메뉴 건너뛰기




Volumn 54, Issue 12, 1997, Pages 1271-1280

New strategies for chemokine inhibition and modulation. You take the high road and I'll take the low road

Author keywords

Chemotactic cytokines; Drug therapies; Inflammation; Viral inhibitors

Indexed keywords

ANTIBODY; ANTIINFLAMMATORY AGENT; CHEMOKINE; INTERLEUKIN 8; LYMPHOTACTIN; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MACROPHAGE INFLAMMATORY PROTEIN 1BETA; MONOCYTE CHEMOTACTIC PROTEIN 1; NEUTRALIZING ANTIBODY; RANTES; THROMBOCYTE FACTOR 4;

EID: 0030725180     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00182-2     Document Type: Article
Times cited : (45)

References (94)
  • 1
    • 0025735630 scopus 로고
    • Properties of the novel proinflammatory supergene "intercrine" cytokine family
    • Oppenheim JJ, Zacharier MN, Matsushima K. Properties of the novel proinflammatory supergene "intercrine" cytokine family. Annu Rev Immunol. 9:1991;617-648.
    • (1991) Annu Rev Immunol , vol.9 , pp. 617-648
    • Oppenheim, J.J.1    Zacharier, M.N.2    Matsushima, K.3
  • 2
    • 0030045809 scopus 로고    scopus 로고
    • Chemokines as mediators of allergic inflammation
    • Bacon KB, Schall TJ. Chemokines as mediators of allergic inflammation. Int Arch Allergy Immunol. 109:1996;97-109.
    • (1996) Int Arch Allergy Immunol , vol.109 , pp. 97-109
    • Bacon, K.B.1    Schall, T.J.2
  • 3
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokines - CXC and CC chemokines
    • Baggiolini M, Dewald B, Moser B. Interleukin-8 and related chemotactic cytokines - CXC and CC chemokines. Adv Immunol. 55:1994;97-179.
    • (1994) Adv Immunol , vol.55 , pp. 97-179
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 5
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration The multistep paradigm . Cell. 76:1994;301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 8
    • 0030449961 scopus 로고    scopus 로고
    • Chemokines - Molecular double agents
    • Horuk R, Peiper SC. Chemokines - Molecular double agents. Curr Biol. 6:1996;1581-1582.
    • (1996) Curr Biol , vol.6 , pp. 1581-1582
    • Horuk, R.1    Peiper, S.C.2
  • 9
    • 0029586149 scopus 로고
    • Human chemokines: Enhancement of specific activity and effects in vitro on normal and leukemic progenitors and a factor-dependent cell line and in vivo in mice
    • Broxmeyer HE, Cooper S, Hague N, Benninger L, Sarris A, Cornetta K, Vadhan-Raj S, Hendrie P, Mantel C. Human chemokines Enhancement of specific activity and effects in vitro on normal and leukemic progenitors and a factor-dependent cell line and in vivo in mice . Ann Hematol. 71:1995;235-246.
    • (1995) Ann Hematol , vol.71 , pp. 235-246
    • Broxmeyer, H.E.1    Cooper, S.2    Hague, N.3    Benninger, L.4    Sarris, A.5    Cornetta, K.6    Vadhan-Raj, S.7    Hendrie, P.8    Mantel, C.9
  • 10
    • 0027300330 scopus 로고
    • Comparative analysis of the human macrophage inflammatory protein family of cytokines (chemokines) on proliferation of human myeloid progenitor cells. Interacting effects involving suppression, synergistic suppression, and blocking of suppression
    • Broxmeyer HE, Sherry B, Cooper S, Lu L, Maze R, Beckmann MP, Cerami A, Ralph P. Comparative analysis of the human macrophage inflammatory protein family of cytokines (chemokines) on proliferation of human myeloid progenitor cells. Interacting effects involving suppression, synergistic suppression, and blocking of suppression. J Immunol. 150:1993;3448-3458.
    • (1993) J Immunol , vol.150 , pp. 3448-3458
    • Broxmeyer, H.E.1    Sherry, B.2    Cooper, S.3    Lu, L.4    Maze, R.5    Beckmann, M.P.6    Cerami, A.7    Ralph, P.8
  • 11
    • 0027165675 scopus 로고
    • Signal sequence trap: A cloning strategy for secreted proteins and type I membrane proteins
    • Tashiro K, Tada H, Heilker R, Shirozu M, Nakano T, Honjo T. Signal sequence trap A cloning strategy for secreted proteins and type I membrane proteins . Science. 261:1993;600-603.
    • (1993) Science , vol.261 , pp. 600-603
    • Tashiro, K.1    Tada, H.2    Heilker, R.3    Shirozu, M.4    Nakano, T.5    Honjo, T.6
  • 15
    • 0028989347 scopus 로고
    • Interferon-γ-inducible protein 10 (IP-10), a member of the C-X-C chemokine family, is an inhibitor of angiogenesis
    • Strieter RM, Kunkel SL, Arenberg DA, Burdick MD, Polverini PJ. Interferon-γ-inducible protein 10 (IP-10), a member of the C-X-C chemokine family, is an inhibitor of angiogenesis. Biochem Biophys Res Commun. 210:1995;51-57.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 51-57
    • Strieter, R.M.1    Kunkel, S.L.2    Arenberg, D.A.3    Burdick, M.D.4    Polverini, P.J.5
  • 16
    • 0028843419 scopus 로고
    • Three-dimensional structures of α and β chemokines
    • Clore GM, Gronenborn AM. Three-dimensional structures of α and β chemokines. FASEB J. 9:1995;57-62.
    • (1995) FASEB J , vol.9 , pp. 57-62
    • Clore, G.M.1    Gronenborn, A.M.2
  • 20
    • 0029665212 scopus 로고    scopus 로고
    • 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer
    • 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer. Biochemistry. 35:1996;6569-6584.
    • (1996) Biochemistry , vol.35 , pp. 6569-6584
    • Handel, T.M.1    Domaille, P.J.2
  • 21
    • 0028999259 scopus 로고
    • Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type
    • Skelton NJ, Aspiras F, Ogez J, Schall TJ. Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type. Biochemistry. 34:1995;5329-5342.
    • (1995) Biochemistry , vol.34 , pp. 5329-5342
    • Skelton, N.J.1    Aspiras, F.2    Ogez, J.3    Schall, T.J.4
  • 23
    • 0028202481 scopus 로고
    • The molecular biology of leukocyte chemoattractant receptors
    • Murphy PM. The molecular biology of leukocyte chemoattractant receptors. Annu Rev Immunol. 12:1994;593-633.
    • (1994) Annu Rev Immunol , vol.12 , pp. 593-633
    • Murphy, P.M.1
  • 25
    • 0029856309 scopus 로고    scopus 로고
    • Chemokine receptors: Gateways to inflammation and infection
    • Premack BA, Schall TJ. Chemokine receptors Gateways to inflammation and infection . Nature Med. 2:1996;1174-1178.
    • (1996) Nature Med , vol.2 , pp. 1174-1178
    • Premack, B.A.1    Schall, T.J.2
  • 26
    • 0028429960 scopus 로고
    • Differential binding of chemokines to glycosaminoglycan subpopulations
    • Witt DP, Lander AD. Differential binding of chemokines to glycosaminoglycan subpopulations. Curr Biol. 4:1994;394-400.
    • (1994) Curr Biol , vol.4 , pp. 394-400
    • Witt, D.P.1    Lander, A.D.2
  • 27
    • 0027533286 scopus 로고
    • Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism
    • Rot A. Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism. Eur J Immunol. 23:1993;303-306.
    • (1993) Eur J Immunol , vol.23 , pp. 303-306
    • Rot, A.1
  • 29
    • 0027521594 scopus 로고
    • Prevention of lung reperfusion injury in rabbits by a monoclonal antibody against interleukin-8
    • Sekido N, Mukaida N, Harada A, Nakanishi I, Watanabe Y, Matsushima K. Prevention of lung reperfusion injury in rabbits by a monoclonal antibody against interleukin-8. Nature. 365:1993;654-657.
    • (1993) Nature , vol.365 , pp. 654-657
    • Sekido, N.1    Mukaida, N.2    Harada, A.3    Nakanishi, I.4    Watanabe, Y.5    Matsushima, K.6
  • 31
    • 0028129541 scopus 로고
    • Prevention of proteinuria by the administration of anti-interleukin 8 antibody in experimental acute immune complex-induced glomerulonephritis
    • Wada T, Tomosugi N, Naito T, Yokoyama H, Kobayashi K, Harada A, Mukaida N, Matsushima K. Prevention of proteinuria by the administration of anti-interleukin 8 antibody in experimental acute immune complex-induced glomerulonephritis. J Exp Med. 180:1994;1135-1140.
    • (1994) J Exp Med , vol.180 , pp. 1135-1140
    • Wada, T.1    Tomosugi, N.2    Naito, T.3    Yokoyama, H.4    Kobayashi, K.5    Harada, A.6    Mukaida, N.7    Matsushima, K.8
  • 32
    • 0027203563 scopus 로고
    • Expression of recombinant rabbit IL-8 in Escherichia coli and establishment of the essential involvement of IL-8 in recruiting neutrophils into lipopolysaccharide-induced inflammatory site of rabbit skin
    • Harada A, Sekido N, Kuno K, Akiyama M, Kasahara T, Nakanishi I, Mukaida N, Matsushima K. Expression of recombinant rabbit IL-8 in Escherichia coli and establishment of the essential involvement of IL-8 in recruiting neutrophils into lipopolysaccharide-induced inflammatory site of rabbit skin. Int Immunol. 5:1993;681-690.
    • (1993) Int Immunol , vol.5 , pp. 681-690
    • Harada, A.1    Sekido, N.2    Kuno, K.3    Akiyama, M.4    Kasahara, T.5    Nakanishi, I.6    Mukaida, N.7    Matsushima, K.8
  • 35
    • 0026005126 scopus 로고
    • Scanning mutagenesis of interleukin-8 identifies a cluster of residues required for receptor binding
    • Hebert CA, Vitangcol RV, Baker JB. Scanning mutagenesis of interleukin-8 identifies a cluster of residues required for receptor binding. J Biol Chem. 266:1991;18989-18994.
    • (1991) J Biol Chem , vol.266 , pp. 18989-18994
    • Hebert, C.A.1    Vitangcol, R.V.2    Baker, J.B.3
  • 36
    • 0026333179 scopus 로고
    • 2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities
    • 2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities. J Biol Chem. 266:1991;23128-23134.
    • (1991) J Biol Chem , vol.266 , pp. 23128-23134
    • Clark-Lewis, I.1    Schumacher, C.2    Baggiolini, M.3    Moser, B.4
  • 37
    • 0027516840 scopus 로고
    • Platelet factor 4 binds to interleukin 8 receptors and activates neutrophils when its N terminus is modified with Glu-Leu-Arg
    • Clark-Lewis I, Dewald B, Geiser T, Moser B, Baggiolini M. Platelet factor 4 binds to interleukin 8 receptors and activates neutrophils when its N terminus is modified with Glu-Leu-Arg. Proc Natl Acad Sci USA. 90:1993;3574-3577.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3574-3577
    • Clark-Lewis, I.1    Dewald, B.2    Geiser, T.3    Moser, B.4    Baggiolini, M.5
  • 41
    • 0028302305 scopus 로고
    • Structure/activity analysis of human monocyte chemoattractant protein-1 (MCP-1) by mutagenesis
    • Zhang YJ, Rutledge BJ, Rollins BJ. Structure/activity analysis of human monocyte chemoattractant protein-1 (MCP-1) by mutagenesis. J Biol Chem. 269:1994;15918-15924.
    • (1994) J Biol Chem , vol.269 , pp. 15918-15924
    • Zhang, Y.J.1    Rutledge, B.J.2    Rollins, B.J.3
  • 42
    • 0029131699 scopus 로고
    • A dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer
    • Zhang Y, Rollins BJ. A dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer. Mol Cell Biol. 15:1995;4851-4855.
    • (1995) Mol Cell Biol , vol.15 , pp. 4851-4855
    • Zhang, Y.1    Rollins, B.J.2
  • 45
    • 0030581183 scopus 로고    scopus 로고
    • Chemokine receptors and HIV-1: An attractive pair?
    • Bates P. Chemokine receptors and HIV-1 An attractive pair? Cell. 86:1996;1-3.
    • (1996) Cell , vol.86 , pp. 1-3
    • Bates, P.1
  • 47
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion co-factors
    • Doranz BJ, Rucker J, Yi Y, Smyth RJ, Samson M, Peiper SC, Parmentier M, Collman RJ, Doms RW. A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion co-factors. Cell. 85:1996;1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmentier, M.7    Collman, R.J.8    Doms, R.W.9
  • 50
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA. HIV-1 entry cofactor Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor . Science. 272:1996;872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 52
    • 0028802046 scopus 로고
    • Synthetic hexa- And heptapeptides that inhibit IL-8 from binding to and activating human blood neutrophils
    • Hayashi S, Kurdowska A, Miller EJ, Albright ME, Girten BE, Cohen AB. Synthetic hexa- and heptapeptides that inhibit IL-8 from binding to and activating human blood neutrophils. J Immunol. 154:1995;814-824.
    • (1995) J Immunol , vol.154 , pp. 814-824
    • Hayashi, S.1    Kurdowska, A.2    Miller, E.J.3    Albright, M.E.4    Girten, B.E.5    Cohen, A.B.6
  • 53
    • 0030281494 scopus 로고    scopus 로고
    • Interleukin 8 as a novel target for intervention therapy in acute inflammatory diseases
    • Harada A, Mukaida N, Matsushima K. Interleukin 8 as a novel target for intervention therapy in acute inflammatory diseases. Mol Med Today. 11:1996;482-489.
    • (1996) Mol Med Today , vol.11 , pp. 482-489
    • Harada, A.1    Mukaida, N.2    Matsushima, K.3
  • 54
    • 0030058539 scopus 로고    scopus 로고
    • Chemokines: Toward identifying molecular targets for therapeutic agents
    • Howard O, Ben-Baruch A, Oppenheim JJ. Chemokines Toward identifying molecular targets for therapeutic agents . Trends Biotechnol. 14:1996;46-51.
    • (1996) Trends Biotechnol , vol.14 , pp. 46-51
    • Howard, O.1    Ben-Baruch, A.2    Oppenheim, J.J.3
  • 55
    • 0027408343 scopus 로고
    • Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes
    • Tanaka Y, Adams DH, Shaw S. Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes. Immunol Today. 14:1993;111-115.
    • (1993) Immunol Today , vol.14 , pp. 111-115
    • Tanaka, Y.1    Adams, D.H.2    Shaw, S.3
  • 56
    • 0027141953 scopus 로고
    • Regulation of leukocyte recruitment by proadhesive cytokines immobilized on endothelial proteoglycan
    • Tanaka Y, Adams DH, Shaw S. Regulation of leukocyte recruitment by proadhesive cytokines immobilized on endothelial proteoglycan. Curr Top Microbiol Immunol. 184:1993;99-106.
    • (1993) Curr Top Microbiol Immunol , vol.184 , pp. 99-106
    • Tanaka, Y.1    Adams, D.H.2    Shaw, S.3
  • 57
    • 0029548190 scopus 로고
    • Interactions of migrating T lymphocytes, inflammatory mediators, and the extracellular matrix
    • Lider O, Hershkoviz R, Kachalsky SG. Interactions of migrating T lymphocytes, inflammatory mediators, and the extracellular matrix. Crit Rev Immunol. 15:1995;271-283.
    • (1995) Crit Rev Immunol , vol.15 , pp. 271-283
    • Lider, O.1    Hershkoviz, R.2    Kachalsky, S.G.3
  • 58
    • 0027229259 scopus 로고
    • Cytokines and proteoglycans
    • Nietfeld JJ. Cytokines and proteoglycans. Experientia. 49:1993;456-469.
    • (1993) Experientia , vol.49 , pp. 456-469
    • Nietfeld, J.J.1
  • 60
    • 0028134835 scopus 로고
    • + T lymphocytes to intact or heparinase-treated subendothelial extracellular matrix by diffusible or anchored RANTES and MIP-1β
    • + T lymphocytes to intact or heparinase-treated subendothelial extracellular matrix by diffusible or anchored RANTES and MIP-1β J Immunol. 153:1994;4899-4906.
    • (1994) J Immunol , vol.153 , pp. 4899-4906
    • Gilat, D.1    Hershkoviz, R.2    Mekori, Y.A.3    Vlodavsky, I.4    Lider, O.5
  • 61
    • 0023928595 scopus 로고
    • Heparan sulphate bound growth factors: A mechanism for stromal cell mediated haemopoiesis
    • Roberts R, Gallagher J, Spooncer E, Allen TD, Bloomfield F, Dexter TM. Heparan sulphate bound growth factors A mechanism for stromal cell mediated haemopoiesis . Nature. 332:1988;376-378.
    • (1988) Nature , vol.332 , pp. 376-378
    • Roberts, R.1    Gallagher, J.2    Spooncer, E.3    Allen, T.D.4    Bloomfield, F.5    Dexter, T.M.6
  • 62
    • 0030060311 scopus 로고    scopus 로고
    • Interplay of T cells and cytokines in the context of enzymatically modified extracellular matrix
    • Gilat D, Cahalon L, Hershkoviz R, Lider O. Interplay of T cells and cytokines in the context of enzymatically modified extracellular matrix. Immunol Today. 17:1996;16-20.
    • (1996) Immunol Today , vol.17 , pp. 16-20
    • Gilat, D.1    Cahalon, L.2    Hershkoviz, R.3    Lider, O.4
  • 63
    • 0029010483 scopus 로고
    • Interaction of interleukin 7 (IL-7) with glycosaminoglycans and its biological relevance
    • Clarke D, Katoh O, Gibbs RV, Griffiths SD, Gordon MY. Interaction of interleukin 7 (IL-7) with glycosaminoglycans and its biological relevance. Cytokine. 7:1995;325-330.
    • (1995) Cytokine , vol.7 , pp. 325-330
    • Clarke, D.1    Katoh, O.2    Gibbs, R.V.3    Griffiths, S.D.4    Gordon, M.Y.5
  • 64
    • 0029926101 scopus 로고    scopus 로고
    • Sulfate moieties in the subendothelial extracellular matrix are involved in basic fibroblast growth factor sequestration, dimerization, and stimulation of cell proliferation
    • Miao H-Q, Ishai-Michaeli R, Atzmon R, Peretz T, Vlodavsky I. Sulfate moieties in the subendothelial extracellular matrix are involved in basic fibroblast growth factor sequestration, dimerization, and stimulation of cell proliferation. J Biol Chem. 271:1996;4879-4886.
    • (1996) J Biol Chem , vol.271 , pp. 4879-4886
    • Miao H-Q1    Ishai-Michaeli, R.2    Atzmon, R.3    Peretz, T.4    Vlodavsky, I.5
  • 65
    • 0030018209 scopus 로고    scopus 로고
    • Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor
    • Vlodavsky I, Miao H-Q, Medalion B, Danagher P, Ron D. Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor. Cancer Metastasis Rev. 15:1996;177-186.
    • (1996) Cancer Metastasis Rev , vol.15 , pp. 177-186
    • Vlodavsky, I.1    Miao H-Q2    Medalion, B.3    Danagher, P.4    Ron, D.5
  • 66
    • 0029095985 scopus 로고
    • Fibroblast growth factors: At the heart of angiogenesis
    • Slavin J. Fibroblast growth factors At the heart of angiogenesis . Cell Biol Int. 19:1995;431-444.
    • (1995) Cell Biol Int , vol.19 , pp. 431-444
    • Slavin, J.1
  • 67
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure interactions with basic fibroblast growth factor
    • Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. Heparin structure interactions with basic fibroblast growth factor. Science. 271:1996;1116-1120.
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 69
    • 0030218948 scopus 로고    scopus 로고
    • Promiscuity of fibroblast growth factor receptors
    • Green PJ, Walsh FS, Doherty P. Promiscuity of fibroblast growth factor receptors. Bioessays. 18:1996;639-646.
    • (1996) Bioessays , vol.18 , pp. 639-646
    • Green, P.J.1    Walsh, F.S.2    Doherty, P.3
  • 71
    • 0027428744 scopus 로고
    • Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4
    • Guimond S, Maccarana M, Olwin BB, Lindahl U, Rapraeger AC. Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4. J Biol Chem. 268:1993;23906-23914.
    • (1993) J Biol Chem , vol.268 , pp. 23906-23914
    • Guimond, S.1    MacCarana, M.2    Olwin, B.B.3    Lindahl, U.4    Rapraeger, A.C.5
  • 72
    • 0028589613 scopus 로고
    • Differential effect of cell-associated heparan sulfates on the binding of keratinocyte growth factor (KGF) and acidic fibroblast growth factor to the KGF receptor
    • Reich-Slotky R, Bonneh-Barkay D, Shaoul E, Bluma B, Svahn CM, Ron D. Differential effect of cell-associated heparan sulfates on the binding of keratinocyte growth factor (KGF) and acidic fibroblast growth factor to the KGF receptor. J Biol Chem. 269:1994;32279-32285.
    • (1994) J Biol Chem , vol.269 , pp. 32279-32285
    • Reich-Slotky, R.1    Bonneh-Barkay, D.2    Shaoul, E.3    Bluma, B.4    Svahn, C.M.5    Ron, D.6
  • 73
    • 0026012415 scopus 로고
    • Characterization and molecular cloning of putative binding protein for heparin-binding growth factors
    • Wu D, Kan M, Sato GH, Okamoto T, Sato JD. Characterization and molecular cloning of putative binding protein for heparin-binding growth factors. J Biol Chem. 266:1991;16778-16785.
    • (1991) J Biol Chem , vol.266 , pp. 16778-16785
    • Wu, D.1    Kan, M.2    Sato, G.H.3    Okamoto, T.4    Sato, J.D.5
  • 74
    • 0028132218 scopus 로고
    • Tumor growth and angiogenesis induced by a secreted binding protein for fibroblast growth factors
    • Czubayko F, Smith RV, Chung HC, Wellstein A. Tumor growth and angiogenesis induced by a secreted binding protein for fibroblast growth factors. J Biol Chem. 269:1994;28243-28248.
    • (1994) J Biol Chem , vol.269 , pp. 28243-28248
    • Czubayko, F.1    Smith, R.V.2    Chung, H.C.3    Wellstein, A.4
  • 75
    • 0029810023 scopus 로고    scopus 로고
    • Regulation of gene expression of a binding protein for fibroblast growth factors by retinoic acid
    • Liaudet-Coopman ED, Wellstein A. Regulation of gene expression of a binding protein for fibroblast growth factors by retinoic acid. J Biol Chem. 271:1996;21303-21308.
    • (1996) J Biol Chem , vol.271 , pp. 21303-21308
    • Liaudet-Coopman, E.D.1    Wellstein, A.2
  • 77
    • 0030218952 scopus 로고    scopus 로고
    • Virus proteins that bind cytokines, chemokines or interferons
    • Smith GL. Virus proteins that bind cytokines, chemokines or interferons. Curr Opin Immunol. 8:1996;467-471.
    • (1996) Curr Opin Immunol , vol.8 , pp. 467-471
    • Smith, G.L.1
  • 78
    • 0029764593 scopus 로고    scopus 로고
    • Genome sequence of a human tumorigenic poxvirus - Prediction of specific host response-evasion genes
    • Senkevich TG, Bugert JJ, Sisler JR, Koonin EV, Darai G, Moss B. Genome sequence of a human tumorigenic poxvirus - Prediction of specific host response-evasion genes. Science. 273:1996;813-816.
    • (1996) Science , vol.273 , pp. 813-816
    • Senkevich, T.G.1    Bugert, J.J.2    Sisler, J.R.3    Koonin, E.V.4    Darai, G.5    Moss, B.6
  • 79
    • 0031033038 scopus 로고    scopus 로고
    • Late expression of a β chemokine homolog by murine cytomegalovirus
    • MacDonald MR, Li X-Y, Virgin HW. Late expression of a β chemokine homolog by murine cytomegalovirus. J Virol. 71:1997;1671-1678.
    • (1997) J Virol , vol.71 , pp. 1671-1678
    • MacDonald, M.R.1    Li X-Y2    Virgin, H.W.3
  • 80
    • 0029837991 scopus 로고    scopus 로고
    • Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV
    • Moore PS, Boshoff C, Weiss RA, Chang Y. Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV. Science. 274:1996;1739-1744.
    • (1996) Science , vol.274 , pp. 1739-1744
    • Moore, P.S.1    Boshoff, C.2    Weiss, R.A.3    Chang, Y.4
  • 81
    • 0028098746 scopus 로고
    • Molecular piracy of chemokine receptors by herpesviruses
    • Murphy PM. Molecular piracy of chemokine receptors by herpesviruses. Infect Agents Dis. 3:1994;137-154.
    • (1994) Infect Agents Dis , vol.3 , pp. 137-154
    • Murphy, P.M.1
  • 82
    • 85045417468 scopus 로고    scopus 로고
    • Virus-encoded cytokines and cytokine receptors
    • in press
    • Barry M and McFadden G, Virus-encoded cytokines and cytokine receptors. Parasitology (Suppl), in press.
    • Parasitology , Issue.SUPPL
    • Barry, M.1    McFadden, G.2
  • 83
    • 0026621761 scopus 로고
    • Encoding of a homolog of the IFN-γ receptor by myxoma virus
    • Upton C, Mossman K, McFadden G. Encoding of a homolog of the IFN-γ receptor by myxoma virus. Science. 258:1992;1369-1372.
    • (1992) Science , vol.258 , pp. 1369-1372
    • Upton, C.1    Mossman, K.2    McFadden, G.3
  • 84
    • 0028980327 scopus 로고
    • The myxoma virus-soluble interferon-γ receptor homolog, M-T7, inhibits interferon-γ In a species-specific manner
    • Mossman K, Upton C, McFadden G. The myxoma virus-soluble interferon-γ receptor homolog, M-T7, inhibits interferon-γ in a species-specific manner. J Biol Chem. 270:1995;3031-3038.
    • (1995) J Biol Chem , vol.270 , pp. 3031-3038
    • Mossman, K.1    Upton, C.2    McFadden, G.3
  • 85
    • 0030048279 scopus 로고    scopus 로고
    • Myxoma virus M-T7, a secreted homolog of the interferon-γ receptor, is a critical virulence factor for the development of myxomatosis in European rabbits
    • Mossman K, Nation P, Macen J, Garbutt M, Lucas A, McFadden G. Myxoma virus M-T7, a secreted homolog of the interferon-γ receptor, is a critical virulence factor for the development of myxomatosis in European rabbits. Virology. 215:1996;17-30.
    • (1996) Virology , vol.215 , pp. 17-30
    • Mossman, K.1    Nation, P.2    MacEn, J.3    Garbutt, M.4    Lucas, A.5    McFadden, G.6
  • 88
    • 0025088047 scopus 로고
    • DNA sequence of the gene encoding a major secreted protein of vaccinia virus, strain Lister
    • Patel AH, Gaffney DF, Subak-Sharpe JH, Stow ND. DNA sequence of the gene encoding a major secreted protein of vaccinia virus, strain Lister. J Gen Virol. 71:1990;2013-2021.
    • (1990) J Gen Virol , vol.71 , pp. 2013-2021
    • Patel, A.H.1    Gaffney, D.F.2    Subak-Sharpe, J.H.3    Stow, N.D.4
  • 89
    • 0028890737 scopus 로고
    • Mapping and investigation of the role in pathogenesis of the major unique secreted 35-kDa protein of rabbitpox virus
    • Martinez-Pomares L, Thompson JP, Moyer RW. Mapping and investigation of the role in pathogenesis of the major unique secreted 35-kDa protein of rabbitpox virus. Virology. 206:1995;591-600.
    • (1995) Virology , vol.206 , pp. 591-600
    • Martinez-Pomares, L.1    Thompson, J.P.2    Moyer, R.W.3
  • 90
    • 0026781082 scopus 로고
    • Control of angiogenesis by heparin and other sulfated polysaccharides
    • Folkman J, Shing Y. Control of angiogenesis by heparin and other sulfated polysaccharides. Adv Exp Med Biol. 313:1992;355-364.
    • (1992) Adv Exp Med Biol , vol.313 , pp. 355-364
    • Folkman, J.1    Shing, Y.2
  • 91
    • 0030198685 scopus 로고    scopus 로고
    • Suramin is a potent inhibitor of vascular endothelial growth factor. A contribution to the molecular basis of its antiangiogenic action
    • Waltenberger J, Mayr U, Frank H, Hombach V. Suramin is a potent inhibitor of vascular endothelial growth factor. A contribution to the molecular basis of its antiangiogenic action. J Mol Cell Cardiol. 28:1996;1523-1529.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 1523-1529
    • Waltenberger, J.1    Mayr, U.2    Frank, H.3    Hombach, V.4
  • 92
    • 0029060187 scopus 로고
    • The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation
    • Luster AD, Greenberg SM, Leder P. The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation. J Exp Med. 182:1995;219-231.
    • (1995) J Exp Med , vol.182 , pp. 219-231
    • Luster, A.D.1    Greenberg, S.M.2    Leder, P.3
  • 93
    • 0029098320 scopus 로고
    • A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4
    • Gupta SK, Hassel T, Singh JP. A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4. Proc Natl Acad Sci USA. 92:1995;7799-7803.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7799-7803
    • Gupta, S.K.1    Hassel, T.2    Singh, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.