메뉴 건너뛰기




Volumn 54, Issue , 2003, Pages 101-123

Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ADAM11 PROTEIN, HUMAN; MEMBRANE PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 0043272529     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0070-2153(03)54006-6     Document Type: Review
Times cited : (89)

References (126)
  • 1
    • 0031568847 scopus 로고    scopus 로고
    • ADAM13: A novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development
    • D Alfandari T.G Wolfsberg J.M White D.W Desimone ADAM13: A novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development Dev. Biol. 182 1997 314 330
    • (1997) Dev. Biol. , vol.182 , pp. 314-330
    • Alfandari, D1    Wolfsberg, T.G2    White, J.M3    Desimone, D.W4
  • 6
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • A Anders S Gilbert W Garten R Postina F Fahrenholz Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases FASEB J. 15 10 2001 1837 1839
    • (2001) FASEB J. , vol.15 , Issue.10 , pp. 1837-1839
    • Anders, A1    Gilbert, S2    Garten, W3    Postina, R4    Fahrenholz, F5
  • 8
    • 85112900674 scopus 로고    scopus 로고
    • The TNF converting enzyme
    • J Becherer M Lamber R Andrews The TNF converting enzyme K Von der Helm B Korant J Cheronis Proteases as Targets for Therapy 2000 Springer Berlin 235 258
    • (2000) , pp. 235-258
    • Becherer, J1    Lamber, M2    Andrews, R3
  • 11
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: focus on the protease domain
    • R.A Black J.M White ADAMs: focus on the protease domain Curr. Opin. Cell Biol. 10 5 1998 654 659
    • (1998) Curr. Opin. Cell Biol. , vol.10 , Issue.5 , pp. 654-659
    • Black, R.A1    White, J.M2
  • 12
    • 0026471735 scopus 로고
    • Structure, function and evolutionary relationship of proteins containing a disintegrin domain
    • C.P Blobel J.M White Structure, function and evolutionary relationship of proteins containing a disintegrin domain Curr. Opin. Cell Biol. 4 1992 760 765
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 760-765
    • Blobel, C.P1    White, J.M2
  • 13
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and Notch
    • C.P Blobel Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and Notch Cell 90 1997 589 592
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P1
  • 14
    • 0000117001 scopus 로고    scopus 로고
    • Roles of metalloprotease-disintegrins in cell-cell interactions, in neurogenesis, and in the cleavage of TNF-alpha
    • C.P Blobel Roles of metalloprotease-disintegrins in cell-cell interactions, in neurogenesis, and in the cleavage of TNF-alpha P.M Wassarman Advances in Developmental Biochemistry 1999 JAI Press Inc Stamford, Connecticut 165 198
    • (1999) , pp. 165-198
    • Blobel, C.P1
  • 15
    • 0033817591 scopus 로고    scopus 로고
    • Remarkable roles of proteolysis on and beyond the cell surface
    • C.P Blobel Remarkable roles of proteolysis on and beyond the cell surface Curr. Opin. Cell Biol. 12 5 2000 606 612
    • (2000) Curr. Opin. Cell Biol. , vol.12 , Issue.5 , pp. 606-612
    • Blobel, C.P1
  • 16
    • 0028382520 scopus 로고
    • Metalloproteinase superfamily and drug design
    • T.L Blundell Metalloproteinase superfamily and drug design Struct. Biol. 1 1994 73 75
    • (1994) Struct. Biol. , vol.1 , pp. 73-75
    • Blundell, T.L1
  • 17
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Metturn) and topologies and should be grouped into a common family, the “etzincins”
    • W Bode F.X Gomis-Ruth W Stockler Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Metturn) and topologies and should be grouped into a common family, the “etzincins” FEBS Lett. 331 1–2 1993 134 140
    • (1993) FEBS Lett. , vol.331 , Issue.1–2 , pp. 134-140
    • Bode, W1    Gomis-Ruth, F.X2    Stockler, W3
  • 18
    • 0033613949 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes
    • G Borland G Murphy A Ager Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes J. Biol. Chem. 274 5 1999 2810 2815
    • (1999) J. Biol. Chem. , vol.274 , Issue.5 , pp. 2810-2815
    • Borland, G1    Murphy, G2    Ager, A3
  • 19
    • 0036479289 scopus 로고    scopus 로고
    • The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1
    • L.C Bridges P.H Tani K.R Hanson C.M Roberts M.B Judkins R.D Bowditch The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1 J. Biol. Chem. 277 5 2002 3784 3792
    • (2002) J. Biol. Chem. , vol.277 , Issue.5 , pp. 3784-3792
    • Bridges, L.C1    Tani, P.H2    Hanson, K.R3    Roberts, C.M4    Judkins, M.B5    Bowditch, R.D6
  • 20
    • 0344428129 scopus 로고    scopus 로고
    • Neural crest-specific and general expression of distinct metalloprotease-disintegrins in early Xenopus laevis development
    • H Cai J Krätzschmar D Alfandari G Hunnicutt C.P Blobel Neural crest-specific and general expression of distinct metalloprotease-disintegrins in early Xenopus laevis development Dev. Biol. 204 1998 508 524
    • (1998) Dev. Biol. , vol.204 , pp. 508-524
    • Cai, H1    Krätzschmar, J2    Alfandari, D3    Hunnicutt, G4    Blobel, C.P5
  • 21
    • 0035878794 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1
    • Y Cao Q Kang A Zolkiewska Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1 Biochem. J. 357 2001 353 361 (Pt 2)
    • (2001) Biochem. J. , vol.357 , pp. 353-361
    • Cao, Y1    Kang, Q2    Zolkiewska, A3
  • 22
    • 0037135599 scopus 로고    scopus 로고
    • Intracellular processing of metalloprotease disintegrin ADAM12
    • Y Cao Q Kang Z Zhao A Zolkiewska Intracellular processing of metalloprotease disintegrin ADAM12 J. Biol. Chem. 277 29 2002 26403 26411
    • (2002) J. Biol. Chem. , vol.277 , Issue.29 , pp. 26403-26411
    • Cao, Y1    Kang, Q2    Zhao, Z3    Zolkiewska, A4
  • 23
    • 0024818172 scopus 로고
    • A novel metalloproteinase associated with brain myelin membranes
    • A Chantry N.A Gregson P Glynn A novel metalloproteinase associated with brain myelin membranes Isolation and characterization J. Biol. Chem. 264 1989 21603 21607 (36)
    • (1989) , pp. 21603-21607
    • Chantry, A1    Gregson, N.A2    Glynn, P3
  • 25
    • 0034331252 scopus 로고    scopus 로고
    • PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13
    • H Cousin A Gaultier C Bleux T Darribere D Alfandari PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13 Dev. Biol. 227 1 2000 197 210
    • (2000) Dev. Biol. , vol.227 , Issue.1 , pp. 197-210
    • Cousin, H1    Gaultier, A2    Bleux, C3    Darribere, T4    Alfandari, D5
  • 26
    • 0033681301 scopus 로고    scopus 로고
    • Notch1 signaling promotes the maturation of CD4 and CD8 SP thymocytes
    • M.L Deftos E Huang E.W Ojala K.A Forbush M.J Bevan Notch1 signaling promotes the maturation of CD4 and CD8 SP thymocytes Immunity 13 1 2000 73 84
    • (2000) Immunity , vol.13 , Issue.1 , pp. 73-84
    • Deftos, M.L1    Huang, E2    Ojala, E.W3    Forbush, K.A4    Bevan, M.J5
  • 27
    • 0033215445 scopus 로고    scopus 로고
    • The effect of a metalloproteinase inhibitor (GI5402) on tumor necrosis factor-alpha (TNF-alpha) and TNF-alpha receptors during human endotoxemia
    • P.E Dekkers F.N Lauw T ten Hove A.A te Velde P Lumley D Becherer S.J van Deventer T van der Poll The effect of a metalloproteinase inhibitor (GI5402) on tumor necrosis factor-alpha (TNF-alpha) and TNF-alpha receptors during human endotoxemia Blood 94 7 1999 2252 2258
    • (1999) Blood , vol.94 , Issue.7 , pp. 2252-2258
    • Dekkers, P.E1    Lauw, F.N2    ten Hove, T3    te Velde, A.A4    Lumley, P5    Becherer, D6    van Deventer, S.J7    van der Poll, T8
  • 28
    • 0034799491 scopus 로고    scopus 로고
    • A novel inhibitor of tumor necrosis factor-alpha converting enzyme ameliorates polycystic kidney disease
    • K.M Dell R Nemo W.E Sweeney Jr. J.I Levin P Frost E.D Avner A novel inhibitor of tumor necrosis factor-alpha converting enzyme ameliorates polycystic kidney disease Kidney Int. 60 4 2001 1240 1248
    • (2001) Kidney Int. , vol.60 , Issue.4 , pp. 1240-1248
    • Dell, K.M1    Nemo, R2    Sweeney, W.E3    Levin, J.I4    Frost, P5    Avner, E.D6
  • 30
    • 0034640428 scopus 로고    scopus 로고
    • Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
    • J.R Doedens R.A Black Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme J. Biol. Chem. 275 19 2000 14598 14607
    • (2000) J. Biol. Chem. , vol.275 , Issue.19 , pp. 14598-14607
    • Doedens, J.R1    Black, R.A2
  • 31
    • 0034634458 scopus 로고    scopus 로고
    • RGD-independent binding of integrin a9b1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction
    • K Eto W Puzon-Mclaughlin D Sheppard A Sehara-Fujisawa X.P Zhang Y Takada RGD-independent binding of integrin a9b1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction J. Biol. Chem. 275 45 2000 34922 34930
    • (2000) J. Biol. Chem. , vol.275 , Issue.45 , pp. 34922-34930
    • Eto, K1    Puzon-Mclaughlin, W2    Sheppard, D3    Sehara-Fujisawa, A4    Zhang, X.P5    Takada, Y6
  • 32
    • 0033555056 scopus 로고    scopus 로고
    • Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions
    • J.P Evans Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions Front. Biosci. 4 1999 D114 D131
    • (1999) Front. Biosci. , vol.4 , pp. D114-D131
    • Evans, J.P1
  • 33
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • H Fan R Derynck Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades EMBO J. 18 24 1999 6962 6972
    • (1999) EMBO J. , vol.18 , Issue.24 , pp. 6962-6972
    • Fan, H1    Derynck, R2
  • 34
    • 0031593468 scopus 로고    scopus 로고
    • TNFalpha processing enzyme inhibitors prevent aspirin-induced TNFalpha release and protect against gastric mucosal injury in rats
    • S Fiorucci E Antonelli G Migliorati L Santucci O Morelli B Federici A Morelli TNFalpha processing enzyme inhibitors prevent aspirin-induced TNFalpha release and protect against gastric mucosal injury in rats Aliment. Pharmacol. Ther. 12 11 1998 1139 1153
    • (1998) Aliment. Pharmacol. Ther. , vol.12 , Issue.11 , pp. 1139-1153
    • Fiorucci, S1    Antonelli, E2    Migliorati, G3    Santucci, L4    Morelli, O5    Federici, B6    Morelli, A7
  • 35
    • 0034661829 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human metalloprotease disintegrin—a novel marker for dendritic cell differentiation
    • J Fritsche M Moser S Faust A Peuker R Buttner R Andreesen M Kreutz Molecular cloning and characterization of a human metalloprotease disintegrin—a novel marker for dendritic cell differentiation Blood 96 2 2000 732 739
    • (2000) Blood , vol.96 , Issue.2 , pp. 732-739
    • Fritsche, J1    Moser, M2    Faust, S3    Peuker, A4    Buttner, R5    Andreesen, R6    Kreutz, M7
  • 36
    • 0034608081 scopus 로고    scopus 로고
    • Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion
    • M.F Galliano C Huet J Frygelius A Polgren U.M Wewer E Engvall Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion J. Biol. Chem. 275 18 2000 13933 13999
    • (2000) J. Biol. Chem. , vol.275 , Issue.18 , pp. 13933-13999
    • Galliano, M.F1    Huet, C2    Frygelius, J3    Polgren, A4    Wewer, U.M5    Engvall, E6
  • 38
    • 0031961873 scopus 로고    scopus 로고
    • A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo
    • B.J Gilpin F Loechel M.G Mattei E Engvall R Albrechtsen U.M Wewer A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo J. Biol. Chem. 273 1 1998 157 166
    • (1998) J. Biol. Chem. , vol.273 , Issue.1 , pp. 157-166
    • Gilpin, B.J1    Loechel, F2    Mattei, M.G3    Engvall, E4    Albrechtsen, R5    Wewer, U.M6
  • 39
    • 0032491435 scopus 로고    scopus 로고
    • The HHQK domain of beta-amyloid provides a structural basis for the immunopathology of Alzheimer's disease
    • D Giulian L.J Haverkamp J Yu W Karshin D Tom J Li A Kazanskaia J Kirkpatrick A.E Rocher The HHQK domain of beta-amyloid provides a structural basis for the immunopathology of Alzheimer's disease J. Biol. Chem. 273 45 1998 29719 29726
    • (1998) J. Biol. Chem. , vol.273 , Issue.45 , pp. 29719-29726
    • Giulian, D1    Haverkamp, L.J2    Yu, J3    Karshin, W4    Tom, D5    Li, J6    Kazanskaia, A7    Kirkpatrick, J8    Rocher, A.E9
  • 41
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • M Hattori M Osterfield J.G Flanagan Regulated cleavage of a contact-mediated axon repellent Science 289 5483 2000 1360 1365
    • (2000) Science , vol.289 , Issue.5483 , pp. 1360-1365
    • Hattori, M1    Osterfield, M2    Flanagan, J.G3
  • 42
    • 0033943398 scopus 로고    scopus 로고
    • Treatment with BB-94, a broad spectrum inhibitor of zinc-dependent metalloproteinases, causes deviation of the cytokine profile towards type-2 in experimental pulmonary tuberculosis in Balb/c mice
    • R Hernandez-Pando H Orozco K Arriaga L Pavon G Rook Treatment with BB-94, a broad spectrum inhibitor of zinc-dependent metalloproteinases, causes deviation of the cytokine profile towards type-2 in experimental pulmonary tuberculosis in Balb/c mice Int. J. Exp. Pathol. 81 3 2000 199 209
    • (2000) Int. J. Exp. Pathol. , vol.81 , Issue.3 , pp. 199-209
    • Hernandez-Pando, R1    Orozco, H2    Arriaga, K3    Pavon, L4    Rook, G5
  • 45
    • 0027459878 scopus 로고
    • Adipose expression of tumor necrosis factor-alpha: direct role in obesity-linked insulin resistance
    • G.S Hotamisligil N.S Shargill B.M Spiegelman Adipose expression of tumor necrosis factor-alpha: direct role in obesity-linked insulin resistance Science 259 5091 1993 87 91
    • (1993) Science , vol.259 , Issue.5091 , pp. 87-91
    • Hotamisligil, G.S1    Shargill, N.S2    Spiegelman, B.M3
  • 46
    • 0029057781 scopus 로고
    • Membrane-associated metalloproteinase recognized by characterisitic cleavage of myelin basic protein: assay and isolation
    • L Howard P Glynn Membrane-associated metalloproteinase recognized by characterisitic cleavage of myelin basic protein: assay and isolation A.J Barrett Proteolytic Enzymes: Aspartic and Metalloproteases 1995 Academic Press San Diego 388 395
    • (1995) , pp. 388-395
    • Howard, L1    Glynn, P2
  • 47
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: a catalytically active disintegrin-metalloprotease expressed in various cell types
    • L Howard X Lu S Mitchell S Griffiths P Glynn Molecular cloning of MADM: a catalytically active disintegrin-metalloprotease expressed in various cell types Biochem. J. 317 1996 45 50
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L1    Lu, X2    Mitchell, S3    Griffiths, S4    Glynn, P5
  • 48
    • 0033615602 scopus 로고    scopus 로고
    • Interaction of the metalloprotase disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1
    • L Howard K.K Nelson R.A Maciewizc C.P Blobel Interaction of the metalloprotase disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1 J. Biol. Chem. 274 44 1999 31693 31699
    • (1999) J. Biol. Chem. , vol.274 , Issue.44 , pp. 31693-31699
    • Howard, L1    Nelson, K.K2    Maciewizc, R.A3    Blobel, C.P4
  • 49
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • L Howard R.A Maciewicz C.P Blobel Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28 Biochem. J. 348 2000 21 27 Pt 1
    • (2000) Biochem. J. , vol.348 , pp. 21-27
    • Howard, L1    Maciewicz, R.A2    Blobel, C.P3
  • 50
    • 0035370612 scopus 로고    scopus 로고
    • Catalytic activity of ADAM28
    • L Howard Catalytic activity of ADAM28 FEBS Lett. 498 1 2001 82 86
    • (2001) FEBS Lett. , vol.498 , Issue.1 , pp. 82-86
    • Howard, L1
  • 52
    • 0033520318 scopus 로고    scopus 로고
    • ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases
    • T.L Hurskainen S Hirohata M.F Seldin S.S Apte ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases General features and genomic distribution of the ADAM-TS family J. Biol. Chem. 274 1999 25555 25563 (36)
    • (1999) , pp. 25555-25563
    • Hurskainen, T.L1    Hirohata, S2    Seldin, M.F3    Apte, S.S4
  • 54
    • 0032512831 scopus 로고    scopus 로고
    • Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells
    • D Inoue M Reid L Lum J Krätzschmar G Weskamp Y.M Myung R Baron C.P Blobel Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells J. Biol. Chem. 273 1998 4180 4187
    • (1998) J. Biol. Chem. , vol.273 , pp. 4180-4187
    • Inoue, D1    Reid, M2    Lum, L3    Krätzschmar, J4    Weskamp, G5    Myung, Y.M6    Baron, R7    Blobel, C.P8
  • 55
    • 0034844231 scopus 로고    scopus 로고
    • Processing of tumor necrosis factor by the membrane-bound TNF-alpha-converting enzyme, but not its truncated soluble form
    • T Itai M Tanaka S Nagata Processing of tumor necrosis factor by the membrane-bound TNF-alpha-converting enzyme, but not its truncated soluble form Eur. J. Biochem. 268 7 2001 2074 2082
    • (2001) Eur. J. Biochem. , vol.268 , Issue.7 , pp. 2074-2082
    • Itai, T1    Tanaka, M2    Nagata, S3
  • 56
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • C.V Jongeneel J Bouvier A Bairoch A unique signature identifies a family of zinc-dependent metallopeptidases FEBS Lett. 242 2 1989 211 214
    • (1989) FEBS Lett. , vol.242 , Issue.2 , pp. 211-214
    • Jongeneel, C.V1    Bouvier, J2    Bairoch, A3
  • 57
    • 0032750640 scopus 로고    scopus 로고
    • Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis
    • J.A Jury A.C Perry L Hall Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis Mol. Hum. Reprod. 5 12 1999 1127 1134
    • (1999) Mol. Hum. Reprod. , vol.5 , Issue.12 , pp. 1127-1134
    • Jury, J.A1    Perry, A.C2    Hall, L3
  • 58
    • 0037067764 scopus 로고    scopus 로고
    • Intracellular activation of human Adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites
    • T Kang Y.G Zhao D Pei J.F Sucic Q.X Sang Intracellular activation of human Adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites J. Biol. Chem. 277 28 2002 25583 25591
    • (2002) J. Biol. Chem. , vol.277 , Issue.28 , pp. 25583-25591
    • Kang, T1    Zhao, Y.G2    Pei, D3    Sucic, J.F4    Sang, Q.X5
  • 59
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10
    • E Kojro G Gimpl S Lammich W Marz F Fahrenholz Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10 Proc. Natl. Acad. Sci. USA 98 2001 5815 5820 (10)
    • (2001) , pp. 5815-5820
    • Kojro, E1    Gimpl, G2    Lammich, S3    Marz, W4    Fahrenholz, F5
  • 60
    • 0031310583 scopus 로고    scopus 로고
    • Notch on the cutting edge
    • R Kopan R Cagan Notch on the cutting edge Trends Genet. 13 12 1997 465 467
    • (1997) Trends Genet. , vol.13 , Issue.12 , pp. 465-467
    • Kopan, R1    Cagan, R2
  • 61
    • 0037161592 scopus 로고    scopus 로고
    • Beta-aryl-succinic acid hydroxamates as dual inhibitors of matrix metalloproteinases and tumor necrosis factor alpha converting enzyme
    • G Kottirsch G Koch R Feifel U Neumann Beta-aryl-succinic acid hydroxamates as dual inhibitors of matrix metalloproteinases and tumor necrosis factor alpha converting enzyme J. Med. Chem. 45 11 2002 2289 2293
    • (2002) J. Med. Chem. , vol.45 , Issue.11 , pp. 2289-2293
    • Kottirsch, G1    Koch, G2    Feifel, R3    Neumann, U4
  • 62
    • 0029670028 scopus 로고    scopus 로고
    • Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence
    • J Krätzschmar L Lum C.P Blobel Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence J. Biol. Chem. 271 1996 4593 4596
    • (1996) J. Biol. Chem. , vol.271 , pp. 4593-4596
    • Krätzschmar, J1    Lum, L2    Blobel, C.P3
  • 63
    • 0032079067 scopus 로고    scopus 로고
    • Spatially- and temporally-restricted expression of meltrin alpha (ADAM12) and beta (ADAM19) in mouse embryo
    • T Kurisaki A Masuda N Osumi Y Nabeshima A Fujisawa-Sehara Spatially- and temporally-restricted expression of meltrin alpha (ADAM12) and beta (ADAM19) in mouse embryo Mech. Dev. 73 2 1998 211 215
    • (1998) Mech. Dev. , vol.73 , Issue.2 , pp. 211-215
    • Kurisaki, T1    Masuda, A2    Osumi, N3    Nabeshima, Y4    Fujisawa-Sehara, A5
  • 66
    • 0034845846 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases and tumor necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis
    • S Lieb J Clements R Lindberg C Heimgartner J Loeffler L.-A Pfister M Tauber L D Inhibition of matrix metalloproteinases and tumor necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis Brain 124 2001 1734 1742
    • (2001) Brain , vol.124 , pp. 1734-1742
    • Lieb, S1    Clements, J2    Lindberg, R3    Heimgartner, C4    Loeffler, J5    Pfister, L.-A6    Tauber, M7    D, L8
  • 67
    • 0037080699 scopus 로고    scopus 로고
    • Kuzbanian-mediated cleavage of Drosophila Notch
    • T Lieber S Kidd M.W Young Kuzbanian-mediated cleavage of Drosophila Notch Genes Dev. 16 2 2002 209 221
    • (2002) Genes Dev. , vol.16 , Issue.2 , pp. 209-221
    • Lieber, T1    Kidd, S2    Young, M.W3
  • 69
    • 0033532144 scopus 로고    scopus 로고
    • Regulation of human ADAM 12 protease by the prodomain
    • F Loechel M.T Overgaard C Oxvig R Albrechtsen U.M Wewer Regulation of human ADAM 12 protease by the prodomain Evidence for a functional cysteine switch J. Biol. Chem. 274 1999 13427 13433 (19)
    • (1999) , pp. 13427-13433
    • Loechel, F1    Overgaard, M.T2    Oxvig, C3    Albrechtsen, R4    Wewer, U.M5
  • 71
    • 0031282021 scopus 로고    scopus 로고
    • Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin
    • L Lum C.P Blobel Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin Dev. Biol. 191 1 1997 131 145
    • (1997) Dev. Biol. , vol.191 , Issue.1 , pp. 131-145
    • Lum, L1    Blobel, C.P2
  • 72
    • 0032475960 scopus 로고    scopus 로고
    • Intracellular maturation of the mouse metalloprotease disintegrin MDC15
    • L Lum M.S Reid C.P Blobel Intracellular maturation of the mouse metalloprotease disintegrin MDC15 J. Biol. Chem. 273 1998 26236 26247
    • (1998) J. Biol. Chem. , vol.273 , pp. 26236-26247
    • Lum, L1    Reid, M.S2    Blobel, C.P3
  • 73
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • L Lum B.R Wong R Josien J.D Becherer H Erdjument-Bromage J Schlondorff P Tempst Y Choi C.P Blobel Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival J. Biol. Chem. 274 19 1999 13613 13618
    • (1999) J. Biol. Chem. , vol.274 , Issue.19 , pp. 13613-13618
    • Lum, L1    Wong, B.R2    Josien, R3    Becherer, J.D4    Erdjument-Bromage, H5    Schlondorff, J6    Tempst, P7    Choi, Y8    Blobel, C.P9
  • 74
    • 0034714890 scopus 로고    scopus 로고
    • The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone
    • D.R McCulloch M Harvey A.C Herington The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone Mol. Cell. Endocrinol. 167 1–2 2000 11 21
    • (2000) Mol. Cell. Endocrinol. , vol.167 , Issue.1–2 , pp. 11-21
    • McCulloch, D.R1    Harvey, M2    Herington, A.C3
  • 78
    • 18444368391 scopus 로고    scopus 로고
    • The tumor necrosis factor alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity
    • M Mohan T Seaton J Mitchell A Howe K Blackburn W Burkhart M Moyer I Patel J Becherer M Moss M Milla The tumor necrosis factor alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity Biochemistry 41 30 2002 9462 9469
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9462-9469
    • Mohan, M1    Seaton, T2    Mitchell, J3    Howe, A4    Blackburn, K5    Burkhart, W6    Moyer, M7    Patel, I8    Becherer, J9    Moss, M10    Milla, M11
  • 80
    • 0031577286 scopus 로고    scopus 로고
    • KB-R7785, a novel matrix metalloproteinase inhibitor, exerts its antidiabetic effect by inhibiting tumor necrosis factor-alpha production
    • Y Morimoto K Nishikawa M Ohashi KB-R7785, a novel matrix metalloproteinase inhibitor, exerts its antidiabetic effect by inhibiting tumor necrosis factor-alpha production Life Sci. 61 8 1997 795 803
    • (1997) Life Sci. , vol.61 , Issue.8 , pp. 795-803
    • Morimoto, Y1    Nishikawa, K2    Ohashi, M3
  • 82
    • 0034020230 scopus 로고    scopus 로고
    • The importance of shedding of membrane proteins for cytokine biology
    • J Mullberg K Althoff T Jostock S Rose-John The importance of shedding of membrane proteins for cytokine biology Eur. Cytokine Netw. 11 1 2000 27 38
    • (2000) Eur. Cytokine Netw. , vol.11 , Issue.1 , pp. 27-38
    • Mullberg, J1    Althoff, K2    Jostock, T3    Rose-John, S4
  • 84
    • 0031049748 scopus 로고    scopus 로고
    • Why did the sperm cross the cumulus? To get to the oocyte
    • D.G Myles P Primakoff Why did the sperm cross the cumulus? To get to the oocyte Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg Biol. Reprod. 56 1997 320 327 (2)
    • (1997) , pp. 320-327
    • Myles, D.G1    Primakoff, P2
  • 86
    • 0033933982 scopus 로고    scopus 로고
    • Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility
    • D Nath P.M Slocombe A Webster P.E Stephens A.J Docherty G Murphy Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility J. Cell. Sci. 113 2000 2319 2328 (Pt 12)
    • (2000) J. Cell. Sci. , vol.113 , pp. 2319-2328
    • Nath, D1    Slocombe, P.M2    Webster, A3    Stephens, P.E4    Docherty, A.J5    Murphy, G6
  • 87
    • 2442732615 scopus 로고    scopus 로고
    • Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta
    • K.K Nelson J Schlondorff C.P Blobel Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta Biochem. J. 343 1999 673 680 Pt 3
    • (1999) Biochem. J. , vol.343 , pp. 673-680
    • Nelson, K.K1    Schlondorff, J2    Blobel, C.P3
  • 90
    • 0031282592 scopus 로고    scopus 로고
    • Developmental signaling: notch signals Kuz it's cleaved
    • J.S Nye Developmental signaling: notch signals Kuz it's cleaved Curr. Biol. 7 11 1997 R716 R720
    • (1997) Curr. Biol. , vol.7 , Issue.11 , pp. R716-R720
    • Nye, J.S1
  • 91
    • 0343196671 scopus 로고    scopus 로고
    • KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • D Pan J Rubin KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis Cell 90 1997 271 280
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D1    Rubin, J2
  • 92
    • 0037117753 scopus 로고    scopus 로고
    • Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-alpha
    • E.T Parkin A Trew G Christie A Faller R Mayer A.J Turner N.M Hooper Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-alpha Biochemistry 41 15 2002 4972 4981
    • (2002) Biochemistry , vol.41 , Issue.15 , pp. 4972-4981
    • Parkin, E.T1    Trew, A2    Christie, G3    Faller, A4    Mayer, R5    Turner, A.J6    Hooper, N.M7
  • 94
    • 0037085256 scopus 로고    scopus 로고
    • Phosphorylation-dependent Interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases
    • Z Poghosyan S.M Robbins M.D Houslay A Webster G Murphy D.R Edwards Phosphorylation-dependent Interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases J. Biol. Chem. 277 7 2002 4999 5007
    • (2002) J. Biol. Chem. , vol.277 , Issue.7 , pp. 4999-5007
    • Poghosyan, Z1    Robbins, S.M2    Houslay, M.D3    Webster, A4    Murphy, G5    Edwards, D.R6
  • 95
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: surface proteins with an adhesion and protease activity packed into a single molecule
    • P Primakoff D.G Myles The ADAM gene family: surface proteins with an adhesion and protease activity packed into a single molecule Trends Genet. 16 2000 83 87
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P1    Myles, D.G2
  • 101
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • J Rooke D Pan T Xu G.M Rubin KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis Science 273 1996 1227 1230
    • (1996) Science , vol.273 , pp. 1227-1230
    • Rooke, J1    Pan, D2    Xu, T3    Rubin, G.M4
  • 104
    • 0034332481 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuronglia interactions during neurodegeneration
    • U Schlomann S Rathke-Hartlieb S Yamamoto H Jockusch J.W Bartsch Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuronglia interactions during neurodegeneration J. Neurosci. 20 21 2000 7964 7971
    • (2000) J. Neurosci. , vol.20 , Issue.21 , pp. 7964-7971
    • Schlomann, U1    Rathke-Hartlieb, S2    Yamamoto, S3    Jockusch, H4    Bartsch, J.W5
  • 105
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding
    • J Schlöndorff C.P Blobel Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding J. Cell. Sci. 112 1999 3603 3617 (Pt 21)
    • (1999) J. Cell. Sci. , vol.112 , pp. 3603-3617
    • Schlöndorff, J1    Blobel, C.P2
  • 106
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • J Schlöndorff J.D Becherer C.P Blobel Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE) Biochem. J. 347 2000 131 138 Pt 1
    • (2000) Biochem. J. , vol.347 , pp. 131-138
    • Schlöndorff, J1    Becherer, J.D2    Blobel, C.P3
  • 107
    • 0034957288 scopus 로고    scopus 로고
    • Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin
    • L Schwettmann H Tschesche Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin Protein Expr. Purif. 21 1 2001 65 70
    • (2001) Protein Expr. Purif. , vol.21 , Issue.1 , pp. 65-70
    • Schwettmann, L1    Tschesche, H2
  • 109
    • 0028969678 scopus 로고
    • The metzincins—topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • W Stocker F Grams U Baumann P Reinemer F.X Gomis-Ruth D.B McKay W Bode The metzincins—topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases Protein Sci. 4 5 1995 823 840
    • (1995) Protein Sci. , vol.4 , Issue.5 , pp. 823-840
    • Stocker, W1    Grams, F2    Baumann, U3    Reinemer, P4    Gomis-Ruth, F.X5    McKay, D.B6    Bode, W7
  • 110
    • 0032809940 scopus 로고    scopus 로고
    • Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review)
    • A.L Stone M Kroeger Q.X Sang Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins (review) J. Protein Chem. 18 4 1999 447 465
    • (1999) J. Protein Chem. , vol.18 , Issue.4 , pp. 447-465
    • Stone, A.L1    Kroeger, M2    Sang, Q.X3
  • 111
    • 0034735912 scopus 로고    scopus 로고
    • Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src
    • A Suzuki N Kadota T Hara Y Nakagami T Izumi T Takenawa H Sabe T Endo Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src Oncogene 19 51 2000 5842 5850
    • (2000) Oncogene , vol.19 , Issue.51 , pp. 5842-5850
    • Suzuki, A1    Kadota, N2    Hara, T3    Nakagami, Y4    Izumi, T5    Takenawa, T6    Sabe, H7    Endo, T8
  • 112
    • 0032978988 scopus 로고    scopus 로고
    • ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats
    • B.L Tang W Hong ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats FEBS Lett. 445 2–3 1999 223 225
    • (1999) FEBS Lett. , vol.445 , Issue.2–3 , pp. 223-225
    • Tang, B.L1    Hong, W2
  • 113
    • 0036175563 scopus 로고    scopus 로고
    • Effect of TNF-alpha—converting enzyme inhibitor on insulin resistance in fructose-fed rats
    • N Togashi N Ura K Higashiura H Murakami K Shimamoto Effect of TNF-alpha—converting enzyme inhibitor on insulin resistance in fructose-fed rats Hypertension 39 2 2002 578 580 Pt 2
    • (2002) Hypertension , vol.39 , Issue.2 , pp. 578-580
    • Togashi, N1    Ura, N2    Higashiura, K3    Murakami, H4    Shimamoto, K5
  • 114
    • 0036971187 scopus 로고    scopus 로고
    • Pharmacological profile of PKF242-484 and PKF241-446, novel dual inhibitors of TNF-alpha converting enzyme and matrix metalloproteinases, in model of airway inflammation
    • A Trifilieff C Walker T Keller G Kottirsch U Neumann Pharmacological profile of PKF242-484 and PKF241-446, novel dual inhibitors of TNF-alpha converting enzyme and matrix metalloproteinases, in model of airway inflammation Br. J. Pharm. 135 2002 1655 1664
    • (2002) Br. J. Pharm. , vol.135 , pp. 1655-1664
    • Trifilieff, A1    Walker, C2    Keller, T3    Kottirsch, G4    Neumann, U5
  • 115
    • 0032976525 scopus 로고    scopus 로고
    • Role for ADAM-family proteinases as membrane protein secretases
    • A.J Turner N.M Hooper Role for ADAM-family proteinases as membrane protein secretases Biochem. Soc. Trans. 27 2 1999 255 259
    • (1999) Biochem. Soc. Trans. , vol.27 , Issue.2 , pp. 255-259
    • Turner, A.J1    Hooper, N.M2
  • 116
    • 0030756346 scopus 로고    scopus 로고
    • Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function
    • K.T Uysal S.M Wiesbrock M.W Marino G.S Hotamisligil Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function Nature 389 6651 1997 610 614
    • (1997) Nature , vol.389 , Issue.6651 , pp. 610-614
    • Uysal, K.T1    Wiesbrock, S.M2    Marino, M.W3    Hotamisligil, G.S4
  • 117
    • 0025025442 scopus 로고
    • The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • H.E Van Wart H Birkedal-Hansen The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family Proc. Natl. Acad. Sci. USA 87 1990 5578 5582 (14)
    • (1990) , pp. 5578-5582
    • Van Wart, H.E1    Birkedal-Hansen, H2
  • 118
    • 0034815337 scopus 로고    scopus 로고
    • Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/Meltrin beta
    • P Wei Y.G Zhao L Zhuang S Ruben Q.X Sang Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/Meltrin beta Biochem. Biophys. Res. Commun. 280 3 2001 744 755
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , Issue.3 , pp. 744-755
    • Wei, P1    Zhao, Y.G2    Zhuang, L3    Ruben, S4    Sang, Q.X5
  • 119
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
    • G Weskamp J.R Krätzschmar M Reid C.P Blobel MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains J. Cell Biol. 132 1996 717 726
    • (1996) J. Cell Biol. , vol.132 , pp. 717-726
    • Weskamp, G1    Krätzschmar, J.R2    Reid, M3    Blobel, C.P4
  • 120
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • G Weskamp H Cai T Brodie S Higashyama K Manova T Ludwig C Blobel Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life Mol. Cell Biol. 22 5 2002 1537 1544
    • (2002) Mol. Cell Biol. , vol.22 , Issue.5 , pp. 1537-1544
    • Weskamp, G1    Cai, H2    Brodie, T3    Higashyama, S4    Manova, K5    Ludwig, T6    Blobel, C7
  • 121
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • T.G Wolfsberg J.M White ADAMs in fertilization and development Dev. Biol. 180 1996 389 401
    • (1996) Dev. Biol. , vol.180 , pp. 389-401
    • Wolfsberg, T.G1    White, J.M2
  • 122
    • 0036266125 scopus 로고    scopus 로고
    • Altered tumor necrosis factor-alpha (TNF-alpha) processing in adipocytes and increased expression of transmembrane TNF-alpha in obesity
    • H Xu K.T Uysal J.D Becherer P Arner G.S Hotamisligil Altered tumor necrosis factor-alpha (TNF-alpha) processing in adipocytes and increased expression of transmembrane TNF-alpha in obesity Diabetes 51 6 2002 1876 1883
    • (2002) Diabetes , vol.51 , Issue.6 , pp. 1876-1883
    • Xu, H1    Uysal, K.T2    Becherer, J.D3    Arner, P4    Hotamisligil, G.S5
  • 123
    • 0035846068 scopus 로고    scopus 로고
    • Discovery of macrocyclic hydroxamic acids containing biphenylmethyl derivatives at P1′, a series of selective TNF-alpha converting enzyme inhibitors with potent cellular activity in the inhibition of TNF-alpha release
    • C.B Xue X He R.L Corbett J Roderick Z.R Wasserman R.Q Liu B.D Jaffee M.B Covington M Qian J.M Trzaskos R.C Newton R.L Magolda R.R Wexler C.P Decicco Discovery of macrocyclic hydroxamic acids containing biphenylmethyl derivatives at P1′, a series of selective TNF-alpha converting enzyme inhibitors with potent cellular activity in the inhibition of TNF-alpha release J. Med. Chem. 44 21 2001 3351 3354
    • (2001) J. Med. Chem. , vol.44 , Issue.21 , pp. 3351-3354
    • Xue, C.B1    He, X2    Corbett, R.L3    Roderick, J4    Wasserman, Z.R5    Liu, R.Q6    Jaffee, B.D7    Covington, M.B8    Qian, M9    Trzaskos, J.M10    Newton, R.C11    Magolda, R.L12    Wexler, R.R13    Decicco, C.P14
  • 125
    • 0032571315 scopus 로고    scopus 로고
    • Specific interaction of the recombinant disintegrin-like domain of MDC15 (metargidin, ADAM-15) with integrin (alpha)v(beta)3
    • X.-P Zhang T Kamata K Yokoyama W Puzon-Mclaughlin J Takada Specific interaction of the recombinant disintegrin-like domain of MDC15 (metargidin, ADAM-15) with integrin (alpha)v(beta)3 J. Biol. Chem. 273 1998 7345 7350
    • (1998) J. Biol. Chem. , vol.273 , pp. 7345-7350
    • Zhang, X.-P1    Kamata, T2    Yokoyama, K3    Puzon-Mclaughlin, W4    Takada, J5
  • 126
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein tyrosine phosphatase PTPHI
    • Y Zheng Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein tyrosine phosphatase PTPHI J. Biol. Chem. 277 45 2002 42463 42470
    • (2002) J. Biol. Chem. , vol.277 , Issue.45 , pp. 42463-42470
    • Zheng, Y1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.