메뉴 건너뛰기




Volumn 272, Issue 6, 2005, Pages 1425-1439

Identification of the heparin-binding domains of the interferon-induced protein kinase, PKR

Author keywords

Domain mapping; dsRNA; Heparin; Interferon; Protein kinase

Indexed keywords

ANTIVIRUS AGENT; HEPARIN; INITIATION FACTOR 2ALPHA; INTERFERON; PROTEIN KINASE R;

EID: 15944409863     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04575.x     Document Type: Article
Times cited : (19)

References (65)
  • 2
    • 0027352378 scopus 로고
    • Interferon-induced antiviral actions and their regulation
    • Sen GC & Ransohoff RM (1993) Interferon-induced antiviral actions and their regulation. Adv Virus Res 42, 57-102.
    • (1993) Adv Virus Res , vol.42 , pp. 57-102
    • Sen, G.C.1    Ransohoff, R.M.2
  • 3
    • 0030664277 scopus 로고    scopus 로고
    • PKR - A protein kinase regulated by double-stranded RNA
    • Clemens MJ (1997) PKR - a protein kinase regulated by double-stranded RNA. Int J Biochem Cell Biol 29, 945-949.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 945-949
    • Clemens, M.J.1
  • 4
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E, Chong K, Galabru J, Thomas NS, Kerr IM, Williams BR & Hovanessian AG (1990) Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62, 379-390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.6    Hovanessian, A.G.7
  • 5
    • 0023180020 scopus 로고
    • The double-stranded RNA-dependent protein kinase is also activated by heparin
    • Hovanessian AG & Galabru J (1987) The double-stranded RNA-dependent protein kinase is also activated by heparin. Eur J Biochem 167, 467-473.
    • (1987) Eur J Biochem , vol.167 , pp. 467-473
    • Hovanessian, A.G.1    Galabru, J.2
  • 6
    • 0032480017 scopus 로고    scopus 로고
    • PACT, a protein activator of the interferon-induced protein kinase, PKR
    • Patel RC & Sen GC (1998) PACT, a protein activator of the interferon-induced protein kinase, PKR. Embo J 17, 4379-4390.
    • (1998) Embo J , vol.17 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 7
    • 0033056848 scopus 로고    scopus 로고
    • RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling
    • Ito T, Yang M & May WS (1999) RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J Biol Chem 274, 15427-15432.
    • (1999) J Biol Chem , vol.274 , pp. 15427-15432
    • Ito, T.1    Yang, M.2    May, W.S.3
  • 8
    • 0034531395 scopus 로고    scopus 로고
    • PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR
    • Patel CV, Handy I, Goldsmith T & Patel RC (2000) PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR. J Biol Chem 275, 37993-37998.
    • (2000) J Biol Chem , vol.275 , pp. 37993-37998
    • Patel, C.V.1    Handy, I.2    Goldsmith, T.3    Patel, R.C.4
  • 9
    • 0023655517 scopus 로고
    • Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled represser and by the double-stranded RNA-activated inhibitor
    • Colthurst DR, Campbell DG & Proud CG (1987) Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled represser and by the double-stranded RNA-activated inhibitor. Eur J Biochem 166, 357-363.
    • (1987) Eur J Biochem , vol.166 , pp. 357-363
    • Colthurst, D.R.1    Campbell, D.G.2    Proud, C.G.3
  • 10
    • 0027418321 scopus 로고
    • The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel CE (1993) The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. J Biol Chem 268, 7603-7606.
    • (1993) J Biol Chem , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 12
    • 0033230617 scopus 로고    scopus 로고
    • PKR; a sentinel kinase for cellular stress
    • Williams BR (1999) PKR; a sentinel kinase for cellular stress. Oncogene 18, 6112-6120.
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 13
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas AE, Roy S, Barber GN, Katze MG & Sonenberg N (1992) Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science 257, 1685-1689.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 14
    • 0027396813 scopus 로고
    • Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase
    • Meurs EF, Galabru J, Barber GN, Katze MG & Hovanessian AG (1993) Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase. Proc Natl Acad Sci USA 90, 232-236.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 232-236
    • Meurs, E.F.1    Galabru, J.2    Barber, G.N.3    Katze, M.G.4    Hovanessian, A.G.5
  • 15
    • 0035800333 scopus 로고    scopus 로고
    • Signal integration via PKR
    • Williams BR (2001) Signal integration via PKR. Sci STKE 2001, RE2.
    • (2001) Sci STKE , vol.2001
    • Williams, B.R.1
  • 16
    • 0025819309 scopus 로고
    • Partial characterization of a cellular factor that regulates the double-stranded RNA-dependent eIF-2 alpha kinase in 3T3-F442A fibroblasts
    • Judware R & Petryshyn R (1991) Partial characterization of a cellular factor that regulates the double-stranded RNA-dependent eIF-2 alpha kinase in 3T3-F442A fibroblasts. Mol Cell Biol 11, 3259-3267.
    • (1991) Mol Cell Biol , vol.11 , pp. 3259-3267
    • Judware, R.1    Petryshyn, R.2
  • 17
    • 0029093904 scopus 로고
    • Interruption of myogenesis by transforming growth factor beta 1 or EGTA inhibits expression and activity of the myogenic-associated (2′-5′) oligoadenylate synthetase and PKR
    • Salzberg S, Mandelbaum M, Zalcberg M & Shainberg A (1995) Interruption of myogenesis by transforming growth factor beta 1 or EGTA inhibits expression and activity of the myogenic-associated (2′-5′) oligoadenylate synthetase and PKR. Exp Cell Res 219, 223-232.
    • (1995) Exp Cell Res , vol.219 , pp. 223-232
    • Salzberg, S.1    Mandelbaum, M.2    Zalcberg, M.3    Shainberg, A.4
  • 18
    • 0026042013 scopus 로고
    • Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system
    • Katze MG, Wambach M, Wong ML, Garfinkel M, Meurs E, Chong K, Williams BR, Hovanessian AG & Barber GN (1991) Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system. Mol Cell Biol 11, 5497-5505.
    • (1991) Mol Cell Biol , vol.11 , pp. 5497-5505
    • Katze, M.G.1    Wambach, M.2    Wong, M.L.3    Garfinkel, M.4    Meurs, E.5    Chong, K.6    Williams, B.R.7    Hovanessian, A.G.8    Barber, G.N.9
  • 19
    • 0026686791 scopus 로고
    • Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase
    • Patel RC & Sen GC (1992) Identification of the double-stranded RNA-binding domain of the human interferon-inducible protein kinase. J Biol Chem 267, 7671-7676.
    • (1992) J Biol Chem , vol.267 , pp. 7671-7676
    • Patel, R.C.1    Sen, G.C.2
  • 20
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • Green SR & Mathews MB (1992) Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev 6, 2478-2490.
    • (1992) Genes Dev , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 21
    • 0026716255 scopus 로고
    • Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase
    • McCormack SJ, Thomis DC & Samuel CE (1992) Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase. Virology 188, 47-56.
    • (1992) Virology , vol.188 , pp. 47-56
    • McCormack, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 22
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • Nanduri S, Carpick BW, Yang Y, Williams BR & Qin J (1998) Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. Embo J 17, 5458-5465.
    • (1998) Embo J , vol.17 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.4    Qin, J.5
  • 23
    • 0028241859 scopus 로고
    • Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin
    • Patel RC, Stanton P & Sen GC (1994) Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin. J Biol Chem 269, 18593-18598.
    • (1994) J Biol Chem , vol.269 , pp. 18593-18598
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 24
    • 0028924758 scopus 로고
    • Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF2a kinase DAI in Saccharomyces cerevisiae
    • Romano PR, Green SR, Barber GN, Mathews MB & Hennebusch AG (1995) Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF2a kinase DAI in Saccharomyces cerevisiae. Mol Cell Biol 15, 365-378.
    • (1995) Mol Cell Biol , vol.15 , pp. 365-378
    • Romano, P.R.1    Green, S.R.2    Barber, G.N.3    Mathews, M.B.4    Hennebusch, A.G.5
  • 25
    • 0029078852 scopus 로고
    • Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR)
    • Schmedt C, Green SR, Manche L, Taylor DR, Ma Y & Mathews MB (1995) Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR). J Mol Biol 249, 29-44.
    • (1995) J Mol Biol , vol.249 , pp. 29-44
    • Schmedt, C.1    Green, S.R.2    Manche, L.3    Taylor, D.R.4    Ma, Y.5    Mathews, M.B.6
  • 27
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplexed RNA: One motif, multiple functions
    • Fierro-Monti I & Mathews MB (2000) Proteins binding to duplexed RNA: one motif, multiple functions. Trends Biochem Sci 25, 241-246.
    • (2000) Trends Biochem Sci , vol.25 , pp. 241-246
    • Fierro-Monti, I.1    Mathews, M.B.2
  • 28
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA
    • Carpick BW, Graziano V, Schneider D, Maitra RK, Lee X & Williams BR (1997) Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA. J Biol Chem 272, 9510-9516.
    • (1997) J Biol Chem , vol.272 , pp. 9510-9516
    • Carpick, B.W.1    Graziano, V.2    Schneider, D.3    Maitra, R.K.4    Lee, X.5    Williams, B.R.6
  • 29
    • 0034675856 scopus 로고    scopus 로고
    • A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR
    • Nanduri S, Rahman F, Williams BR & Qin J (2000) A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR. Embo J 19, 5567-5574.
    • (2000) Embo J , vol.19 , pp. 5567-5574
    • Nanduri, S.1    Rahman, F.2    Williams, B.R.3    Qin, J.4
  • 30
    • 0031723958 scopus 로고    scopus 로고
    • Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: Role of complex formation and the E3 N-terminal domain
    • Romano PR, Zhang F, Tan SL, Garcia-Barrio MT, Katze MG, Dever TE & Hinnebusch AG (1998) Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain. Mol Cell Biol 18, 7304-7316.
    • (1998) Mol Cell Biol , vol.18 , pp. 7304-7316
    • Romano, P.R.1    Zhang, F.2    Tan, S.L.3    Garcia-Barrio, M.T.4    Katze, M.G.5    Dever, T.E.6    Hinnebusch, A.G.7
  • 32
    • 0035816675 scopus 로고    scopus 로고
    • Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop
    • Zhang F, Romano PR, Nagamura-Inoue T, Tian B, Dever TE, Mathews MB, Ozato K & Hinnebusch AG (2001) Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop. J Biol Chem 276, 24946-24958.
    • (2001) J Biol Chem , vol.276 , pp. 24946-24958
    • Zhang, F.1    Romano, P.R.2    Nagamura-Inoue, T.3    Tian, B.4    Dever, T.E.5    Mathews, M.B.6    Ozato, K.7    Hinnebusch, A.G.8
  • 33
    • 0029115903 scopus 로고
    • The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo
    • Patel RC, Stanton P, McMillan NM, Williams BR & Sen GC (1995) The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo. Proc Natl Acad Sci USA 92, 8283-8287.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8283-8287
    • Patel, R.C.1    Stanton, P.2    McMillan, N.M.3    Williams, B.R.4    Sen, G.C.5
  • 35
    • 0030030997 scopus 로고    scopus 로고
    • Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR)
    • Wu S & Kaufman RJ (1996) Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR). J Biol Chem 271, 1756-1763.
    • (1996) J Biol Chem , vol.271 , pp. 1756-1763
    • Wu, S.1    Kaufman, R.J.2
  • 36
    • 0031723954 scopus 로고    scopus 로고
    • Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeast
    • Patel RC & Sen GC (1998) Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeast. Mol Cell Biol 18, 7009-7019.
    • (1998) Mol Cell Biol , vol.18 , pp. 7009-7019
    • Patel, R.C.1    Sen, G.C.2
  • 37
    • 0030198564 scopus 로고    scopus 로고
    • Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase
    • George CX, Thomis DC, McCormack SJ, Svahn CM & Samuel CE (1996) Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase. Virology 221, 180-188.
    • (1996) Virology , vol.221 , pp. 180-188
    • George, C.X.1    Thomis, D.C.2    McCormack, S.J.3    Svahn, C.M.4    Samuel, C.E.5
  • 38
    • 0036739922 scopus 로고    scopus 로고
    • Contribution of double-stranded RNA-activated protein kinase toward antiproliferative actions of heparin on vascular smooth muscle cells
    • Patel RC, Handy I & Patel CV (2002) Contribution of double-stranded RNA-activated protein kinase toward antiproliferative actions of heparin on vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 22, 1439-1444.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 1439-1444
    • Patel, R.C.1    Handy, I.2    Patel, C.V.3
  • 39
    • 0019829625 scopus 로고
    • Cultured endothelial cells produce a heparinlike inhibitor of smooth muscle cell growth
    • Castellot JJ Jr, Addonizio ML, Rosenberg R & Karnovsky MJ (1981) Cultured endothelial cells produce a heparinlike inhibitor of smooth muscle cell growth. J Cell Biol 90, 372-379.
    • (1981) J Cell Biol , vol.90 , pp. 372-379
    • Castellot Jr., J.J.1    Addonizio, M.L.2    Rosenberg, R.3    Karnovsky, M.J.4
  • 40
    • 0017576983 scopus 로고
    • Suppression by heparin of smooth muscle cell proliferation in injured arteries
    • Clowes AW & Karnowsky MJ (1977) Suppression by heparin of smooth muscle cell proliferation in injured arteries. Nature 265, 625-626.
    • (1977) Nature , vol.265 , pp. 625-626
    • Clowes, A.W.1    Karnowsky, M.J.2
  • 42
    • 0034567257 scopus 로고    scopus 로고
    • Low-molecular-weight heparin therapy in percutaneous coronary intervention: The NICE 1 and NICE 4 trials
    • National investigators collaborating on enoxaparin investigators; discussion E25-18
    • Young JJ, Kereiakes DJ & Grines CL (2000) Low-molecular-weight heparin therapy in percutaneous coronary intervention: the NICE 1 and NICE 4 trials. National investigators collaborating on enoxaparin investigators. J Invasive Cardiol 12, E14-E18; discussion E25-18.
    • (2000) J Invasive Cardiol , vol.12
    • Young, J.J.1    Kereiakes, D.J.2    Grines, C.L.3
  • 43
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • Ross R (1993) The pathogenesis of atherosclerosis: a perspective for the 1990s. Nature 362, 801-809.
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 44
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin AD & Weintraub HJ (1989) Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9, 21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 45
    • 0029841348 scopus 로고    scopus 로고
    • Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties
    • Patel RC, Stanton P & Sen GC (1996) Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties. J Biol Chem 271, 25657-25663.
    • (1996) J Biol Chem , vol.271 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 46
    • 0023136956 scopus 로고
    • Translational control mediated by eucaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells
    • Kaufman RJ & Murtha P (1987) Translational control mediated by eucaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells. Mol Cell Biol 7, 1568-1571.
    • (1987) Mol Cell Biol , vol.7 , pp. 1568-1571
    • Kaufman, R.J.1    Murtha, P.2
  • 47
    • 0024326946 scopus 로고
    • Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor
    • Davies MV, Furtado M, Hershey JW, Thimmappaya B & Kaufman RJ (1989) Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor. Proc Natl Acad Sci USA 86, 9163-9167.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9163-9167
    • Davies, M.V.1    Furtado, M.2    Hershey, J.W.3    Thimmappaya, B.4    Kaufman, R.J.5
  • 49
    • 0035012516 scopus 로고    scopus 로고
    • Modular structure of PACT: Distinct domains for binding and activating PKR
    • Peters GA, Hartmann R, Qin J & Sen GC (2001) Modular structure of PACT: distinct domains for binding and activating PKR. Mol Cell Biol 21, 1908-.
    • (2001) Mol Cell Biol , vol.21 , pp. 1908
    • Peters, G.A.1    Hartmann, R.2    Qin, J.3    Sen, G.C.4
  • 51
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM & Hunter T (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 52
    • 0023656671 scopus 로고
    • Autophosphorylation of the protein kinase dependent on double-stranded RNA
    • Galabru J & Hovanessian A (1987) Autophosphorylation of the protein kinase dependent on double-stranded RNA. J Biol Chem 262, 15538-15544.
    • (1987) J Biol Chem , vol.262 , pp. 15538-15544
    • Galabru, J.1    Hovanessian, A.2
  • 53
    • 0031897318 scopus 로고    scopus 로고
    • Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor
    • Tan SL, Gale MJ Jr & Katze MG (1998) Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor. Mol Cell Biol 18, 2431-2443.
    • (1998) Mol Cell Biol , vol.18 , pp. 2431-2443
    • Tan, S.L.1    Gale Jr., M.J.2    Katze, M.G.3
  • 54
    • 0030030724 scopus 로고    scopus 로고
    • Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells
    • Ortega LG, McCotter MD, Henry GL, McCormack SJ, Thomis DC & Samuel CE (1996) Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells. Virology 215, 31-39.
    • (1996) Virology , vol.215 , pp. 31-39
    • Ortega, L.G.1    McCotter, M.D.2    Henry, G.L.3    McCormack, S.J.4    Thomis, D.C.5    Samuel, C.E.6
  • 55
    • 0018950165 scopus 로고
    • Inhibition of rat arterial smooth muscle cell proliferation by heparin. II. In vitro studies
    • Hoover RL, Rosenberg R, Haering W & Karnovsky MJ (1980) Inhibition of rat arterial smooth muscle cell proliferation by heparin, II. In vitro studies. Circ Res 47, 578-583.
    • (1980) Circ Res , vol.47 , pp. 578-583
    • Hoover, R.L.1    Rosenberg, R.2    Haering, W.3    Karnovsky, M.J.4
  • 56
    • 0030785344 scopus 로고    scopus 로고
    • Local drug delivery systems and prevention of restenosis
    • Brieger D & Topol E (1997) Local drug delivery systems and prevention of restenosis. Cardiovasc Res 35, 405-413.
    • (1997) Cardiovasc Res , vol.35 , pp. 405-413
    • Brieger, D.1    Topol, E.2
  • 57
    • 0021911622 scopus 로고
    • An antiproliferative heparan sulfate species produced by postconfluent smooth muscle cells
    • Fritze LM, Reilly CF & Rosenberg RD (1985) An antiproliferative heparan sulfate species produced by postconfluent smooth muscle cells. J Cell Biol 100, 1041-1049.
    • (1985) J Cell Biol , vol.100 , pp. 1041-1049
    • Fritze, L.M.1    Reilly, C.F.2    Rosenberg, R.D.3
  • 58
    • 0028149288 scopus 로고
    • Mutagenesis in four candidate heparin binding regions (residues 279-282, 291-304, 390-393, and 439-448) and identification of residues affecting heparin binding of human lipoprotein lipase
    • Ma Y, Henderson HE, Liu MS, Zhang H, Forsythe IJ, Clarke-Lewis I, Hayden MR & Brunzell JD (1994) Mutagenesis in four candidate heparin binding regions (residues 279-282, 291-304, 390-393, and 439-448) and identification of residues affecting heparin binding of human lipoprotein lipase. J Lipid Res 35, 2049-2059.
    • (1994) J Lipid Res , vol.35 , pp. 2049-2059
    • Ma, Y.1    Henderson, H.E.2    Liu, M.S.3    Zhang, H.4    Forsythe, I.J.5    Clarke-Lewis, I.6    Hayden, M.R.7    Brunzell, J.D.8
  • 59
    • 0031811576 scopus 로고    scopus 로고
    • Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis
    • Sendak RA & Bensadoun A (1998) Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis. J Lipid Res 39, 1310-1315.
    • (1998) J Lipid Res , vol.39 , pp. 1310-1315
    • Sendak, R.A.1    Bensadoun, A.2
  • 60
    • 0033998074 scopus 로고    scopus 로고
    • Binding of hepatic lipase to heparin. Identification of specific heparin-binding residues in two distinct positive charge clusters
    • Sendak RA, Berryman DE, Gellman G, Melford K & Bensadoun A (2000) Binding of hepatic lipase to heparin. Identification of specific heparin-binding residues in two distinct positive charge clusters. J Lipid Res 41, 260-268.
    • (2000) J Lipid Res , vol.41 , pp. 260-268
    • Sendak, R.A.1    Berryman, D.E.2    Gellman, G.3    Melford, K.4    Bensadoun, A.5
  • 61
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
    • Thompson LD, Pantoliano MW & Springer BA (1994) Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain. Biochemistry 33, 3831-3840.
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 62
    • 0025847743 scopus 로고
    • Glycosaminoglycans: Molecular properties, protein interactions, and role in physiological processes
    • Jackson RL, Busch SJ & Cardin AD (1991) Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol Rev 71, 481-539.
    • (1991) Physiol Rev , vol.71 , pp. 481-539
    • Jackson, R.L.1    Busch, S.J.2    Cardin, A.D.3
  • 63
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit H, Fischer N & Ben-Sasson SA (1993) Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J Biol Chem 268, 19228-19231.
    • (1993) J Biol Chem , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 64
    • 2342495084 scopus 로고    scopus 로고
    • The hydrogen bonds between Arg423 and Glu472 and other key residues. Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+) /K(+)-ATPase
    • Lansky Z, Kubala M, Ettrich R, Kuty M, Plasek J, Teisinger J, Schoner W & Amler E (2004) The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+) /K(+)-ATPase. Biochemistry 43, 8303-8311.
    • (2004) Biochemistry , vol.43 , pp. 8303-8311
    • Lansky, Z.1    Kubala, M.2    Ettrich, R.3    Kuty, M.4    Plasek, J.5    Teisinger, J.6    Schoner, W.7    Amler, E.8
  • 65
    • 4344689863 scopus 로고    scopus 로고
    • The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: Analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F
    • Morgan CT, Tsivkovskii R, Kosinsky YA, Efremov RG & Lutsenko S (2004) The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F. J Biol Chem 279, 36363-36371.
    • (2004) J Biol Chem , vol.279 , pp. 36363-36371
    • Morgan, C.T.1    Tsivkovskii, R.2    Kosinsky, Y.A.3    Efremov, R.G.4    Lutsenko, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.