메뉴 건너뛰기




Volumn 9, Issue 2, 2009, Pages 95-106

Red cell glycolytic enzyme disorders caused by mutations: An update

Author keywords

Glycolytic enzymes; Mutation; Red cells; Structure

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; ASPARTIC ACID; BISPHOSPHOGLYCERATE MUTASE; CYSTEINE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLUTAMIC ACID; GLUTAMINE; GLYCINE; GLYCOLYTIC ENZYME; HISTIDINE; ISOLEUCINE; LEUCINE; LYSINE; METHIONINE; PHENYLALANINE; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE MUTASE; PYRUVATE KINASE; THREONINE; TRIOSEPHOSPHATE ISOMERASE; TRYPTOPHAN; TYROSINE; VALINE;

EID: 68349120552     PISSN: 1871529X     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152909788488636     Document Type: Article
Times cited : (21)

References (147)
  • 1
    • 0029099402 scopus 로고
    • Structure and organization of the human glucose phosphate isomerase gene (GPI)
    • Walker, J.I.H.; Morgan, M.J.; Faik, P. Structure and organization of the human glucose phosphate isomerase gene (GPI). Genomics, 1995, 29, 261-265.
    • (1995) Genomics , vol.29 , pp. 261-265
    • Walker, J.I.H.1    Morgan, M.J.2    Faik, P.3
  • 3
    • 20444385302 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/ autocrine motility factor/neuroleukine
    • Sun, Y.J.; Chou, C.C.; Chen, W.S.; Wu, R.T.; Men, M.; Hsiao, C.D. The crystal structure of a multifunctional protein: phosphoglucose isomerase/ autocrine motility factor/neuroleukine. Proc. Nat. Acad. Sci. USA, 1999, 243, 1401-1414.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.243 , pp. 1401-1414
    • Sun, Y.J.1    Chou, C.C.2    Chen, W.S.3    Wu, R.T.4    Men, M.5    Hsiao, C.D.6
  • 4
    • 0034620506 scopus 로고    scopus 로고
    • Jeffery, C.J.; Bahnson, B.J.; Chien, W.; Ringe, Petsko, A. Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukine, autocrine motility factor and differentiation mediator. Biochemistry, 2000, 39, 955-964.
    • Jeffery, C.J.; Bahnson, B.J.; Chien, W.; Ringe, Petsko, A. Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukine, autocrine motility factor and differentiation mediator. Biochemistry, 2000, 39, 955-964.
  • 5
    • 0035369540 scopus 로고    scopus 로고
    • The crystal structure of human phosphoglucose isoemerase at 1.6 A resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia
    • Read, J.; Pearce, J.; Li, H.; Muirhead, H.; Chirwing, J.; Davies, C. The crystal structure of human phosphoglucose isoemerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia. J. Mol. Biol. 2001, 309, 447-463.
    • (2001) J. Mol. Biol , vol.309 , pp. 447-463
    • Read, J.1    Pearce, J.2    Li, H.3    Muirhead, H.4    Chirwing, J.5    Davies, C.6
  • 6
  • 8
    • 0023032240 scopus 로고
    • Molecular cloning and expression of neuroleukin, a neurotrophic factor for spinal and sensory neurons
    • Gurney, M. E.; Heinrich, S.P.; Lee, M. R.; Yin, H. Molecular cloning and expression of neuroleukin, a neurotrophic factor for spinal and sensory neurons. Science. 1986, 234, 566-574.
    • (1986) Science , vol.234 , pp. 566-574
    • Gurney, M.E.1    Heinrich, S.P.2    Lee, M.R.3    Yin, H.4
  • 11
    • 0022378710 scopus 로고
    • Generalised glucosephosphate isomerase (GPI) deficiency causing haemolytic anaemia, neuromuscular symptoms and impairment of granulocytic function: A new syndrome due to a new stable GPI variant with diminished specific activity (GPI Homburg)
    • Schroter, W.; Eber, S.W.; Bardosi, A.; Gahr, M.; Gabriel, M.; Sitzman, F.C. Generalised glucosephosphate isomerase (GPI) deficiency causing haemolytic anaemia, neuromuscular symptoms and impairment of granulocytic function: a new syndrome due to a new stable GPI variant with diminished specific activity (GPI Homburg). Eur. J. Pediatr., 1985, 144, 301-305.
    • (1985) Eur. J. Pediatr , vol.144 , pp. 301-305
    • Schroter, W.1    Eber, S.W.2    Bardosi, A.3    Gahr, M.4    Gabriel, M.5    Sitzman, F.C.6
  • 12
    • 27644504936 scopus 로고    scopus 로고
    • Expression analysis of neuroleukin, calmodulin, cortactin and Rho7/Rnd2 in the intact and injured mouse brain
    • Decourt, B.; Bouleau, Y.; Dulon, D.; Hafidi, A. Expression analysis of neuroleukin, calmodulin, cortactin and Rho7/Rnd2 in the intact and injured mouse brain. Brain Res. Des. Brain Res., 2005, 159, 36-54.
    • (2005) Brain Res. Des. Brain Res , vol.159 , pp. 36-54
    • Decourt, B.1    Bouleau, Y.2    Dulon, D.3    Hafidi, A.4
  • 13
    • 51249108652 scopus 로고    scopus 로고
    • Expression patterns in mouse embryos of neuroleukin/glucose-6-phosphate isomerase and autocrine motility factor receptor
    • Repiso, A.; Andrés, R.; Climent, F.; Ureña, J.M. Expression patterns in mouse embryos of neuroleukin/glucose-6-phosphate isomerase and autocrine motility factor receptor. Anat. Histol. Embryol., 2008, 37, 380-382.
    • (2008) Anat. Histol. Embryol , vol.37 , pp. 380-382
    • Repiso, A.1    Andrés, R.2    Climent, F.3    Ureña, J.M.4
  • 14
    • 0026572472 scopus 로고
    • Autocrine motility factor and its receptor: Role in cell locomotion and metastasis
    • Nabi, I.; Watanabe, H.; Raz, A. Autocrine motility factor and its receptor: role in cell locomotion and metastasis. Cancer Metastasis Rev., 1992, 11, 5-20
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 5-20
    • Nabi, I.1    Watanabe, H.2    Raz, A.3
  • 15
    • 0030012538 scopus 로고    scopus 로고
    • Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase peptide
    • Watanabe, H.; Takehana, K.; Date, M.; Shinozaki, T.; Raz A. Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase peptide. Cancer Res., 1996, 56, 2960-2963.
    • (1996) Cancer Res , vol.56 , pp. 2960-2963
    • Watanabe, H.1    Takehana, K.2    Date, M.3    Shinozaki, T.4    Raz, A.5
  • 16
    • 0037224507 scopus 로고    scopus 로고
    • Overexpression of the autocrine motility factor/phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts
    • Tsutsumi, S.; Hogan, V.; Nabi, I.R.; Raz A. Overexpression of the autocrine motility factor/phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts. Cancer Res., 2003, 63, 242-249.
    • (2003) Cancer Res , vol.63 , pp. 242-249
    • Tsutsumi, S.1    Hogan, V.2    Nabi, I.R.3    Raz, A.4
  • 17
    • 37549032762 scopus 로고    scopus 로고
    • Down-regulation of phosphoglucose isomerase/autocrine motility factor expression sensitizes human fibrosome cells to oxidative stress leading to cellular senescense
    • Funasaka, T.; Hu, H.; Hogan, V.; Raz, A. Down-regulation of phosphoglucose isomerase/autocrine motility factor expression sensitizes human fibrosome cells to oxidative stress leading to cellular senescense. J. Biol. Chem., 2007, 282, 36362-36369.
    • (2007) J. Biol. Chem , vol.282 , pp. 36362-36369
    • Funasaka, T.1    Hu, H.2    Hogan, V.3    Raz, A.4
  • 18
    • 0029898821 scopus 로고    scopus 로고
    • The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase
    • Xu, W.; Seiter, K.; Feldman, E.; Ahmed, T.; Chiao J.W. The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase. Blood, 1996, 87, 4502-4506.
    • (1996) Blood , vol.87 , pp. 4502-4506
    • Xu, W.1    Seiter, K.2    Feldman, E.3    Ahmed, T.4    Chiao, J.W.5
  • 19
    • 20444382410 scopus 로고    scopus 로고
    • Glucose phosphate isomerase deficiency: Enzymatic and familial characterization of Arg346His mutation
    • Repiso, A.; Oliva, B.; Vives corrons, J.L.; Carreras, J.; Climent, F. Glucose phosphate isomerase deficiency: enzymatic and familial characterization of Arg346His mutation. Biochim. Biophys. Acta, 2005, 1740, 467-471.
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 467-471
    • Repiso, A.1    Oliva, B.2    Vives corrons, J.L.3    Carreras, J.4    Climent, F.5
  • 20
    • 39049196100 scopus 로고    scopus 로고
    • Red cell glucose phosphate isomerase (GPI): A molecular study of three novel mutations associated with hereditary nonspherocytic hemolytic anemia
    • Repiso, A.; Oliva, B.; Vives Corrons, J.L.; Beutler, E.; Carreras, J.; Climent, F. Red cell glucose phosphate isomerase (GPI): a molecular study of three novel mutations associated with hereditary nonspherocytic hemolytic anemia. Hum. Mutat., 2006, 937, 27, 1159.
    • (2006) Hum. Mutat , vol.937 , Issue.27 , pp. 1159
    • Repiso, A.1    Oliva, B.2    Vives Corrons, J.L.3    Beutler, E.4    Carreras, J.5    Climent, F.6
  • 23
    • 0016714616 scopus 로고
    • Glucose phosphate isomerase deficiency with hereditary hemolytic anemia in a Spanish family: Clinical and familial studies
    • Vives-Corrons, J.L.; Rozman, C.; Kahn.; Carrera, A.; Triginer J. Glucose phosphate isomerase deficiency with hereditary hemolytic anemia in a Spanish family: clinical and familial studies. Hum. Genet., 1975, 29, 291-297.
    • (1975) Hum. Genet , vol.29 , pp. 291-297
    • Vives-Corrons, J.L.1    Rozman, C.2    Kahn3    Carrera, A.4    Triginer, J.5
  • 24
    • 0016873788 scopus 로고
    • Glucose-phosphate isomerase deficiency due to a new variant (GPI-Barcelona) and to a silent gene: Biochemical, immunological and genetic studies
    • Kahn, A.; Vives J.L.; Bertrand, O.; Cottreau, D.; Marie, J.; Boivin, P. Glucose-phosphate isomerase deficiency due to a new variant (GPI-Barcelona) and to a silent gene: biochemical, immunological and genetic studies. Clin. Chim. Acta, 1976, 66, 145-155.
    • (1976) Clin. Chim. Acta , vol.66 , pp. 145-155
    • Kahn, A.1    Vives, J.L.2    Bertrand, O.3    Cottreau, D.4    Marie, J.5    Boivin, P.6
  • 25
    • 0015024231 scopus 로고
    • Combined glucose phosphate isomerase and glucose-6-phosphate dehydrogenase deficiency of the erythrocytes: A new haemolytic syndrome
    • Schroter, W.; Brittinger, G.; Zimmerschmitt, E.; Konig, E.; Schareder, D. Combined glucose phosphate isomerase and glucose-6-phosphate dehydrogenase deficiency of the erythrocytes: a new haemolytic syndrome. Br. J. Haemat., 1971, 20, 249-261
    • (1971) Br. J. Haemat , vol.20 , pp. 249-261
    • Schroter, W.1    Brittinger, G.2    Zimmerschmitt, E.3    Konig, E.4    Schareder, D.5
  • 26
    • 0015799363 scopus 로고
    • Combined erythrocyte phosphohexose isomerase and glucose-6-phosphate dehydrogenase deficiency
    • Sanpitak, N.; Supalert, Y.; Chayutimonkul, L.; Flatz, G. Combined erythrocyte phosphohexose isomerase and glucose-6-phosphate dehydrogenase deficiency. Hum. Hered, 1973, 23, 83-87.
    • (1973) Hum. Hered , vol.23 , pp. 83-87
    • Sanpitak, N.1    Supalert, Y.2    Chayutimonkul, L.3    Flatz, G.4
  • 27
    • 0018239270 scopus 로고
    • Combined glucose phosphate isomerase and glucose-6-posphate dehydrogenase deficiency of erythrocytes
    • Steidman, I.; Kaufman, S.; Zaidman, J.L.; Laiba, H. Combined glucose phosphate isomerase and glucose-6-posphate dehydrogenase deficiency of erythrocytes. Isr. J. Med. Sci., 1978, 14, 1186-1190.
    • (1978) Isr. J. Med. Sci , vol.14 , pp. 1186-1190
    • Steidman, I.1    Kaufman, S.2    Zaidman, J.L.3    Laiba, H.4
  • 28
    • 0019475023 scopus 로고
    • Combined erythrocyte glucose phosphate isomerase (GPI) and glucose-6-posphate dehydrogenase (G6PDH) deficiency in an Italian family
    • Arnold, H.; Lohr, G.W.; Hasslinger, K.; Ludwig, R. Combined erythrocyte glucose phosphate isomerase (GPI) and glucose-6-posphate dehydrogenase (G6PDH) deficiency in an Italian family. Hum. Genet., 1981, 57, 226-229.
    • (1981) Hum. Genet , vol.57 , pp. 226-229
    • Arnold, H.1    Lohr, G.W.2    Hasslinger, K.3    Ludwig, R.4
  • 29
    • 0021885041 scopus 로고
    • Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family
    • Brown, J.R.; Daar, I.O.; Krug, J.R.; Maquat, L.E. Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family. Mol. Cell Biol., 1985, 5, 1694-1706.
    • (1985) Mol. Cell Biol , vol.5 , pp. 1694-1706
    • Brown, J.R.1    Daar, I.O.2    Krug, J.R.3    Maquat, L.E.4
  • 30
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosephosphate isomerase at 2.8A resolution. Triosephosphate isomerase-related human genetics disorders and comparison with the trypanosomal enzyme
    • Mande, S.C.; Mainfrod, V.; Kalk, K.H.; Goraj, K.; Martial, J.A.; Hol, W.G.H. Crystal structure of recombinant human triosephosphate isomerase at 2.8A resolution. Triosephosphate isomerase-related human genetics disorders and comparison with the trypanosomal enzyme. Prot. Sci., 1994, 3, 810-821.
    • (1994) Prot. Sci , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfrod, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.H.6
  • 31
    • 38849181675 scopus 로고    scopus 로고
    • Dimerization affects collective dynamics of triodephosphate ismerase
    • Cansu, S.; Doruker, P. Dimerization affects collective dynamics of triodephosphate ismerase. Biochemistry, 2008, 47, 1388-1368.
    • (2008) Biochemistry , vol.47 , pp. 1388-1368
    • Cansu, S.1    Doruker, P.2
  • 32
    • 0000790027 scopus 로고
    • Hereditary hemolytic anemia with triosephosphate isomerase deficiency
    • Sneider, A.S.; Valentine, W. N.; Hattori, M.D.; Heins, L.H. Hereditary hemolytic anemia with triosephosphate isomerase deficiency. N. Engl. J. Med., 1965, 272, 229-235.
    • (1965) N. Engl. J. Med , vol.272 , pp. 229-235
    • Sneider, A.S.1    Valentine, W.N.2    Hattori, M.D.3    Heins, L.H.4
  • 33
    • 34250165399 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: Facts and Doubts
    • Orosz, F.; Oláh, J.; Ovádi, J. Triosephosphate isomerase deficiency: Facts and Doubts. IUBMB Life, 2006, 58, 703-715.
    • (2006) IUBMB Life , vol.58 , pp. 703-715
    • Orosz, F.1    Oláh, J.2    Ovádi, J.3
  • 34
    • 0033981372 scopus 로고    scopus 로고
    • Orosz, F.; Wágner, G.; Liliom, K.; Kovács, J.; Baróti, K.; Horány M.; Farkas, T.; Hollán.S.; Ovádi, J. Enhanced association of mutant triosephosphate isomerase to red cell membranes and to brain microtubules. Proc. Natl. Acad. Sci. USA, 2000, 97, 1026-1031.
    • Orosz, F.; Wágner, G.; Liliom, K.; Kovács, J.; Baróti, K.; Horány M.; Farkas, T.; Hollán.S.; Ovádi, J. Enhanced association of mutant triosephosphate isomerase to red cell membranes and to brain microtubules. Proc. Natl. Acad. Sci. USA, 2000, 97, 1026-1031.
  • 36
    • 29644434568 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: Consequences of an inherited mutation at mRNA, protein and metabolic levels
    • Oláh, J.; Orosz, F.; Puskás, L.G.; Hackler, L.; Horány, M.; Polgár, L.; Hollán, S.; Ovádi, J. Triosephosphate isomerase deficiency: consequences of an inherited mutation at mRNA, protein and metabolic levels. Biochem. J., 2005, 392, 675-683.
    • (2005) Biochem. J , vol.392 , pp. 675-683
    • Oláh, J.1    Orosz, F.2    Puskás, L.G.3    Hackler, L.4    Horány, M.5    Polgár, L.6    Hollán, S.7    Ovádi, J.8
  • 37
    • 0034431493 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: Historical perspectives and molecular aspects
    • Schneider, A.S. Triosephosphate isomerase deficiency: historical perspectives and molecular aspects. Baillière's Clin. Haematol., 2000, 13, 119-140.
    • (2000) Baillière's Clin. Haematol , vol.13 , pp. 119-140
    • Schneider, A.S.1
  • 38
    • 0001221883 scopus 로고
    • In Triosephosphate isomerase deficiency
    • Beutler, E, Ed, City of Hope, New York, London
    • Schneider, A.S.; Dunn, I.; Weinstein, I.M. In Triosephosphate isomerase deficiency.; Beutler, E., Ed.; City of Hope Symposium Series: New York, London, 1968; Vol. 1, pp. 273-279.
    • (1968) Symposium Series , vol.1 , pp. 273-279
    • Schneider, A.S.1    Dunn, I.2    Weinstein, I.M.3
  • 40
    • 0019486967 scopus 로고
    • Origin of the triosephosphate isomerase isozymes in humans: Genetic evidence for the expression of a single structural locus
    • Decker, R.S.; Mohrenweiser, H.W. Origin of the triosephosphate isomerase isozymes in humans: genetic evidence for the expression of a single structural locus. Am. J. Hum. Gen., 1981, 33, 683-691.
    • (1981) Am. J. Hum. Gen , vol.33 , pp. 683-691
    • Decker, R.S.1    Mohrenweiser, H.W.2
  • 41
    • 0015997629 scopus 로고
    • Evidence for synteny between the human loci for triose phosphate isomerase, lactate dehydrogenase-B and peptidase-B and the regional mapping on chromosome 12 of man
    • Jongsma, A.P.M.; Los, W.R.T.; Hagemeijer, A. Evidence for synteny between the human loci for triose phosphate isomerase, lactate dehydrogenase-B and peptidase-B and the regional mapping on chromosome 12 of man. Cytogen. Cell Genet., 1974, 13, 106-107.
    • (1974) Cytogen. Cell Genet , vol.13 , pp. 106-107
    • Jongsma, A.P.M.1    Los, W.R.T.2    Hagemeijer, A.3
  • 42
    • 0016814115 scopus 로고
    • Regional mapping of TPI, LDH-B and Pep-B on chromosome 12 of man
    • Jongsma, A.P.M.; Hagemeijer, A.; Khan, P.M. Regional mapping of TPI, LDH-B and Pep-B on chromosome 12 of man. Birth Defects 1975, 11, 189-191.
    • (1975) Birth Defects , vol.11 , pp. 189-191
    • Jongsma, A.P.M.1    Hagemeijer, A.2    Khan, P.M.3
  • 43
    • 0021984052 scopus 로고
    • Human triosephosphate isomerase cDNA and protein structure: Studies of triosephosphate isomerase in man
    • Maquat, L.E.; Chilcote, R.; Ryan, P.H. Human triosephosphate isomerase cDNA and protein structure: studies of triosephosphate isomerase in man. J. Biol. Chem., 1985, 260, 3748-3753.
    • (1985) J. Biol. Chem , vol.260 , pp. 3748-3753
    • Maquat, L.E.1    Chilcote, R.2    Ryan, P.H.3
  • 44
    • 0025222846 scopus 로고
    • Minimal sequence and factor requirements for the initiation of transcription from an atypical TATA-TAA box-containing housekeeping promoter
    • Boyer, T.G.; Maquat, L.E. Minimal sequence and factor requirements for the initiation of transcription from an atypical TATA-TAA box-containing housekeeping promoter. J. Biol. Chem., 1990, 265, 20524-20532.
    • (1990) J. Biol. Chem , vol.265 , pp. 20524-20532
    • Boyer, T.G.1    Maquat, L.E.2
  • 45
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase
    • Wierenga, R.K.; Noble, M.E.M.; Davenport, R.C. Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J. Mol. Biol., 1992, 224, 1115-1126.
    • (1992) J. Mol. Biol , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.M.2    Davenport, R.C.3
  • 46
    • 55149086824 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency is caused by altered dimerization-non catalytic activity of the mutant enzyme
    • Ralser, M.; Breitenbach, M,.; Lehrach, H.; Kroitschs, S. Triosephosphate isomerase deficiency is caused by altered dimerization-non catalytic activity of the mutant enzyme. PloS One, 2006, 1, e30.
    • (2006) PloS One , vol.1
    • Ralser, M.1    Breitenbach, M.2    Lehrach, H.3    Kroitschs, S.4
  • 48
    • 0030058707 scopus 로고    scopus 로고
    • Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus
    • Watanabe, M.; Zing, B.C.; Mohrenweiser, H.W. Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus. Am. J. Hum. Genet., 1996, 58, 308-316.
    • (1996) Am. J. Hum. Genet , vol.58 , pp. 308-316
    • Watanabe, M.1    Zing, B.C.2    Mohrenweiser, H.W.3
  • 49
    • 0011245017 scopus 로고    scopus 로고
    • Hematologically important mutations: Triosephosphate isomerase
    • Sneider, A.; Cohen-Solal, M. Hematologically important mutations: triosephosphate isomerase. Blood Cells Mol. Dis., 1996, 22, 82-84.
    • (1996) Blood Cells Mol. Dis , vol.22 , pp. 82-84
    • Sneider, A.1    Cohen-Solal, M.2
  • 50
    • 0032532355 scopus 로고    scopus 로고
    • The relationship of the -5, -8 and -24 variant alleles in African Americans to triosephosphate isomerase (TPI) enzyme activity and to TPI deficiency
    • Schneider, A.; Forman, L.; Westwood, B.; Yim, C.; Lin, J.; Singh, S.; Beuler, E. The relationship of the -5, -8 and -24 variant alleles in African Americans to triosephosphate isomerase (TPI) enzyme activity and to TPI deficiency. Blood, 1998, 92, 2959-2962.
    • (1998) Blood , vol.92 , pp. 2959-2962
    • Schneider, A.1    Forman, L.2    Westwood, B.3    Yim, C.4    Lin, J.5    Singh, S.6    Beuler, E.7
  • 51
    • 0034254248 scopus 로고    scopus 로고
    • Triosephosphate isoemerase deficiency in 3 French families: Two novel null alleles, a frameshift mutation (TPI Alfortville) and an alteration in the initiation codon (TPI Paris)
    • Valentine, C.; Pissard, S.; Artin, J.; Heron, D.; Labrune, P.; Livet, M.O.; Mayer, M.; Gelbart, T.; Schneider, A.; Mav-Audit, P.; Cohen-Solal, M. Triosephosphate isoemerase deficiency in 3 French families: two novel null alleles, a frameshift mutation (TPI Alfortville) and an alteration in the initiation codon (TPI Paris). Blood, 2000, 96, 1130-1135.
    • (2000) Blood , vol.96 , pp. 1130-1135
    • Valentine, C.1    Pissard, S.2    Artin, J.3    Heron, D.4    Labrune, P.5    Livet, M.O.6    Mayer, M.7    Gelbart, T.8    Schneider, A.9    Mav-Audit, P.10    Cohen-Solal, M.11
  • 52
    • 0022996859 scopus 로고
    • Human triose-phosphate isomerase deficiency: A single aminoacid substitution results in a thermolabile enzyme
    • Daar, I.O.; Artymiuk, P.J.; Phillips, D.C.; Maquat, L.E. Human triose-phosphate isomerase deficiency: a single aminoacid substitution results in a thermolabile enzyme. Proc. Natl. Acad. Sci. USA, 1986, 83, 7903-7907.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7903-7907
    • Daar, I.O.1    Artymiuk, P.J.2    Phillips, D.C.3    Maquat, L.E.4
  • 53
  • 54
    • 33751316738 scopus 로고    scopus 로고
    • Drosophila model of human inherited triosephosphate isomerase deficiency glycolytic enzymopathy
    • Celotto, A.M.; Frank, A.C.; Seigle, J.L.; Palladino, M.J. Drosophila model of human inherited triosephosphate isomerase deficiency glycolytic enzymopathy. Genetics, 2006, 174, 1237-1246.
    • (2006) Genetics , vol.174 , pp. 1237-1246
    • Celotto, A.M.1    Frank, A.C.2    Seigle, J.L.3    Palladino, M.J.4
  • 55
    • 49849101871 scopus 로고    scopus 로고
    • Degradation of functional TPI protein underlies sugar kill pathology
    • Eagle, J.L.; Celotto, A.M.; Palladino, M. Degradation of functional TPI protein underlies sugar kill pathology. Genetics, 2008, 179, 855-862.
    • (2008) Genetics , vol.179 , pp. 855-862
    • Eagle, J.L.1    Celotto, A.M.2    Palladino, M.3
  • 56
    • 0025996530 scopus 로고
    • Structure and expression of the triosephosphate isomerase (Tpi) gene of Drosophila melanogaster
    • Shaw-Lee, R.L.; Lissemora, J.L.; Sullivan, D.T. Structure and expression of the triosephosphate isomerase (Tpi) gene of Drosophila melanogaster. Mol. Gen. Genet., 1991, 230, 225-229.
    • (1991) Mol. Gen. Genet , vol.230 , pp. 225-229
    • Shaw-Lee, R.L.1    Lissemora, J.L.2    Sullivan, D.T.3
  • 57
    • 25144522232 scopus 로고    scopus 로고
    • New haplotype for the Glu104Asp mutation in triose-phosphate isomerase deficiency and prenatal diagnosis in a Spanish family
    • Repiso, A.; Vives-Corrons, J.L.; Vulliamy, T.; Killeen, N.; Layton,.; Carreras, J.; Climent, F. New haplotype for the Glu104Asp mutation in triose-phosphate isomerase deficiency and prenatal diagnosis in a Spanish family. J. Inherit. Metab. Dis., 2005, 28, 807-809.
    • (2005) J. Inherit. Metab. Dis , vol.28 , pp. 807-809
    • Repiso, A.1    Vives-Corrons, J.L.2    Vulliamy, T.3    Killeen, N.4    Layton5    Carreras, J.6    Climent, F.7
  • 58
    • 0025101035 scopus 로고
    • Myopathy with altered mitochondria due to a triosephosphate isomerase deficiency
    • Bardosi, A.; Eber, S.W.; Hendrys, M.; Pekrun, A. Myopathy with altered mitochondria due to a triosephosphate isomerase deficiency. Acta Neuropathologica,, 1990, 79, 387-384.
    • (1990) Acta Neuropathologica , vol.79 , pp. 387-384
    • Bardosi, A.1    Eber, S.W.2    Hendrys, M.3    Pekrun, A.4
  • 59
    • 0025909126 scopus 로고
    • Triose phosphate isomerase deficiency: Haemolytic anaemia myopathy with altered mitochondria and mental retardation due to a new variant with accelerated enzyme catabolism and diminished specific activity
    • Eber, S.W.; Pekrun, A.; Bardosi, A.; Gahr, M.; Kristach, W.K.; Krüger, J.; Matthei, R.; Schröter, W. Triose phosphate isomerase deficiency: haemolytic anaemia myopathy with altered mitochondria and mental retardation due to a new variant with accelerated enzyme catabolism and diminished specific activity. Eur. J. Pediatr., 1991, 150, 761-766.
    • (1991) Eur. J. Pediatr , vol.150 , pp. 761-766
    • Eber, S.W.1    Pekrun, A.2    Bardosi, A.3    Gahr, M.4    Kristach, W.K.5    Krüger, J.6    Matthei, R.7    Schröter, W.8
  • 60
    • 0020030163 scopus 로고
    • Characterization of two new electrophoretic variants of human triose phosphate isomerase: Stability, kinetic and immunological properties
    • Asakawa, J.; Mohrenwisser, H. W. Characterization of two new electrophoretic variants of human triose phosphate isomerase: stability, kinetic and immunological properties. Biochem. Genet., 1982, 20, 5976.
    • (1982) Biochem. Genet , vol.20 , pp. 5976
    • Asakawa, J.1    Mohrenwisser, H.W.2
  • 61
    • 0026589145 scopus 로고
    • Humantriosephosphate isomerase: Substitution of Arg for Gly at position 122 in a thermolabile electrophorm variant
    • Perry, B.A.; Mohrenweisser, H.W. Humantriosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electrophorm variant. Hum. Genet., 1992, 88, 634-638.
    • (1992) Hum. Genet , vol.88 , pp. 634-638
    • Perry, B.A.1    Mohrenweisser, H.W.2
  • 62
    • 0030967792 scopus 로고    scopus 로고
    • Evidence for founder effect of the Glu104Asp substitution and identification of a new mutation in triosephosphate isomerase
    • Arya, R.; Lalloz, M.R.; Bellingham, A.J.; Layton, D.M. Evidence for founder effect of the Glu104Asp substitution and identification of a new mutation in triosephosphate isomerase. Hum. Mut., 1997, 10, 290-294.
    • (1997) Hum. Mut , vol.10 , pp. 290-294
    • Arya, R.1    Lalloz, M.R.2    Bellingham, A.J.3    Layton, D.M.4
  • 63
    • 1342324115 scopus 로고    scopus 로고
    • Chronic axonal neuropathy with triosephosphate isomerase deficiency
    • Wilmshurst, J.M.; Wise, G.A.; Pollard, J.M.; Ouvrier, R.A. Chronic axonal neuropathy with triosephosphate isomerase deficiency. Ped. Neurol., 2004, 30, 146-148.
    • (2004) Ped. Neurol , vol.30 , pp. 146-148
    • Wilmshurst, J.M.1    Wise, G.A.2    Pollard, J.M.3    Ouvrier, R.A.4
  • 64
    • 0030221532 scopus 로고    scopus 로고
    • The 1591C mutation in triosephosphate isomerase (TPI) deficiency. Tightly linked polymorphisms and a common haplotype in all known families
    • Sneider, A.; Westwood, B.; Yim, C.; Cohen-Solal, M.; Rosa, R.; Labotka, R.; Eber, S., Wolf, R.; Lammi, A.; Beutler, E. The 1591C mutation in triosephosphate isomerase (TPI) deficiency. Tightly linked polymorphisms and a common haplotype in all known families. Blood Cells Mol. Dis., 1996, 22, 115-125.
    • (1996) Blood Cells Mol. Dis , vol.22 , pp. 115-125
    • Sneider, A.1    Westwood, B.2    Yim, C.3    Cohen-Solal, M.4    Rosa, R.5    Labotka, R.6    Eber, S.7    Wolf, R.8    Lammi, A.9    Beutler, E.10
  • 65
    • 0023871662 scopus 로고
    • Premature translation mediates triosephosphate isomerase mRNA degradation
    • Daar, I.O.; Maquat, L.E. Premature translation mediates triosephosphate isomerase mRNA degradation. Mol. Cell Biol., 1988, 8, 802-813.
    • (1988) Mol. Cell Biol , vol.8 , pp. 802-813
    • Daar, I.O.1    Maquat, L.E.2
  • 66
    • 0027490726 scopus 로고
    • Hereditary triosephosphate isomerase (TPI) deficiency: Two severely affected brothers one with and one without neurological symptoms
    • Hollán, S.; Fujii, H.; Hirono, A.; Hirono, K.; Karro, H.; Miwa, S.; Harsányi, V.; Inselt-Kovács, M. Hereditary triosephosphate isomerase (TPI) deficiency: two severely affected brothers one with and one without neurological symptoms. Hum. Genet., 1993, 92, 486-490.
    • (1993) Hum. Genet , vol.92 , pp. 486-490
    • Hollán, S.1    Fujii, H.2    Hirono, A.3    Hirono, K.4    Karro, H.5    Miwa, S.6    Harsányi, V.7    Inselt-Kovács, M.8
  • 67
  • 68
    • 0032712086 scopus 로고    scopus 로고
    • Humphries, A.; Ationu, A.; Wild, Layton, D.M. The consequence of nucleotide substitutions in the triosephosphate isoemerase (TPI) gene promoter. Blood Cells Mol. Dis., 1999, 25, 210-217.
    • Humphries, A.; Ationu, A.; Wild, Layton, D.M. The consequence of nucleotide substitutions in the triosephosphate isoemerase (TPI) gene promoter. Blood Cells Mol. Dis., 1999, 25, 210-217.
  • 69
    • 0025239322 scopus 로고
    • Functional identity of a primer recognition protein as phosphoglycerate kinase
    • Jindal, H.K.; Vishwanatha, J.K.; Functional identity of a primer recognition protein as phosphoglycerate kinase. J. Biol. Chem., 1990, 265, 6540-6543.
    • (1990) J. Biol. Chem , vol.265 , pp. 6540-6543
    • Jindal, H.K.1    Vishwanatha, J.K.2
  • 70
    • 4444342914 scopus 로고    scopus 로고
    • Two proliferation-related proteins, TYMS and PGA1, could be new cytotoxic T lymphocyte-directed tumor-associated antigens of HLA-A2+ colon cancer
    • Shichijo, S.; Azuma, K.; Komatsu, N.; Ito, M.; Maeda, Y.; Ishihara, Y.; Itoh, K. Two proliferation-related proteins, TYMS and PGA1, could be new cytotoxic T lymphocyte-directed tumor-associated antigens of HLA-A2+ colon cancer. Clin. Cancer Res., 2004, 10, 5828-5436.
    • (2004) Clin. Cancer Res , vol.10 , pp. 5828-5436
    • Shichijo, S.1    Azuma, K.2    Komatsu, N.3    Ito, M.4    Maeda, Y.5    Ishihara, Y.6    Itoh, K.7
  • 71
    • 0023091937 scopus 로고
    • Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene
    • Mc Carrey, J.R.; Thomas, K. Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene. Nature, 1987, 326, 501-505.
    • (1987) Nature , vol.326 , pp. 501-505
    • Mc Carrey, J.R.1    Thomas, K.2
  • 72
    • 0017113656 scopus 로고
    • Characterization of phosphoglycerate kinase, an X-linked polymorphism in man
    • Chen, S.H.; Donahue, R.P.; Scott, C.R. Characterization of phosphoglycerate kinase, an X-linked polymorphism in man. Fertil. Steril., 1976, 27, 699-701.
    • (1976) Fertil. Steril , vol.27 , pp. 699-701
    • Chen, S.H.1    Donahue, R.P.2    Scott, C.R.3
  • 73
    • 0021838357 scopus 로고
    • The human phosphoglyerate kinase multigene family. HLA-associated sequences and an X-linked locus containing a processed pseudogene and its functional counterpart
    • Michelson, A.M.; Bruns, G.A.; Morton, C.C.; Orkin, S.H. The human phosphoglyerate kinase multigene family. HLA-associated sequences and an X-linked locus containing a processed pseudogene and its functional counterpart. J. Biol. Chem., 1985, 260, 6982-6992.
    • (1985) J. Biol. Chem , vol.260 , pp. 6982-6992
    • Michelson, A.M.1    Bruns, G.A.2    Morton, C.C.3    Orkin, S.H.4
  • 74
    • 33845499042 scopus 로고    scopus 로고
    • PGK deficiency
    • Beutler, E. PGK deficiency. Br. J. Haematol., 2007, 136, 3-11.
    • (2007) Br. J. Haematol , vol.136 , pp. 3-11
    • Beutler, E.1
  • 75
    • 12144285772 scopus 로고    scopus 로고
    • Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: Binding, kinetic and crystallographic studies with ATP and MgATP
    • Flachner, B.; Vargas, A.; Gugolya, Z.; Vonderviszt, F.; Vas, M. Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic and crystallographic studies with ATP and MgATP. Biochemistry, 2004, 43, 34-36
    • (2004) Biochemistry , vol.43 , pp. 34-36
    • Flachner, B.1    Vargas, A.2    Gugolya, Z.3    Vonderviszt, F.4    Vas, M.5
  • 77
    • 0034457289 scopus 로고    scopus 로고
    • Phosphoglycerate kinase deficiency in two brothers with McArdle-like clinical symstoms
    • Aasly, J.; van Diggelen, P.P.; Boer, A.M.; Brønstad, G. Phosphoglycerate kinase deficiency in two brothers with McArdle-like clinical symstoms. Eur. J. Neurol., 2000, 7, 111-113.
    • (2000) Eur. J. Neurol , vol.7 , pp. 111-113
    • Aasly, J.1    van Diggelen, P.P.2    Boer, A.M.3    Brønstad, G.4
  • 78
    • 35448968951 scopus 로고    scopus 로고
    • Altered expression of PGK1 in a family with phosphoglycerate kinase deficiency
    • Svaansand, E.V.; Aasly, J.; MalmLandsem, V.; Klungland, H. Altered expression of PGK1 in a family with phosphoglycerate kinase deficiency. Muscle Nerve, 2007, 36, 679-684.
    • (2007) Muscle Nerve , vol.36 , pp. 679-684
    • Svaansand, E.V.1    Aasly, J.2    MalmLandsem, V.3    Klungland, H.4
  • 81
    • 0022919709 scopus 로고
    • Bisphosphorylated metabolites of glycerate, glucose and fructose: Functions, metabolism and molecular pathology
    • Carreras J.; Bartrons, R.; Climent, F.; Cussó, R. Bisphosphorylated metabolites of glycerate, glucose and fructose: functions, metabolism and molecular pathology. Clin. Biochem., 1986, 19, 348-358.
    • (1986) Clin. Biochem , vol.19 , pp. 348-358
    • Carreras, J.1    Bartrons, R.2    Climent, F.3    Cussó, R.4
  • 83
    • 0020674545 scopus 로고
    • The complete aminoacid sequence of human erythrocyte diphosphoglycerate mutase
    • Haggarty, N.; Dunbar, B.; Fothergill, L.A. The complete aminoacid sequence of human erythrocyte diphosphoglycerate mutase. EMBO J., 1983, 2, 1213-1220.
    • (1983) EMBO J , vol.2 , pp. 1213-1220
    • Haggarty, N.1    Dunbar, B.2    Fothergill, L.A.3
  • 85
    • 0025777664 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase
    • Cherfils, J.; Rosa, R.; Garel.; Calvin.; Rosa J, Janin J. Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase. J. Mol. Biol., 1991, 218, 269-270.
    • (1991) J. Mol. Biol , vol.218 , pp. 269-270
    • Cherfils, J.1    Rosa, R.2    Garel3    Calvin4    Rosa, J.5    Janin, J.6
  • 86
    • 4644262393 scopus 로고    scopus 로고
    • Crystal structure of human bisphosphoglycerate mutase
    • Wang, Y.; Wei, Z.; Biab, Q.; Cheng, Z., Wan, M.; Liu, L.; Gong, W. Crystal structure of human bisphosphoglycerate mutase. J. Biol. Chem., 2004, 279, 39132-39138.
    • (2004) J. Biol. Chem , vol.279 , pp. 39132-39138
    • Wang, Y.1    Wei, Z.2    Biab, Q.3    Cheng, Z.4    Wan, M.5    Liu, L.6    Gong, W.7
  • 87
    • 0018249672 scopus 로고
    • The first case of a complete deficiency of diphosphoglycerate mutase in human erythrocytes
    • Rosa, R.; Prehu, M.O.; Benzard, Y.; Rosa, J. The first case of a complete deficiency of diphosphoglycerate mutase in human erythrocytes. J. Clin. Invest., 1978, 62, 907-915.
    • (1978) J. Clin. Invest , vol.62 , pp. 907-915
    • Rosa, R.1    Prehu, M.O.2    Benzard, Y.3    Rosa, J.4
  • 88
    • 3543148643 scopus 로고
    • Familial diphosphoglycerate mutase deficiency. Influence of the oxygen affinity curves of hemoglobin
    • Labie, D.; Leroux, J.P.; Najman, A.; Reyrolle, C. Familial diphosphoglycerate mutase deficiency. Influence of the oxygen affinity curves of hemoglobin. FEBS Lett. 1970, 9, 37-40.
    • (1970) FEBS Lett , vol.9 , pp. 37-40
    • Labie, D.1    Leroux, J.P.2    Najman, A.3    Reyrolle, C.4
  • 89
    • 68349091162 scopus 로고
    • Study of a kindred with red cell 2, 3-diphosphoglycerate mutase deficiency and compensated hemolysis
    • Abstract
    • Travis, S.F.; Martinez, J. Garvin, J. Study of a kindred with red cell 2, 3-diphosphoglycerate mutase deficiency and compensated hemolysis. Blood, 1976, 48, 104 (Abstract).
    • (1976) Blood , vol.48 , pp. 104
    • Travis, S.F.1    Martinez, J.2    Garvin, J.3
  • 90
    • 0024321162 scopus 로고
    • Isolation, characterization and structure of a mutant 89Arg→Cys bisphosphoglycerate mutase
    • Rosa, R.; Blouquit, Y.; Calvin, M.C.; Prome, D.; Prome, J.C. Isolation, characterization and structure of a mutant 89Arg→Cys bisphosphoglycerate mutase. J. Biol. Chem., 1989, 264, 7837-7843.
    • (1989) J. Biol. Chem , vol.264 , pp. 7837-7843
    • Rosa, R.1    Blouquit, Y.2    Calvin, M.C.3    Prome, D.4    Prome, J.C.5
  • 91
    • 0026466962 scopus 로고
    • Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency
    • Lemarchel, V.; Joulin, V.; Valentin.; Rosa, R.; Galactéros, F., Rosa, J.; Cohen-Solal, M. Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency. Blood, 1992, 80, 2643-2649.
    • (1992) Blood , vol.80 , pp. 2643-2649
    • Lemarchel, V.1    Joulin, V.2    Valentin3    Rosa, R.4    Galactéros, F.5    Rosa, J.6    Cohen-Solal, M.7
  • 92
    • 1842426964 scopus 로고    scopus 로고
    • Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency
    • Hoyer, J.D.; Allen, S.L.; Beutler, E.; Kubik, K.; West, C.; Fairbanks, V.F. Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Am. J. Hematol., 2004, 75, 2005-2008.
    • (2004) Am. J. Hematol , vol.75 , pp. 2005-2008
    • Hoyer, J.D.1    Allen, S.L.2    Beutler, E.3    Kubik, K.4    West, C.5    Fairbanks, V.F.6
  • 93
    • 0024803006 scopus 로고
    • Purification, characterization and immunological properties of 2, 3-bisphosphoglycerate-independent phosphoglycerate mutase of maize ( Zea mays) seeds
    • Graña, X.; Ureña. J.; Ludevid. D.; Carreras. J.; Climent, F. Purification, characterization and immunological properties of 2, 3-bisphosphoglycerate-independent phosphoglycerate mutase of maize ( Zea mays) seeds. Eur. J. Biochem., 1989, 186, 149-153.
    • (1989) Eur. J. Biochem , vol.186 , pp. 149-153
    • Graña, X.1    Ureña, J.2    Ludevid, D.3    Carreras, J.4    Climent, F.5
  • 95
    • 38249004373 scopus 로고
    • Phosphoglycerate mutase activity and mRNA levels during germination of maiza embryos
    • Graña, X.; Broceño, C.; Garriga, J.; Pérez de la Ossa, P.; Climent, F. Phosphoglycerate mutase activity and mRNA levels during germination of maiza embryos. Plant Sci., 1993, 89, 147-151.
    • (1993) Plant Sci , vol.89 , pp. 147-151
    • Graña, X.1    Broceño, C.2    Garriga, J.3    Pérez de la Ossa, P.4    Climent, F.5
  • 97
    • 0027955469 scopus 로고
    • The amino sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe
    • Nairn, J.; Price, N.C.; Fothergill-Gilmore, L.A.; Walker, G.E.; Fothrgill, J.E.; Dunbar, B. The amino sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe. Biochem. J., 1994, 297, 603-608.
    • (1994) Biochem. J , vol.297 , pp. 603-608
    • Nairn, J.1    Price, N.C.2    Fothergill-Gilmore, L.A.3    Walker, G.E.4    Fothrgill, J.E.5    Dunbar, B.6
  • 98
    • 0028336824 scopus 로고
    • Cloning and nucleotide sequences of the gene encoding triosephosphate isomerase, phosphoglycerate mutase and enolase from Bacillus subtilis
    • Leyva-Vazques, M.A.; Setlow, P. Cloning and nucleotide sequences of the gene encoding triosephosphate isomerase, phosphoglycerate mutase and enolase from Bacillus subtilis. J. Bacteriol., 1994, 176, 3309-3910.
    • (1994) J. Bacteriol , vol.176 , pp. 3309-3910
    • Leyva-Vazques, M.A.1    Setlow, P.2
  • 99
    • 0027990388 scopus 로고
    • Isolation and characterization of cofactor-independent phosphoglycerate mutase gene from maize
    • Pérez de la Ossa, P.; Graña, X.; Ruiz-Lozano, P.; Climent, F. Isolation and characterization of cofactor-independent phosphoglycerate mutase gene from maize. Biochem. Biophys. Res. Commun., 1994, 203, 1204-1209.
    • (1994) Biochem. Biophys. Res. Commun , vol.203 , pp. 1204-1209
    • Pérez de la Ossa, P.1    Graña, X.2    Ruiz-Lozano, P.3    Climent, F.4
  • 100
    • 0034599751 scopus 로고    scopus 로고
    • Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus
    • Jedrzejas, M.; Chander, M.; Setlow, P.; Krihnasamy, G. Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus. EMBO J. 2000, 19, 1419-1431.
    • (2000) EMBO J , vol.19 , pp. 1419-1431
    • Jedrzejas, M.1    Chander, M.2    Setlow, P.3    Krihnasamy, G.4
  • 101
    • 34447538639 scopus 로고    scopus 로고
    • Characterization of cofactor-dependent and cofactor- independent phosphoglycerate mutases from Archaea
    • Johnsen, U.; Schöuheit, P. Characterization of cofactor-dependent and cofactor- independent phosphoglycerate mutases from Archaea. Extremophiles, 2007, 11, 647-657.
    • (2007) Extremophiles , vol.11 , pp. 647-657
    • Johnsen, U.1    Schöuheit, P.2
  • 102
    • 0000694446 scopus 로고
    • Human phosphoglycerate mutase: Isozyme marker for muscle differentiation and for neoplasia
    • Market, C.L, Ed, Academic Press, New York
    • Omenn, G.G.; Hermodson, M.A. Human phosphoglycerate mutase: isozyme marker for muscle differentiation and for neoplasia. In Developmental Biology, Market, C.L., Ed.; Academic Press.; New York, 1994; Vol. III, pp. 1005-10018.
    • (1994) Developmental Biology , vol.3 , pp. 1005-10018
    • Omenn, G.G.1    Hermodson, M.A.2
  • 105
    • 0020004430 scopus 로고
    • Assignment of phosphoglycerate mutase (PGAMA) to human chromosome 10. Regional mapping of GOT1 and PGAMA to subbands 10q26.1 (or q23.3)
    • Junien, C.; Despoisse, S.; Turlean, C.; de Grouchy, J.; Bucher, T.; Fundele, R. Assignment of phosphoglycerate mutase (PGAMA) to human chromosome 10. Regional mapping of GOT1 and PGAMA to subbands 10q26.1 (or q23.3). Ann. Genet., 1982, 25, 25-27.
    • (1982) Ann. Genet , vol.25 , pp. 25-27
    • Junien, C.1    Despoisse, S.2    Turlean, C.3    de Grouchy, J.4    Bucher, T.5    Fundele, R.6
  • 106
    • 0035925059 scopus 로고    scopus 로고
    • Mouse phosphoglycerate mutase M and B isozyme: CDNA cloning, enzyme activity assay and mapping
    • Zhang, J.; Yu. L.; Quiang, F.; Gao, J.; Xie, Y.; Chen, J.; Zhang, P.; Liu. Q.; Zhao, S. Mouse phosphoglycerate mutase M and B isozyme: cDNA cloning, enzyme activity assay and mapping. Gene, 2001, 264, 273-279.
    • (2001) Gene , vol.264 , pp. 273-279
    • Zhang, J.1    Yu, L.2    Quiang, F.3    Gao, J.4    Xie, Y.5    Chen, J.6    Zhang, P.7    Liu, Q.8    Zhao, S.9
  • 107
    • 18844380675 scopus 로고    scopus 로고
    • Gong. Crystal structure of human B-type phosphoglycerate mutase bound with citrate
    • Wang. Y.; Wei. Z.; Liu, L.; Cheng. Z.; Lin, Y.; Fengyuan, J.; Gong. Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem. Biopys, Res. Commun., 2005, 331, 1207-1215.
    • (2005) Biochem. Biopys, Res. Commun , vol.331 , pp. 1207-1215
    • Wang, Y.1    Wei, Z.2    Liu, L.3    Cheng, Z.4    Lin, Y.5    Fengyuan, J.6
  • 108
    • 0019327231 scopus 로고
    • Vanadate inhibits 2, 3-bisphosphoglycerate dependent phosphoglycerate mutases but not affect the 2, 3-bisphosphoglycerate independent phosphoglycerate mutases
    • Carreras, J.; Bartons, R.; Grisolia, S. Vanadate inhibits 2, 3-bisphosphoglycerate dependent phosphoglycerate mutases but not affect the 2, 3-bisphosphoglycerate independent phosphoglycerate mutases. Biochem. Biophys. Acta, 1980, 96, 1267-1273.
    • (1980) Biochem. Biophys. Acta , vol.96 , pp. 1267-1273
    • Carreras, J.1    Bartons, R.2    Grisolia, S.3
  • 110
    • 0019843365 scopus 로고
    • Effect of vanadate on phosphoryl transfer enzymes involved in glucose metabolism
    • Climent, F.; Bartrons. R.; Pons, G.; Carreras, J. Effect of vanadate on phosphoryl transfer enzymes involved in glucose metabolism. Biochem. Biophys. Res. Commun., 1981, 101, 570-576.
    • (1981) Biochem. Biophys. Res. Commun , vol.101 , pp. 570-576
    • Climent, F.1    Bartrons, R.2    Pons, G.3    Carreras, J.4
  • 111
    • 0020491881 scopus 로고
    • Effect of vanadate on the formation and stability of the phosphoenzyme forms of 2, 3-bisphosphoglycerate-dependent phosphoglycerate mutase and of phosphoglucomutase
    • Carreras, J.; Climent, F.; Bartrons, R.; Pons, G. Effect of vanadate on the formation and stability of the phosphoenzyme forms of 2, 3-bisphosphoglycerate-dependent phosphoglycerate mutase and of phosphoglucomutase. Biochim. Biophys. Acta, 1982, 705, 238-242.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 238-242
    • Carreras, J.1    Climent, F.2    Bartrons, R.3    Pons, G.4
  • 112
    • 0028198540 scopus 로고
    • Thyroid hormone stimulates phosphoglycerate mutase activity and isozyme transition in rat muscle tissues
    • Esteller, M.; Ureña. J.; Carreras, J.; Martelly, I.; Climent, F. Thyroid hormone stimulates phosphoglycerate mutase activity and isozyme transition in rat muscle tissues. Life Sci., 1994, 59, 533-538.
    • (1994) Life Sci , vol.59 , pp. 533-538
    • Esteller, M.1    Ureña, J.2    Carreras, J.3    Martelly, I.4    Climent, F.5
  • 113
    • 0036095650 scopus 로고    scopus 로고
    • Effects of thyroid hormone on mRNA of phosphoglycerate mutase subunits in rat muscle during development
    • Gonzalez-Cinca, N.; Gonzalo, S.; Ascaso, C.; Carreras, J.; Climent F. Effects of thyroid hormone on mRNA of phosphoglycerate mutase subunits in rat muscle during development. Horm. Res., 2002, 57, 48-52.
    • (2002) Horm. Res , vol.57 , pp. 48-52
    • Gonzalez-Cinca, N.1    Gonzalo, S.2    Ascaso, C.3    Carreras, J.4    Climent, F.5
  • 114
    • 7544233138 scopus 로고    scopus 로고
    • Effects of thyroid hormone and hypoxia on 2, 3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in vivo
    • Gonzalez-Cinca N.; Pérez de la Ossa, P.; Carreras, J.; Climent, F. Effects of thyroid hormone and hypoxia on 2, 3-bisphosphoglycerate, bisphosphoglycerate synthase and phosphoglycerate mutase in rabbit erythroblasts and reticulocytes in vivo. Horm. Res., 2004, 62, 191-196.
    • (2004) Horm. Res , vol.62 , pp. 191-196
    • Gonzalez-Cinca, N.1    Pérez de la Ossa, P.2    Carreras, J.3    Climent, F.4
  • 115
    • 0346665877 scopus 로고    scopus 로고
    • Effects of hypoxia and thyroid hormone on mRNA levels and activity of phosphoglycerate mutase in rabbit tissues
    • Gonzalez-Cinca N.; Ribera, F.; Carreras, J.; Climent, F. Effects of hypoxia and thyroid hormone on mRNA levels and activity of phosphoglycerate mutase in rabbit tissues. Horm. Res., 2003, 59, 16-20.
    • (2003) Horm. Res , vol.59 , pp. 16-20
    • Gonzalez-Cinca, N.1    Ribera, F.2    Carreras, J.3    Climent, F.4
  • 116
    • 0026062558 scopus 로고
    • Thyroid hormonere gulation of gene expression
    • Brent, G.A.; Moore, D. D.; Larsen, P.R. Thyroid hormonere gulation of gene expression. Annu. Rev. Physiol., 1991, 53, 17-35.
    • (1991) Annu. Rev. Physiol , vol.53 , pp. 17-35
    • Brent, G.A.1    Moore, D.D.2    Larsen, P.R.3
  • 117
    • 0027384527 scopus 로고
    • Dominant negative activity of an endogenous thyroid receptor variant (alpha 2) is due to competition for binding sites on target tissues
    • Katz, D.; Lazar, M.H. Dominant negative activity of an endogenous thyroid receptor variant (alpha 2) is due to competition for binding sites on target tissues. J. Biol. Chem., 1993, 268, 20904-20910.
    • (1993) J. Biol. Chem , vol.268 , pp. 20904-20910
    • Katz, D.1    Lazar, M.H.2
  • 118
    • 0028782187 scopus 로고
    • Mechanism of disease: The molecular basis of thyroid hormone action
    • Brent, G.A. Mechanism of disease: The molecular basis of thyroid hormone action. N. Engl. J. Med., 1994, 331, 847-853.
    • (1994) N. Engl. J. Med , vol.331 , pp. 847-853
    • Brent, G.A.1
  • 119
    • 0002599840 scopus 로고    scopus 로고
    • DeGroot, L.U, Jameson, L.J, Eds, Saunders: Philadelphia
    • Jameson, J.L. In Endocrinology.; DeGroot, L.U.; Jameson, L.J.; Eds.; Saunders: Philadelphia, 2001.; Vol. 2, pp.1327-1344.
    • (2001) Endocrinology , vol.2 , pp. 1327-1344
    • Jameson, J.L.1
  • 120
  • 122
    • 33645112975 scopus 로고
    • Enzyme und substrate der glykolyse in isolierten zellkernen
    • Sibert, G. Enzyme und substrate der glykolyse in isolierten zellkernen. Biochem. Zeitschr. 1961, 334, 369-387.
    • (1961) Biochem. Zeitschr , vol.334 , pp. 369-387
    • Sibert, G.1
  • 123
    • 37049183458 scopus 로고
    • Human muscle phosphoglycerate mutase deficiency: Newly discovered metabolic myopathy
    • Di Mauro, S.; Miranda, A.F.; Khan, S.; Gitlin, K.; Friedman, R. Human muscle phosphoglycerate mutase deficiency: newly discovered metabolic myopathy. Science, 1981, 212, 1277-1279.
    • (1981) Science , vol.212 , pp. 1277-1279
    • Di Mauro, S.1    Miranda, A.F.2    Khan, S.3    Gitlin, K.4    Friedman, R.5
  • 125
  • 126
    • 0028218316 scopus 로고
    • Muscle phosphoglycerate mutase deficiency: A study of a family with metabolic myopathy
    • Poulton, K. R.; Khan, A. A.; Rossi, M. L.; Riddoch, D. Muscle phosphoglycerate mutase deficiency: a study of a family with metabolic myopathy. Func. Neurol., 1994, 9, 47-58.
    • (1994) Func. Neurol , vol.9 , pp. 47-58
    • Poulton, K.R.1    Khan, A.A.2    Rossi, M.L.3    Riddoch, D.4
  • 128
    • 0027495730 scopus 로고
    • The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency
    • Tsujino, S.; Shanske, S.; Sakoda, S.; Fenichel, G.; Di Mauro, S. The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency. Am. J. Hum. Genet. 1993, 52, 472-477.
    • (1993) Am. J. Hum. Genet , vol.52 , pp. 472-477
    • Tsujino, S.1    Shanske, S.2    Sakoda, S.3    Fenichel, G.4    Di Mauro, S.5
  • 129
    • 0029189757 scopus 로고
    • Molecular genetic studies in muscle phosphoglycerate mutase (PGAM) deficiency
    • Tsujino, S.; Shanske, S.; Sakoda, S.; Toscano, A.; Di Mauro, S. Molecular genetic studies in muscle phosphoglycerate mutase (PGAM) deficiency. Muscle Nerve, 1995, Suppl 3, S50-S53.
    • (1995) Muscle Nerve , Issue.SUPPL. 3
    • Tsujino, S.1    Shanske, S.2    Sakoda, S.3    Toscano, A.4    Di Mauro, S.5
  • 131
    • 0029814303 scopus 로고    scopus 로고
    • Molecular basis of muscle phosphoglycerate mutase (PGAM) deficiency in the Italian kindred
    • Toscano, A.; Tsujino, S.; Vita, G.; Shanske. S.; Messina, C.; Di Mauro, S. Molecular basis of muscle phosphoglycerate mutase (PGAM) deficiency in the Italian kindred. Muscle Nerve, 1996, 19, 1134-1137.
    • (1996) Muscle Nerve , vol.19 , pp. 1134-1137
    • Toscano, A.1    Tsujino, S.2    Vita, G.3    Shanske, S.4    Messina, C.5    Di Mauro, S.6
  • 132
    • 0030255417 scopus 로고    scopus 로고
    • Partial deficiency of phosphoglycerate mutase with diabetic polyneuropathy: The first Japanese patient
    • Kawashima, N.; Mishima. M.; Shindo, R.; Hirano, M.; Kuwabara, S.; Saitoh, H.; Miyazaki, T. Partial deficiency of phosphoglycerate mutase with diabetic polyneuropathy: the first Japanese patient. Internal. Med., 1996, 35, 799-802.
    • (1996) Internal. Med , vol.35 , pp. 799-802
    • Kawashima, N.1    Mishima, M.2    Shindo, R.3    Hirano, M.4    Kuwabara, S.5    Saitoh, H.6    Miyazaki, T.7
  • 133
    • 0032829329 scopus 로고    scopus 로고
    • Hadjigeourgiou, G.; Kawashima, N.; Bruno.C.; Andreu, A.L.; Sue, C.M.; Ridgen, D.J.; Kawashima, A.; Shanske, S.; Di Mauro, S. Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene. Neuromuscul. Dis., 1999, 9, 399-402.
    • Hadjigeourgiou, G.; Kawashima, N.; Bruno.C.; Andreu, A.L.; Sue, C.M.; Ridgen, D.J.; Kawashima, A.; Shanske, S.; Di Mauro, S. Manifesting heterozygotes in a Japanese family with a novel mutation in the muscle-specific phosphoglycerate mutase (PGAM-M) gene. Neuromuscul. Dis., 1999, 9, 399-402.
  • 134
    • 14344263143 scopus 로고    scopus 로고
    • Phosphoglycerate mutase BB isozyme deficiency in a patient with non-spherocytic anemia: Familial and metabolic studies
    • Repiso, A.; Ramirez Bajo, M.J.; Vives Corrons, J.L.; Carreras, J.; Climent, F. Phosphoglycerate mutase BB isozyme deficiency in a patient with non-spherocytic anemia: familial and metabolic studies. Haematologica, 2005, 90, 257-259.
    • (2005) Haematologica , vol.90 , pp. 257-259
    • Repiso, A.1    Ramirez Bajo, M.J.2    Vives Corrons, J.L.3    Carreras, J.4    Climent, F.5
  • 135
    • 0025047619 scopus 로고
    • Regulation of muscle phosphofructokinase by physiological concentrations of bisphosphorylated hexoses: Effect of alkalinization
    • Andrés, V.; Carreras, J.; Cussó, R. Regulation of muscle phosphofructokinase by physiological concentrations of bisphosphorylated hexoses: effect of alkalinization. Biochem. Biophys. Res. Commun., 1990, 172, 328-338.
    • (1990) Biochem. Biophys. Res. Commun , vol.172 , pp. 328-338
    • Andrés, V.1    Carreras, J.2    Cussó, R.3
  • 136
  • 138
    • 0024166362 scopus 로고
    • Human M2-type pyruvate kinase: CDNA cloning, chromosomal assignment and expression in hepatoma
    • Tani, K.; Yoshida, M.C.; Satoh, H.; Mitamura, K.; Noguchi, T.; Tanaka, T.; Fujii, H.; Miwa, S. Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene, 1988, 20, 509-516.
    • (1988) Gene , vol.20 , pp. 509-516
    • Tani, K.1    Yoshida, M.C.2    Satoh, H.3    Mitamura, K.4    Noguchi, T.5    Tanaka, T.6    Fujii, H.7    Miwa, S.8
  • 139
    • 0022930036 scopus 로고
    • The M1 and M2 type isozymes of pyruvate kinase are produced from a same gene by alternative RNA splicing
    • Noguchi, T.; Inoue, H.; Tanaka, T. The M1 and M2 type isozymes of pyruvate kinase are produced from a same gene by alternative RNA splicing. J. Biol. Chem., 1986, 261, 13807-13812.
    • (1986) J. Biol. Chem , vol.261 , pp. 13807-13812
    • Noguchi, T.1    Inoue, H.2    Tanaka, T.3
  • 140
    • 22144484881 scopus 로고    scopus 로고
    • Red cell pyruvate kinase deficiency: Molecular and clinical aspects
    • Zanella, A.; Fermo, E.; Bianchi, P.; Valentini. Red cell pyruvate kinase deficiency: molecular and clinical aspects. Br. J. Haematol., 2005, 130, 11-25.
    • (2005) Br. J. Haematol , vol.130 , pp. 11-25
    • Zanella, A.1    Fermo, E.2    Bianchi, P.3    Valentini4
  • 141
    • 0023813414 scopus 로고
    • The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21
    • Satoh, H.; Tani, K.; Yoshida, M.C.; Sasaki, M.; Miwa, S.; Fujii, H. The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21. Cytogenet. Cell Genet., 1988, 47, 132-133.
    • (1988) Cytogenet. Cell Genet , vol.47 , pp. 132-133
    • Satoh, H.1    Tani, K.2    Yoshida, M.C.3    Sasaki, M.4    Miwa, S.5    Fujii, H.6
  • 142
    • 0025824449 scopus 로고
    • cDNA cloning of human R-type pyruvate kinase and identification of a single amino-acid substitution (Thr384→Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia
    • Kanno, H.; Fujii, H.; Hirono, A.; Miwa, S. cDNA cloning of human R-type pyruvate kinase and identification of a single amino-acid substitution (Thr384→Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc. Nat. Acad Sci. USA, 1991, 88, 8218-8221.
    • (1991) Proc. Nat. Acad Sci. USA , vol.88 , pp. 8218-8221
    • Kanno, H.1    Fujii, H.2    Hirono, A.3    Miwa, S.4
  • 143
    • 0035892103 scopus 로고    scopus 로고
    • Human erythrocyte pyruvate kinase: Characterization of the recombinant enzyme and a mutant form (R510Q) causing hemolytic anemia
    • Wang, C.; Chiarelli, L.R.; Bianchi, P.; Abraham, D.J.; Galizzi, A.; Mattewi, A.; Zanella, A.; Valentine, G. Human erythrocyte pyruvate kinase: characterization of the recombinant enzyme and a mutant form (R510Q) causing hemolytic anemia. Blood, 2001, 98, 3113-3120.
    • (2001) Blood , vol.98 , pp. 3113-3120
    • Wang, C.1    Chiarelli, L.R.2    Bianchi, P.3    Abraham, D.J.4    Galizzi, A.5    Mattewi, A.6    Zanella, A.7    Valentine, G.8
  • 144
  • 146
    • 0002185739 scopus 로고
    • A specific erythrocyte glycolytic enzyme defect (pyruvate kinase) in three subjects with congenital non-specific hemolytic anemia
    • Valentine, W.N.; Tanaka, K.R.; Miwa, S. A specific erythrocyte glycolytic enzyme defect (pyruvate kinase) in three subjects with congenital non-specific hemolytic anemia. Trans. Assoc. Am. Phys., 1961, 74, 100-110.
    • (1961) Trans. Assoc. Am. Phys , vol.74 , pp. 100-110
    • Valentine, W.N.1    Tanaka, K.R.2    Miwa, S.3
  • 147
    • 0034431029 scopus 로고    scopus 로고
    • Red cell pyruvate kinase deficiency: From genetics to clinical manifestations
    • Zanella, A.; Bianchi, P. Red cell pyruvate kinase deficiency: from genetics to clinical manifestations. Baillière's Clin. Haematol., 2000, 13, 57-81.
    • (2000) Baillière's Clin. Haematol , vol.13 , pp. 57-81
    • Zanella, A.1    Bianchi, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.