메뉴 건너뛰기




Volumn 70, Issue 14, 2013, Pages 2569-2583

Vaspin inhibits kallikrein 7 by serpin mechanism

Author keywords

Crystal structure; Diabetes; Insulin; Kallikrein 7; SerpinA12; Vaspin

Indexed keywords

GLUCOSE; INSULIN; SERINE PROTEINASE INHIBITOR; STRATUM CORNEUM CHYMOTRYPTIC ENZYME; VASPIN;

EID: 84879604629     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1258-8     Document Type: Article
Times cited : (122)

References (61)
  • 1
    • 1642405087 scopus 로고    scopus 로고
    • The obesity epidemic, metabolic syndrome and future prevention strategies
    • 15167200 10.1097/01.hjr.0000114707.27531.48
    • James PT, Rigby N, Leach R (2004) The obesity epidemic, metabolic syndrome and future prevention strategies. Eur J Cardiovasc Prev Rehabil 11(1):3-8
    • (2004) Eur J Cardiovasc Prev Rehabil , vol.11 , Issue.1 , pp. 3-8
    • James, P.T.1    Rigby, N.2    Leach, R.3
  • 3
    • 33845914986 scopus 로고    scopus 로고
    • Mechanisms linking obesity with cardiovascular disease
    • 17167476 10.1038/nature05487
    • Van Gaal LF, Mertens IL, De Block CE (2006) Mechanisms linking obesity with cardiovascular disease. Nature 444(7121):875-880
    • (2006) Nature , vol.444 , Issue.7121 , pp. 875-880
    • Van Gaal, L.F.1    Mertens, I.L.2    De Block, C.E.3
  • 4
    • 2942650969 scopus 로고    scopus 로고
    • Adipose tissue as an endocrine organ
    • 15181022 10.1210/jc.2004-0395 1:CAS:528:DC%2BD2cXmtlGqt7s%3D
    • Kershaw EE, Flier JS (2004) Adipose tissue as an endocrine organ. J Clin Endocrinol Metab 89(6):2548-2556
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.6 , pp. 2548-2556
    • Kershaw, E.E.1    Flier, J.S.2
  • 8
    • 79959740793 scopus 로고    scopus 로고
    • Central vaspin administration acutely reduces food intake and has sustained blood glucose-lowering effects
    • 21465327 10.1007/s00125-011-2137-1 1:STN:280:DC%2BC3MrosVKgsQ%3D%3D
    • Kloting N, Kovacs P, Kern M, Heiker JT, Fasshauer M, Schon MR, Stumvoll M, Beck-Sickinger AG, Bluher M (2011) Central vaspin administration acutely reduces food intake and has sustained blood glucose-lowering effects. Diabetologia 54(7):1819-1823
    • (2011) Diabetologia , vol.54 , Issue.7 , pp. 1819-1823
    • Kloting, N.1    Kovacs, P.2    Kern, M.3    Heiker, J.T.4    Fasshauer, M.5    Schon, M.R.6    Stumvoll, M.7    Beck-Sickinger, A.G.8    Bluher, M.9
  • 9
    • 80052771304 scopus 로고    scopus 로고
    • Effects of vaspin, chemerin and omentin-1 on feeding behavior and hypothalamic peptide gene expression in the rat
    • 21855588 10.1016/j.peptides.2011.08.003 1:CAS:528:DC%2BC3MXhtFGltbzE
    • Brunetti L, Di Nisio C, Recinella L, Chiavaroli A, Leone S, Ferrante C, Orlando G, Vacca M (2011) Effects of vaspin, chemerin and omentin-1 on feeding behavior and hypothalamic peptide gene expression in the rat. Peptides 32(9):1866-1871
    • (2011) Peptides , vol.32 , Issue.9 , pp. 1866-1871
    • Brunetti, L.1    Di Nisio, C.2    Recinella, L.3    Chiavaroli, A.4    Leone, S.5    Ferrante, C.6    Orlando, G.7    Vacca, M.8
  • 12
    • 76449099287 scopus 로고    scopus 로고
    • Xds
    • 20124692 10.1107/S0907444909047337 1:CAS:528:DC%2BC3cXhs1SisLc%3D
    • Kabsch W (2010) Xds. Acta Crystallogr D Biol Crystallogr 66(Pt 2):125-132
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 125-132
    • Kabsch, W.1
  • 14
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • 10.1107/S0021889808006985 1:CAS:528:DC%2BD1cXlvFKgurY%3D
    • Stein N (2008) CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J Appl Crystallogr 41:641-643
    • (2008) J Appl Crystallogr , vol.41 , pp. 641-643
    • Stein, N.1
  • 15
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N 10.1107/S0907444994003112
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 16
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • PT 1 15572765 10.1107/S0907444904019158
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 17
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 15299926 10.1107/S0907444996012255 1:STN:280:DC%2BD2czpsFegsw%3D%3D
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(Pt 3):240-255
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 18
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • PT 1 15572774 10.1107/S0907444904016427 1:STN:280:DC%2BD2cnjs1SgsA%3D%3D
    • Blanc E, Roversi P, Vonrhein C, Flensburg C, Lea SM, Bricogne G (2004) Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2210-2221
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2210-2221
    • Blanc, E.1    Roversi, P.2    Vonrhein, C.3    Flensburg, C.4    Lea, S.M.5    Bricogne, G.6
  • 20
    • 0347753704 scopus 로고    scopus 로고
    • Measurement of the kinetic parameters mediating protease-serpin inhibition
    • 14698628 10.1016/S1046-2023(03)00207-X 1:CAS:528:DC%2BD3sXpvFymu7k%3D
    • Schechter NM, Plotnick MI (2004) Measurement of the kinetic parameters mediating protease-serpin inhibition. Methods 32(2):159-168
    • (2004) Methods , vol.32 , Issue.2 , pp. 159-168
    • Schechter, N.M.1    Plotnick, M.I.2
  • 21
    • 50949125470 scopus 로고    scopus 로고
    • Autocrine IGF-1 action in adipocytes controls systemic IGF-1 concentrations and growth
    • 18443199 10.2337/db07-1538
    • Kloting N, Koch L, Wunderlich T, Kern M, Ruschke K, Krone W, Bruning JC, Bluher M (2008) Autocrine IGF-1 action in adipocytes controls systemic IGF-1 concentrations and growth. Diabetes 57(8):2074-2082
    • (2008) Diabetes , vol.57 , Issue.8 , pp. 2074-2082
    • Kloting, N.1    Koch, L.2    Wunderlich, T.3    Kern, M.4    Ruschke, K.5    Krone, W.6    Bruning, J.C.7    Bluher, M.8
  • 22
    • 0037324750 scopus 로고    scopus 로고
    • Insulin signaling is required for insulin's direct and indirect action on hepatic glucose production
    • 12588884 1:CAS:528:DC%2BD3sXhtlGis74%3D
    • Fisher SJ, Kahn CR (2003) Insulin signaling is required for insulin's direct and indirect action on hepatic glucose production. J Clin Invest 111(4):463-468
    • (2003) J Clin Invest , vol.111 , Issue.4 , pp. 463-468
    • Fisher, S.J.1    Kahn, C.R.2
  • 23
    • 34548156165 scopus 로고    scopus 로고
    • Ex vivo gene transfer of viral interleukin-10 to BB rat islets: No protection after transplantation to diabetic BB rats
    • 17760846 10.1111/j.1582-4934.2007.00059.x 1:CAS:528:DC%2BD2sXhtFSks77O
    • Kuttler B, Wanka H, Kloting N, Gerstmayer B, Volk HD, Sawitzki B, Ritter T (2007) Ex vivo gene transfer of viral interleukin-10 to BB rat islets: no protection after transplantation to diabetic BB rats. J Cell Mol Med 11(4):868-880
    • (2007) J Cell Mol Med , vol.11 , Issue.4 , pp. 868-880
    • Kuttler, B.1    Wanka, H.2    Kloting, N.3    Gerstmayer, B.4    Volk, H.D.5    Sawitzki, B.6    Ritter, T.7
  • 24
    • 24944519995 scopus 로고    scopus 로고
    • Glucose concentration and AMP-dependent kinase activation regulate expression of insulin receptor family members in rat islets and INS-1E beta cells
    • 16052330 10.1007/s00125-005-1860-x 1:CAS:528:DC%2BD2MXhtVSqtL%2FF
    • Raile K, Klammt J, Laue S, Garten A, Bluher M, Kralisch S, Kloting N, Kiess W (2005) Glucose concentration and AMP-dependent kinase activation regulate expression of insulin receptor family members in rat islets and INS-1E beta cells. Diabetologia 48(9):1798-1809
    • (2005) Diabetologia , vol.48 , Issue.9 , pp. 1798-1809
    • Raile, K.1    Klammt, J.2    Laue, S.3    Garten, A.4    Bluher, M.5    Kralisch, S.6    Kloting, N.7    Kiess, W.8
  • 26
    • 0035557506 scopus 로고    scopus 로고
    • Human tissue kallikrein gene family: A rich source of novel disease biomarkers
    • 10.1586/14737159.1.2.182 1:CAS:528:DC%2BD3MXmvVemsrk%3D
    • Diamandis EP, Yousef GM (2001) Human tissue kallikrein gene family: a rich source of novel disease biomarkers. Exp Rev Mol Diagn 1(2):182-190
    • (2001) Exp Rev Mol Diagn , vol.1 , Issue.2 , pp. 182-190
    • Diamandis, E.P.1    Yousef, G.M.2
  • 27
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • 11057674 10.1038/35038119 1:CAS:528:DC%2BD3cXns1OksLw%3D
    • Huntington JA, Read RJ, Carrell RW (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407(6806):923-926
    • (2000) Nature , vol.407 , Issue.6806 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 28
    • 0014211618 scopus 로고
    • On the size of the active site in proteases I. Papain
    • 6035483 10.1016/S0006-291X(67)80055-X 1:CAS:528:DyaF2sXktVyhsrg%3D
    • Schechter I, Berger A (1967) On the size of the active site in proteases I. Papain. Biochem Biophys Res Commun 27(2):157-162
    • (1967) Biochem Biophys Res Commun , vol.27 , Issue.2 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 29
    • 0021747157 scopus 로고
    • Human alpha-1-proteinase inhibitor - Crystal structure analysis of 2 crystal modifications, molecular model and preliminary analysis of the implications for function
    • 6332197 10.1016/0022-2836(84)90298-5 1:CAS:528:DyaL2cXls1Kitb8%3D
    • Loebermann H, Tokuoka R, Deisenhofer J, Huber R (1984) Human alpha-1-proteinase inhibitor - crystal structure analysis of 2 crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 177(3):531-556
    • (1984) J Mol Biol , vol.177 , Issue.3 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 30
    • 0028879762 scopus 로고
    • The contribution of the conserved hinge region residues of alpha(1)-antitrypsin to its reaction with elastase
    • 7495819 10.1021/bi00048a033 1:CAS:528:DyaK2MXpt12rs78%3D
    • Hopkins PCR, Stone SR (1995) The contribution of the conserved hinge region residues of alpha(1)-antitrypsin to its reaction with elastase. Biochemistry 34(48):15872-15879
    • (1995) Biochemistry , vol.34 , Issue.48 , pp. 15872-15879
    • Hopkins, P.C.R.1    Stone, S.R.2
  • 31
    • 0035920162 scopus 로고    scopus 로고
    • The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop
    • 11325972 10.1074/jbc.M102594200 1:CAS:528:DC%2BD3MXlsV2isLk%3D
    • Zhou A, Carrell RW, Huntington JA (2001) The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop. J Biol Chem 276(29):27541-27547
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27541-27547
    • Zhou, A.1    Carrell, R.W.2    Huntington, J.A.3
  • 33
    • 0027182969 scopus 로고
    • Effects of mutations in the hinge region of serpins
    • 8347575 10.1021/bi00081a008 1:CAS:528:DyaK3sXkvV2ktb4%3D
    • Hopkins PC, Carrell RW, Stone SR (1993) Effects of mutations in the hinge region of serpins. Biochemistry 32(30):7650-7657
    • (1993) Biochemistry , vol.32 , Issue.30 , pp. 7650-7657
    • Hopkins, P.C.1    Carrell, R.W.2    Stone, S.R.3
  • 34
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • 8379949 10.1002/bies.950150705 1:CAS:528:DyaK2cXhvVGksb8%3D
    • Gettins P, Patston PA, Schapira M (1993) The role of conformational change in serpin structure and function. BioEssays 15(7):461-467
    • (1993) BioEssays , vol.15 , Issue.7 , pp. 461-467
    • Gettins, P.1    Patston, P.A.2    Schapira, M.3
  • 35
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
    • 2690952 10.1021/bi00449a001 1:CAS:528:DyaL1MXmtFSku7Y%3D
    • Huber R, Carrell RW (1989) Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28(23):8951-8966
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 36
    • 0028168253 scopus 로고
    • Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways
    • 8031789 10.1021/bi00194a020 1:CAS:528:DyaK2cXksFaqsrs%3D
    • Hood DB, Huntington JA, Gettins PG (1994) Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 33(28):8538-8547
    • (1994) Biochemistry , vol.33 , Issue.28 , pp. 8538-8547
    • Hood, D.B.1    Huntington, J.A.2    Gettins, P.G.3
  • 37
    • 33748646005 scopus 로고    scopus 로고
    • Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences
    • 16740631 10.1074/jbc.M602372200 1:CAS:528:DC%2BD28XoslKlt7g%3D
    • Debela M, Magdolen V, Schechter N, Valachova M, Lottspeich F, Craik CS, Choe Y, Bode W, Goettig P (2006) Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences. J Biol Chem 281(35):25678-25688
    • (2006) J Biol Chem , vol.281 , Issue.35 , pp. 25678-25688
    • Debela, M.1    Magdolen, V.2    Schechter, N.3    Valachova, M.4    Lottspeich, F.5    Craik, C.S.6    Choe, Y.7    Bode, W.8    Goettig, P.9
  • 38
    • 0029058938 scopus 로고
    • Primary substrate-specificity of recombinant human stratum-corneum chymotryptic enzyme
    • 7794273 10.1006/bbrc.1995.1853 1:CAS:528:DyaK2MXmtlChu70%3D
    • Skytt A, Stromqvist M, Egelrud T (1995) Primary substrate-specificity of recombinant human stratum-corneum chymotryptic enzyme. Biochem Biophys Res Commun 211(2):586-589
    • (1995) Biochem Biophys Res Commun , vol.211 , Issue.2 , pp. 586-589
    • Skytt, A.1    Stromqvist, M.2    Egelrud, T.3
  • 39
    • 38649139900 scopus 로고    scopus 로고
    • Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
    • 18163887 10.1515/BC.2008.013 1:CAS:528:DC%2BD1cXhvVOmsL4%3D
    • Dong Y, Matigian N, Harvey TJ, Samaratunga H, Hooper JD, Clements JA (2008) Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function. Biol Chem 389(2):99-109
    • (2008) Biol Chem , vol.389 , Issue.2 , pp. 99-109
    • Dong, Y.1    Matigian, N.2    Harvey, T.J.3    Samaratunga, H.4    Hooper, J.D.5    Clements, J.A.6
  • 40
    • 34247597726 scopus 로고    scopus 로고
    • Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin
    • 17354228 10.1002/cncr.22606 1:CAS:528:DC%2BD2sXlsF2nuro%3D
    • Johnson SK, Ramani VC, Hennings L, Haun RS (2007) Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin. Cancer 109(9):1811-1820
    • (2007) Cancer , vol.109 , Issue.9 , pp. 1811-1820
    • Johnson, S.K.1    Ramani, V.C.2    Hennings, L.3    Haun, R.S.4
  • 45
    • 0037884919 scopus 로고    scopus 로고
    • Human tissue kallikreins and testicular cancer
    • 12752266 10.1034/j.1600-0463.2003.11101261.x 1:CAS:528: DC%2BD3sXjs1entbg%3D
    • Luo LY, Yousef G, Diamandis EP (2003) Human tissue kallikreins and testicular cancer. APMIS 111(1):225-232
    • (2003) APMIS , vol.111 , Issue.1 , pp. 225-232
    • Luo, L.Y.1    Yousef, G.2    Diamandis, E.P.3
  • 46
    • 33745653318 scopus 로고    scopus 로고
    • Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells
    • 16800744 10.1515/BC.2006.102 1:CAS:528:DC%2BD28XmvVCiu7o%3D
    • Prezas P, Arlt MJ, Viktorov P, Soosaipillai A, Holzscheiter L, Schmitt M, Talieri M, Diamandis EP, Kruger A, Magdolen V (2006) Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells. Biol Chem 387(6):807-811
    • (2006) Biol Chem , vol.387 , Issue.6 , pp. 807-811
    • Prezas, P.1    Arlt, M.J.2    Viktorov, P.3    Soosaipillai, A.4    Holzscheiter, L.5    Schmitt, M.6    Talieri, M.7    Diamandis, E.P.8    Kruger, A.9    Magdolen, V.10
  • 49
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: Progress and potential
    • 9793760 10.1210/er.19.5.608 1:CAS:528:DyaK1cXntV2rtb8%3D
    • Duckworth WC, Bennett RG, Hamel FG (1998) Insulin degradation: progress and potential. Endocr Rev 19(5):608-624
    • (1998) Endocr Rev , vol.19 , Issue.5 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 50
    • 1842608440 scopus 로고    scopus 로고
    • Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids
    • 14764643 10.1373/clinchem.2003.029538 1:CAS:528:DC%2BD2cXivVCmsbc%3D
    • Kishi T, Soosaipillai A, Grass L, Little SP, Johnstone EM, Diamandis EP (2004) Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids. Clin Chem 50(4):709-716
    • (2004) Clin Chem , vol.50 , Issue.4 , pp. 709-716
    • Kishi, T.1    Soosaipillai, A.2    Grass, L.3    Little, S.P.4    Johnstone, E.M.5    Diamandis, E.P.6
  • 53
    • 0022294758 scopus 로고
    • Concentrations of protease and anti-protease in serum of patients with pancreatic cancer
    • 2581724 1:STN:280:DyaL2M3gt1egtQ%3D%3D
    • Buamah PK, Skillen AW (1985) Concentrations of protease and anti-protease in serum of patients with pancreatic cancer. Clin Chem 31(6):876-877
    • (1985) Clin Chem , vol.31 , Issue.6 , pp. 876-877
    • Buamah, P.K.1    Skillen, A.W.2
  • 54
    • 0034295588 scopus 로고    scopus 로고
    • Discovery of PAI-1 in plasma
    • 11203376 1:CAS:528:DC%2BD3cXosVSnt7o%3D
    • Wiman B (2000) Discovery of PAI-1 in plasma. Thromb Res 100(1):7-8
    • (2000) Thromb Res , vol.100 , Issue.1 , pp. 7-8
    • Wiman, B.1
  • 57
    • 0022396629 scopus 로고
    • Reaction of serine proteases with substituted 3-alkoxy-4- chloroisocoumarins and 3-alkoxy-7-amino-4-chloroisocoumarins: New reactive mechanism-based inhibitors
    • 3910097 10.1021/bi00346a028 1:CAS:528:DyaL28Xis1Cg
    • Harper JW, Powers JC (1985) Reaction of serine proteases with substituted 3-alkoxy-4-chloroisocoumarins and 3-alkoxy-7-amino-4-chloroisocoumarins: new reactive mechanism-based inhibitors. Biochemistry 24(25):7200-7213
    • (1985) Biochemistry , vol.24 , Issue.25 , pp. 7200-7213
    • Harper, J.W.1    Powers, J.C.2
  • 58
    • 77950818717 scopus 로고    scopus 로고
    • Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma
    • 20332224 10.1158/0008-5472.CAN-09-3415 1:CAS:528:DC%2BC3cXktFynsb4%3D
    • Dong Y, Tan OL, Loessner D, Stephens C, Walpole C, Boyle GM, Parsons PG, Clements JA (2010) Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma. Cancer Res 70(7):2624-2633
    • (2010) Cancer Res , vol.70 , Issue.7 , pp. 2624-2633
    • Dong, Y.1    Tan, O.L.2    Loessner, D.3    Stephens, C.4    Walpole, C.5    Boyle, G.M.6    Parsons, P.G.7    Clements, J.A.8
  • 59
    • 70350223357 scopus 로고
    • The inactivation of insulin by tissue extracts; The distribution and properties of insulin inactivating extracts
    • 18104389 1:CAS:528:DyaH1MXjsVeqtg%3D%3D
    • Mirsky IA, Broh-Kahn RH (1949) The inactivation of insulin by tissue extracts; the distribution and properties of insulin inactivating extracts. Arch Biochem 20(1):1-9
    • (1949) Arch Biochem , vol.20 , Issue.1 , pp. 1-9
    • Mirsky, I.A.1    Broh-Kahn, R.H.2
  • 60
    • 0025336126 scopus 로고
    • Identification of a serpin-enzyme complex receptor on human hepatoma cells and human monocytes
    • 2160076 10.1073/pnas.87.10.3753 1:CAS:528:DyaK3cXkt1Whu7c%3D
    • Perlmutter DH, Glover GI, Rivetna M, Schasteen CS, Fallon RJ (1990) Identification of a serpin-enzyme complex receptor on human hepatoma cells and human monocytes. Proc Natl Acad Sci USA 87(10):3753-3757
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.10 , pp. 3753-3757
    • Perlmutter, D.H.1    Glover, G.I.2    Rivetna, M.3    Schasteen, C.S.4    Fallon, R.J.5
  • 61
    • 0025130625 scopus 로고
    • Endocytosis and degradation of alpha 1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor
    • 2211587 1:CAS:528:DyaK3cXlvVyksro%3D
    • Perlmutter DH, Joslin G, Nelson P, Schasteen C, Adams SP, Fallon RJ (1990) Endocytosis and degradation of alpha 1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor. J Biol Chem 265(28):16713-16716
    • (1990) J Biol Chem , vol.265 , Issue.28 , pp. 16713-16716
    • Perlmutter, D.H.1    Joslin, G.2    Nelson, P.3    Schasteen, C.4    Adams, S.P.5    Fallon, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.