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Volumn 21, Issue 1, 2013, Pages 27-43

Receptors, endocytosis, and trafficking: The biological basis of targeted delivery of antisense and siRNA oligonucleotides

Author keywords

Antisense; Delivery; Endocytosis; Oligonucleotides; Receptors; SiRNA; Trafficking

Indexed keywords

ANTISENSE OLIGODEOXYNUCLEOTIDE; ASIALOGLYCOPROTEIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; INTEGRIN; LIPOPROTEIN RECEPTOR; RECEPTOR; SMALL INTERFERING RNA; TIROFIBAN; TYROSINE KINASE RECEPTOR;

EID: 84872038857     PISSN: 1061186X     EISSN: 10292330     Source Type: Journal    
DOI: 10.3109/1061186X.2012.740674     Document Type: Review
Times cited : (70)

References (159)
  • 1
    • 77958454568 scopus 로고    scopus 로고
    • Cationic nanosystems for the delivery of small interfering ribonucleic acid therapeutics: A focus on toxicogenomics
    • Akhtar S. (2010). Cationic nanosystems for the delivery of small interfering ribonucleic acid therapeutics: a focus on toxicogenomics. Expert Opin Drug Metab Toxicol, 6, 1347-1362.
    • (2010) Expert Opin Drug Metab Toxicol , vol.6 , pp. 1347-1362
    • Akhtar, S.1
  • 3
    • 77951957881 scopus 로고    scopus 로고
    • The biological efect of an antisense oligonucleotide depends on its route of endocytosis and trafcking
    • Alam MR, Ming X, Dixit V, Fisher M, Chen X, Juliano RL. (2010). The biological efect of an antisense oligonucleotide depends on its route of endocytosis and trafcking. Oligonucleotides, 20, 103-109.
    • (2010) Oligonucleotides , vol.20 , pp. 103-109
    • Alam, M.R.1    Ming, X.2    Dixit, V.3    Fisher, M.4    Chen, X.5    Juliano, R.L.6
  • 6
    • 78751705945 scopus 로고    scopus 로고
    • New links between vesicle coats and Rab-mediated vesicle targeting
    • Angers CG, Merz AJ. (2011). New links between vesicle coats and Rab-mediated vesicle targeting. Semin Cell Dev Biol, 22, 18-26.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 18-26
    • Angers, C.G.1    Merz, A.J.2
  • 7
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin AE, Stewart SA, Assoian RK, Juliano RL. (2001). Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J Cell Biol, 153, 273-282.
    • (2001) J Cell Biol , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 8
    • 14044267526 scopus 로고    scopus 로고
    • Mining the receptorome
    • Armbruster BN, Roth BL. (2005). Mining the receptorome. J Biol Chem, 280, 5129-5132.
    • (2005) J Biol Chem , vol.280 , pp. 5129-5132
    • Armbruster, B.N.1    Roth, B.L.2
  • 10
    • 0028040812 scopus 로고
    • Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
    • Batzer AG, Rotin D, Ureña JM, Skolnik EY, Schlessinger J. (1994). Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol Cell Biol, 14, 5192-5201.
    • (1994) Mol Cell Biol , vol.14 , pp. 5192-5201
    • Batzer, A.G.1    Rotin, D.2    Ureña, J.M.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 11
    • 0032899156 scopus 로고    scopus 로고
    • Albumin modifed with mannose 6-phosphate: A potential carrier for selective delivery of antifbrotic drugs to rat and human hepatic stellate cells
    • Beljaars L, Molema G, Weert B, Bonnema H, Olinga P, Groothuis GM, Meijer DK, Poelstra K. (1999). Albumin modifed with mannose 6-phosphate: A potential carrier for selective delivery of antifbrotic drugs to rat and human hepatic stellate cells. Hepatology, 29, 1486-1493.
    • (1999) Hepatology , vol.29 , pp. 1486-1493
    • Beljaars, L.1    Molema, G.2    Weert, B.3    Bonnema, H.4    Olinga, P.5    Groothuis, G.M.6    Meijer, D.K.7    Poelstra, K.8
  • 12
    • 77949512140 scopus 로고    scopus 로고
    • RNA targeting therapeutics: Molecular mechanisms of antisense oligonucleotides as a therapeutic platform
    • Bennett CF, Swayze EE. (2010). RNA targeting therapeutics: molecular mechanisms of antisense oligonucleotides as a therapeutic platform. Annu Rev Pharmacol Toxicol, 50, 259-293.
    • (2010) Annu Rev Pharmacol Toxicol , vol.50 , pp. 259-293
    • Bennett, C.F.1    Swayze, E.E.2
  • 13
    • 4043172801 scopus 로고    scopus 로고
    • Increased expression of urotensin II and its cognate receptor GPR14 in atherosclerotic lesions of the human aorta
    • Bousette N, Patel L, Douglas SA, Ohlstein EH, Giaid A. (2004). Increased expression of urotensin II and its cognate receptor GPR14 in atherosclerotic lesions of the human aorta. Atherosclerosis, 176, 117-123.
    • (2004) Atherosclerosis , vol.176 , pp. 117-123
    • Bousette, N.1    Patel, L.2    Douglas, S.A.3    Ohlstein, E.H.4    Giaid, A.5
  • 14
    • 0026541137 scopus 로고
    • Circulating integrins: α 5 β 1, α 6 β 4 and Mac-1, but not α 3 β 1 α 4 β 1 or LFA-1
    • Bretscher MS. (1992). Circulating integrins: α 5 β 1, α 6 β 4 and Mac-1, but not α 3 β 1, α 4 β 1 or LFA-1. EMBO J, 11, 405-410.
    • (1992) EMBO J , vol.11 , pp. 405-410
    • Bretscher, M.S.1
  • 16
    • 0022272786 scopus 로고
    • The receptor model for transport of cholesterol in plasma
    • Brown MS, Goldstein JL. (1985). The receptor model for transport of cholesterol in plasma. Ann N Y Acad Sci, 454, 178-182.
    • (1985) Ann N y Acad Sci , vol.454 , pp. 178-182
    • Brown, M.S.1    Goldstein, J.L.2
  • 17
    • 84856389509 scopus 로고    scopus 로고
    • RNA-based therapeutics: Current progress and future prospects
    • Burnett JC, Rossi JJ. (2012). RNA-based therapeutics: current progress and future prospects. Chem Biol, 19, 60-71.
    • (2012) Chem Biol , vol.19 , pp. 60-71
    • Burnett, J.C.1    Rossi, J.J.2
  • 21
    • 53749092962 scopus 로고    scopus 로고
    • Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
    • Caswell PT, Chan M, Lindsay AJ, McCafrey MW, Boettiger D, Norman JC. (2008). Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J Cell Biol, 183, 143-155.
    • (2008) J Cell Biol , vol.183 , pp. 143-155
    • Caswell, P.T.1    Chan, M.2    Lindsay, A.J.3    McCafrey, M.W.4    Boettiger, D.5    Norman, J.C.6
  • 22
  • 23
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M. (2001). Mammalian MAP kinase signalling cascades. Nature, 410, 37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 24
    • 33646057302 scopus 로고    scopus 로고
    • Multimodality imaging of tumor integrin αvβ3 expression
    • Chen X. (2006). Multimodality imaging of tumor integrin αvβ3 expression. Mini Rev Med Chem, 6, 227-234.
    • (2006) Mini Rev Med Chem , vol.6 , pp. 227-234
    • Chen, X.1
  • 25
    • 40849147041 scopus 로고    scopus 로고
    • EGFR antagonists in cancer treatment
    • Ciardiello F, Tortora G. (2008). EGFR antagonists in cancer treatment. N Engl J Med, 358, 1160-1174.
    • (2008) N Engl J Med , vol.358 , pp. 1160-1174
    • Ciardiello, F.1    Tortora, G.2
  • 26
    • 34548459014 scopus 로고    scopus 로고
    • Gastrin-releasing peptide receptor as a molecular target in experimental anticancer therapy
    • Cornelio DB, Roesler R, Schwartsmann G. (2007). Gastrin-releasing peptide receptor as a molecular target in experimental anticancer therapy. Ann Oncol, 18, 1457-1466.
    • (2007) Ann Oncol , vol.18 , pp. 1457-1466
    • Cornelio, D.B.1    Roesler, R.2    Schwartsmann, G.3
  • 27
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • Desgrosellier JS, Cheresh DA. (2010). Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer, 10, 9-22.
    • (2010) Nat Rev Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 29
    • 78649448612 scopus 로고    scopus 로고
    • Drug targeting to the kidney: Advances in the active targeting of therapeutics to proximal tubular cells
    • Dolman ME, Harmsen S, Storm G, Hennink WE, Kok RJ. (2010). Drug targeting to the kidney: Advances in the active targeting of therapeutics to proximal tubular cells. Adv Drug Deliv Rev, 62, 1344-1357.
    • (2010) Adv Drug Deliv Rev , vol.62 , pp. 1344-1357
    • Dolman, M.E.1    Harmsen, S.2    Storm, G.3    Hennink, W.E.4    Kok, R.J.5
  • 30
    • 0037042532 scopus 로고    scopus 로고
    • Congestive heart failure and expression of myocardial urotensin II
    • Douglas SA, Tayara L, Ohlstein EH, Halawa N, Giaid A. (2002). Congestive heart failure and expression of myocardial urotensin II. Lancet, 359, 1990-1997.
    • (2002) Lancet , vol.359 , pp. 1990-1997
    • Douglas, S.A.1    Tayara, L.2    Ohlstein, E.H.3    Halawa, N.4    Giaid, A.5
  • 31
    • 33748751670 scopus 로고    scopus 로고
    • Trafcking of G protein-coupled receptors
    • Drake MT, Shenoy SK, Lefkowitz RJ. (2006). Trafcking of G protein-coupled receptors. Circ Res, 99, 570-582.
    • (2006) Circ Res , vol.99 , pp. 570-582
    • Drake, M.T.1    Shenoy, S.K.2    Lefkowitz, R.J.3
  • 33
    • 18944400789 scopus 로고    scopus 로고
    • Raf-1 serine 338 phosphorylation plays a key role in adhesion-dependent activation of extracellular signal-regulated kinase by epidermal growth factor
    • Edin ML, Juliano RL. (2005). Raf-1 serine 338 phosphorylation plays a key role in adhesion-dependent activation of extracellular signal-regulated kinase by epidermal growth factor. Mol Cell Biol, 25, 4466-4475.
    • (2005) Mol Cell Biol , vol.25 , pp. 4466-4475
    • Edin, M.L.1    Juliano, R.L.2
  • 34
    • 0029585762 scopus 로고
    • Rab 7: An important regulator of late endocytic membrane trafc
    • Feng Y, Press B, Wandinger-Ness A. (1995). Rab 7: an important regulator of late endocytic membrane trafc. J Cell Biol, 131, 1435-1452.
    • (1995) J Cell Biol , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 35
    • 33845890639 scopus 로고    scopus 로고
    • Its a GPCR world
    • Filmore D. (2004). Its a GPCR world. Mod Drug Discov, 7, 24-28.
    • (2004) Mod Drug Discov , vol.7 , pp. 24-28
    • Filmore, D.1
  • 36
    • 79952987831 scopus 로고    scopus 로고
    • In search of the Holy Grail: Folate-targeted nanoparticles for cancer therapy
    • Garcia-Bennett A, Nees M, Fadeel B. (2011). In search of the Holy Grail: Folate-targeted nanoparticles for cancer therapy. Biochem Pharmacol, 81, 976-984.
    • (2011) Biochem Pharmacol , vol.81 , pp. 976-984
    • Garcia-Bennett, A.1    Nees, M.2    Fadeel, B.3
  • 37
    • 34547730701 scopus 로고    scopus 로고
    • In vivo evaluation and small-animal PET/CT of a prostate cancer mouse model using 64Cu bombesin analogs: Side-by-side comparison of the CB-TE2A and DOTA chelation systems
    • Garrison JC, Rold TL, Sieckman GL, Figueroa SD, Volkert WA, Jurisson SS, Hofman TJ. (2007). In vivo evaluation and small-animal PET/CT of a prostate cancer mouse model using 64Cu bombesin analogs: side-by-side comparison of the CB-TE2A and DOTA chelation systems. J Nucl Med, 48, 1327-1337.
    • (2007) J Nucl Med , vol.48 , pp. 1327-1337
    • Garrison, J.C.1    Rold, T.L.2    Sieckman, G.L.3    Figueroa, S.D.4    Volkert, W.A.5    Jurisson, S.S.6    Hofman, T.J.7
  • 39
    • 0029282131 scopus 로고
    • Nobel Lecture. G proteins and regulation of adenylyl cyclase
    • Gilman AG. (1995). Nobel Lecture. G proteins and regulation of adenylyl cyclase. Biosci Rep, 15, 65-97.
    • (1995) Biosci Rep , vol.15 , pp. 65-97
    • Gilman, A.G.1
  • 40
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defnes a clathrin-independent endocytic pathway in mammalian cells
    • Glebov OO, Bright NA, Nichols BJ. (2006). Flotillin-1 defnes a clathrin-independent endocytic pathway in mammalian cells. Nat Cell Biol, 8, 46-54.
    • (2006) Nat Cell Biol , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 41
    • 77953167957 scopus 로고    scopus 로고
    • Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor
    • Goh LK, Huang F, Kim W, Gygi S, Sorkin A. (2010). Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J Cell Biol, 189, 871-883.
    • (2010) J Cell Biol , vol.189 , pp. 871-883
    • Goh, L.K.1    Huang, F.2    Kim, W.3    Gygi, S.4    Sorkin, A.5
  • 42
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their efectors: Achieving specifcity in membrane trafc
    • Grosshans BL, Ortiz D, Novick P. (2006). Rabs and their efectors: achieving specifcity in membrane trafc. Proc Natl Acad Sci USA, 103, 11821-11827.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 43
    • 2342591455 scopus 로고    scopus 로고
    • The discovery of receptor tyrosine kinases: Targets for cancer therapy
    • Gschwind A, Fischer OM, Ullrich A. (2004). The discovery of receptor tyrosine kinases: targets for cancer therapy. Nat Rev Cancer, 4, 361-370.
    • (2004) Nat Rev Cancer , vol.4 , pp. 361-370
    • Gschwind, A.1    Fischer, O.M.2    Ullrich, A.3
  • 44
    • 79955493637 scopus 로고    scopus 로고
    • Integrins trafc rapidly via circular dorsal rufes and macropinocytosis during stimulated cell migration
    • Gu Z, Noss EH, Hsu VW, Brenner MB. (2011). Integrins trafc rapidly via circular dorsal rufes and macropinocytosis during stimulated cell migration. J Cell Biol, 193, 61-70.
    • (2011) J Cell Biol , vol.193 , pp. 61-70
    • Gu, Z.1    Noss, E.H.2    Hsu, V.W.3    Brenner, M.B.4
  • 45
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo W, Giancotti FG. (2004). Integrin signalling during tumour progression. Nat Rev Mol Cell Biol, 5, 816-826.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 46
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafcking and its potential implications
    • Hanyaloglu AC, von Zastrow M. (2008). Regulation of GPCRs by endocytic membrane trafcking and its potential implications. Annu Rev Pharmacol Toxicol, 48, 537-568.
    • (2008) Annu Rev Pharmacol Toxicol , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    Von Zastrow, M.2
  • 49
    • 33644823661 scopus 로고    scopus 로고
    • [32P]2-iodo-N6-methyl-(N)-methanocarba-2'-deoxyadenosine-3, '5'-bisphosphate ([32P]MRS2500), a novel radioligand for quantifcation of native P2Y1 receptors
    • Houston D, Ohno M, Nicholas RA, Jacobson KA, Harden TK. (2006). [32P]2-iodo-N6-methyl-(N)-methanocarba-2'-deoxyadenosine-3, '5'-bisphosphate ([32P]MRS2500), a novel radioligand for quantifcation of native P2Y1 receptors. Br J Pharmacol, 147, 459-467.
    • (2006) Br J Pharmacol , vol.147 , pp. 459-467
    • Houston, D.1    Ohno, M.2    Nicholas, R.A.3    Jacobson, K.A.4    Harden, T.K.5
  • 50
    • 77955057786 scopus 로고    scopus 로고
    • Molecules, mechanisms, and cellular roles of clathrin-independent endocytosis
    • Howes MT, Mayor S, Parton RG. (2010). Molecules, mechanisms, and cellular roles of clathrin-independent endocytosis. Curr Opin Cell Biol, 22, 519-527.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 519-527
    • Howes, M.T.1    Mayor, S.2    Parton, R.G.3
  • 52
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J, Helenius A. (2011). Endosome maturation. EMBO J, 30, 3481-3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 53
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling-crosstalk between integrins, Src and Rho
    • Huveneers S, Danen EH. (2009). Adhesion signaling-crosstalk between integrins, Src and Rho. J Cell Sci, 122, 1059-1069.
    • (2009) J Cell Sci , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 55
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. (2002a). Integrins: bidirectional, allosteric signaling machines. Cell, 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 56
    • 0036734093 scopus 로고    scopus 로고
    • A reevaluation of integrins as regulators of angiogenesis
    • Hynes RO. (2002b). A reevaluation of integrins as regulators of angiogenesis. Nat Med, 8, 918-921.
    • (2002) Nat Med , vol.8 , pp. 918-921
    • Hynes, R.O.1
  • 57
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes NE, Lane HA. (2005). ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer, 5, 341-354.
    • (2005) Nat Rev Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 58
    • 0020361562 scopus 로고
    • Epidermal growth factor receptors and efect of epidermal growth factor on growth of human breast cancer cells in long-term tissue culture
    • Imai Y, Leung CK, Friesen HG, Shiu R P. (1982). Epidermal growth factor receptors and efect of epidermal growth factor on growth of human breast cancer cells in long-term tissue culture. Cancer Res, 42, 4394-4398.
    • (1982) Cancer Res , vol.42 , pp. 4394-4398
    • Imai, Y.1    Leung, C.K.2    Friesen, H.G.3    Shiu, R.P.4
  • 59
    • 0036259277 scopus 로고    scopus 로고
    • α 4 integrin antagonists
    • Jackson DY. (2002). α 4 integrin antagonists. Curr Pharm Des, 8, 1229-1253.
    • (2002) Curr Pharm des , vol.8 , pp. 1229-1253
    • Jackson, D.Y.1
  • 60
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano RL. (2002). Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu Rev Pharmacol Toxicol, 42, 283-323.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 62
    • 67249122712 scopus 로고    scopus 로고
    • Biological barriers to therapy with antisense and siRNA oligonucleotides
    • Juliano R, Bauman J, Kang H, Ming X. (2009). Biological barriers to therapy with antisense and siRNA oligonucleotides. Mol Pharm, 6, 686-695.
    • (2009) Mol Pharm , vol.6 , pp. 686-695
    • Juliano, R.1    Bauman, J.2    Kang, H.3    Ming, X.4
  • 64
    • 84856834692 scopus 로고    scopus 로고
    • Cellular uptake and intracellular trafcking of antisense and siRNA oligonucleotides
    • Juliano RL, Ming X, Nakagawa O. (2012a). Cellular uptake and intracellular trafcking of antisense and siRNA oligonucleotides. Bioconjug Chem, 23, 147-157.
    • (2012) Bioconjug Chem , vol.23 , pp. 147-157
    • Juliano, R.L.1    Ming, X.2    Nakagawa, O.3
  • 65
    • 84860707063 scopus 로고    scopus 로고
    • The chemistry and biology of oligonucleotide conjugates
    • Juliano RL, Ming X, Nakagawa O. (2012b). The chemistry and biology of oligonucleotide conjugates. Acc Chem Res, 45, 1067-1076.
    • (2012) Acc Chem Res , vol.45 , pp. 1067-1076
    • Juliano, R.L.1    Ming, X.2    Nakagawa, O.3
  • 67
    • 51649130231 scopus 로고    scopus 로고
    • Receptor trafcking controls weak signal delivery: A strategy used by c-Met for STAT3 nuclear accumulation
    • Kermorgant S, Parker PJ. (2008). Receptor trafcking controls weak signal delivery: a strategy used by c-Met for STAT3 nuclear accumulation. J Cell Biol, 182, 855-863.
    • (2008) J Cell Biol , vol.182 , pp. 855-863
    • Kermorgant, S.1    Parker, P.J.2
  • 68
    • 63049113263 scopus 로고    scopus 로고
    • Defning macropinocytosis
    • Kerr MC, Teasdale RD. (2009). Defning macropinocytosis. Trafc, 10, 364-371.
    • (2009) Trafc , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 69
    • 43049125473 scopus 로고    scopus 로고
    • Trivalent, Gal/GalNAc-containing ligands designed for the asialoglycoprotein receptor
    • Khorev O, Stokmaier D, Schwardt O, Cutting B, Ernst B. (2008). Trivalent, Gal/GalNAc-containing ligands designed for the asialoglycoprotein receptor. Bioorg Med Chem, 16, 5216-5231.
    • (2008) Bioorg Med Chem , vol.16 , pp. 5216-5231
    • Khorev, O.1    Stokmaier, D.2    Schwardt, O.3    Cutting, B.4    Ernst, B.5
  • 71
    • 79960671811 scopus 로고    scopus 로고
    • Regulators of G-protein signaling and their Ga substrates: Promises and challenges in their use as drug discovery targets
    • Kimple AJ, Bosch DE, Giguère PM, Siderovski DP. (2011). Regulators of G-protein signaling and their Ga substrates: promises and challenges in their use as drug discovery targets. Pharmacol Rev, 63, 728-749.
    • (2011) Pharmacol Rev , vol.63 , pp. 728-749
    • Kimple, A.J.1    Bosch, D.E.2    Giguère, P.M.3    Siderovski, D.P.4
  • 72
    • 33746172167 scopus 로고    scopus 로고
    • Antibody targeting of long-circulating lipidic nanoparticles does not increase tumor localization but does increase internalization in animal models
    • Kirpotin DB, Drummond DC, Shao Y, Shalaby MR, Hong K, Nielsen UB, Marks JD, Benz CC, Park JW. (2006). Antibody targeting of long-circulating lipidic nanoparticles does not increase tumor localization but does increase internalization in animal models. Cancer Res, 66, 6732-6740.
    • (2006) Cancer Res , vol.66 , pp. 6732-6740
    • Kirpotin, D.B.1    Drummond, D.C.2    Shao, Y.3    Shalaby, M.R.4    Hong, K.5    Nielsen, U.B.6    Marks, J.D.7    Benz, C.C.8    Park, J.W.9
  • 73
    • 84880742193 scopus 로고    scopus 로고
    • Signal transduction by vascular endothelial growth factor receptors
    • Koch S, Claesson-Welsh L. (2012). Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harb Perspect Med, 2, a006502.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Koch, S.1    Claesson-Welsh, L.2
  • 74
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of β 1 integrins
    • Kornberg LJ, Earp HS, Turner CE, Prockop C, Juliano RL. (1991). Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of β 1 integrins. Proc Natl Acad Sci USA, 88, 8392-8396.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 75
    • 22044442973 scopus 로고    scopus 로고
    • Tyrosine kinases as targets for cancer therapy
    • Krause DS, Van Etten RA. (2005). Tyrosine kinases as targets for cancer therapy. N Engl J Med, 353, 172-187.
    • (2005) N Engl J Med , vol.353 , pp. 172-187
    • Krause, D.S.1    Van Etten, R.A.2
  • 76
    • 84864342346 scopus 로고    scopus 로고
    • P2Y12 inhibitors in acute coronary syndromes: How do we choose the best drug for our patients?
    • Kristensen SD, Grove EL, Hvas AM. (2012). P2Y12 inhibitors in acute coronary syndromes: how do we choose the best drug for our patients? Tromb Haemost, 108, 203-205.
    • (2012) Tromb Haemost , vol.108 , pp. 203-205
    • Kristensen, S.D.1    Grove, E.L.2    Hvas, A.M.3
  • 77
    • 64849106106 scopus 로고    scopus 로고
    • Receptor binding and cell entry of Old World arenaviruses reveal novel aspects of virus-host interaction
    • Kunz S. (2009). Receptor binding and cell entry of Old World arenaviruses reveal novel aspects of virus-host interaction. Virology, 387, 245-249.
    • (2009) Virology , vol.387 , pp. 245-249
    • Kunz, S.1
  • 78
    • 77957895194 scopus 로고    scopus 로고
    • Lipid rafts, caveolae, and their endocytosis
    • Lajoie P, Nabi IR. (2010). Lipid rafts, caveolae, and their endocytosis. Int Rev Cell Mol Biol, 282, 135-163.
    • (2010) Int Rev Cell Mol Biol , vol.282 , pp. 135-163
    • Lajoie, P.1    Nabi, I.R.2
  • 79
    • 62649169295 scopus 로고    scopus 로고
    • Quantitative modeling perspectives on the ErbB system of cell regulatory processes
    • Lazzara MJ, Laufenburger DA. (2009). Quantitative modeling perspectives on the ErbB system of cell regulatory processes. Exp Cell Res, 315, 717-725.
    • (2009) Exp Cell Res , vol.315 , pp. 717-725
    • Lazzara, M.J.1    Laufenburger, D.A.2
  • 80
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. (2010). Cell signaling by receptor tyrosine kinases. Cell, 141, 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 81
    • 0016235664 scopus 로고
    • The binding characteristics and number of β-adrenergic receptors on the turkey erythrocyte
    • Levitzki A, Atlas D, Steer ML. (1974). The binding characteristics and number of β-adrenergic receptors on the turkey erythrocyte. Proc Natl Acad Sci USA, 71, 2773-2776.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 2773-2776
    • Levitzki, A.1    Atlas, D.2    Steer, M.L.3
  • 82
    • 33644662506 scopus 로고    scopus 로고
    • Overexpression of G protein-coupled receptors in cancer cells: Involvement in tumor progression
    • Li S, Huang S, Peng SB. (2005). Overexpression of G protein-coupled receptors in cancer cells: involvement in tumor progression. Int J Oncol, 27, 1329-1339.
    • (2005) Int J Oncol , vol.27 , pp. 1329-1339
    • Li, S.1    Huang, S.2    Peng, S.B.3
  • 83
    • 0031003237 scopus 로고    scopus 로고
    • Cell anchorage permits efcient signal transduction between ras and its downstream kinases
    • Lin TH, Chen Q, Howe A, Juliano RL. (1997). Cell anchorage permits efcient signal transduction between ras and its downstream kinases. J Biol Chem, 272, 8849-8852.
    • (1997) J Biol Chem , vol.272 , pp. 8849-8852
    • Lin, T.H.1    Chen, Q.2    Howe, A.3    Juliano, R.L.4
  • 84
    • 79960944046 scopus 로고    scopus 로고
    • A nanoparticle for tumor targeted delivery of oligomers
    • Liu X, Wang Y, Hnatowich DJ. (2011). A nanoparticle for tumor targeted delivery of oligomers. Methods Mol Biol, 764, 91-105.
    • (2011) Methods Mol Biol , vol.764 , pp. 91-105
    • Liu, X.1    Wang, Y.2    Hnatowich, D.J.3
  • 85
    • 77954902702 scopus 로고    scopus 로고
    • Ubiquitination of α 5 β 1 integrin controls fbroblast migration through lysosomal degradation of fbronectin-integrin complexes
    • Lobert VH, Brech A, Pedersen NM, Wesche J, Oppelt A, Malerød L, Stenmark H. (2010). Ubiquitination of α 5 β 1 integrin controls fbroblast migration through lysosomal degradation of fbronectin-integrin complexes. Dev Cell, 19, 148-159.
    • (2010) Dev Cell , vol.19 , pp. 148-159
    • Lobert, V.H.1    Brech, A.2    Pedersen, N.M.3    Wesche, J.4    Oppelt, A.5    Malerød, L.6    Stenmark, H.7
  • 86
    • 67649849650 scopus 로고    scopus 로고
    • Folate-targeted therapeutic and imaging agents for cancer
    • Low PS, Kularatne SA. (2009). Folate-targeted therapeutic and imaging agents for cancer. Curr Opin Chem Biol, 13, 256-262.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 256-262
    • Low, P.S.1    Kularatne, S.A.2
  • 87
    • 79961101608 scopus 로고    scopus 로고
    • Competitive binding of Rab21 and p120RasGAP to integrins regulates receptor trafc and migration
    • Mai A, Veltel S, Pellinen T, Padzik A, Cofey E, Marjomäki V, Ivaska J. (2011). Competitive binding of Rab21 and p120RasGAP to integrins regulates receptor trafc and migration. J Cell Biol, 194, 291-306.
    • (2011) J Cell Biol , vol.194 , pp. 291-306
    • Mai, A.1    Veltel, S.2    Pellinen, T.3    Padzik, A.4    Cofey, E.5    Marjomäki, V.6    Ivaska, J.7
  • 88
    • 84865101799 scopus 로고    scopus 로고
    • Transport to late endosomes is required for efcient reovirus infection
    • Mainou BA, Dermody TS. (2012). Transport to late endosomes is required for efcient reovirus infection. J Virol, 86, 8346-8358.
    • (2012) J Virol , vol.86 , pp. 8346-8358
    • Mainou, B.A.1    Dermody, T.S.2
  • 90
    • 77955053223 scopus 로고    scopus 로고
    • Signaling endosomes: Seeing is believing
    • Miaczynska M, Bar-Sagi D. (2010). Signaling endosomes: seeing is believing. Curr Opin Cell Biol, 22, 535-540.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 535-540
    • Miaczynska, M.1    Bar-Sagi, D.2
  • 91
    • 80255122951 scopus 로고    scopus 로고
    • Integrin targeted therapeutics
    • Millard M, Odde S, Neamati N. (2011). Integrin targeted therapeutics. Teranostics, 1, 154-188.
    • (2011) Teranostics , vol.1 , pp. 154-188
    • Millard, M.1    Odde, S.2    Neamati, N.3
  • 92
    • 78049363846 scopus 로고    scopus 로고
    • Intracellular delivery of an antisense oligonucleotide via endocytosis of a G protein-coupled receptor
    • Ming X, Alam MR, Fisher M, Yan Y, Chen X, Juliano RL. (2010). Intracellular delivery of an antisense oligonucleotide via endocytosis of a G protein-coupled receptor. Nucleic Acids Res, 38, 6567-6576.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6567-6576
    • Ming, X.1    Alam, M.R.2    Fisher, M.3    Yan, Y.4    Chen, X.5    Juliano, R.L.6
  • 93
    • 79960098388 scopus 로고    scopus 로고
    • Unconventional internalization mechanisms underlying functional delivery of antisense oligonucleotides via cationic lipoplexes and polyplexes
    • Ming X, Sato K, Juliano RL. (2011). Unconventional internalization mechanisms underlying functional delivery of antisense oligonucleotides via cationic lipoplexes and polyplexes. J Control Release, 153, 83-92.
    • (2011) J Control Release , vol.153 , pp. 83-92
    • Ming, X.1    Sato, K.2    Juliano, R.L.3
  • 97
    • 84863878959 scopus 로고    scopus 로고
    • Cross talk among TGF-ß signaling pathways, integrins, and the extracellular matrix
    • Munger JS, Sheppard D. (2011). Cross talk among TGF-ß signaling pathways, integrins, and the extracellular matrix. Cold Spring Harb Perspect Biol, 3, a005017.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Munger, J.S.1    Sheppard, D.2
  • 98
    • 77954298422 scopus 로고    scopus 로고
    • Targeted intracellular delivery of antisense oligonucleotides via conjugation with small-molecule ligands
    • Nakagawa O, Ming X, Huang L, Juliano RL. (2010). Targeted intracellular delivery of antisense oligonucleotides via conjugation with small-molecule ligands. J Am Chem Soc, 132, 8848-8849.
    • (2010) J Am Chem Soc , vol.132 , pp. 8848-8849
    • Nakagawa, O.1    Ming, X.2    Huang, L.3    Juliano, R.L.4
  • 100
    • 33747395791 scopus 로고    scopus 로고
    • Crosstalk coregulation mechanisms of G protein-coupled receptors and receptor tyrosine kinases
    • Natarajan K, Berk BC. (2006). Crosstalk coregulation mechanisms of G protein-coupled receptors and receptor tyrosine kinases. Methods Mol Biol, 332, 51-77.
    • (2006) Methods Mol Biol , vol.332 , pp. 51-77
    • Natarajan, K.1    Berk, B.C.2
  • 101
    • 84863903929 scopus 로고    scopus 로고
    • Nucleic acid delivery: The missing pieces of the puzzle?
    • Nguyen J, Szoka FC. (2012). Nucleic acid delivery: the missing pieces of the puzzle? Acc Chem Res, 45, 1153-1162.
    • (2012) Acc Chem Res , vol.45 , pp. 1153-1162
    • Nguyen, J.1    Szoka, F.C.2
  • 102
    • 79959271064 scopus 로고    scopus 로고
    • Why integrin as a primary target for imaging and therapy
    • Niu G, Chen X. (2011). Why integrin as a primary target for imaging and therapy. Teranostics, 1, 30-47.
    • (2011) Teranostics , vol.1 , pp. 30-47
    • Niu, G.1    Chen, X.2
  • 103
    • 84860490667 scopus 로고    scopus 로고
    • Dynamics of receptor trafcking in tumorigenicity
    • Parachoniak CA, Park M. (2012). Dynamics of receptor trafcking in tumorigenicity. Trends Cell Biol, 22, 231-240.
    • (2012) Trends Cell Biol , vol.22 , pp. 231-240
    • Parachoniak, C.A.1    Park, M.2
  • 104
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The frst ten years
    • Parsons JT. (2003). Focal adhesion kinase: the frst ten years. J Cell Sci, 116, 1409-1416.
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 105
    • 84856756381 scopus 로고    scopus 로고
    • Entry at the trans-face of the Golgi
    • DOI: 10.1101/cshperspect.a005272
    • Pfefer SR. (2011). Entry at the trans-face of the Golgi. Cold Spring Harb Perspect Biol, 3. DOI: 10.1101/cshperspect.a005272
    • (2011) Cold Spring Harb Perspect Biol , pp. 3
    • Pfefer, S.R.1
  • 106
    • 0021271957 scopus 로고
    • Cell attachment activity of fbronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. (1984). Cell attachment activity of fbronectin can be duplicated by small synthetic fragments of the molecule. Nature, 309, 30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 108
    • 0029132693 scopus 로고
    • Quantifcation of signalling components and amplifcation in the β-adrenergic-receptor-adenylate cyclase pathway in isolated adult rat ventricular myocytes
    • Post SR, Hilal-Dandan R, Urasawa K, Brunton LL, Insel PA. (1995). Quantifcation of signalling components and amplifcation in the β-adrenergic-receptor-adenylate cyclase pathway in isolated adult rat ventricular myocytes. Biochem J, 311, 75-80.
    • (1995) Biochem J , vol.311 , pp. 75-80
    • Post, S.R.1    Hilal-Dandan, R.2    Urasawa, K.3    Brunton, L.L.4    Insel, P.A.5
  • 109
    • 12744280988 scopus 로고    scopus 로고
    • Involvement of a cytoplasmic-tail serine cluster in urotensin II receptor internalization
    • Proulx CD, Simaan M, Escher E, Laporte SA, Guillemette G, Leduc R. (2005). Involvement of a cytoplasmic-tail serine cluster in urotensin II receptor internalization. Biochem J, 385, 115-123.
    • (2005) Biochem J , vol.385 , pp. 115-123
    • Proulx, C.D.1    Simaan, M.2    Escher, E.3    Laporte, S.A.4    Guillemette, G.5    Leduc, R.6
  • 110
    • 79960944056 scopus 로고    scopus 로고
    • Receptor tyrosine kinase-G-protein-coupled receptor signalling platforms: Out of the shadow?
    • Pyne NJ, Pyne S. (2011). Receptor tyrosine kinase-G-protein-coupled receptor signalling platforms: out of the shadow? Trends Pharmacol Sci, 32, 443-450.
    • (2011) Trends Pharmacol Sci , vol.32 , pp. 443-450
    • Pyne, N.J.1    Pyne, S.2
  • 111
    • 58149237830 scopus 로고    scopus 로고
    • Modelling cellular signalling systems
    • Rangamani P, Iyengar R. (2008). Modelling cellular signalling systems. Essays Biochem, 45, 83-94.
    • (2008) Essays Biochem , vol.45 , pp. 83-94
    • Rangamani, P.1    Iyengar, R.2
  • 115
    • 33947527882 scopus 로고    scopus 로고
    • Cardiac GPCRs: GPCR signaling in healthy and failing hearts
    • Salazar NC, Chen J, Rockman HA. (2007). Cardiac GPCRs: GPCR signaling in healthy and failing hearts. Biochim Biophys Acta, 1768, 1006-1018.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1006-1018
    • Salazar, N.C.1    Chen, J.2    Rockman, H.A.3
  • 116
    • 0028098065 scopus 로고
    • Transforming growth factor-β 1 and mannose 6-phosphate/insulin-like growth factor-II receptor expression during intrahepatic bile duct hyperplasia and biliary fbrosis in the rat
    • Saperstein LA, Jirtle RL, Farouk M, Tompson HJ, Chung KS, Meyers WC. (1994). Transforming growth factor-β 1 and mannose 6-phosphate/insulin-like growth factor-II receptor expression during intrahepatic bile duct hyperplasia and biliary fbrosis in the rat. Hepatology, 19, 412-417.
    • (1994) Hepatology , vol.19 , pp. 412-417
    • Saperstein, L.A.1    Jirtle, R.L.2    Farouk, M.3    Tompson, H.J.4    Chung, K.S.5    Meyers, W.C.6
  • 118
    • 0025290037 scopus 로고
    • Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function
    • Savage B, Marzec UM, Chao BH, Harker LA, Maraganore JM, Ruggeri ZM. (1990). Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function. J Biol Chem, 265, 11766-11772.
    • (1990) J Biol Chem , vol.265 , pp. 11766-11772
    • Savage, B.1    Marzec, U.M.2    Chao, B.H.3    Harker, L.A.4    Maraganore, J.M.5    Ruggeri, Z.M.6
  • 122
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • Schwartz MA. (2010). Integrins and extracellular matrix in mechanotransduction. Cold Spring Harb Perspect Biol, 2, a005066.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Schwartz, M.A.1
  • 123
    • 0025217957 scopus 로고
    • Internalization of the fbronectin receptor is a constitutive process
    • Sczekan MM, Juliano RL. (1990). Internalization of the fbronectin receptor is a constitutive process. J Cell Physiol, 142, 574-580.
    • (1990) J Cell Physiol , vol.142 , pp. 574-580
    • Sczekan, M.M.1    Juliano, R.L.2
  • 124
    • 79952279499 scopus 로고    scopus 로고
    • Hepatic stellate cell (vitamin A-storing cell) and its relative-past, present and future
    • Senoo H, Yoshikawa K, Morii M, Miura M, Imai K, Mezaki Y. (2010). Hepatic stellate cell (vitamin A-storing cell) and its relative-past, present and future. Cell Biol Int, 34, 1247-1272.
    • (2010) Cell Biol Int , vol.34 , pp. 1247-1272
    • Senoo, H.1    Yoshikawa, K.2    Morii, M.3    Miura, M.4    Imai, K.5    Mezaki, Y.6
  • 126
    • 0142026204 scopus 로고    scopus 로고
    • Terapeutic antagonists and conformational regulation of integrin function
    • Shimaoka M, Springer TA. (2003). Terapeutic antagonists and conformational regulation of integrin function. Nat Rev Drug Discov, 2, 703-716.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 703-716
    • Shimaoka, M.1    Springer, T.A.2
  • 128
    • 80052359992 scopus 로고    scopus 로고
    • Emerging paradigms of ß-arrestin-dependent seven transmembrane receptor signaling
    • Shukla AK, Xiao K, Lefkowitz RJ. (2011). Emerging paradigms of ß-arrestin-dependent seven transmembrane receptor signaling. Trends Biochem Sci, 36, 457-469.
    • (2011) Trends Biochem Sci , vol.36 , pp. 457-469
    • Shukla, A.K.1    Xiao, K.2    Lefkowitz, R.J.3
  • 129
    • 83555166124 scopus 로고    scopus 로고
    • Subcellular fate and of-target efects of siRNA, shRNA, and miRNA
    • Singh S, Narang AS, Mahato RI. (2011). Subcellular fate and of-target efects of siRNA, shRNA, and miRNA. Pharm Res, 28, 2996-3015.
    • (2011) Pharm Res , vol.28 , pp. 2996-3015
    • Singh, S.1    Narang, A.S.2    Mahato, R.I.3
  • 130
    • 64549134275 scopus 로고    scopus 로고
    • Deciphering the code of innate immunity recognition of siRNAs
    • Sioud M. (2009). Deciphering the code of innate immunity recognition of siRNAs. Methods Mol Biol, 487, 41-59.
    • (2009) Methods Mol Biol , vol.487 , pp. 41-59
    • Sioud, M.1
  • 131
    • 77951684623 scopus 로고    scopus 로고
    • Signal transduction by protease-activated receptors
    • Soh UJ, Dores MR, Chen B, Trejo J. (2010). Signal transduction by protease-activated receptors. Br J Pharmacol, 160, 191-203.
    • (2010) Br J Pharmacol , vol.160 , pp. 191-203
    • Soh, U.J.1    Dores, M.R.2    Chen, B.3    Trejo, J.4
  • 132
    • 54849372300 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafcking of ErbBs
    • Sorkin A, Goh LK. (2008). Endocytosis and intracellular trafcking of ErbBs. Exp Cell Res, 314, 3093-3106.
    • (2008) Exp Cell Res , vol.314 , pp. 3093-3106
    • Sorkin, A.1    Goh, L.K.2
  • 133
    • 69249137477 scopus 로고    scopus 로고
    • Endocytosis and signalling: Intertwining molecular networks
    • Sorkin A, von Zastrow M. (2009). Endocytosis and signalling: intertwining molecular networks. Nat Rev Mol Cell Biol, 10, 609-622.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 609-622
    • Sorkin, A.1    Von Zastrow, M.2
  • 136
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle trafc
    • Stenmark H. (2009). Rab GTPases as coordinators of vesicle trafc. Nat Rev Mol Cell Biol, 10, 513-525.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 137
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • Stockert RJ. (1995). The asialoglycoprotein receptor: relationships between structure, function, and expression. Physiol Rev, 75, 591-609.
    • (1995) Physiol Rev , vol.75 , pp. 591-609
    • Stockert, R.J.1
  • 138
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli CH, Akhtar N. (2009). Signal co-operation between integrins and other receptor systems. Biochem J, 418, 491-506.
    • (2009) Biochem J , vol.418 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 139
    • 42049094825 scopus 로고    scopus 로고
    • Another ligand fshing for G protein-coupled receptor 14. Discovery of urotensin II-related peptide in the rat brain
    • Sugo T, Mori M. (2008). Another ligand fshing for G protein-coupled receptor 14. Discovery of urotensin II-related peptide in the rat brain. Peptides, 29, 809-812.
    • (2008) Peptides , vol.29 , pp. 809-812
    • Sugo, T.1    Mori, M.2
  • 140
    • 84857345852 scopus 로고    scopus 로고
    • Development and validation of competition binding assays for afnity to the extracellular matrix receptors, a(v)β(3) and a(IIb) β(3) integrin
    • Szabo AM, Howell NR, Pellegrini P, Greguric I, Katsifs A. (2012). Development and validation of competition binding assays for afnity to the extracellular matrix receptors, a(v)β(3) and a(IIb) β(3) integrin. Anal Biochem, 423, 70-77.
    • (2012) Anal Biochem , vol.423 , pp. 70-77
    • Szabo, A.M.1    Howell, N.R.2    Pellegrini, P.3    Greguric, I.4    Katsifs, A.5
  • 141
    • 84858033688 scopus 로고    scopus 로고
    • Molecular considerations for development of phage antibody libraries
    • Tohidkia MR, Barar J, Asadi F, Omidi Y. (2012). Molecular considerations for development of phage antibody libraries. J Drug Target, 20, 195-208.
    • (2012) J Drug Target , vol.20 , pp. 195-208
    • Tohidkia, M.R.1    Barar, J.2    Asadi, F.3    Omidi, Y.4
  • 144
    • 33746070441 scopus 로고    scopus 로고
    • Intravenously administered short interfering RNA accumulates in the kidney and selectively suppresses gene function in renal proximal tubules
    • van de Water FM, Boerman OC, Wouterse AC, Peters JG, Russel FG, Masereeuw R. (2006). Intravenously administered short interfering RNA accumulates in the kidney and selectively suppresses gene function in renal proximal tubules. Drug Metab Dispos, 34, 1393-1397.
    • (2006) Drug Metab Dispos , vol.34 , pp. 1393-1397
    • Van De Water, F.M.1    Boerman, O.C.2    Wouterse, A.C.3    Peters, J.G.4    Russel, F.G.5    Masereeuw, R.6
  • 146
    • 84858279102 scopus 로고    scopus 로고
    • At the crossroads of chemistry and cell biology: Inhibiting membrane trafc by small molecules
    • DOI: 10.1111/j.1600-0854.2011.01292.x
    • von Kleist L, Haucke V. (2011). At the Crossroads of Chemistry and Cell Biology: Inhibiting Membrane Trafc by Small Molecules. Trafc. DOI: 10.1111/j.1600-0854.2011.01292.x
    • (2011) Trafc
    • Von Kleist, L.1    Haucke, V.2
  • 147
    • 0023147391 scopus 로고
    • Distribution and properties of β-adrenergic receptors in human iris-ciliary body
    • Wax MB, Molinof PB. (1987). Distribution and properties of β-adrenergic receptors in human iris-ciliary body. Invest Ophthalmol Vis Sci, 28, 420-430.
    • (1987) Invest Ophthalmol Vis Sci , vol.28 , pp. 420-430
    • Wax, M.B.1    Molinof, P.B.2
  • 148
    • 79955527964 scopus 로고    scopus 로고
    • Regulation of membrane trafc by integrin signaling
    • Wickström SA, Fässler R. (2011). Regulation of membrane trafc by integrin signaling. Trends Cell Biol, 21, 266-273.
    • (2011) Trends Cell Biol , vol.21 , pp. 266-273
    • Wickström, S.A.1    Fässler, R.2
  • 149
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • Wolfe BL, Trejo J. (2007). Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Trafc, 8, 462-470.
    • (2007) Trafc , vol.8 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 153
    • 5144222594 scopus 로고    scopus 로고
    • Role of urotensin II in peripheral tissue as an autocrine/paracrine growth factor
    • Yoshimoto T, Matsushita M, Hirata Y. (2004). Role of urotensin II in peripheral tissue as an autocrine/paracrine growth factor. Peptides, 25, 1775-1781.
    • (2004) Peptides , vol.25 , pp. 1775-1781
    • Yoshimoto, T.1    Matsushita, M.2    Hirata, Y.3
  • 154
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky AN, Gready JE. (2005). The C-type lectin-like domain superfamily. FEBS J, 272, 6179-6217.
    • (2005) FEBS J , vol.272 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 156
    • 0033396950 scopus 로고    scopus 로고
    • Inhibition of tumor growth and metastasis by targeting tumor-associated angiogenesis with antagonists to the receptors of vascular endothelial growth factor
    • Zhu Z, Witte L. (1999). Inhibition of tumor growth and metastasis by targeting tumor-associated angiogenesis with antagonists to the receptors of vascular endothelial growth factor. Invest New Drugs, 17, 195-212.
    • (1999) Invest New Drugs , vol.17 , pp. 195-212
    • Zhu, Z.1    Witte, L.2
  • 157
    • 33749371071 scopus 로고    scopus 로고
    • The role of urotensin II in cardiovascular and renal physiology and diseases
    • Zhu YC, Zhu YZ, Moore PK. (2006). The role of urotensin II in cardiovascular and renal physiology and diseases. Br J Pharmacol, 148, 884-901.
    • (2006) Br J Pharmacol , vol.148 , pp. 884-901
    • Zhu, Y.C.1    Zhu, Y.Z.2    Moore, P.K.3
  • 158
    • 78649260473 scopus 로고    scopus 로고
    • Targeted delivery of siRNA to hepatocytes and hepatic stellate cells by bioconjugation
    • Zhu L, Mahato RI. (2010). Targeted delivery of siRNA to hepatocytes and hepatic stellate cells by bioconjugation. Bioconjug Chem, 21, 2119-2127.
    • (2010) Bioconjug Chem , vol.21 , pp. 2119-2127
    • Zhu, L.1    Mahato, R.I.2
  • 159
    • 63049107267 scopus 로고    scopus 로고
    • Systems biology of growth factor-induced receptor endocytosis
    • Zwang Y, Yarden Y. (2009). Systems biology of growth factor-induced receptor endocytosis. Trafc, 10, 349-363.
    • (2009) Trafc , vol.10 , pp. 349-363
    • Zwang, Y.1    Yarden, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.