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Volumn 13, Issue 10, 2012, Pages 13118-13133

Inhibition of enzyme activity of rhipicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodies

Author keywords

Glycolytic pathway; Monoclonal antibody; Rhipicephalus (Boophilus) microplus; Triosephosphate isomerase

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY BRBM37; MONOCLONAL ANTIBODY BRBM38; RECOMBINANT PROTEIN; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

EID: 84867800354     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms131013118     Document Type: Article
Times cited : (8)

References (71)
  • 1
    • 33644899658 scopus 로고    scopus 로고
    • The productivity effects of cattle tick (Boophilus microplus) infestation on cattle, with particular reference to Bos indicus cattle and their crosses
    • Jonsson, N.N. The productivity effects of cattle tick (Boophilus microplus) infestation on cattle, with particular reference to Bos indicus cattle and their crosses. Vet. Parasitol. 2006, 137, 1-10.
    • (2006) Vet. Parasitol , vol.137 , pp. 1-10
    • Jonsson, N.N.1
  • 2
    • 0020855060 scopus 로고
    • The Use of Tick transmission by Boophilus microplus to isolate pure strains of Babesia bovis, Babesia bigemina and Anaplasma marginale from cattle with mixed infections
    • Dalgliesh, R.J.; Stewart, N.P. The Use of Tick transmission by Boophilus microplus to isolate pure strains of Babesia bovis, Babesia bigemina and Anaplasma marginale from cattle with mixed infections. Vet. Parasitol. 1983, 13, 317-323.
    • (1983) Vet. Parasitol , vol.13 , pp. 317-323
    • Dalgliesh, R.J.1    Stewart, N.P.2
  • 3
    • 45549088980 scopus 로고    scopus 로고
    • Productivity and health effects of Anaplasmosis and Babesiosis on Bos indicus cattle and their crosses, and the effects of differing intensity of tick control in Australia
    • Jonsson, N.N.; Bock, R.E.; Jorgensen, W.K. Productivity and health effects of Anaplasmosis and Babesiosis on Bos indicus cattle and their crosses, and the effects of differing intensity of tick control in Australia. Vet. Parasitol. 2008, 155, 1-9.
    • (2008) Vet. Parasitol , vol.155 , pp. 1-9
    • Jonsson, N.N.1    Bock, R.E.2    Jorgensen, W.K.3
  • 4
    • 34250624492 scopus 로고    scopus 로고
    • Accumulation of acaricide resistance mechanisms in Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) populations from New Caledonia island
    • Chevillon, C.; Ducornez, S.; de Meeûs, T.; Koffi, B.B.; Gaia, H.; Delathiere, J.M.; Barre, N. Accumulation of acaricide resistance mechanisms in Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) populations from New Caledonia island. Vet. Parasitol. 2007, 147, 276-288.
    • (2007) Vet. Parasitol , vol.147 , pp. 276-288
    • Chevillon, C.1    Ducornez, S.2    de Meeûs, T.3    Koffi, B.B.4    Gaia, H.5    Delathiere, J.M.6    Barre, N.7
  • 6
    • 63449093708 scopus 로고    scopus 로고
    • Identification of a Mutation in the para sodium channel gene of the Cattle Tick Rhipicephalus (Boophilus) microplus associated with resistance to synthetic pyrethroid acaricides
    • Morgan, J.A.; Corley, S.W.; Jackson, L.A.; Lew-Tabor, A.E.; Moolhuijzen, P.M.; Jonsson, N.N. Identification of a Mutation in the para sodium channel gene of the Cattle Tick Rhipicephalus (Boophilus) microplus associated with resistance to synthetic pyrethroid acaricides. Int. J. Parasitol. 2009, 7, 775-779.
    • (2009) Int. J. Parasitol , vol.7 , pp. 775-779
    • Morgan, J.A.1    Corley, S.W.2    Jackson, L.A.3    Lew-Tabor, A.E.4    Moolhuijzen, P.M.5    Jonsson, N.N.6
  • 10
    • 77954677564 scopus 로고    scopus 로고
    • Comparative Microarray Analysis of Rhipicephalus (Boophilus) microplus Expression Profiles of Larvae Pre-Attachment and Feeding Adult Female Stages on Bos indicus and Bos taurus Cattle
    • Rodriguez-Valle, M.; Lew-Tabor, A.; Gondro, C.; Moolhuijzen, P.; Vance, M.; Guerrero, F.D.; Bellgard, M.; Jorgensen, W. Comparative Microarray Analysis of Rhipicephalus (Boophilus) microplus Expression Profiles of Larvae Pre-Attachment and Feeding Adult Female Stages on Bos indicus and Bos taurus Cattle. BMC Genomics 2010, 11, 437.
    • (2010) BMC Genomics , vol.11 , pp. 437
    • Rodriguez-Valle, M.1    Lew-Tabor, A.2    Gondro, C.3    Moolhuijzen, P.4    Vance, M.5    Guerrero, F.D.6    Bellgard, M.7    Jorgensen, W.8
  • 14
    • 0028172007 scopus 로고
    • A protective "Concealed" antigen from Boophilus microplus. Purification, localization, and possible function
    • Riding, G.A.; Jarmey, J.; McKenna, R.V.; Pearson, R.; Cobon, G.S.; Willadsen, P. A protective "Concealed" antigen from Boophilus microplus. Purification, localization, and possible function. J. Immunol. 1994, 153, 5158-5166.
    • (1994) J. Immunol , vol.153 , pp. 5158-5166
    • Riding, G.A.1    Jarmey, J.2    McKenna, R.V.3    Pearson, R.4    Cobon, G.S.5    Willadsen, P.6
  • 15
    • 0343775873 scopus 로고    scopus 로고
    • Control of Ticks Resistant to Immunization With Bm86 in Cattle Vaccinated With the Recombinant Antigen Bm95 Isolated From the Cattle Tick, Boophilus microplus
    • Garcia-Garcia, J.C.; Montero, C.; Redondo, M.; Vargas, M.; Canales, M.; Boue, O.; Rodriguez, M.; Joglar, M.; Machado, H.; Gonzalez, I.L. et al. Control of Ticks Resistant to Immunization With Bm86 in Cattle Vaccinated With the Recombinant Antigen Bm95 Isolated From the Cattle Tick, Boophilus microplus. Vaccine 2000, 18, 2275-2287.
    • (2000) Vaccine , vol.18 , pp. 2275-2287
    • Garcia-Garcia, J.C.1    Montero, C.2    Redondo, M.3    Vargas, M.4    Canales, M.5    Boue, O.6    Rodriguez, M.7    Joglar, M.8    Machado, H.9    Gonzalez, I.L.10
  • 18
    • 78650525090 scopus 로고    scopus 로고
    • Cross Immunity with Haemaphysalis longicornis Glutathione S-Transferase Reduces an Experimental Rhipicephalus (Boophilus) microplus Infestation
    • Parizi, L.F.; Utiumi, K.U.; Imamura, S.; Onuma, M.; Ohashi, K.; Masuda, A.; da Silva, V.I., Jr. Cross Immunity with Haemaphysalis longicornis Glutathione S-Transferase Reduces an Experimental Rhipicephalus (Boophilus) microplus Infestation. Exp. Parasitol. 2011, 127, 113-118.
    • (2011) Exp. Parasitol , vol.127 , pp. 113-118
    • Parizi, L.F.1    Utiumi, K.U.2    Imamura, S.3    Onuma, M.4    Ohashi, K.5    Masuda, A.6    da Silva Jr., V.I.7
  • 21
    • 0029836936 scopus 로고    scopus 로고
    • Species-Specific Inhibition of Homologous Enzymes by Modification of Nonconserved Amino Acids Residues. The Cysteine Residues of Triosephosphate Isomerase
    • Garza-Ramos, G.; Perez-Montfort, R.; Rojo-Dominguez, A.; de Gomez-Puyou, M.T.; Gomez-Puyou, A. Species-Specific Inhibition of Homologous Enzymes by Modification of Nonconserved Amino Acids Residues. The Cysteine Residues of Triosephosphate Isomerase. Eur. J. Biochem. 1996, 241, 114-120.
    • (1996) Eur. J. Biochem , vol.241 , pp. 114-120
    • Garza-Ramos, G.1    Perez-Montfort, R.2    Rojo-Dominguez, A.3    de Gomez-Puyou, M.T.4    Gomez-Puyou, A.5
  • 24
    • 0037006981 scopus 로고    scopus 로고
    • Catalysis and Stability of Triosephosphate Isomerase From Trypanosoma brucei With Different Residues at Position 14 of the Dimer Interface. Characterization of a Catalytically Competent Monomeric Enzyme
    • Hernandez-Alcantara, G.; Garza-Ramos, G.; Hernandez, G.M.; Gomez-Puyou, A.; Perez-Montfort, R. Catalysis and Stability of Triosephosphate Isomerase From Trypanosoma brucei With Different Residues at Position 14 of the Dimer Interface. Characterization of a Catalytically Competent Monomeric Enzyme. Biochemistry 2002, 41, 4230-4238.
    • (2002) Biochemistry , vol.41 , pp. 4230-4238
    • Hernandez-Alcantara, G.1    Garza-Ramos, G.2    Hernandez, G.M.3    Gomez-Puyou, A.4    Perez-Montfort, R.5
  • 26
    • 0029557025 scopus 로고
    • Using Evolutionary Changes to Achieve Species-Specific Inhibition of Enzyme Action-Studies With Triosephosphate Isomerase
    • Gomez-Puyou, A.; Saavedra-Lira, E.; Becker, I.; Zubillaga, R.A.; Rojo-Dominguez, A.; Perez-Montfort, R. Using Evolutionary Changes to Achieve Species-Specific Inhibition of Enzyme Action-Studies With Triosephosphate Isomerase. Chem. Biol. 1995, 2, 847-855.
    • (1995) Chem. Biol , vol.2 , pp. 847-855
    • Gomez-Puyou, A.1    Saavedra-Lira, E.2    Becker, I.3    Zubillaga, R.A.4    Rojo-Dominguez, A.5    Perez-Montfort, R.6
  • 27
    • 0036596660 scopus 로고    scopus 로고
    • The Protective Immunity Produced in Infected C57BL/6 Mice of a DNA Vaccine Encoding Schistosoma japonicum Chinese Strain Triose-Phosphate Isomerase
    • Zhu, Y.; Si, J.; Ham, D.A.; Yu, C.; He, W.; Hua, W.; Yin, X.; Liang, Y.; Xu, M.; Xu, R. The Protective Immunity Produced in Infected C57BL/6 Mice of a DNA Vaccine Encoding Schistosoma japonicum Chinese Strain Triose-Phosphate Isomerase. Southeast Asian J. Trop. Med. Public Health 2002, 33, 207-213.
    • (2002) Southeast Asian J. Trop. Med. Public Health , vol.33 , pp. 207-213
    • Zhu, Y.1    Si, J.2    Ham, D.A.3    Yu, C.4    He, W.5    Hua, W.6    Yin, X.7    Liang, Y.8    Xu, M.9    Xu, R.10
  • 28
    • 0242600845 scopus 로고    scopus 로고
    • A Comparative Study of Biochemical and Immunological Properties of Triosephosphate Isomerase From Taenia solium and Sus scrofa
    • Jimenez, L.; Fernandez-Velasco, D.A.; Willms, K.; Landa, A. A Comparative Study of Biochemical and Immunological Properties of Triosephosphate Isomerase From Taenia solium and Sus scrofa. J. Parasitol. 2003, 89, 209-214.
    • (2003) J. Parasitol , vol.89 , pp. 209-214
    • Jimenez, L.1    Fernandez-Velasco, D.A.2    Willms, K.3    Landa, A.4
  • 29
    • 8444239770 scopus 로고    scopus 로고
    • The Protective Immunity of a DNA Vaccine Encoding Schistosoma japonicum Chinese Strain Triose-Phosphate Isomerase in Infected BALB/C Mice
    • Zhu, Y.; Si, J.; Harn, D.A.; Yu, C.; Liang, Y.; Ren, J.; Yin, X.; He, W.; Hua, W. The Protective Immunity of a DNA Vaccine Encoding Schistosoma japonicum Chinese Strain Triose-Phosphate Isomerase in Infected BALB/C Mice. Southeast Asian J. Trop. Med. Public Health 2004, 35, 518-522.
    • (2004) Southeast Asian J. Trop. Med. Public Health , vol.35 , pp. 518-522
    • Zhu, Y.1    Si, J.2    Harn, D.A.3    Yu, C.4    Liang, Y.5    Ren, J.6    Yin, X.7    He, W.8    Hua, W.9
  • 30
    • 30144445625 scopus 로고    scopus 로고
    • Schistosoma Japonicum Triose-Phosphate Isomerase Plasmid DNA Vaccine Protects Pigs Against Challenge Infection
    • Zhu, Y.; Si, J.; Harn, D.A.; Xu, M.; Ren, J.; Yu, C.; Liang, Y.; Yin, X.; He, W.; Cao, G. Schistosoma Japonicum Triose-Phosphate Isomerase Plasmid DNA Vaccine Protects Pigs Against Challenge Infection. Parasitology 2006, 132, 67-71.
    • (2006) Parasitology , vol.132 , pp. 67-71
    • Zhu, Y.1    Si, J.2    Harn, D.A.3    Xu, M.4    Ren, J.5    Yu, C.6    Liang, Y.7    Yin, X.8    He, W.9    Cao, G.10
  • 31
    • 47149102882 scopus 로고    scopus 로고
    • Schistosoma mansoni Triose Phosphate Isomerase Peptide MAP4 Is Able to Trigger Naive Donor Immune Response Towards a Type-1 Cytokine Profile
    • Reis, E.A.; Mauadi Carmo, T.A.; Athanazio, R.; Reis, M.G.; Harn, D.A., Jr. Schistosoma mansoni Triose Phosphate Isomerase Peptide MAP4 Is Able to Trigger Naive Donor Immune Response Towards a Type-1 Cytokine Profile. Scand. J. Immunol. 2008, 68, 169-176.
    • (2008) Scand. J. Immunol , vol.68 , pp. 169-176
    • Reis, E.A.1    Mauadi, C.T.A.2    Athanazio, R.3    Reis, M.G.4    Harn Jr., D.A.5
  • 32
    • 0343442445 scopus 로고    scopus 로고
    • Cloning, Expression and Characterisation of a Recombinant Triosephosphate Isomerase From Taenia solium
    • Jimenez, L.; Vibanco-Perez, N.; Navarro, L.; Landa, A. Cloning, Expression and Characterisation of a Recombinant Triosephosphate Isomerase From Taenia solium. Int. J. Parasitol. 2000, 30, 1007-1012.
    • (2000) Int. J. Parasitol , vol.30 , pp. 1007-1012
    • Jimenez, L.1    Vibanco-Perez, N.2    Navarro, L.3    Landa, A.4
  • 34
    • 74549159066 scopus 로고    scopus 로고
    • Production and Characterization of Monoclonal Antibodies Recognizing a Common 57-KDa Antigen of Leishmania Species
    • Nejad-Moghaddam, A.; Abolhassani, M. Production and Characterization of Monoclonal Antibodies Recognizing a Common 57-KDa Antigen of Leishmania Species. Iran Biomed. J. 2009, 13, 245-251.
    • (2009) Iran Biomed. J , vol.13 , pp. 245-251
    • Nejad-Moghaddam, A.1    Abolhassani, M.2
  • 35
    • 0344837285 scopus 로고    scopus 로고
    • Passive Immunization with Monoclonal Antibodies: Effects on Haemaphysalis longicornis Tick Infestation of BALB/c Mice
    • Nakajima, M.; Yanase, H.; Iwanaga, T.; Kodama, M.; Ohashi, K.; Onuma, M. Passive Immunization with Monoclonal Antibodies: Effects on Haemaphysalis longicornis Tick Infestation of BALB/c Mice. Jpn. J. Vet. Res. 2003, 50, 157-163.
    • (2003) Jpn. J. Vet. Res , vol.50 , pp. 157-163
    • Nakajima, M.1    Yanase, H.2    Iwanaga, T.3    Kodama, M.4    Ohashi, K.5    Onuma, M.6
  • 37
    • 84859417694 scopus 로고    scopus 로고
    • A Paradigm for Enzyme-Catalyzed Proton Transfer at Carbon: Triosephosphate Isomerase
    • Richard, J.P. A Paradigm for Enzyme-Catalyzed Proton Transfer at Carbon: Triosephosphate Isomerase. Biochemistry 2012, 51, 2652-2661.
    • (2012) Biochemistry , vol.51 , pp. 2652-2661
    • Richard, J.P.1
  • 40
    • 70350455314 scopus 로고    scopus 로고
    • New Approaches Toward Anti-Rhipicephalus (Boophilus) microplus Tick Vaccine
    • Parizi, L.F.; Pohl, P.C.; Masuda, A.; Vaz Ida, S., Jr. New Approaches Toward Anti-Rhipicephalus (Boophilus) microplus Tick Vaccine. Rev. Bras. Parasitol. Vet. 2009, 18, 1-7.
    • (2009) Rev. Bras. Parasitol. Vet , vol.18 , pp. 1-7
    • Parizi, L.F.1    Pohl, P.C.2    Masuda, A.3    Vaz Jr., I.S.4
  • 41
    • 0029561993 scopus 로고
    • Spectroscopic, Calorimetric, and Kinetic Demonstration of Conformational Adaptation in Peptide-Antibody Recognition
    • Leder, L.; Berger, C.; Bornhauser, S.; Wendt, H.; Ackermann, F.; Jelesarov, I.; Bosshard, H.R. Spectroscopic, Calorimetric, and Kinetic Demonstration of Conformational Adaptation in Peptide-Antibody Recognition. Biochemistry 1995, 34, 16509-16518.
    • (1995) Biochemistry , vol.34 , pp. 16509-16518
    • Leder, L.1    Berger, C.2    Bornhauser, S.3    Wendt, H.4    Ackermann, F.5    Jelesarov, I.6    Bosshard, H.R.7
  • 42
    • 0032530246 scopus 로고    scopus 로고
    • Thermodynamics and Kinetics of the Reaction of a Single-Chain Antibody Fragment (ScFv) With the Leucine Zipper Domain of Transcription Factor GCN4
    • Weber-Bornhauser, S.; Eggenberger, J.; Jelesarov, I.; Bernard, A.; Berger, C.; Bosshard, H.R. Thermodynamics and Kinetics of the Reaction of a Single-Chain Antibody Fragment (ScFv) With the Leucine Zipper Domain of Transcription Factor GCN4. Biochemistry 1998, 37, 13011-13020.
    • (1998) Biochemistry , vol.37 , pp. 13011-13020
    • Weber-Bornhauser, S.1    Eggenberger, J.2    Jelesarov, I.3    Bernard, A.4    Berger, C.5    Bosshard, H.R.6
  • 43
    • 67449093446 scopus 로고    scopus 로고
    • Structural and Functional Analysis of a C3b-Specific Antibody That Selectively Inhibits the Alternative Pathway of Complement
    • Katschke, K.J., Jr.; Stawicki, S.; Yin, J.; Steffek, M.; Xi, H.; Sturgeon, L.; Hass, P.E.; Loyet, K.M.; Deforge, L.; Wu, Y. et al. Structural and Functional Analysis of a C3b-Specific Antibody That Selectively Inhibits the Alternative Pathway of Complement. J. Biol. Chem. 2009, 284, 10473-10479.
    • (2009) J. Biol. Chem , vol.284 , pp. 10473-10479
    • Katschke Jr., K.J.1    Stawicki, S.2    Yin, J.3    Steffek, M.4    Xi, H.5    Sturgeon, L.6    Hass, P.E.7    Loyet, K.M.8    Deforge, L.9    Wu, Y.10
  • 44
    • 0020071879 scopus 로고
    • Monoclonal Antibodies That Inhibit Enzyme Activity of 3-Methylcholanthrene-Induced Cytochrome P-450
    • Park, S.S.; Fujino, T.; West, D.; Guengerich, F.P.; Gelboin, H.V. Monoclonal Antibodies That Inhibit Enzyme Activity of 3-Methylcholanthrene-Induced Cytochrome P-450. Cancer Res. 1982, 42, 1798-1808.
    • (1982) Cancer Res , vol.42 , pp. 1798-1808
    • Park, S.S.1    Fujino, T.2    West, D.3    Guengerich, F.P.4    Gelboin, H.V.5
  • 45
    • 0020038791 scopus 로고
    • Monoclonal Antibodies to Rabbit Liver Cytochrome P-450LM2 and Cytochrome P-450LM4
    • Park, S.S.; Cha, S.J.; Miller, H.; Persson, A.V.; Coon, M.J.; Gelboin, H.V. Monoclonal Antibodies to Rabbit Liver Cytochrome P-450LM2 and Cytochrome P-450LM4. Mol. Pharmacol. 1982, 21, 248-258.
    • (1982) Mol. Pharmacol , vol.21 , pp. 248-258
    • Park, S.S.1    Cha, S.J.2    Miller, H.3    Persson, A.V.4    Coon, M.J.5    Gelboin, H.V.6
  • 46
    • 0021753962 scopus 로고
    • Structural and Functional Influence of Enzyme-Antibody Interactions: Effects of Eight Different Monoclonal Antibodies on the Enzymatic Activity of Escherichia coli Tryptophan Synthase
    • Djavadi-Ohaniance, L.; Friguet, B.; Goldberg, M.E. Structural and Functional Influence of Enzyme-Antibody Interactions: Effects of Eight Different Monoclonal Antibodies on the Enzymatic Activity of Escherichia coli Tryptophan Synthase. Biochemistry 1984, 23, 97-104.
    • (1984) Biochemistry , vol.23 , pp. 97-104
    • Djavadi-Ohaniance, L.1    Friguet, B.2    Goldberg, M.E.3
  • 47
    • 0025758158 scopus 로고
    • Peptide/Antibody Recognition: Synthetic Peptides Derived From the E. Coli Tryptophan Synthase Beta 2 Subunit Interact With High Affinity With an Anti-Beta 2 Monoclonal Antibody
    • Larvor, M.P.; Djavadi-Ohaniance, L.; Friguet, B.; Baleux, F.; Goldberg, M.E. Peptide/Antibody Recognition: Synthetic Peptides Derived From the E. Coli Tryptophan Synthase Beta 2 Subunit Interact With High Affinity With an Anti-Beta 2 Monoclonal Antibody. Mol. Immunol. 1991, 28, 523-531.
    • (1991) Mol. Immunol , vol.28 , pp. 523-531
    • Larvor, M.P.1    Djavadi-Ohaniance, L.2    Friguet, B.3    Baleux, F.4    Goldberg, M.E.5
  • 48
    • 0016812692 scopus 로고
    • Mechanism by Which Antibodies Inhibit Hapten-Malate Dehydrogenase Conjugates. An Enzyme Immunoassay for Morphine
    • Rowley, G.L.; Rubenstein, K.E.; Huisjen, J.; Ullman, E.F. Mechanism by Which Antibodies Inhibit Hapten-Malate Dehydrogenase Conjugates. An Enzyme Immunoassay for Morphine. J. Biol. Chem. 1975, 250, 3759-3766.
    • (1975) J. Biol. Chem , vol.250 , pp. 3759-3766
    • Rowley, G.L.1    Rubenstein, K.E.2    Huisjen, J.3    Ullman, E.F.4
  • 49
    • 0014030812 scopus 로고
    • Antibody to Lactate Dehydrogenase. I. Inhibition of Glycolysis in Tumor and Liver Homogenates
    • Gregory, K.F.; Ng, C.W.; Pantekoek, J.F. Antibody to Lactate Dehydrogenase. I. Inhibition of Glycolysis in Tumor and Liver Homogenates. Biochim. Biophys. Acta 1966, 130, 469-476.
    • (1966) Biochim. Biophys. Acta , vol.130 , pp. 469-476
    • Gregory, K.F.1    Ng, C.W.2    Pantekoek, J.F.3
  • 51
    • 0342502243 scopus 로고    scopus 로고
    • Simulation of Control Strategies for the Cattle Tick Boophilus microplus Employing Vaccination With a Recombinant Bm86 Antigen Preparation
    • Labarta, V.; Rodriguez, M.; Penichet, M.; Lleonart, R.; Luaces, L.L.; de la, F.J. Simulation of Control Strategies for the Cattle Tick Boophilus microplus Employing Vaccination With a Recombinant Bm86 Antigen Preparation. Vet. Parasitol. 1996, 63, 131-160.
    • (1996) Vet. Parasitol , vol.63 , pp. 131-160
    • Labarta, V.1    Rodriguez, M.2    Penichet, M.3    Lleonart, R.4    Luaces, L.L.5    de la, F.J.6
  • 53
    • 0029258664 scopus 로고
    • Schistosomiasis Vaccine Development: Approaches and Prospects
    • Bergquist, N.R. Schistosomiasis Vaccine Development: Approaches and Prospects. Mem. Inst. Oswaldo Cruz 1995, 90, 221-227.
    • (1995) Mem. Inst. Oswaldo Cruz , vol.90 , pp. 221-227
    • Bergquist, N.R.1
  • 55
    • 78149471547 scopus 로고    scopus 로고
    • Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: Potential role of Cdk2
    • Lee, W.H.; Choi, J.S.; Byun, M.R.; Koo, K.T.; Shin, S.; Lee, S.K.; Surh, Y.J. Functional inactivation of triosephosphate isomerase through phosphorylation during etoposide-induced apoptosis in HeLa cells: Potential role of Cdk2. Toxicology 2010, 278, 224-228.
    • (2010) Toxicology , vol.278 , pp. 224-228
    • Lee, W.H.1    Choi, J.S.2    Byun, M.R.3    Koo, K.T.4    Shin, S.5    Lee, S.K.6    Surh, Y.J.7
  • 56
    • 0034730527 scopus 로고    scopus 로고
    • Caspase 3-mediated cleavage of P21WAF1/CIP1 associated with the cyclin A-cyclin-dependent kinase 2 complex is a prerequisite for apoptosis in SK-HEP-1 cells
    • Jin, Y.H.; Yoo, K.J.; Lee, Y.H.; Lee, S.K. Caspase 3-mediated cleavage of P21WAF1/CIP1 associated with the cyclin A-cyclin-dependent kinase 2 complex is a prerequisite for apoptosis in SK-HEP-1 cells. J. Biol. Chem. 2000, 275, 30256-30263.
    • (2000) J. Biol. Chem , vol.275 , pp. 30256-30263
    • Jin, Y.H.1    Yoo, K.J.2    Lee, Y.H.3    Lee, S.K.4
  • 57
    • 0038581046 scopus 로고    scopus 로고
    • Cdk2 Activity is associated with depolarization of mitochondrial membrane potential during apoptosis
    • Jin, Y.H.; Yim, H.; Park, J.H.; Lee, S.K. Cdk2 Activity is associated with depolarization of mitochondrial membrane potential during apoptosis. Biochem. Biophys. Res. Commun. 2003, 305, 974-980.
    • (2003) Biochem. Biophys. Res. Commun , vol.305 , pp. 974-980
    • Jin, Y.H.1    Yim, H.2    Park, J.H.3    Lee, S.K.4
  • 59
    • 0018867679 scopus 로고
    • The effect of methyl glyoxal on cell Division and the synthesis of protein and DNA in synchronous and asynchronous Cultures of Escherichia coli B/r
    • Fraval, H.N.; McBrien, D.C. The effect of methyl glyoxal on cell Division and the synthesis of protein and DNA in synchronous and asynchronous Cultures of Escherichia coli B/r. J. Gen. Microbiol. 1980, 117, 127-134.
    • (1980) J. Gen. Microbiol , vol.117 , pp. 127-134
    • Fraval, H.N.1    McBrien, D.C.2
  • 60
    • 31044442243 scopus 로고    scopus 로고
    • Methylglyoxal comes of AGE
    • Ramasamy, R.; Yan, S.F.; Schmidt, A.M. Methylglyoxal comes of AGE. Cell 2006, 124, 258-260.
    • (2006) Cell , vol.124 , pp. 258-260
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 61
    • 31944446983 scopus 로고    scopus 로고
    • The glycolytic enzymes, glyceraldehyde- 3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function
    • Dhar-Chowdhury, P.; Harrell, M.D.; Han, S.Y.; Jankowska, D.; Parachuru, L.; Morrissey, A.; Srivastava, S.; Liu, W.; Malester, B.; Yoshida, H. et al. The glycolytic enzymes, glyceraldehyde- 3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function. J. Biol. Chem. 2005, 280, 38464-38470.
    • (2005) J. Biol. Chem , vol.280 , pp. 38464-38470
    • Dhar-Chowdhury, P.1    Harrell, M.D.2    Han, S.Y.3    Jankowska, D.4    Parachuru, L.5    Morrissey, A.6    Srivastava, S.7    Liu, W.8    Malester, B.9    Yoshida, H.10
  • 62
    • 0028302859 scopus 로고
    • Serum of Boophilus microplus infested cattle reacts with different tick tissues
    • Da Silva, V.I., Jr.; Ozaki, L.S.; Masuda, A. Serum of Boophilus microplus infested cattle reacts with different tick tissues. Vet. Parasitol. 1994, 52, 71-78.
    • (1994) Vet. Parasitol , vol.52 , pp. 71-78
    • da Silva Jr., V.I.1    Ozaki, L.S.2    Masuda, A.3
  • 63
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 64
    • 0016756272 scopus 로고
    • Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity
    • Kohler, G.; Milstein, C. Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity. Nature 1975, 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 65
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Harlow, E.; Lane, D. Antibodies: A Laboratory Manual; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 1988, p. 123.
    • (1988) Antibodies: A Laboratory Manual , pp. 123
    • Harlow, E.1    Lane, D.2
  • 66
    • 0027234980 scopus 로고
    • Identification of a Fifth Neutralizable Site on Type O Foot-and-Mouth Disease Virus Following Characterization of Single and Quintuple Monoclonal Antibody Escape Mutants
    • Crowther, J.R.; Farias, S.; Carpenter, W.C.; Samuel, A.R. Identification of a Fifth Neutralizable Site on Type O Foot-and-Mouth Disease Virus Following Characterization of Single and Quintuple Monoclonal Antibody Escape Mutants. J. Gen. Virol. 1993, 74, 1547-1553.
    • (1993) J. Gen. Virol , vol.74 , pp. 1547-1553
    • Crowther, J.R.1    Farias, S.2    Carpenter, W.C.3    Samuel, A.R.4
  • 67
    • 0022553775 scopus 로고
    • Effects of the Modification of Transfer Buffer Composition and the Renaturation of Proteins in Gels on the Recognition of Proteins on Western Blots by Monoclonal Antibodies
    • Dunn, S.D. Effects of the Modification of Transfer Buffer Composition and the Renaturation of Proteins in Gels on the Recognition of Proteins on Western Blots by Monoclonal Antibodies. Anal. Biochem. 1986, 157, 144-153.
    • (1986) Anal. Biochem , vol.157 , pp. 144-153
    • Dunn, S.D.1
  • 68
    • 0009482260 scopus 로고
    • Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets: Procedure and Some Applications
    • Towbin, H.; Staehelin, T.; Gordon, J. Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets: Procedure and Some Applications. Proc. Natl. Acad. Sci. USA 1979, 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 69
    • 0019551730 scopus 로고
    • Western Blotting: Electrophoretic Transfer of Proteins From Sodium Dodecyl Sulfate--Polyacrylamide Gels to Unmodified Nitrocellulose and Radiographic Detection With Antibody and Radioiodinated Protein A
    • Burnette, W.N. "Western Blotting": Electrophoretic Transfer of Proteins From Sodium Dodecyl Sulfate--Polyacrylamide Gels to Unmodified Nitrocellulose and Radiographic Detection With Antibody and Radioiodinated Protein A. Anal. Biochem. 1981, 112, 195-203.
    • (1981) Anal. Biochem , vol.112 , pp. 195-203
    • Burnette, W.N.1


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