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Volumn 20, Issue 6, 2005, Pages 374-381

Ecto-ADP-ribose transferases: Cell-surface response to local tissue injury

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 29144526631     PISSN: 15489213     EISSN: None     Source Type: Journal    
DOI: 10.1152/physiol.00028.2005     Document Type: Review
Times cited : (36)

References (106)
  • 1
    • 0034945603 scopus 로고    scopus 로고
    • Changing patterns of cell surface mono (ADP-ribosyl) transferase antigen ART2.2 on resting versus cytopathically-activated T cells in NOD/Lt mice
    • Ablamunits V, Bridgett M, Duffy T, Haag F, Nissen M, Koch-Nolte F, and Leiter H. Changing patterns of cell surface mono (ADP-ribosyl) transferase antigen ART2.2 on resting versus cytopathically-activated T cells in NOD/Lt mice. Diabetologia 44: 848-858, 2001.
    • (2001) Diabetologia , vol.44 , pp. 848-858
    • Ablamunits, V.1    Bridgett, M.2    Duffy, T.3    Haag, F.4    Nissen, M.5    Koch-Nolte, F.6    Leiter, H.7
  • 2
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili D and Arden KC. FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 117: 421-426, 2004.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 3
    • 0035400028 scopus 로고    scopus 로고
    • Rapid induction of naive T cell apoptosis by ecto-nicotinamide adenine dinucleotide: Requirement for mono(ADP-ribosyl)transferase 2 and a downstream effector
    • Adriouch S, Ohlrogge W, Haag F, Koch-Nolte F, and Seman M. Rapid induction of naive T cell apoptosis by ecto-nicotinamide adenine dinucleotide: requirement for mono(ADP-ribosyl)transferase 2 and a downstream effector. J Immunol 167: 196-203, 2001.
    • (2001) J Immunol , vol.167 , pp. 196-203
    • Adriouch, S.1    Ohlrogge, W.2    Haag, F.3    Koch-Nolte, F.4    Seman, M.5
  • 4
    • 0030802038 scopus 로고    scopus 로고
    • Rho proteins: Targets for bacterial toxins
    • Aktories K. Rho proteins: targets for bacterial toxins. Trends Microbiol 5: 282-288, 1997.
    • (1997) Trends Microbiol , vol.5 , pp. 282-288
    • Aktories, K.1
  • 6
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal D and Campbell KP. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol 14: 206-213, 2004.
    • (2004) Trends Cell Biol , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 7
    • 0028858576 scopus 로고
    • 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J Biol Chem 270: 25570-25577, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 9
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD(P)
    • Berger F, Ramirez-Hernandez MH, and Ziegler M. The new life of a centenarian: signalling functions of NAD(P). Trends Biochem Sci 29: 111-118, 2004.
    • (2004) Trends Biochem Sci , vol.29 , pp. 111-118
    • Berger, F.1    Ramirez-Hernandez, M.H.2    Ziegler, M.3
  • 10
    • 0035337703 scopus 로고    scopus 로고
    • 1 integrin signals secondary myofiber formation
    • 1 integrin signals secondary myofiber formation. Dev Biol 233:148-160, 2001.
    • (2001) Dev Biol , vol.233 , pp. 148-160
    • Blanco-Bose, W.E.1    Blau, H.M.2
  • 11
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G and Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem 73: 417-435, 2004.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 12
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone L and Guarente L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat Rev Mol Cell Biol 6: 298-305, 2005.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 15
    • 0038367667 scopus 로고    scopus 로고
    • Permeability of C2C12 myotube membranes is influenced by stretch velocity
    • Burkholder TJ. Permeability of C2C12 myotube membranes is influenced by stretch velocity. Biochem Biophys Res Commun 305: 266-270, 2003.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 266-270
    • Burkholder, T.J.1
  • 16
    • 0032588041 scopus 로고    scopus 로고
    • 1 integrin in muscle development and disease
    • 1 integrin in muscle development and disease. Cell Tissue Res 296: 183-190, 1999.
    • (1999) Cell Tissue Res , vol.296 , pp. 183-190
    • Burkin, D.J.1    Kaufman, S.J.2
  • 17
    • 11144231268 scopus 로고    scopus 로고
    • 1 integrin maintains muscle integrity, increases regenerative capacity, promotes hypertrophy, and reduces cardiomyopathy in dystrophic mice
    • 1 integrin maintains muscle integrity, increases regenerative capacity, promotes hypertrophy, and reduces cardiomyopathy in dystrophic mice. Am J Pathol 166: 253-263, 2005.
    • (2005) Am J Pathol , vol.166 , pp. 253-263
    • Burkin, D.J.1    Wallace, G.Q.2    Milner, D.J.3    Chaney, E.J.4    Mulligan, J.A.5    Kaufman, S.J.6
  • 19
    • 9644270706 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation and aging
    • Burkle A, Beneke S, and Muiras ML. Poly(ADP-ribosyl)ation and aging. Exp Gerontol 39: 1599-1601, 2004.
    • (2004) Exp Gerontol , vol.39 , pp. 1599-1601
    • Burkle, A.1    Beneke, S.2    Muiras, M.L.3
  • 20
    • 0029052618 scopus 로고
    • Contraction-induced cell wounding and release of fibroblast growth factor in heart
    • Clarke MS, Caldwell RW, Chiao H, Miyake K, and McNeil PL. Contraction-induced cell wounding and release of fibroblast growth factor in heart. Circ Res 76: 927-934, 1995.
    • (1995) Circ Res , vol.76 , pp. 927-934
    • Clarke, M.S.1    Caldwell, R.W.2    Chiao, H.3    Miyake, K.4    McNeil, P.L.5
  • 23
  • 24
    • 0037881920 scopus 로고    scopus 로고
    • Functional aspects of protein mono-ADP-ribosylation
    • Corda D and Di Girolamo M. Functional aspects of protein mono-ADP-ribosylation. EMBO J 22: 1953-1958, 2003.
    • (2003) EMBO J , vol.22 , pp. 1953-1958
    • Corda, D.1    Di Girolamo, M.2
  • 25
    • 0042427273 scopus 로고    scopus 로고
    • Repairing the tears: Dysferlin in muscle membrane repair
    • Doherty KR and McNally EM. Repairing the tears: dysferlin in muscle membrane repair. Trends Mol Med 9: 327-330, 2003.
    • (2003) Trends Mol Med , vol.9 , pp. 327-330
    • Doherty, K.R.1    McNally, E.M.2
  • 26
    • 0029996048 scopus 로고    scopus 로고
    • Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes
    • Donnelly LE, Rendell NB, Murray S, Allport JR, Lo G, Kefalas P, Taylor GW, and MacDermot J. Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leucocytes. Biochem J 315: 635-641, 1996.
    • (1996) Biochem J , vol.315 , pp. 635-641
    • Donnelly, L.E.1    Rendell, N.B.2    Murray, S.3    Allport, J.R.4    Lo, G.5    Kefalas, P.6    Taylor, G.W.7    MacDermot, J.8
  • 27
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM and Campbell KP. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 809-823, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 29
    • 0142057431 scopus 로고    scopus 로고
    • Mechanical stretch to neurons results in a strain rate and magnitude-dependent increase in plasma membrane permeability
    • Geddes DM, Cargill RS 2nd, and LaPlaca MC. Mechanical stretch to neurons results in a strain rate and magnitude-dependent increase in plasma membrane permeability. J Neurotrauma 20: 1039-1049, 2003.
    • (2003) J Neurotrauma , vol.20 , pp. 1039-1049
    • Geddes, D.M.1    Cargill II, R.S.2    LaPlaca, M.C.3
  • 30
    • 0035913724 scopus 로고    scopus 로고
    • Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP- ribosyl)transferase ART5
    • Glowacki G, Braren R, Cetkovic-Cvrlje M, Leiter EH, Haag F, and Koch-Nolte F. Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP- ribosyl)transferase ART5. Gene 275: 267-277, 2001.
    • (2001) Gene , vol.275 , pp. 267-277
    • Glowacki, G.1    Braren, R.2    Cetkovic-Cvrlje, M.3    Leiter, E.H.4    Haag, F.5    Koch-Nolte, F.6
  • 34
    • 5444266511 scopus 로고    scopus 로고
    • Regulation of integrin functions by N-glycans
    • Gu J and Taniguchi N. Regulation of integrin functions by N-glycans. Glycoconj J 21: 9-15, 2004.
    • (2004) Glycoconj J , vol.21 , pp. 9-15
    • Gu, J.1    Taniguchi, N.2
  • 35
    • 0041829981 scopus 로고    scopus 로고
    • T cells of different developmental stages differ in sensitivity to apoptosis induced by extracellular NAD
    • Haag F, Freese D, Scheublein F, Ohlrogge W, Adriouch S, Seman M, and Koch-Nolte F. T cells of different developmental stages differ in sensitivity to apoptosis induced by extracellular NAD. Dev Immunol 9: 197-202, 2002.
    • (2002) Dev Immunol , vol.9 , pp. 197-202
    • Haag, F.1    Freese, D.2    Scheublein, F.3    Ohlrogge, W.4    Adriouch, S.5    Seman, M.6    Koch-Nolte, F.7
  • 36
    • 0027960632 scopus 로고
    • Premature stop codons inactivate the RT6 genes of the human and chimpanzee species
    • Haag F, Koch-Nolte F, Kuhl M, Lorenzen S, and Thiele HG. Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. J Mol Biol 243: 537-546, 1994.
    • (1994) J Mol Biol , vol.243 , pp. 537-546
    • Haag, F.1    Koch-Nolte, F.2    Kuhl, M.3    Lorenzen, S.4    Thiele, H.G.5
  • 37
    • 0036205065 scopus 로고    scopus 로고
    • Evans blue dye as an in vivo marker of myofibre damage: Optimising parameters for detecting initial myofibre membrane permeability
    • Hamer PW, McGeachie JM, Davies MJ, and Grounds MD. Evans blue dye as an in vivo marker of myofibre damage: optimising parameters for detecting initial myofibre membrane permeability. J Anat 200: 69-79, 2002.
    • (2002) J Anat , vol.200 , pp. 69-79
    • Hamer, P.W.1    McGeachie, J.M.2    Davies, M.J.3    Grounds, M.D.4
  • 40
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman EP, Brown RH Jr, and Kunkel LM. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 51: 919-928, 1987.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown Jr., R.H.2    Kunkel, L.M.3
  • 42
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 110: 673-687, 2002.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 44
    • 0030908945 scopus 로고    scopus 로고
    • Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
    • Jones EM and Baird A. Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase. Biochem J 323: 173-177, 1997.
    • (1997) Biochem J , vol.323 , pp. 173-177
    • Jones, E.M.1    Baird, A.2
  • 45
    • 0032524894 scopus 로고    scopus 로고
    • Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria
    • Jorcke D, Ziegler M, Herrero-Yraola A, and Schweiger M. Enzymic, cysteine-specific ADP-ribosylation in bovine liver mitochondria. Biochem J 332: 189-193, 1998.
    • (1998) Biochem J , vol.332 , pp. 189-193
    • Jorcke, D.1    Ziegler, M.2    Herrero-Yraola, A.3    Schweiger, M.4
  • 46
    • 0025915586 scopus 로고
    • Bacterial ADP-ribosylating toxins: Molecular structures and signal transducing functions
    • Kato I. Bacterial ADP-ribosylating toxins: molecular structures and signal transducing functions. Microbiol Immunol 35: 349-359, 1991.
    • (1991) Microbiol Immunol , vol.35 , pp. 349-359
    • Kato, I.1
  • 48
    • 0027180293 scopus 로고
    • Purification and characterization of NAD glycohydrolase from rabbit erythrocytes
    • Kim UH, Kim MK, Kim JS, Han MK, Park BH, and Kim HR. Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch Biochem Biophys 305: 147-152, 1993.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 147-152
    • Kim, U.H.1    Kim, M.K.2    Kim, J.S.3    Han, M.K.4    Park, B.H.5    Kim, H.R.6
  • 49
  • 50
    • 0025020302 scopus 로고
    • Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol- linked surface marker of postthymic T cells
    • Koch F, Haag F, Kashan A, and Thiele HG. Primary structure of rat RT6.2, a nonglycosylated phosphatidylinositol-linked surface marker of postthymic T cells. Proc Natl Acad Sci USA 87: 964-967, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 964-967
    • Koch, F.1    Haag, F.2    Kashan, A.3    Thiele, H.G.4
  • 51
    • 0029980483 scopus 로고    scopus 로고
    • Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins
    • Koch-Nolte F, Petersen D, Balasubramanian S, Haag F, Kahlke D, Willer T, Kastelein R, Bazan F, and Thiele HG. Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J Biol Chem 271: 7686-7693, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 7686-7693
    • Koch-Nolte, F.1    Petersen, D.2    Balasubramanian, S.3    Haag, F.4    Kahlke, D.5    Willer, T.6    Kastelein, R.7    Bazan, F.8    Thiele, H.G.9
  • 53
    • 0347915657 scopus 로고    scopus 로고
    • Loss of dystrophin causes aberrant mechanotransduction in skeletal muscle fibers
    • Kumar A, Khandelwal N, Malya R, Reid MB, and Boriek AM. Loss of dystrophin causes aberrant mechanotransduction in skeletal muscle fibers. FASEB J 18: 102-113, 2004.
    • (2004) FASEB J , vol.18 , pp. 102-113
    • Kumar, A.1    Khandelwal, N.2    Malya, R.3    Reid, M.B.4    Boriek, A.M.5
  • 54
    • 0026057333 scopus 로고
    • Determination of the kinetic mechanism of arginine-specific ADP-ribosyltransferases using a high performance liquid chromatographic assay
    • Larew JS, Peterson JE, and Graves DJ. Determination of the kinetic mechanism of arginine-specific ADP-ribosyltransferases using a high performance liquid chromatographic assay. J Biol Chem 266: 52-57, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 52-57
    • Larew, J.S.1    Peterson, J.E.2    Graves, D.J.3
  • 55
    • 0030882314 scopus 로고    scopus 로고
    • Direct demonstration of mechanically induced release of cellular DTP and its implication for uridine nucleotide receptor activation
    • Lazarowski ER, Homolya L, Boucher RC, and Harden TK. Direct demonstration of mechanically induced release of cellular DTP and its implication for uridine nucleotide receptor activation. J Biol Chem 272: 24348-24354, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 24348-24354
    • Lazarowski, E.R.1    Homolya, L.2    Boucher, R.C.3    Harden, T.K.4
  • 56
    • 0034996586 scopus 로고    scopus 로고
    • The best defense is a good offense - Salmonella deploys an ADP-ribosylating toxin
    • Lesnick ML and Guiney DG. The best defense is a good offense - Salmonella deploys an ADP-ribosylating toxin. Trends Microbiol 9: 2-4, 2001.
    • (2001) Trends Microbiol , vol.9 , pp. 2-4
    • Lesnick, M.L.1    Guiney, D.G.2
  • 57
    • 0033588325 scopus 로고    scopus 로고
    • 11,12-Epoxyeicosatrienoic acid stimulates endogenous mono-ADP- ribosylation in bovine coronary arterial smooth muscle
    • Li PL, Chen CL, Bortell R, and Campbell WB. 11,12-Epoxyeicosatrienoic acid stimulates endogenous mono-ADP-ribosylation in bovine coronary arterial smooth muscle. Circ Res 85: 349-356, 1999.
    • (1999) Circ Res , vol.85 , pp. 349-356
    • Li, P.L.1    Chen, C.L.2    Bortell, R.3    Campbell, W.B.4
  • 58
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington RC and Ginsberg MH. Integrin activation takes shape. J Cell Biol 158: 833-839, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 59
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt G, Ford E, Kurtev M, and Guarente L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem 280: 21313-21320, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 60
    • 0035501101 scopus 로고    scopus 로고
    • Extracellular nicotinamide adenine dinucleotide induces T cell apoptosis in vivo and in vitro
    • Liu ZX, Azhipa O, Okamoto S, Govindarajan S, and Dennert G. Extracellular nicotinamide adenine dinucleotide induces T cell apoptosis in vivo and in vitro. J Immunol 167: 4942-4947, 2001.
    • (2001) J Immunol , vol.167 , pp. 4942-4947
    • Liu, Z.X.1    Azhipa, O.2    Okamoto, S.3    Govindarajan, S.4    Dennert, G.5
  • 61
    • 0033581006 scopus 로고    scopus 로고
    • A cell surface ADP-ribosyltransferase modulates T cell receptor association and signaling
    • Liu ZX, Yu Y, and Dennert G. A cell surface ADP-ribosyltransferase modulates T cell receptor association and signaling. J Biol Chem 274: 17399-17401, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 17399-17401
    • Liu, Z.X.1    Yu, Y.2    Dennert, G.3
  • 62
    • 14844346910 scopus 로고    scopus 로고
    • Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering
    • Luo BH, Carman CV, Takagi J, and Springer TA. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proc Natl Acad Sci USA 102: 3679-3684, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3679-3684
    • Luo, B.H.1    Carman, C.V.2    Takagi, J.3    Springer, T.A.4
  • 63
    • 18644377447 scopus 로고    scopus 로고
    • Endogenous mono-ADP-ribosylation of the free Gβγ prevents stimulation of phosphoinositide 3-kinase-γ and phospholipase C-β2 and is activated by G-protein-coupled receptors
    • Lupi R, Dani N, Dietrich A, Marchegiani A, Turacchio S, Berrie CP, Moss J, Gierschik P, Corda D, and Di Girolamo M. Endogenous mono-ADP-ribosylation of the free Gβγ prevents stimulation of phosphoinositide 3-kinase-γ and phospholipase C-β2 and is activated by G-protein-coupled receptors. Biochem J 367: 825-832, 2002.
    • (2002) Biochem J , vol.367 , pp. 825-832
    • Lupi, R.1    Dani, N.2    Dietrich, A.3    Marchegiani, A.4    Turacchio, S.5    Berrie, C.P.6    Moss, J.7    Gierschik, P.8    Corda, D.9    Di Girolamo, M.10
  • 64
    • 0028027749 scopus 로고
    • Time course of changes in plasma membrane permeability in the dystrophin-deficient mdx mouse
    • McArdle A, Edwards RH, and Jackson MJ. Time course of changes in plasma membrane permeability in the dystrophin-deficient mdx mouse. Muscle Nerve 17: 1378-1384, 1994.
    • (1994) Muscle Nerve , vol.17 , pp. 1378-1384
    • McArdle, A.1    Edwards, R.H.2    Jackson, M.J.3
  • 65
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil PL and Khakee R. Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage. Am J Pathol 140: 1097-1109, 1992.
    • (1992) Am J Pathol , vol.140 , pp. 1097-1109
    • McNeil, P.L.1    Khakee, R.2
  • 66
    • 20344402550 scopus 로고    scopus 로고
    • Opinion: An emergency response team for membrane repair
    • McNeil PL and Kirchhausen T. Opinion: an emergency response team for membrane repair. Nat Rev Mol Cell Biol 6: 499-505, 2005.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 67
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: Repair, prevention, adaptation
    • McNeil PL and Steinhardt RA. Plasma membrane disruption: repair, prevention, adaptation. Annu Rev Cell Dev Biol 19: 697-731, 2003.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 68
    • 0028907196 scopus 로고
    • Extent of shock-induced membrane leakage in human and mouse myotubes depends on dystrophin
    • Menke A and Jockusch H. Extent of shock-induced membrane leakage in human and mouse myotubes depends on dystrophin. J Cell Sci 108: 727-733, 1995.
    • (1995) J Cell Sci , vol.108 , pp. 727-733
    • Menke, A.1    Jockusch, H.2
  • 70
    • 0030587933 scopus 로고    scopus 로고
    • Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells
    • Nemoto E, Yu Y, and Dennert G. Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells. J Immunol 157: 3341-3349, 1996.
    • (1996) J Immunol , vol.157 , pp. 3341-3349
    • Nemoto, E.1    Yu, Y.2    Dennert, G.3
  • 71
    • 9244227657 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerases: Homology, structural domains and functions. Novel therapeutical applications
    • Nguewa PA, Fuertes MA, Valladares B, Alonso C, and Perez JM. Poly(ADP-ribose) polymerases: homology, structural domains and functions. Novel therapeutical applications. Prog Biophys Mol Biol 88: 143-172, 2005.
    • (2005) Prog Biophys Mol Biol , vol.88 , pp. 143-172
    • Nguewa, P.A.1    Fuertes, M.A.2    Valladares, B.3    Alonso, C.4    Perez, J.M.5
  • 72
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North RA. Molecular physiology of P2X receptors. Physiol Rev 82: 1013-1067, 2002.
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 73
    • 0032080818 scopus 로고    scopus 로고
    • Expression of ADP-ribosyltransferase on normal T lymphocytes and effects of nicotinamide adenine dinucleotide on their function
    • Okamoto S, Azhipa O, Yu Y, Russo E, and Dennert G. Expression of ADP-ribosyltransferase on normal T lymphocytes and effects of nicotinamide adenine dinucleotide on their function. J Immunol 160: 4190-4198, 1998.
    • (1998) J Immunol , vol.160 , pp. 4190-4198
    • Okamoto, S.1    Azhipa, O.2    Yu, Y.3    Russo, E.4    Dennert, G.5
  • 74
    • 0029834653 scopus 로고    scopus 로고
    • Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
    • Okazaki IJ, Kim HJ, and Moss J. Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase. J Biol Chem 271: 22052-22057, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 22052-22057
    • Okazaki, I.J.1    Kim, H.J.2    Moss, J.3
  • 75
    • 0027992925 scopus 로고
    • Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases
    • Okazaki IJ, Zolkiewska A, Nightingale MS, and Moss J. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases. Biochemistry 33: 12828-12836, 1994.
    • (1994) Biochemistry , vol.33 , pp. 12828-12836
    • Okazaki, I.J.1    Zolkiewska, A.2    Nightingale, M.S.3    Moss, J.4
  • 81
    • 0034874385 scopus 로고    scopus 로고
    • Inactivation of platelet-derived growth factor-BB following modification by ADP-ribosyltransferase
    • Saxty BA, Yadollahi-Farsani M, Upton PD, Johnstone SR, and MacDermot J. Inactivation of platelet-derived growth factor-BB following modification by ADP-ribosyltransferase. Br J Pharmacol 133: 1219-1226, 2001.
    • (2001) Br J Pharmacol , vol.133 , pp. 1219-1226
    • Saxty, B.A.1    Yadollahi-Farsani, M.2    Upton, P.D.3    Johnstone, S.R.4    MacDermot, J.5
  • 82
    • 1842430537 scopus 로고    scopus 로고
    • Ecto-ADP-ribosyltransferases (ARTs): Emerging actors in cell communication and signaling
    • Seman M, Adriouch S, Haag F, and Koch-Nolte F. Ecto-ADP- ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr Med Chem 11: 857-872, 2004.
    • (2004) Curr Med Chem , vol.11 , pp. 857-872
    • Seman, M.1    Adriouch, S.2    Haag, F.3    Koch-Nolte, F.4
  • 86
    • 10344226219 scopus 로고    scopus 로고
    • Release of β-nicotinamide adenine dinucleotide upon stimulation of postganglionic nerve terminals in blood vessels and urinary bladder
    • Smyth LM, Bobalova J, Mendoza MG, Lew C, and Mutafova-Yambolieva VN. Release of β-nicotinamide adenine dinucleotide upon stimulation of postganglionic nerve terminals in blood vessels and urinary bladder. J Biol Chem 279: 48893-48903, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 48893-48903
    • Smyth, L.M.1    Bobalova, J.2    Mendoza, M.G.3    Lew, C.4    Mutafova-Yambolieva, V.N.5
  • 87
    • 0027787640 scopus 로고
    • 7 integrin cytoplasmic domains during skeletal muscle development: Alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases
    • 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases. J Cell Sci 106: 1139-1152, 1993.
    • (1993) J Cell Sci , vol.106 , pp. 1139-1152
    • Song, W.K.1    Wang, W.2    Sato, H.3    Bielser, D.A.4    Kaufman, S.J.5
  • 88
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • Straub V, Rafael JA, Chamberlain JS, and Campbell KP. Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J Cell Biol 139: 375-385, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3    Campbell, K.P.4
  • 90
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, and Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110: 599-611, 2002.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 91
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
    • Tanner KG, Landry J, Sternglanz R, and Denu JM. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA 97: 14178-14182, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 92
    • 0032887914 scopus 로고    scopus 로고
    • ADP-ribosylation of tubulin by chicken NAD-arginine ADP- ribosyltransferase suppresses microtubule formation
    • Terashima M, Yamamori C, Tsuchiya M, and Shimoyama M. ADP-ribosylation of tubulin by chicken NAD-arginine ADP-ribosyltransferase suppresses microtubule formation. J Nutr Sci Vitaminol (Tokyo) 45: 393-400, 1999.
    • (1999) J Nutr Sci Vitaminol (Tokyo) , vol.45 , pp. 393-400
    • Terashima, M.1    Yamamori, C.2    Tsuchiya, M.3    Shimoyama, M.4
  • 93
    • 0035704778 scopus 로고    scopus 로고
    • The RT6 system of the rat: Developmental, molecular and functional aspects
    • Thiele HG and Haag F. The RT6 system of the rat: developmental, molecular and functional aspects. Immunol Rev 184: 96-108, 2001.
    • (2001) Immunol Rev , vol.184 , pp. 96-108
    • Thiele, H.G.1    Haag, F.2
  • 94
    • 0037389585 scopus 로고    scopus 로고
    • An unraveling tale of how integrins are activated from within
    • Travis MA, Humphries JD, and Humphries MJ. An unraveling tale of how integrins are activated from within. Trends Pharmacol Sci 24: 192-197, 2003.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 192-197
    • Travis, M.A.1    Humphries, J.D.2    Humphries, M.J.3
  • 95
    • 0034941724 scopus 로고    scopus 로고
    • Cardiac gap junction channels: Modulation of expression and channel properties
    • Van Veen AA, van Rijen HV, and Opthof T. Cardiac gap junction channels: modulation of expression and channel properties. Cardiovasc Res 51: 217-229, 2001.
    • (2001) Cardiovasc Res , vol.51 , pp. 217-229
    • Van Veen, A.A.1    Van Rijen, H.V.2    Opthof, T.3
  • 97
    • 0037155254 scopus 로고    scopus 로고
    • Alternative splice variants of α7β1 integrin selectively recognize different laminin isoforms
    • Von der Mark H, Williams I, Wendler O, Sorokin L, von der Mark K, and Poschl E. Alternative splice variants of α7β1 integrin selectively recognize different laminin isoforms. J Biol Chem 277: 6012-6016, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 6012-6016
    • Von Der Mark, H.1    Williams, I.2    Wendler, O.3    Sorokin, L.4    Von Der Mark, K.5    Poschl, E.6
  • 98
    • 0030584706 scopus 로고    scopus 로고
    • Regulation of CTL by ecto-nicotinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein
    • Wang J, Nemoto E, and Dennert G. Regulation of CTL by ecto-nicotinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein. J Immunol 156: 2819-2827, 1996.
    • (1996) J Immunol , vol.156 , pp. 2819-2827
    • Wang, J.1    Nemoto, E.2    Dennert, G.3
  • 100
    • 0038448143 scopus 로고    scopus 로고
    • Modulation of CD11b/CD18 adhesive activity by its extracellular, membrane-proximal regions
    • Xiong YM, Chen J, and Zhang L. Modulation of CD11b/CD18 adhesive activity by its extracellular, membrane-proximal regions. J Immunol 171: 1042-1050, 2003.
    • (2003) J Immunol , vol.171 , pp. 1042-1050
    • Xiong, Y.M.1    Chen, J.2    Zhang, L.3
  • 102
    • 0033152765 scopus 로고    scopus 로고
    • Polymorphic forms of human ADP-ribosyltransferase-1 differences in their catalytic activities revealed by labeling of membrane-associated substrates
    • Yadollahi-Farsani M, Kefalas P, Saxty BA, and MacDermot J. Polymorphic forms of human ADP-ribosyltransferase-1 differences in their catalytic activities revealed by labeling of membrane-associated substrates. Eur J Biochem 262: 342-348, 1999.
    • (1999) Eur J Biochem , vol.262 , pp. 342-348
    • Yadollahi-Farsani, M.1    Kefalas, P.2    Saxty, B.A.3    MacDermot, J.4
  • 104
    • 0027331555 scopus 로고
    • 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J Biol Chem 268: 25273-25276, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 25273-25276
    • Zolkiewska, A.1    Moss, J.2
  • 105
    • 0028901021 scopus 로고
    • 7 in skeletal muscle myotubes
    • 7 in skeletal muscle myotubes. J Biol Chem 270: 9227-9233, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 9227-9233
    • Zolkiewska, A.1    Moss, J.2
  • 106
    • 0026445547 scopus 로고
    • Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle
    • Zolkiewska A, Nightingale MS, and Moss J. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc Natl Acad Sci USA 89: 11352-11356, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11352-11356
    • Zolkiewska, A.1    Nightingale, M.S.2    Moss, J.3


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