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Volumn 58, Issue 7, 2001, Pages 902-920

Multifunctional α-enolase: Its role in diseases

Author keywords

Autoimmunity; Enolase; Rheumatic fever; SLE

Indexed keywords

ALPHA ENOLASE; ENOLASE; HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 0034947535     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000910     Document Type: Review
Times cited : (771)

References (119)
  • 2
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
    • (1997) J. Biol. Chem. , vol.272 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 3
    • 0029691198 scopus 로고    scopus 로고
    • Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • (1996) Life Sci , vol.58 , pp. 2271-2272
    • Sirover, M.1
  • 4
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 5
    • 0038119479 scopus 로고
    • Über die enzymatische Umwandlung von Phosphoglyzerinsäure in Brenztraubensäure und Phosphorsäure
    • (1934) Biochem. Z. , vol.273 , pp. 60-72
    • Lohman, K.1    Meyerhof, O.2
  • 6
    • 77956903746 scopus 로고
    • Enolase
    • Boyer P. D. (ed.), Academic Press, New York
    • (1971) The Enzymes , pp. 499-538
    • Wold, F.1
  • 11
    • 84882379709 scopus 로고
    • Enolase
    • Boyer P. D., Lardy H. and Myrback K. (eds.), Academic Press, New York
    • (1961) The Enzymes , pp. 471-494
    • Malstrom, B.G.1
  • 21
    • 0021960451 scopus 로고
    • Specificity and mechanism of action of metal ions in yeast enolase
    • (1985) FEBS Lett. , vol.182 , pp. 8-14
    • Brewer, J.M.1
  • 24
    • 0024289934 scopus 로고
    • Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor
    • (1988) Nature , vol.333 , pp. 683-686
    • Lebioda, L.1    Stec, B.2
  • 26
    • 0025804778 scopus 로고
    • Mechanism of enolase: The crystal structure of enolase-Mg2(+)2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-Å resolution
    • (1991) Biochemistry , vol.30 , pp. 2817-2822
    • Lebioda, L.1    Stec, B.2
  • 32
    • 0028901184 scopus 로고
    • Octahedral coordination at the high-affinity metal site in enolase: Crystallographic analysis of the MgI1-enzyme complex from yeast at 1.9 Å resolution
    • (1995) Biochemistry , vol.34 , pp. 4325-4330
    • Wedekind, J.E.1    Reed, G.H.2    Rayment, I.3
  • 34
    • 0030009782 scopus 로고    scopus 로고
    • A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: Structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 Å resolution
    • (1996) Biochemistry , vol.35 , pp. 4349-4358
    • Larsen, T.M.1    Wedekind, J.E.2    Rayment, I.3    Reed, G.H.4
  • 46
    • 0026738431 scopus 로고
    • Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme
    • (1992) J. Bacteriol. , vol.174 , pp. 6789-6799
    • Sundstrom, P.1    Aliaga, G.R.2
  • 47
    • 0028047655 scopus 로고
    • A subset of proteins found in culture supernatants of Candida albicans includes the abundant, immunodominant, glycolytic enzyme enolase
    • (1994) J. Infect. Dis. , vol.169 , pp. 452-456
    • Sundstrom, P.1    Aliaga, G.R.2
  • 50
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate dehydrogenase with multiple binding activity
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 64
    • 0034009502 scopus 로고    scopus 로고
    • Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene
    • (2000) J. Biol. Chem. , vol.275 , pp. 5958-5965
    • Subramanian, A.1    Miller, D.M.2
  • 77
    • 0021746842 scopus 로고
    • A heat shock-resistant mutant of Saccharomyces cerevisiae shows constitutive synthesis of two heat shock proteins and altered growth
    • (1984) J. Cell Biol. , vol.99 , pp. 1441-1450
    • Iida, H.1    Yahara, I.2
  • 91
    • 0016822849 scopus 로고
    • Glucose transport in Streptococcus mutans: Preparation of cytoplasmic membranes and characteristics of phosphotransferase activity
    • (1975) J. Dent. Res. , vol.54 , pp. 330-338
    • Schachtele, C.F.1
  • 97
    • 0028236442 scopus 로고
    • Serum neurone-specific enolase and other neuroendocrine markers in lung cancer
    • (1994) Eur. J. Cancer , vol.30 A , pp. 574-576
    • Ledermann, J.A.1
  • 101
    • 0022016661 scopus 로고
    • Partial purification and some properties of phi C2(W) lysin, a lytic enzyme produced by phage-infected cells of Streptococcus lactis C2
    • (1985) J. Dairy. Res. , vol.52 , pp. 123-138
    • Mullan, W.M.1    Crawford, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.