo, D.4
  • 11
    • 0000500410 scopus 로고
    • Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes
    • Almarsson, O.; Bruice, T.C. Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes. J. Am. Chem. Soc. 1993, 115, 2125-2138.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2125-2138
    • Almarsson, O.1    Bruice, T.C.2
  • 12
    • 0034676326 scopus 로고    scopus 로고
    • Computational studies on HIV-1 protease inhibitors: Influence of calculated inhibitor-enzyme binding affinities on the statistical quality of 3D-QSAR CoMFA models
    • Jayateilleke, P.R.N.; Nair, A.C.; Zauhar, R.; Welsh, W.J. Computational studies on HIV-1 protease inhibitors: Influence of calculated inhibitor-enzyme binding affinities on the statistical quality of 3D-QSAR CoMFA models. J. Med. Chem. 2000, 43, 4446-4451.
    • (2000) J. Med. Chem. , vol.43 , pp. 4446-4451
    • Jayateilleke, P.R.N.1    Nair, A.C.2    Zauhar, R.3    Welsh, W.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.