메뉴 건너뛰기




Volumn 11, Issue 6, 2010, Pages 693-700

Molecular recognition mechanisms for detecting cell death in vivo

Author keywords

Apoptosis; Imaging; Necrosis; Probe

Indexed keywords

CASPASE; CASPASE 10; CASPASE 2; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; COMPLEMENT COMPONENT C2A; LANCOVUTIDE; LANTHIOPEPTIN; LIPOCORTIN 5; MEMBRANE PHOSPHOLIPID; METHYLMALONIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; SYNAPTOTAGMIN I; BIOLOGICAL MARKER; DIAGNOSTIC AGENT;

EID: 79952115191     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/138920110792246591     Document Type: Review
Times cited : (3)

References (87)
  • 1
    • 0033429233 scopus 로고    scopus 로고
    • Death by design: Mechanism and control of apoptosis
    • Song, Z.; Steller, H. Death by design: mechanism and control of apoptosis. Trends Cell Biol., 1999, 9. M49-52.
    • (1999) Trends Cell Biol. , vol.9
    • Song, Z.1    Steller, H.2
  • 2
    • 0030829777 scopus 로고
    • Apoptosis: An overview
    • Wyllie, A.H. Apoptosis: an overview. Br. Med. Bull., 1972, 53. 451-465.
    • (1972) Br. Med. Bull. , vol.53 , pp. 451-465
    • Wyllie, A.H.1
  • 3
    • 0015383455 scopus 로고    scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F.; Wyllie, A.H.; Currie, A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 1997, 26. 239-257.
    • (1997) Br. J. Cancer. , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 4
    • 0034522342 scopus 로고    scopus 로고
    • Caspases: Key players in programmed cell death
    • Grutter, M.G. Caspases: key players in programmed cell death. Curr. Opin. Struct. Biol., 2000, 10. 649-655.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 649-655
    • Grutter, M.G.1
  • 5
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • Green, D.R. Apoptotic pathways: the roads to ruin. Cell. 1998, 94. 695-698.
    • (1998) Cell. , vol.94 , pp. 695-698
    • Green, D.R.1
  • 6
    • 0017256034 scopus 로고
    • Radionuclide methods in the evaluation of myocardial ischemia and infarction
    • Holman, B.L. Radionuclide methods in the evaluation of myocardial ischemia and infarction. Circulation. 1976, 53(3 Suppl I1), 12-119.
    • (1976) Circulation. , vol.53 , Issue.3 SUPPL I1 , pp. 12-119
    • Holman, B.L.1
  • 8
    • 0026564326 scopus 로고
    • Comparison of technetium-99m-glucarate and thallium-201 for the identification of acute myocardial infarction in rats
    • Ohtani, H.; Callahan, R.J.; Khaw, B.A.; Fishman, A.J.; Wilkinson, R.A.; Strauss, H.W. Comparison of technetium-99m-glucarate and thallium-201 for the identification of acute myocardial infarction in rats. J. Nucl. Med., 1992, 33. 1988-1993.
    • (1992) J. Nucl. Med. , vol.33 , pp. 1988-1993
    • Ohtani, H.1    Callahan, R.J.2    Khaw, B.A.3    Fishman, A.J.4    Wilkinson, R.A.5    Strauss, H.W.6
  • 10
    • 0020638868 scopus 로고
    • Relation of immediate and delayed thallium-201 distribution to localization of iodine-125 antimyosin antibody in acute experimental myocardial infarction
    • Khaw, B.A.; Strauss, H.W.; Pohost, G.M.; Fallon, J.T.; Katus, H.A.; Haber, E. Relation of immediate and delayed thallium-201 distribution to localization of iodine-125 antimyosin antibody in acute experimental myocardial infarction. Am. J. Cardiol., 1983, 51. 1428-32.
    • (1983) Am. J. Cardiol. , vol.51 , pp. 1428-1432
    • Khaw, B.A.1    Strauss, H.W.2    Pohost, G.M.3    Fallon, J.T.4    Katus, H.A.5    Haber, E.6
  • 12
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A.; Lazebnik, Y. Caspases: enemies within. Science, 1998, 281. 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 13
    • 0029859388 scopus 로고    scopus 로고
    • Granzyme B-induced apoptosis
    • Greenberg, A.H. Granzyme B-induced apoptosis. Adv. Exp. Med. Biol., 1996, 406. 219-228.
    • (1996) Adv. Exp. Med. Biol. , vol.406 , pp. 219-228
    • Greenberg, A.H.1
  • 15
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ., 1999, 6. 1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 16
  • 17
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases
    • Margolin, N.; Raybuck, S.A.; Wilson, K.P.; Chen, W.; Fox, T.; Gu, Y.; Livingston, D.J. Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. J. Biol. Chem., 1997, 272. 7223-7228.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7223-7228
    • Margolin, N.1    Raybuck, S.A.2    Wilson, K.P.3    Chen, W.4    Fox, T.5    Gu, Y.6    Livingston, D.J.7
  • 19
    • 0033777736 scopus 로고    scopus 로고
    • Development and application of a GFP-FRET intracellular caspase assay for drug screening
    • Jones, J.; Heim, R.; Hare, E.; Stack, J.; Pollok, B.A. Development and application of a GFP-FRET intracellular caspase assay for drug screening. J. Biomol. Screen., 2000, 5. 307-318.
    • (2000) J. Biomol. Screen. , vol.5 , pp. 307-318
    • Jones, J.1    Heim, R.2    Hare, E.3    Stack, J.4    Pollok, B.A.5
  • 20
    • 0035122528 scopus 로고    scopus 로고
    • Imaging FRET between spectrally similar GFP molecules in single cells
    • Harpur, A.G.; Wouters, F.S.; Bastiaens, P.I. Imaging FRET between spectrally similar GFP molecules in single cells. Nat. Biotechnol., 2001, 19, 167-169.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 167-169
    • Harpur, A.G.1    Wouters, F.S.2    Bastiaens, P.I.3
  • 21
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A.W.; Daugherty, P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol., 2005, 23. 355-360.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 22
    • 0034801529 scopus 로고    scopus 로고
    • Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells
    • Luo, K.Q.; Yu, V.C.; Pu, Y.; Chang, D.C. Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells. Biochem. Biophys. Res. Commun., 2001, 283, 1054-1060.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 1054-1060
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 23
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3
    • Rehm, M.; Dussmann, H.; Janicke, R.U.; Tavare, J.M.; Kogel. D.; Prehn, J.H. Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem., 2002, 277. 24506-24514.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavare, J.M.4    Kogel, D.5    Prehn, J.H.6
  • 24
    • 0037069360 scopus 로고    scopus 로고
    • Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation
    • Onuki, R.; Nagasaki, A.; Kawasaki, H.; Baba, T.; Uyeda, T.Q.; Taira, K. Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation. Proc. Natl. Acad. Sci. USA, 2002, 99, 14716-14721.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14716-14721
    • Onuki, R.1    Nagasaki, A.2    Kawasaki, H.3    Baba, T.4    Uyeda, T.Q.5    Taira, K.6
  • 25
    • 0037414451 scopus 로고    scopus 로고
    • Measuring dynamics of caspase-8 activation in a single living HeLa cell during TNFalphainduced apoptosis
    • Luo, K.Q.; Yu, V.C.; Pu, Y.; Chang, D.C. Measuring dynamics of caspase-8 activation in a single living HeLa cell during TNFalphainduced apoptosis. Biochem. Biophys. Res. Commun., 2003, 304. 217-222.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 217-222
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 26
  • 27
    • 77149159480 scopus 로고    scopus 로고
    • Intravital Imaging of tumor apoptosis with FRET probes during tumor therapy
    • Zhou. F.; Xing, D.; Wu, S.; Chen, W.R. Intravital Imaging of tumor apoptosis with FRET probes during tumor therapy. Mol. Imaging Biol., 2010, 12. 63-70.
    • (2010) Mol. Imaging Biol. , vol.12 , pp. 63-70
    • Zhou, F.1    Xing, D.2    Wu, S.3    Chen, W.R.4
  • 28
    • 64649101405 scopus 로고    scopus 로고
    • Activatable molecular systems using homologous near-infrared fluorescent probes for monitoring enzyme activities in vitro. in cellulo, and in vivo
    • Zhang, Z.; Fan, J.; Cheney, P.P.; Berezin, M.Y.; Edwards, W.B.; Akers, W.J.; Shen, D.; Liang, K.; Culver, J.P.; Achilefu, S. Activatable molecular systems using homologous near-infrared fluorescent probes for monitoring enzyme activities in vitro. in cellulo, and in vivo. Mol. Pharm., 2009, 6. 416-427.
    • (2009) Mol. Pharm. , vol.6 , pp. 416-427
    • Zhang, Z.1    Fan, J.2    Cheney, P.P.3    Berezin, M.Y.4    Edwards, W.B.5    Akers, W.J.6    Shen, D.7    Liang, K.8    Culver, J.P.9    Achilefu, S.10
  • 29
    • 73449109886 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy of chemotherapyinduced apoptosis resistance in a syngenic mouse tumor model
    • Keese, M.; Yagublu, V.; Schwenke, K.; Post, S.; Bastiaens, P. Fluorescence lifetime imaging microscopy of chemotherapyinduced apoptosis resistance in a syngenic mouse tumor model. Int. J. Cancer. 2010, 126. 104-113.
    • (2010) Int. J. Cancer. , vol.126 , pp. 104-113
    • Keese, M.1    Yagublu, V.2    Schwenke, K.3    Post, S.4    Bastiaens, P.5
  • 31
    • 66749110952 scopus 로고    scopus 로고
    • [18F]-and [11C]-labeled N-benzyl-isatin sulfonamide analogues as PET tracers for apoptosis: Synthesis, radiolabeling mechanism, and in vivo imaging study of apoptosis in Fas-treated mice using [11C]WC-98
    • Zhou, D.; Chu, W.; Chen, D.L.; Wang, Q.; Reichert, D.E.; Rothfuss, J.; D'Avignon, A.; Welch, M.J.; Mach, R.H. [18F]-and [11C]-labeled N-benzyl-isatin sulfonamide analogues as PET tracers for apoptosis: synthesis, radiolabeling mechanism, and in vivo imaging study of apoptosis in Fas-treated mice using [11C]WC-98. Org. Biomol. Chem., 2009, 7. 1337-1348.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 1337-1348
    • Zhou, D.1    Chu, W.2    Chen, D.L.3    Wang, Q.4    Reichert, D.E.5    Rothfuss, J.6    D'Avignon, A.7    Welch, M.J.8    Mach, R.H.9
  • 32
    • 34249719936 scopus 로고    scopus 로고
    • The nonpeptidyl caspase binding radioligand (S)-1-(4-(2-[18F] Fluoroethoxy)-benzyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl] isatin ([18F]CbR) as potential positron emission tomographycompatible apoptosis imaging agent
    • Faust, A.; Wagner, S.; Law, M.P.; Hermann, S.; Schnöckel, U.; Keul, P.; Schober, O.; Schäfers, M.; Levkau, B.; Kopka K. The nonpeptidyl caspase binding radioligand (S)-1-(4-(2-18F Fluoroethoxy)-benzyl)-5-1-(2-methoxymethylpyrrolidinyl)sulfonyl isatin ([18F]CbR) as potential positron emission tomographycompatible apoptosis imaging agent. Q. J. Nucl. Med. Mol. Imaging, 2007, 51. 67-73.
    • (2007) Q. J. Nucl. Med. Mol. Imaging , vol.51 , pp. 67-73
    • Faust, A.1    Wagner, S.2    Law, M.P.3    Hermann, S.4    Schnöckel, U.5    Keul, P.6    Schober, O.7    Schäfers, M.8    Levkau, B.9    Kopka, K.10
  • 33
    • 66749129069 scopus 로고    scopus 로고
    • Fluorinated isatin derivatives. Part 2 New N-substituted 5-pyrrolidinylsulfonyl isatins as potential tools for molecular imaging of caspases in apoptosis
    • Podichetty, A.K.; Wagner, S.; Schröer, S.; Faust, A.; Schäfers, M.; Schober, O.; Kopka, K.; Haufe, G. Fluorinated isatin derivatives. Part 2. New N-substituted 5-pyrrolidinylsulfonyl isatins as potential tools for molecular imaging of caspases in apoptosis. J. Med. Chem. 2009, 52. 3484-3495.
    • (2009) J. Med. Chem. , vol.52 , pp. 3484-3495
    • Podichetty, A.K.1    Wagner, S.2    Schröer, S.3    Faust, A.4    Schäfers, M.5    Schober, O.6    Kopka, K.7    Haufe, G.8
  • 34
    • 58149090677 scopus 로고    scopus 로고
    • Design, synthesis, and biological characterization of a caspase 3/7 selective isatin labeled with 2-[18F]fluoroethylazide
    • Smith, G.; Glaser, M.; Perumal, M.; Nguyen, Q.D.; Shan, B.; Arstad, E.; Aboagye, E.O. Design, synthesis, and biological characterization of a caspase 3/7 selective isatin labeled with 2-[18F]fluoroethylazide. J. Med. Chem., 2008, 51. 8057-8067.
    • (2008) J. Med. Chem. , vol.51 , pp. 8057-8067
    • Smith, G.1    Glaser, M.2    Perumal, M.3    Nguyen, Q.D.4    Shan, B.5    Arstad, E.6    Aboagye, E.O.7
  • 35
    • 70449521080 scopus 로고    scopus 로고
    • Synthesis of carbon-11-labeled 4-aryl-4H-chromens as new PET agents for imaging of apoptosis in cancer
    • Gao, M.; Wang, M.; Miller, K.D.; Hutchins, G.D.; Zheng, Q.H. Synthesis of carbon-11-labeled 4-aryl-4H-chromens as new PET agents for imaging of apoptosis in cancer. Appl. Radiat. Isot. 2010, 68. 110-611.
    • (2010) Appl. Radiat. Isot. , vol.68 , pp. 110-611
    • Gao, M.1    Wang, M.2    Miller, K.D.3    Hutchins, G.D.4    Zheng, Q.H.5
  • 36
    • 70349481530 scopus 로고    scopus 로고
    • Positron emission tomography imaging of druginduced tumor apoptosis with a caspase-3/7 specific [18F]-labeled isatin sulfonamide
    • Nguyen, Q.D.; Smith, G.; Glaser, M.; Perumal, M.; Arstad, E.; Aboagye, E.O. Positron emission tomography imaging of druginduced tumor apoptosis with a caspase-3/7 specific [18F]-labeled isatin sulfonamide. Proc. Natl. Acad. Sci. USA, 2009, 106. 16375-80.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16375-16380
    • Nguyen, Q.D.1    Smith, G.2    Glaser, M.3    Perumal, M.4    Arstad, E.5    Aboagye, E.O.6
  • 38
    • 0029852111 scopus 로고    scopus 로고
    • Regulatory mechanisms in maintenance and modulation of transmembrane lipid asymmetry: Pathophysiological implications
    • Bevers, E.M.; Comfurius, P.; Zwaal, R.F. Regulatory mechanisms in maintenance and modulation of transmembrane lipid asymmetry: pathophysiological implications. Lupus. 1996, 5. 480-487.
    • (1996) Lupus. , vol.5 , pp. 480-487
    • Bevers, E.M.1    Comfurius, P.2    Zwaal, R.F.3
  • 40
    • 0031711701 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution in blood cells: Control mechanisms and pathophysiological significance
    • Bevers, E.M.; Comfurius, P.; Dekkers, D.W.; Harmsma, M.; Zwaal RF. Transmembrane phospholipid distribution in blood cells: control mechanisms and pathophysiological significance. Biol. Chem., 1998, 379, 973-986.
    • (1998) Biol. Chem. , vol.379 , pp. 973-986
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.3    Harmsma, M.4    Zwaal, R.F.5
  • 41
    • 66649138898 scopus 로고    scopus 로고
    • Membranedependent interaction of factor Xa and prothrombin with factor Va in the prothrombinase complex
    • Qureshi, S.H.; Yang, L.; Manithody, C.; Rezaie, A.R. Membranedependent interaction of factor Xa and prothrombin with factor Va in the prothrombinase complex. Biochemistry. 2009, 48. 5034-5041.
    • (2009) Biochemistry. , vol.48 , pp. 5034-5041
    • Qureshi, S.H.1    Yang, L.2    Manithody, C.3    Rezaie, A.R.4
  • 43
    • 0023821297 scopus 로고    scopus 로고
    • The determination of a calcium-dependent binding constant of the bovine prothrombin Gla domain (residues 1-45) to phospholipid vesicles
    • Weber, D.J.; Pollock, J.S.; Pedersen, L.G.; Hiskey, R.G. The determination of a calcium-dependent binding constant of the bovine prothrombin Gla domain (residues 1-45) to phospholipid vesicles. Biochem. Biophys. Res. Commun., 1998, 155. 230-235.
    • (1998) Biochem. Biophys. Res. Commun. , vol.155 , pp. 230-235
    • Weber, D.J.1    Pollock, J.S.2    Pedersen, L.G.3    Hiskey, R.G.4
  • 45
    • 0037203341 scopus 로고    scopus 로고
    • Transbilayer phospholipid movement and the clearance of apoptotic cells
    • Williamson, P.; Schlegel, R.A. Transbilayer phospholipid movement and the clearance of apoptotic cells. Biochim. Biophys. Acta., 2002, 1585. 53-63.
    • (2002) Biochim. Biophys. Acta. , vol.1585 , pp. 53-63
    • Williamson, P.1    Schlegel, R.A.2
  • 48
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber, R.; Römisch, J.; Paques, E.P. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J., 1990, 9, 3867-3874.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Römisch, J.2    Paques, E.P.3
  • 49
    • 0028631772 scopus 로고
    • Two-dimensional structure of membrane-bound annexin V at 8 A resolution
    • Olofsson, A.; Mallouh, V.; Brisson, A. Two-dimensional structure of membrane-bound annexin V at 8 A resolution. J. Struct. Biol., 1994, 113. 199-205.
    • (1994) J. Struct. Biol. , vol.113 , pp. 199-205
    • Olofsson, A.1    Mallouh, V.2    Brisson, A.3
  • 50
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber, R.; Berendes, R.; Burger, A.; Schneider, M.; Karshikov, A.; Luecke, H.; Römisch, J.; Paques, E. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J. Mol. Biol., 1992, 223, 683-704.
    • (1992) J. Mol. Biol. , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6    Römisch, J.7    Paques, E.8
  • 51
    • 4644314042 scopus 로고    scopus 로고
    • Essential role of B-helix calcium binding sites in annexin V-membrane binding
    • Jin, M.; Smith, C.; Hsieh, H.Y.; Gibson, D.F.; Tait, J.F. Essential role of B-helix calcium binding sites in annexin V-membrane binding. J. Biol. Chem., 2004, 279. 40351-40357.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40351-40357
    • Jin, M.1    Smith, C.2    Hsieh, H.Y.3    Gibson, D.F.4    Tait, J.F.5
  • 60
    • 0036740090 scopus 로고    scopus 로고
    • Development of annexin V mutants suitable for labeling with Tc(i)-carbonyl complex
    • Tait, J.F.; Smith, C.; Gibson, D.F. Development of annexin V mutants suitable for labeling with Tc(i)-carbonyl complex. Bioconjug. Chem., 2002, 13, 1119-1123.
    • (2002) Bioconjug. Chem. , vol.13 , pp. 1119-1123
    • Tait, J.F.1    Smith, C.2    Gibson, D.F.3
  • 61
    • 34248224235 scopus 로고    scopus 로고
    • The role of synaptotagmin I C2A calcium-binding domain in synaptic vesicle clustering during synapse formation
    • Gardzinski, P.; Lee, D.W.; Fei, G.H.; Hui, K.; Huang, G.J.; Sun, H.S.; Feng, Z.P. The role of synaptotagmin I C2A calcium-binding domain in synaptic vesicle clustering during synapse formation. J. Physiol., 2007, 581. 75-90.
    • (2007) J. Physiol. , vol.581 , pp. 75-90
    • Gardzinski, P.1    Lee, D.W.2    Fei, G.H.3    Hui, K.4    Huang, G.J.5    Sun, H.S.6    Feng, Z.P.7
  • 62
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang, X.; Rizo, J.; Südhof, T.C. Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry. 1998, 37. 12395.
    • (1998) Biochemistry. , vol.37 , pp. 12395
    • Zhang, X.1    Rizo, J.2    Südhof, T.C.3
  • 63
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold
    • Sutton, R.B.; Davletov, B.A.; Berghuis, A.M.; Südhof, T.C.; Sprang, S.R. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell, 1995, 80. 929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 64
    • 0027332736 scopus 로고
    • A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding
    • Davletov, B.A.; Südhof, T.C. A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. J. Biol. Chem., 1993, 268. 26386-26390.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26386-26390
    • Davletov, B.A.1    Südhof, T.C.2
  • 65
    • 4644246936 scopus 로고    scopus 로고
    • Detection of apoptosis using the C2A domain of synaptotagmin I
    • Jung, H.I.; Kettunen, M.I.; Davletov, B.; Brindle, K.M. Detection of apoptosis using the C2A domain of synaptotagmin I. Bioconjug. Chem., 2004, 15, 983-987.
    • (2004) Bioconjug. Chem. , vol.15 , pp. 983-987
    • Jung, H.I.1    Kettunen, M.I.2    Davletov, B.3    Brindle, K.M.4
  • 66
    • 0035173736 scopus 로고    scopus 로고
    • Non-invasive detection of apoptosis using magnetic resonance imaging and a targeted contrast agent
    • Zhao, M.; Beauregard, D.A.; Loizou, L.; Davletov, B.; Brindle, K.M. Non-invasive detection of apoptosis using magnetic resonance imaging and a targeted contrast agent. Nat. Med., 2001, 7. 1241-1244.
    • (2001) Nat. Med. , vol.7 , pp. 1241-1244
    • Zhao, M.1    Beauregard, D.A.2    Loizou, L.3    Davletov, B.4    Brindle, K.M.5
  • 67
    • 33749049365 scopus 로고    scopus 로고
    • 99mTc-labeled C2A domain of synaptotagmin I as a target-specific molecular probe for noninvasive imaging of acute myocardial infarction
    • 99mTc-labeled C2A domain of synaptotagmin I as a target-specific molecular probe for noninvasive imaging of acute myocardial infarction. J. Nucl. Med., 2006, 47, 1367-1374.
    • (2006) J. Nucl. Med. , vol.47 , pp. 1367-1374
    • Zhao, M.1    Zhu, X.2    Ji, S.3    Zhou, J.4    Ozker, K.S.5    Fang, W.6    Molthen, R.C.7    Hellman, R.S.8
  • 68
    • 35848938700 scopus 로고    scopus 로고
    • In vivo dynamic imaging of myocardial cell death using 99mTc-labeled C2A domain of synaptotagmin I in a rat model of ischemia and reperfusion
    • Liu, Z.; Zhao, M.; Zhu, X.; Furenlid, L.R.; Chen, Y.C.; Barrett, H.H. In vivo dynamic imaging of myocardial cell death using 99mTc-labeled C2A domain of synaptotagmin I in a rat model of ischemia and reperfusion. Nucl. Med. Biol., 2007, 34. 907-915.
    • (2007) Nucl. Med. Biol. , vol.34 , pp. 907-915
    • Liu, Z.1    Zhao, M.2    Zhu, X.3    Furenlid, L.R.4    Chen, Y.C.5    Barrett, H.H.6
  • 69
    • 40949121437 scopus 로고    scopus 로고
    • Detection of cell death in tumors by using MR imaging and a gadolinium-based targeted contrast agent
    • Krishnan, A.S.; Neves, A.A.; de Backer, M.M.; Hu, D.E.; Davletov, B.; Kettunen, M.I.; Brindle, K.M. Detection of cell death in tumors by using MR imaging and a gadolinium-based targeted contrast agent. Radiology, 2008, 246. 854-862.
    • (2008) Radiology , vol.246 , pp. 854-862
    • Krishnan, A.S.1    Neves, A.A.2    de Backer, M.M.3    Hu, D.E.4    Davletov, B.5    Kettunen, M.I.6    Brindle, K.M.7
  • 70
    • 0027972573 scopus 로고
    • Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C
    • Smirnov, M.D.; Esmon, C.T. Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C. J. Biol. Chem., 1994, 269. 816-819.
    • (1994) J. Biol. Chem. , vol.269 , pp. 816-819
    • Smirnov, M.D.1    Esmon, C.T.2
  • 71
    • 0028804699 scopus 로고
    • On the role of phosphatidylethanolamine in the inhibition of activated protein C activity by antiphospholipid antibodies
    • Smirnov, M.D.; Triplett, D.T.; Comp, P.C.; Esmon, N.L.; Esmon, C.T. On the role of phosphatidylethanolamine in the inhibition of activated protein C activity by antiphospholipid antibodies. J. Clin. Invest., 1995, 95. 309-316.
    • (1995) J. Clin. Invest. , vol.95 , pp. 309-316
    • Smirnov, M.D.1    Triplett, D.T.2    Comp, P.C.3    Esmon, N.L.4    Esmon, C.T.5
  • 72
    • 0032502796 scopus 로고    scopus 로고
    • A chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity
    • Smirnov, M.D.; Safa, O.; Regan, L.; Mather, T.; Stearns-Kurosawa, D.J.; Kurosawa, S.; Rezaie, A.R.; Esmon, N.L.; Esmon, CT. A chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity. J. Biol. Chem., 1998, 273. 9031-9040.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9031-9040
    • Smirnov, M.D.1    Safa, O.2    Regan, L.3    Mather, T.4    Stearns-Kurosawa, D.J.5    Kurosawa, S.6    Rezaie, A.R.7    Esmon, N.L.8    Esmon, C.T.9
  • 73
    • 0028884030 scopus 로고
    • Phosphatidylethanolamine augments factor VIIa-tissue factor activity: Enhancement of sensitivity to phosphatidylserine
    • Neuenschwander, P.F.; Bianco-Fisher, E.; Rezaie, A.R.; Morrissey, J.H. Phosphatidylethanolamine augments factor VIIa-tissue factor activity: enhancement of sensitivity to phosphatidylserine. Biochemistry, 1995, 34. 13988-13993.
    • (1995) Biochemistry , vol.34 , pp. 13988-13993
    • Neuenschwander, P.F.1    Bianco-Fisher, E.2    Rezaie, A.R.3    Morrissey, J.H.4
  • 74
    • 57749169060 scopus 로고    scopus 로고
    • Phosphatidylethanolamine at the endothelial surface of aortic flow dividers
    • Li, Z.; Wells, C.W.; Esmon, C.T.; Zhao, M. Phosphatidylethanolamine at the endothelial surface of aortic flow dividers. J. Thromb. Haemost. 2009, 7. 227-229.
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 227-229
    • Li, Z.1    Wells, C.W.2    Esmon, C.T.3    Zhao, M.4
  • 75
    • 77953285949 scopus 로고    scopus 로고
    • Phosphatidylethanolamine at the luminal endothelial surface: Implications in Hemostasis and thrombotic autoimmunity
    • Nov 10
    • Li, Z.; Wells, C.W.; North, P.E.; Kumar, S.; Duris, C.B.; McIntyre, J.A.; Zhao M. Phosphatidylethanolamine at the luminal endothelial surface: Implications in Hemostasis and thrombotic autoimmunity. Clin. Appl. Thromb. Hemost., 2009 Nov 10.
    • (2009) Clin. Appl. Thromb. Hemost.
    • Li, Z.1    Wells, C.W.2    North, P.E.3    Kumar, S.4    Duris, C.B.5    McIntyre, J.A.6    Zhao, M.7
  • 78
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig, J. Thermodynamics of lipid-peptide interactions. Biochim Biophys Acta. 2004, 1666. 40-50.
    • (2004) Biochim Biophys Acta. , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 79
  • 80
    • 0037065703 scopus 로고    scopus 로고
    • Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine: A thermodynamic analysis
    • Machaidze, G.; Ziegler, A. and Seelig, J. Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine: a thermodynamic analysis. Biochemistry. 2002, 41. 1965-1971.
    • (2002) Biochemistry. , vol.41 , pp. 1965-1971
    • McHaidze, G.1    Ziegler, A.2    Seelig, J.3
  • 81
    • 0030041310 scopus 로고    scopus 로고
    • Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1
    • Hosoda, K.; Ohya, M.; Kohno, T.; Maeda, T.; Endo, S.; Wakamatsu, K. Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1. J. Biochem., 1996, 119. 226-230.
    • (1996) J. Biochem. , vol.119 , pp. 226-230
    • Hosoda, K.1    Ohya, M.2    Kohno, T.3    Maeda, T.4    Endo, S.5    Wakamatsu, K.6
  • 82
    • 0242286671 scopus 로고    scopus 로고
    • Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine. Comparison between micellar and membrane environments
    • Machaidze, G.; Seelig, J. Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine. Comparison between micellar and membrane environments. Biochemistry. 2003, 42. 12570-12576.
    • (2003) Biochemistry. , vol.42 , pp. 12570-12576
    • McHaidze, G.1    Seelig, J.2
  • 83
    • 0025169916 scopus 로고
    • Complex formation of peptide antibiotic Ro09-0198 with lysophosphatidylethanolamine: 1H NMR analyses in dimethyl sulfoxide solution
    • Wakamatsu, K.; Choung, S.Y.; Kobayashi, T.; Inoue, K.; Higashijima, T.; Miyazawa, T. Complex formation of peptide antibiotic Ro09-0198 with lysophosphatidylethanolamine: 1H NMR analyses in dimethyl sulfoxide solution. Biochemistry. 1990, 29. 113-118.
    • (1990) Biochemistry. , vol.29 , pp. 113-118
    • Wakamatsu, K.1    Choung, S.Y.2    Kobayashi, T.3    Inoue, K.4    Higashijima, T.5    Miyazawa, T.6
  • 84
    • 48749103305 scopus 로고    scopus 로고
    • 99mTc-labeled duramycin as a novel phosphatidylethanolamine-binding molecular probe
    • 99mTc-labeled duramycin as a novel phosphatidylethanolamine-binding molecular probe. J. Nucl. Med., 2008, 49. 1345-1352.
    • (2008) J. Nucl. Med. , vol.49 , pp. 1345-1352
    • Zhao, M.1    Li, Z.2    Bugenhagen, S.3
  • 85
    • 67649109027 scopus 로고    scopus 로고
    • From the Gla domain to a novel small-molecule detector of apoptosis
    • Cohen, A.; Shirvan, A.; Levin, G.; Grimberg, H.; Reshef, A.; Ziv, I. From the Gla domain to a novel small-molecule detector of apoptosis. Cell Res., 2009, 19. 625-637.
    • (2009) Cell Res. , vol.19 , pp. 625-637
    • Cohen, A.1    Shirvan, A.2    Levin, G.3    Grimberg, H.4    Reshef, A.5    Ziv, I.6
  • 86
    • 60649115423 scopus 로고    scopus 로고
    • Monitoring of tumor response to chemotherapy in vivo by a novel small-molecule detector of apoptosis
    • Grimberg, H,; Levin, G.; Shirvan, A.; Cohen, A.; Yogev-Falach, M.; Reshef, A.; Ziv, I. Monitoring of tumor response to chemotherapy in vivo by a novel small-molecule detector of apoptosis. Apoptosis. 2009, 14. 257-267.
    • (2009) Apoptosis. , vol.14 , pp. 257-267
    • Grimberg, H.1    Levin, G.2    Shirvan, A.3    Cohen, A.4    Yogev-Falach, M.5    Reshef, A.6    Ziv, I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.