메뉴 건너뛰기




Volumn 17, Issue 1, 2015, Pages 134-143

Strategic Approaches to Optimizing Peptide ADME Properties

Author keywords

ADME; peptides; pharmacokinetics; proteolysis; renal clearance

Indexed keywords

CYCLOSPORIN A; LEUPRORELIN; LIRAGLUTIDE; OCTREOTIDE; PEGINESATIDE; PENETRATION ENHANCING AGENT; PEPTIDE; PLASMA PROTEIN; PROTEINASE INHIBITOR;

EID: 84922005015     PISSN: None     EISSN: 15507416     Source Type: Journal    
DOI: 10.1208/s12248-014-9687-3     Document Type: Article
Times cited : (490)

References (121)
  • 1
    • 0036717194 scopus 로고    scopus 로고
    • Opinion: the druggable genome
    • COI: 1:CAS:528:DC%2BD38XmslamtrY%3D, PID: 12209152
    • Hopkins AL, Groom CR. Opinion: the druggable genome. Nat Rev Drug Discov. 2002;1(9):727–30.
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.9 , pp. 727-730
    • Hopkins, A.L.1    Groom, C.R.2
  • 2
    • 84893119472 scopus 로고    scopus 로고
    • Multifaceted roles of disulfide bonds. Peptides as therapeutics
    • COI: 1:CAS:528:DC%2BC3sXhs1yls7nJ
    • Gongora-Benitez M, Tulla-Puche J, Albericio F. Multifaceted roles of disulfide bonds. Peptides as therapeutics. Chem Rev (Washington, DC, U S). 2014;114(2):901–26.
    • (2014) Chem Rev (Washington, DC, U S) , vol.114 , Issue.2 , pp. 901-926
    • Gongora-Benitez, M.1    Tulla-Puche, J.2    Albericio, F.3
  • 3
    • 84893107423 scopus 로고    scopus 로고
    • Peptide-based drug development
    • Sun L. Peptide-based drug development. Mod Chem Appl. 2013;1(1):1–2.
    • (2013) Mod Chem Appl , vol.1 , Issue.1 , pp. 1-2
    • Sun, L.1
  • 4
    • 84868020147 scopus 로고    scopus 로고
    • Peptides as therapeutics with enhanced bioactivity
    • COI: 1:CAS:528:DC%2BC3sXhtlens74%3D, PID: 22830348
    • Goodwin D, Simerska P, Toth I. Peptides as therapeutics with enhanced bioactivity. Curr Med Chem. 2012;19(26):4451–61.
    • (2012) Curr Med Chem , vol.19 , Issue.26 , pp. 4451-4461
    • Goodwin, D.1    Simerska, P.2    Toth, I.3
  • 5
    • 84871394690 scopus 로고    scopus 로고
    • The future of peptide-based drugs
    • COI: 1:CAS:528:DC%2BC3sXlt1yktA%3D%3D, PID: 23253135
    • Craik DJ, Fairlie DP, Liras S, Price D. The future of peptide-based drugs. Chem Biol Drug Des. 2013;81(1):136–47.
    • (2013) Chem Biol Drug Des , vol.81 , Issue.1 , pp. 136-147
    • Craik, D.J.1    Fairlie, D.P.2    Liras, S.3    Price, D.4
  • 6
    • 84883256420 scopus 로고    scopus 로고
    • Future directions for peptide therapeutics development
    • COI: 1:CAS:528:DC%2BC3sXpsV2ksbs%3D, PID: 23726889
    • Kaspar AA, Reichert JM. Future directions for peptide therapeutics development. Drug Discov Today. 2013;18(17–18):807–17.
    • (2013) Drug Discov Today , vol.18 , Issue.17-18 , pp. 807-817
    • Kaspar, A.A.1    Reichert, J.M.2
  • 7
    • 74149094591 scopus 로고    scopus 로고
    • Synthetic therapeutic peptides: science and market
    • COI: 1:CAS:528:DC%2BC3cXnsV2iug%3D%3D, PID: 19879957
    • Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M. Synthetic therapeutic peptides: science and market. Drug Discov Today. 2010;15(1/2):40–56.
    • (2010) Drug Discov Today , vol.15 , Issue.1-2 , pp. 40-56
    • Vlieghe, P.1    Lisowski, V.2    Martinez, J.3    Khrestchatisky, M.4
  • 8
    • 2942560767 scopus 로고    scopus 로고
    • Phage display-derived peptides as therapeutic alternatives to antibodies
    • COI: 1:CAS:528:DC%2BD2cXks1ert74%3D, PID: 15183160
    • Ladner RC, Sato AK, Gorzelany J, De Souza M. Phage display-derived peptides as therapeutic alternatives to antibodies. Drug Discov Today. 2004;9(12):525–9.
    • (2004) Drug Discov Today , vol.9 , Issue.12 , pp. 525-529
    • Ladner, R.C.1    Sato, A.K.2    Gorzelany, J.3    De Souza, M.4
  • 9
    • 84904057699 scopus 로고    scopus 로고
    • Challenges for therapeutic peptides part 1: on the inside, looking out
    • Lax R, Meenan C. Challenges for therapeutic peptides part 1: on the inside, looking out. Innovations Pharm Technol. 2012;42:54–6.
    • (2012) Innovations Pharm Technol , vol.42 , pp. 54-56
    • Lax, R.1    Meenan, C.2
  • 10
    • 84890462907 scopus 로고    scopus 로고
    • Challenges for therapeutic peptides part 2: delivery systems
    • COI: 1:CAS:528:DC%2BC3sXhslCkurk%3D, 6
    • Lax R, Meenan C. Challenges for therapeutic peptides part 2: delivery systems. Innovations Pharm Technol. 2012;43:42–4. 6.
    • (2012) Innovations Pharm Technol , vol.43 , pp. 42-44
    • Lax, R.1    Meenan, C.2
  • 11
    • 0037667047 scopus 로고    scopus 로고
    • Innovation: large-scale manufacture of peptide therapeutics by chemical synthesis
    • COI: 1:CAS:528:DC%2BD3sXks1Oqsr4%3D, PID: 12815383
    • Bray BL. Innovation: large-scale manufacture of peptide therapeutics by chemical synthesis. Nat Rev Drug Discov. 2003;2(7):587–93.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.7 , pp. 587-593
    • Bray, B.L.1
  • 12
    • 84884159004 scopus 로고    scopus 로고
    • Oral GLP-1 modulators for the treatment of diabetes
    • COI: 1:CAS:528:DC%2BC3sXhvVGqu77I
    • Edmonds DJ, Price DA. Oral GLP-1 modulators for the treatment of diabetes. Annu Rep Med Chem. 2013;48:119–30.
    • (2013) Annu Rep Med Chem , vol.48 , pp. 119-130
    • Edmonds, D.J.1    Price, D.A.2
  • 13
    • 33750482579 scopus 로고    scopus 로고
    • Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: successful in silico prediction of the relative permeabilities of cyclic peptides
    • COI: 1:CAS:528:DC%2BD28XhtVCmur3I, PID: 17061890
    • Rezai T, Bock JE, Zhou MV, Kalyanaraman C, Lokey RS, Jacobson MP. Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: successful in silico prediction of the relative permeabilities of cyclic peptides. J Am Chem Soc. 2006;128(43):14073–80.
    • (2006) J Am Chem Soc , vol.128 , Issue.43 , pp. 14073-14080
    • Rezai, T.1    Bock, J.E.2    Zhou, M.V.3    Kalyanaraman, C.4    Lokey, R.S.5    Jacobson, M.P.6
  • 14
    • 0141997761 scopus 로고    scopus 로고
    • Emerging trends in oral delivery of peptide and protein drugs
    • COI: 1:CAS:528:DC%2BD3sXovVaktbw%3D, PID: 14584523
    • Mahato RI, Narang AS, Thoma L, Miller DD. Emerging trends in oral delivery of peptide and protein drugs. Crit Rev Ther Drug Carrier Syst. 2003;20(2–3):153–214.
    • (2003) Crit Rev Ther Drug Carrier Syst , vol.20 , Issue.2-3 , pp. 153-214
    • Mahato, R.I.1    Narang, A.S.2    Thoma, L.3    Miller, D.D.4
  • 15
    • 84885229737 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacokinetic-pharmacodynamic correlations of therapeutic peptides
    • COI: 1:CAS:528:DC%2BC3sXhvVSmt77I, PID: 23719681
    • Diao L, Meibohm B. Pharmacokinetics and pharmacokinetic-pharmacodynamic correlations of therapeutic peptides. Clin Pharmacokinet. 2013;52(10):855–68.
    • (2013) Clin Pharmacokinet , vol.52 , Issue.10 , pp. 855-868
    • Diao, L.1    Meibohm, B.2
  • 16
    • 84867025688 scopus 로고    scopus 로고
    • Optimizing PK properties of cyclic peptides: the effect of side chain substitutions on permeability and clearance
    • COI: 1:CAS:528:DC%2BC38XhsVWns7%2FM
    • Rand AC, Leung SSF, Eng H, Rotter CJ, Sharma R, Kalgutkar AS, et al. Optimizing PK properties of cyclic peptides: the effect of side chain substitutions on permeability and clearance. Med Chem Comm. 2012;3(10):1282–9.
    • (2012) Med Chem Comm , vol.3 , Issue.10 , pp. 1282-1289
    • Rand, A.C.1    Leung, S.S.F.2    Eng, H.3    Rotter, C.J.4    Sharma, R.5    Kalgutkar, A.S.6
  • 17
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • COI: 1:CAS:528:DC%2BD28Xls1egsrw%3D, PID: 16622600
    • Werle M, Bernkop-Schnuerch A. Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids. 2006;30(4):351–67.
    • (2006) Amino Acids , vol.30 , Issue.4 , pp. 351-367
    • Werle, M.1    Bernkop-Schnuerch, A.2
  • 18
    • 0025744310 scopus 로고
    • Peptide and protein drugs: II. Non-parenteral routes of delivery
    • COI: 1:CAS:528:DyaK3MXmtl2ns7g%3D
    • Zhou XH, Li Wan Po A. Peptide and protein drugs: II. Non-parenteral routes of delivery. Int J Pharm. 1991;75(2–3):117–30.
    • (1991) Int J Pharm , vol.75 , Issue.2-3 , pp. 117-130
    • Zhou, X.H.1    Li Wan Po, A.2
  • 19
    • 0030444901 scopus 로고    scopus 로고
    • Interpatient variability in bioavailability is related to the extent of absorption: implications for bioavailability and bioequivalence studies
    • COI: 1:CAS:528:DyaK2sXms1eqsQ%3D%3D
    • Hellriegel ET, Bjornsson TD, Hauck WW. Interpatient variability in bioavailability is related to the extent of absorption: implications for bioavailability and bioequivalence studies. Clin Pharmacol Ther (St Louis). 1996;60(6):601–7.
    • (1996) Clin Pharmacol Ther (St Louis) , vol.60 , Issue.6 , pp. 601-607
    • Hellriegel, E.T.1    Bjornsson, T.D.2    Hauck, W.W.3
  • 20
    • 84866723704 scopus 로고    scopus 로고
    • Overcoming poor permeability: translating permeation enhancers for oral peptide delivery
    • COI: 1:CAS:528:DC%2BC38XhtFKnsLfI
    • Maher S, Brayden DJ. Overcoming poor permeability: translating permeation enhancers for oral peptide delivery. Drug Discov Today: Technol. 2012;9(2):e113–e9.
    • (2012) Drug Discov Today: Technol , vol.9 , Issue.2 , pp. e113-e119
    • Maher, S.1    Brayden, D.J.2
  • 21
    • 84873081796 scopus 로고    scopus 로고
    • Insight of current technologies for oral delivery of proteins and peptides
    • COI: 1:CAS:528:DC%2BC38XhtFKnsLfN
    • Chin J, Foyez Mahmud KA, Kim SE, Park K, Byun Y. Insight of current technologies for oral delivery of proteins and peptides. Drug Discov Today: Technol. 2012;9(2):e105–e12.
    • (2012) Drug Discov Today: Technol , vol.9 , Issue.2 , pp. e105-e112
    • Chin, J.1    Foyez Mahmud, K.A.2    Kim, S.E.3    Park, K.4    Byun, Y.5
  • 22
    • 72949106918 scopus 로고    scopus 로고
    • Pharmacokinetics of biotech drugs: peptides, proteins and monoclonal antibodies
    • COI: 1:CAS:528:DC%2BC3cXhsFKlu70%3D, PID: 19702530
    • Lin JH. Pharmacokinetics of biotech drugs: peptides, proteins and monoclonal antibodies. Curr Drug Metab. 2009;10(7):661–91.
    • (2009) Curr Drug Metab , vol.10 , Issue.7 , pp. 661-691
    • Lin, J.H.1
  • 23
    • 0036073843 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of depot leuprorelin
    • COI: 1:CAS:528:DC%2BD38Xmt12mtbk%3D, PID: 12083977
    • Periti P, Mazzei T, Mini E. Clinical pharmacokinetics of depot leuprorelin. Clin Pharmacokinet. 2002;41(7):485–504.
    • (2002) Clin Pharmacokinet , vol.41 , Issue.7 , pp. 485-504
    • Periti, P.1    Mazzei, T.2    Mini, E.3
  • 24
    • 77953909559 scopus 로고    scopus 로고
    • Hydrophobicity of peptides containing D-amino acids
    • COI: 1:CAS:528:DC%2BC3cXot1ant7k%3D, PID: 20564676
    • Munegumi T. Hydrophobicity of peptides containing D-amino acids. Chem Biodivers. 2010;7(6):1670–9.
    • (2010) Chem Biodivers , vol.7 , Issue.6 , pp. 1670-1679
    • Munegumi, T.1
  • 25
    • 0347301796 scopus 로고    scopus 로고
    • Relationships between structure and high-throughput screening permeability of peptide derivatives and related compounds with artificial membranes: application to prediction of Caco-2 cell permeability
    • COI: 1:CAS:528:DC%2BD3sXhtVSjtb7O, PID: 14697791
    • Ano R, Kimura Y, Shima M, Matsuno R, Ueno T, Akamatsu M. Relationships between structure and high-throughput screening permeability of peptide derivatives and related compounds with artificial membranes: application to prediction of Caco-2 cell permeability. Bioorg Med Chem. 2004;12(1):257–64.
    • (2004) Bioorg Med Chem , vol.12 , Issue.1 , pp. 257-264
    • Ano, R.1    Kimura, Y.2    Shima, M.3    Matsuno, R.4    Ueno, T.5    Akamatsu, M.6
  • 26
    • 0037474028 scopus 로고    scopus 로고
    • No entry for TAT(44–57) into liposomes and intact MDCK cells: novel approach to study membrane permeation of cell-penetrating peptides
    • COI: 1:CAS:528:DC%2BD3sXltFOjsw%3D%3D
    • Kramer SD, Wunderli-Allenspach H. No entry for TAT(44–57) into liposomes and intact MDCK cells: novel approach to study membrane permeation of cell-penetrating peptides. Biochim Biophys Acta Biomembr. 2003;1609(2):161–9.
    • (2003) Biochim Biophys Acta Biomembr , vol.1609 , Issue.2 , pp. 161-169
    • Kramer, S.D.1    Wunderli-Allenspach, H.2
  • 27
    • 0036288748 scopus 로고    scopus 로고
    • Characterization of the efflux transporter(s) responsible for restricting intestinal mucosa permeation of the coumarinic acid-based cyclic prodrug of the opioid peptide DADLE
    • COI: 1:CAS:528:DC%2BD38XltVSgsb0%3D, PID: 12134948
    • Tang F, Borchardt RT. Characterization of the efflux transporter(s) responsible for restricting intestinal mucosa permeation of the coumarinic acid-based cyclic prodrug of the opioid peptide DADLE. Pharm Res. 2002;19(6):787–93.
    • (2002) Pharm Res , vol.19 , Issue.6 , pp. 787-793
    • Tang, F.1    Borchardt, R.T.2
  • 28
    • 0346040397 scopus 로고    scopus 로고
    • Relationship between structure and permeability of dipeptide derivatives containing tryptophan and related compounds across human intestinal epithelial (Caco-2) cells
    • COI: 1:CAS:528:DC%2BD3sXhtVSjtb7N, PID: 14697790
    • Ano R, Kimura Y, Urakami M, Shima M, Matsuno R, Ueno T, et al. Relationship between structure and permeability of dipeptide derivatives containing tryptophan and related compounds across human intestinal epithelial (Caco-2) cells. Bioorg Med Chem. 2004;12(1):249–55.
    • (2004) Bioorg Med Chem , vol.12 , Issue.1 , pp. 249-255
    • Ano, R.1    Kimura, Y.2    Urakami, M.3    Shima, M.4    Matsuno, R.5    Ueno, T.6
  • 29
    • 0032903489 scopus 로고    scopus 로고
    • Use of Caco-2 cells and LC/MS/MS to screen a peptide combinatorial library for permeable structures
    • COI: 1:CAS:528:DyaK1MXivVeqsA%3D%3D, PID: 10205607
    • Stevenson CL, Augustijns PF, Hendren RW. Use of Caco-2 cells and LC/MS/MS to screen a peptide combinatorial library for permeable structures. Int J Pharm. 1999;177(1):103–15.
    • (1999) Int J Pharm , vol.177 , Issue.1 , pp. 103-115
    • Stevenson, C.L.1    Augustijns, P.F.2    Hendren, R.W.3
  • 30
    • 84864182405 scopus 로고    scopus 로고
    • Intestinal permeability of cyclic peptides: common key backbone motifs identified
    • COI: 1:CAS:528:DC%2BC38Xpt1Cisbw%3D, PID: 22737969
    • Beck JG, Chatterjee J, Laufer B, Kiran MU, Frank AO, Neubauer S, et al. Intestinal permeability of cyclic peptides: common key backbone motifs identified. J Am Chem Soc. 2012;134(29):12125–33.
    • (2012) J Am Chem Soc , vol.134 , Issue.29 , pp. 12125-12133
    • Beck, J.G.1    Chatterjee, J.2    Laufer, B.3    Kiran, M.U.4    Frank, A.O.5    Neubauer, S.6
  • 31
    • 23944470195 scopus 로고    scopus 로고
    • Delineation of human peptide transporter 1 (hPepT1)-mediated uptake and transport of substrates with varying transporter affinities utilizing stably transfected hPepT1/Madin-Darby canine kidney clones and Caco-2 cells
    • COI: 1:CAS:528:DC%2BD2MXpvFSqs78%3D, PID: 15901802
    • Bhardwaj RK, Herrera-Ruiz D, Sinko PJ, Gudmundsson OS, Knipp G. Delineation of human peptide transporter 1 (hPepT1)-mediated uptake and transport of substrates with varying transporter affinities utilizing stably transfected hPepT1/Madin-Darby canine kidney clones and Caco-2 cells. J Pharmacol Exp Ther. 2005;314(3):1093–100.
    • (2005) J Pharmacol Exp Ther , vol.314 , Issue.3 , pp. 1093-1100
    • Bhardwaj, R.K.1    Herrera-Ruiz, D.2    Sinko, P.J.3    Gudmundsson, O.S.4    Knipp, G.5
  • 32
    • 13944269270 scopus 로고    scopus 로고
    • A novel high-throughput PepT1 transporter assay differentiates between substrates and antagonists
    • COI: 1:CAS:528:DC%2BD2cXitFWiug%3D%3D, PID: 15832502
    • Faria TN, Timoszyk JK, Stouch TR, Vig BS, Landowski CP, Amidon GL, et al. A novel high-throughput PepT1 transporter assay differentiates between substrates and antagonists. Mol Pharm. 2004;1(1):67–76.
    • (2004) Mol Pharm , vol.1 , Issue.1 , pp. 67-76
    • Faria, T.N.1    Timoszyk, J.K.2    Stouch, T.R.3    Vig, B.S.4    Landowski, C.P.5    Amidon, G.L.6
  • 33
    • 34248202064 scopus 로고    scopus 로고
    • Peptide transporter substrate identification during permeability screening in drug discovery: comparison of transfected MDCK-hPepT1 cells to Caco-2 cells
    • COI: 1:CAS:528:DC%2BD2sXls1ahsbs%3D
    • Balimane PV, Chong S, Patel K, Quan Y, Timoszyk J, Han Y-H, et al. Peptide transporter substrate identification during permeability screening in drug discovery: comparison of transfected MDCK-hPepT1 cells to Caco-2 cells. Arch Pharmacal Res. 2007;30(4):507–18.
    • (2007) Arch Pharmacal Res , vol.30 , Issue.4 , pp. 507-518
    • Balimane, P.V.1    Chong, S.2    Patel, K.3    Quan, Y.4    Timoszyk, J.5    Han, Y.-H.6
  • 34
    • 84861709697 scopus 로고    scopus 로고
    • Sodium dependent multivitamin transporter (SMVT): a potential target for drug delivery
    • COI: 1:CAS:528:DC%2BC38XovFersr4%3D, PID: 22420308
    • Vadlapudi AD, Vadlapatla RK, Mitra AK. Sodium dependent multivitamin transporter (SMVT): a potential target for drug delivery. Curr Drug Targets. 2012;13(7):994–1003.
    • (2012) Curr Drug Targets , vol.13 , Issue.7 , pp. 994-1003
    • Vadlapudi, A.D.1    Vadlapatla, R.K.2    Mitra, A.K.3
  • 35
    • 0033014577 scopus 로고    scopus 로고
    • Prediction of membrane permeability to peptides from calculated dynamic molecular surface properties
    • COI: 1:CAS:528:DyaK1MXhvFylsbo%3D, PID: 10100304
    • Stenberg P, Luthman K, Artursson P. Prediction of membrane permeability to peptides from calculated dynamic molecular surface properties. Pharm Res. 1999;16(2):205–12.
    • (1999) Pharm Res , vol.16 , Issue.2 , pp. 205-212
    • Stenberg, P.1    Luthman, K.2    Artursson, P.3
  • 36
    • 84859788959 scopus 로고    scopus 로고
    • Predicting and improving the membrane permeability of peptidic small molecules
    • COI: 1:CAS:528:DC%2BC38Xjt1Ogtrg%3D, PID: 22394492
    • Rafi SB, Hearn BR, Vedantham P, Jacobson MP, Renslo AR. Predicting and improving the membrane permeability of peptidic small molecules. J Med Chem. 2012;55(7):3163–9.
    • (2012) J Med Chem , vol.55 , Issue.7 , pp. 3163-3169
    • Rafi, S.B.1    Hearn, B.R.2    Vedantham, P.3    Jacobson, M.P.4    Renslo, A.R.5
  • 37
    • 81855173578 scopus 로고    scopus 로고
    • Effect of dose escalation on the in vivo oral absorption and disposition of glycylsarcosine in wild-type and Pept1 knockout mice
    • COI: 1:CAS:528:DC%2BC3MXhsFCrurfP, PID: 21880829
    • Jappar D, Hu Y, Smith DE. Effect of dose escalation on the in vivo oral absorption and disposition of glycylsarcosine in wild-type and Pept1 knockout mice. Drug Metab Dispos. 2011;39(12):2250–7.
    • (2011) Drug Metab Dispos , vol.39 , Issue.12 , pp. 2250-2257
    • Jappar, D.1    Hu, Y.2    Smith, D.E.3
  • 38
    • 85015728949 scopus 로고    scopus 로고
    • Handbook of LC-MS bioanalysis: best practices, experimental protocols
    • Li W, Zhang J, Tse FLS. Handbook of LC-MS bioanalysis: best practices, experimental protocols, and regulations 2013.
    • (2013) and regulations
    • Li, W.1    Zhang, J.2    Tse, F.L.S.3
  • 41
    • 78650633249 scopus 로고    scopus 로고
    • Strategies in quantitative LC-MS/MS analysis of unstable small molecules in biological matrices
    • PID: 21204113
    • Li W, Zhang J, Tse FLS. Strategies in quantitative LC-MS/MS analysis of unstable small molecules in biological matrices. Biomed Chromatogr. 2011;25(1–2):258–77.
    • (2011) Biomed Chromatogr , vol.25 , Issue.1-2 , pp. 258-277
    • Li, W.1    Zhang, J.2    Tse, F.L.S.3
  • 42
    • 79953114938 scopus 로고    scopus 로고
    • Unique challenges of providing bioanalytical support for biological therapeutic pharmacokinetic programs
    • COI: 1:CAS:528:DC%2BC3MXjs1Sgs74%3D, PID: 21388264
    • Nowatzke WL, Rogers K, Wells E, Bowsher RR, Ray C, Unger S. Unique challenges of providing bioanalytical support for biological therapeutic pharmacokinetic programs. Bioanalysis. 2011;3(5):509–21.
    • (2011) Bioanalysis , vol.3 , Issue.5 , pp. 509-521
    • Nowatzke, W.L.1    Rogers, K.2    Wells, E.3    Bowsher, R.R.4    Ray, C.5    Unger, S.6
  • 43
    • 77949799227 scopus 로고    scopus 로고
    • Intramolecular hydrogen bonding in medicinal chemistry
    • COI: 1:CAS:528:DC%2BC3cXit1Clur8%3D, PID: 20175530
    • Kuhn B, Mohr P, Stahl M. Intramolecular hydrogen bonding in medicinal chemistry. J Med Chem. 2010;53(6):2601–11.
    • (2010) J Med Chem , vol.53 , Issue.6 , pp. 2601-2611
    • Kuhn, B.1    Mohr, P.2    Stahl, M.3
  • 45
    • 33644644973 scopus 로고    scopus 로고
    • Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers
    • COI: 1:CAS:528:DC%2BD28XhtVGqu7k%3D, PID: 16492015
    • Rezai T, Yu B, Millhauser GL, Jacobson MP, Lokey RS. Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers. J Am Chem Soc. 2006;128(8):2510–1.
    • (2006) J Am Chem Soc , vol.128 , Issue.8 , pp. 2510-2511
    • Rezai, T.1    Yu, B.2    Millhauser, G.L.3    Jacobson, M.P.4    Lokey, R.S.5
  • 46
    • 80054853098 scopus 로고    scopus 로고
    • On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds
    • COI: 1:CAS:528:DC%2BC3MXht1anurjL, PID: 21946276
    • White TR, Renzelman CM, Rand AC, Rezai T, McEwen CM, Gelev VM, et al. On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat Chem Biol. 2011;7(11):810–7.
    • (2011) Nat Chem Biol , vol.7 , Issue.11 , pp. 810-817
    • White, T.R.1    Renzelman, C.M.2    Rand, A.C.3    Rezai, T.4    McEwen, C.M.5    Gelev, V.M.6
  • 47
    • 79960153981 scopus 로고    scopus 로고
    • Intramolecular hydrogen bonding to improve membrane permeability and absorption in beyond rule of five chemical space
    • COI: 1:CAS:528:DC%2BC3MXotl2gt7o%3D
    • Alex A, Millan DS, Perez M, Wakenhut F, Whitlock GA. Intramolecular hydrogen bonding to improve membrane permeability and absorption in beyond rule of five chemical space. Med Chem Comm. 2011;2(7):669–74.
    • (2011) Med Chem Comm , vol.2 , Issue.7 , pp. 669-674
    • Alex, A.1    Millan, D.S.2    Perez, M.3    Wakenhut, F.4    Whitlock, G.A.5
  • 48
    • 84864631153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: classes, origin, and current landscape
    • COI: 1:CAS:528:DC%2BC38Xltl2qsrc%3D, PID: 22465171
    • Milletti F. Cell-penetrating peptides: classes, origin, and current landscape. Drug Discov Today. 2012;17(15–16):850–60.
    • (2012) Drug Discov Today , vol.17 , Issue.15-16 , pp. 850-860
    • Milletti, F.1
  • 49
    • 79551584772 scopus 로고    scopus 로고
    • Pharmacology, biodistribution, and efficacy of GPCR-based pepducins in disease models
    • COI: 1:CAS:528:DC%2BC3cXhsFyktbbI, Cell-Penetrating Peptides
    • Tressel SL, Koukos G, Tchernychev B, Jacques SL, Covic L, Kuliopulos A. Pharmacology, biodistribution, and efficacy of GPCR-based pepducins in disease models. Methods Mol Biol (N Y, NY, U S). 2011;683:259–75. Cell-Penetrating Peptides.
    • (2011) Methods Mol Biol (N Y, NY, U S) , vol.683 , pp. 259-275
    • Tressel, S.L.1    Koukos, G.2    Tchernychev, B.3    Jacques, S.L.4    Covic, L.5    Kuliopulos, A.6
  • 50
    • 0032709221 scopus 로고    scopus 로고
    • Preparation, purification, and characterization of a reversibly lipidized desmopressin with potentiated antidiuretic activity
    • COI: 1:CAS:528:DyaK1MXnt1Ggs70%3D, PID: 10571271
    • Wang J, Shen D, Shen W-C. Preparation, purification, and characterization of a reversibly lipidized desmopressin with potentiated antidiuretic activity. Pharm Res. 1999;16(11):1674–9.
    • (1999) Pharm Res , vol.16 , Issue.11 , pp. 1674-1679
    • Wang, J.1    Shen, D.2    Shen, W.-C.3
  • 51
    • 0037467203 scopus 로고    scopus 로고
    • Reversible lipidization for the oral delivery of salmon calcitonin
    • COI: 1:CAS:528:DC%2BD3sXitVGhsLo%3D, PID: 12644363
    • Wang J, Chow D, Heiati H, Shen W-C. Reversible lipidization for the oral delivery of salmon calcitonin. J Control Release. 2003;88(3):369–80.
    • (2003) J Control Release , vol.88 , Issue.3 , pp. 369-380
    • Wang, J.1    Chow, D.2    Heiati, H.3    Shen, W.-C.4
  • 52
    • 0034690960 scopus 로고    scopus 로고
    • Gastric retention and stability of lipidized Bowman-Birk protease inhibitor in mice
    • COI: 1:CAS:528:DC%2BD3cXmvVyktbo%3D, PID: 11011993
    • Wang J, Shen W-C. Gastric retention and stability of lipidized Bowman-Birk protease inhibitor in mice. Int J Pharm. 2000;204(1–2):111–6.
    • (2000) Int J Pharm , vol.204 , Issue.1-2 , pp. 111-116
    • Wang, J.1    Shen, W.-C.2
  • 53
    • 38949154100 scopus 로고    scopus 로고
    • Preparation, characterization, and application of biotinylated and biotin-PEGylated glucagon-like peptide-1 analogues for enhanced oral delivery
    • COI: 1:CAS:528:DC%2BD2sXhsVejtbvE
    • Chae SY, Jin C-H, Shin HJ, Youn YS, Lee S, Lee KC. Preparation, characterization, and application of biotinylated and biotin-PEGylated glucagon-like peptide-1 analogues for enhanced oral delivery. Bioconjugate Chem. 2008;19(1):334–41.
    • (2008) Bioconjugate Chem , vol.19 , Issue.1 , pp. 334-341
    • Chae, S.Y.1    Jin, C.-H.2    Shin, H.J.3    Youn, Y.S.4    Lee, S.5    Lee, K.C.6
  • 54
    • 84875611012 scopus 로고    scopus 로고
    • Synthesis, characterization and pharmacodynamics of vitamin-B12-conjugated glucagon-like peptide-1
    • COI: 1:CAS:528:DC%2BC38XhslKmtLrJ, PID: 23203941
    • Clardy-James S, Chepurny OG, Leech CA, Holz GG, Doyle RP. Synthesis, characterization and pharmacodynamics of vitamin-B12-conjugated glucagon-like peptide-1. ChemMedChem. 2013;8(4):582–6.
    • (2013) ChemMedChem , vol.8 , Issue.4 , pp. 582-586
    • Clardy-James, S.1    Chepurny, O.G.2    Leech, C.A.3    Holz, G.G.4    Doyle, R.P.5
  • 55
    • 78650557242 scopus 로고    scopus 로고
    • Vitamin B12 in drug delivery: breaking through the barriers to a B12 bioconjugate pharmaceutical
    • COI: 1:CAS:528:DC%2BC3cXhs1Srt7jL, PID: 21128823
    • Clardy SM, Allis DG, Fairchild TJ, Doyle RP. Vitamin B12 in drug delivery: breaking through the barriers to a B12 bioconjugate pharmaceutical. Expert Opin Drug Deliv. 2011;8(1):127–40.
    • (2011) Expert Opin Drug Deliv , vol.8 , Issue.1 , pp. 127-140
    • Clardy, S.M.1    Allis, D.G.2    Fairchild, T.J.3    Doyle, R.P.4
  • 56
    • 52149119477 scopus 로고    scopus 로고
    • Protein and peptide drug delivery: oral approaches
    • PID: 20046732
    • Shaji J, Patole V. Protein and peptide drug delivery: oral approaches. Indian J Pharm Sci. 2008;70(3):269–77.
    • (2008) Indian J Pharm Sci , vol.70 , Issue.3 , pp. 269-277
    • Shaji, J.1    Patole, V.2
  • 57
    • 0033816196 scopus 로고    scopus 로고
    • Intestinal permeation enhancers
    • COI: 1:CAS:528:DC%2BD3cXis12ktbw%3D, PID: 10737905
    • Aungst BJ. Intestinal permeation enhancers. J Pharm Sci. 2000;89(4):429–42.
    • (2000) J Pharm Sci , vol.89 , Issue.4 , pp. 429-442
    • Aungst, B.J.1
  • 58
    • 46749122375 scopus 로고    scopus 로고
    • Safe and effective permeation enhancers for oral drug delivery
    • COI: 1:CAS:528:DC%2BD1cXot1Whs78%3D, PID: 18058001
    • Whitehead K, Karr N, Mitragotri S. Safe and effective permeation enhancers for oral drug delivery. Pharm Res. 2008;25(8):1782–8.
    • (2008) Pharm Res , vol.25 , Issue.8 , pp. 1782-1788
    • Whitehead, K.1    Karr, N.2    Mitragotri, S.3
  • 59
    • 0031014265 scopus 로고    scopus 로고
    • In vitro models for selection of development candidates. Permeability studies to define mechanisms of absorption enhancement
    • COI: 1:CAS:528:DyaK2sXktlKltA%3D%3D
    • LeCluyse EL, Sutton SC. In vitro models for selection of development candidates. Permeability studies to define mechanisms of absorption enhancement. Adv Drug Deliv Rev. 1997;23(1–3):163–83.
    • (1997) Adv Drug Deliv Rev , vol.23 , Issue.1-3 , pp. 163-183
    • LeCluyse, E.L.1    Sutton, S.C.2
  • 60
    • 79955006040 scopus 로고    scopus 로고
    • Restoration of rat colonic epithelium after in situ intestinal instillation of the absorption promoter, sodium caprate
    • COI: 1:CAS:528:DC%2BC3cXpvFOmtbw%3D, PID: 22816121
    • Wang X, Maher S, Brayden DJ. Restoration of rat colonic epithelium after in situ intestinal instillation of the absorption promoter, sodium caprate. Ther Deliv. 2010;1(1):75–82.
    • (2010) Ther Deliv , vol.1 , Issue.1 , pp. 75-82
    • Wang, X.1    Maher, S.2    Brayden, D.J.3
  • 61
    • 0037393955 scopus 로고    scopus 로고
    • Challenges for the oral delivery of macromolecules
    • COI: 1:CAS:528:DC%2BD3sXisFWkt7s%3D, PID: 12669028
    • Goldberg M, Gomez-Orellana I. Challenges for the oral delivery of macromolecules. Nat Rev Drug Discov. 2003;2(4):289–95.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.4 , pp. 289-295
    • Goldberg, M.1    Gomez-Orellana, I.2
  • 62
    • 28644432882 scopus 로고    scopus 로고
    • Comparative genomic analysis of human and chimpanzee proteases
    • COI: 1:CAS:528:DC%2BD2MXht12jurvP, PID: 16162398
    • Puente XS, Gutierrez-Fernandez A, Ordonez GR, Hillier LW, Lopez-Otin C. Comparative genomic analysis of human and chimpanzee proteases. Genomics. 2005;86(6):638–47.
    • (2005) Genomics , vol.86 , Issue.6 , pp. 638-647
    • Puente, X.S.1    Gutierrez-Fernandez, A.2    Ordonez, G.R.3    Hillier, L.W.4    Lopez-Otin, C.5
  • 63
    • 0028657017 scopus 로고
    • Enzymatic barriers for GI peptide and protein delivery
    • COI: 1:CAS:528:DyaK2MXlsVClu7g%3D, PID: 7600588
    • Woodley JF. Enzymatic barriers for GI peptide and protein delivery. Crit Rev Ther Drug Carrier Syst. 1994;11(2–3):61–95.
    • (1994) Crit Rev Ther Drug Carrier Syst , vol.11 , Issue.2-3 , pp. 61-95
    • Woodley, J.F.1
  • 64
    • 0027070864 scopus 로고
    • Peptide stability in drug development: a comparison of peptide reactivity in different biological media
    • COI: 1:CAS:528:DyaK38Xls1emsrg%3D, PID: 1403714
    • Powell MF, Grey H, Gaeta F, Sette A, Colon S. Peptide stability in drug development: a comparison of peptide reactivity in different biological media. J Pharm Sci. 1992;81(8):731–5.
    • (1992) J Pharm Sci , vol.81 , Issue.8 , pp. 731-735
    • Powell, M.F.1    Grey, H.2    Gaeta, F.3    Sette, A.4    Colon, S.5
  • 65
    • 0027208560 scopus 로고
    • Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum
    • COI: 1:CAS:528:DyaK3sXmslymsLY%3D, PID: 8234161
    • Powell MF, Stewart T, Otvos Jr L, Urge L, Gaeta FCA, Sette A, et al. Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum. Pharm Res. 1993;10(9):1268–73.
    • (1993) Pharm Res , vol.10 , Issue.9 , pp. 1268-1273
    • Powell, M.F.1    Stewart, T.2    Otvos, L.3    Urge, L.4    Gaeta, F.C.A.5    Sette, A.6
  • 66
    • 46449085181 scopus 로고    scopus 로고
    • Alternative stabilities of a proline-rich antibacterial peptide in vitro and in vivo
    • COI: 1:CAS:528:DC%2BD1cXot1ehsL8%3D, PID: 18413862
    • Noto PB, Abbadessa G, Cassone M, Mateo GD, Agelan A, Wade JD, et al. Alternative stabilities of a proline-rich antibacterial peptide in vitro and in vivo. Protein Sci. 2008;17(7):1249–55.
    • (2008) Protein Sci , vol.17 , Issue.7 , pp. 1249-1255
    • Noto, P.B.1    Abbadessa, G.2    Cassone, M.3    Mateo, G.D.4    Agelan, A.5    Wade, J.D.6
  • 67
    • 84905401781 scopus 로고    scopus 로고
    • Pharmacokinetics and metabolism studies on the glucagon-like peptide-1 (GLP-1)-derived metabolite GLP-1(9–36)amide in male Beagle dogs
    • COI: 1:CAS:528:DC%2BC2cXht1GntL7E, PID: 24588343
    • Eng H, Sharma R, McDonald TS, Landis MS, Stevens BD, Kalgutkar AS. Pharmacokinetics and metabolism studies on the glucagon-like peptide-1 (GLP-1)-derived metabolite GLP-1(9–36)amide in male Beagle dogs. Xenobiotica. 2014;44(9):842–8.
    • (2014) Xenobiotica , vol.44 , Issue.9 , pp. 842-848
    • Eng, H.1    Sharma, R.2    McDonald, T.S.3    Landis, M.S.4    Stevens, B.D.5    Kalgutkar, A.S.6
  • 68
    • 84888581721 scopus 로고    scopus 로고
    • In vitro metabolism of the glucagon-like peptide-1 (GLP-1)-derived metabolites GLP-1(9–36)amide and GLP-1(28–36)amide in mouse and human hepatocytes
    • COI: 1:CAS:528:DC%2BC3sXhvVCjtbjL, PID: 24056839
    • Sharma R, McDonald TS, Eng H, Limberakis C, Stevens BD, Patel S, et al. In vitro metabolism of the glucagon-like peptide-1 (GLP-1)-derived metabolites GLP-1(9–36)amide and GLP-1(28–36)amide in mouse and human hepatocytes. Drug Metab Dispos. 2013;41(12):2148–57.
    • (2013) Drug Metab Dispos , vol.41 , Issue.12 , pp. 2148-2157
    • Sharma, R.1    McDonald, T.S.2    Eng, H.3    Limberakis, C.4    Stevens, B.D.5    Patel, S.6
  • 69
    • 0036257686 scopus 로고    scopus 로고
    • Converting a peptide into a drug: strategies to improve stability and bioavailability
    • COI: 1:CAS:528:DC%2BD38XjtlKjtbk%3D, PID: 11966456
    • Adessi C, Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem. 2002;9(9):963–78.
    • (2002) Curr Med Chem , vol.9 , Issue.9 , pp. 963-978
    • Adessi, C.1    Soto, C.2
  • 70
    • 58149194055 scopus 로고    scopus 로고
    • Structure-activity relationship and metabolic stability studies of backbone cyclization and N-methylation of melanocortin peptides
    • COI: 1:CAS:528:DC%2BD1cXht1ygtbfI, PID: 18655141
    • Linde Y, Ovadia O, Safrai E, Xiang Z, Portillo FP, Shalev DE, et al. Structure-activity relationship and metabolic stability studies of backbone cyclization and N-methylation of melanocortin peptides. Biopolymers. 2008;90(5):671–82.
    • (2008) Biopolymers , vol.90 , Issue.5 , pp. 671-682
    • Linde, Y.1    Ovadia, O.2    Safrai, E.3    Xiang, Z.4    Portillo, F.P.5    Shalev, D.E.6
  • 71
    • 76449116488 scopus 로고    scopus 로고
    • The effect of backbone cyclization on PK/PD properties of bioactive peptide-peptoid hybrids: the melanocortin agonist paradigm
    • COI: 1:CAS:528:DC%2BC3cXot1yrtg%3D%3D, PID: 20056544
    • Ovadia O, Linde Y, Haskell-Luevano C, Dirain ML, Sheynis T, Jelinek R, et al. The effect of backbone cyclization on PK/PD properties of bioactive peptide-peptoid hybrids: the melanocortin agonist paradigm. Bioorg Med Chem. 2010;18(2):580–9.
    • (2010) Bioorg Med Chem , vol.18 , Issue.2 , pp. 580-589
    • Ovadia, O.1    Linde, Y.2    Haskell-Luevano, C.3    Dirain, M.L.4    Sheynis, T.5    Jelinek, R.6
  • 72
    • 39749193898 scopus 로고    scopus 로고
    • Backbone cyclic peptidomimetic melanocortin-4 receptor agonist as a novel orally administrated drug lead for treating obesity
    • COI: 1:CAS:528:DC%2BD1cXhtFSht78%3D, PID: 18220330
    • Hess S, Linde Y, Ovadia O, Safrai E, Shalev DE, Swed A, et al. Backbone cyclic peptidomimetic melanocortin-4 receptor agonist as a novel orally administrated drug lead for treating obesity. J Med Chem. 2008;51(4):1026–34.
    • (2008) J Med Chem , vol.51 , Issue.4 , pp. 1026-1034
    • Hess, S.1    Linde, Y.2    Ovadia, O.3    Safrai, E.4    Shalev, D.E.5    Swed, A.6
  • 73
    • 0029742789 scopus 로고    scopus 로고
    • Synthesis and biological activity of NK-1 selective, N-backbone cyclic analogs of the C-terminal hexapeptide of substance P
    • COI: 1:CAS:528:DyaK28Xkt1ams7s%3D, PID: 8759639
    • Byk G, Halle D, Zeltser I, Bitan G, Selinger Z, Gilon C. Synthesis and biological activity of NK-1 selective, N-backbone cyclic analogs of the C-terminal hexapeptide of substance P. J Med Chem. 1996;39(16):3174–8.
    • (1996) J Med Chem , vol.39 , Issue.16 , pp. 3174-3178
    • Byk, G.1    Halle, D.2    Zeltser, I.3    Bitan, G.4    Selinger, Z.5    Gilon, C.6
  • 74
    • 79955038892 scopus 로고    scopus 로고
    • Strategies to prolong the plasma residence time of peptide drugs
    • COI: 1:CAS:528:DC%2BC3cXhsVeku7%2FJ
    • Pollaro L, Heinis C. Strategies to prolong the plasma residence time of peptide drugs. Med Chem Comm. 2010;1(5):319–24.
    • (2010) Med Chem Comm , vol.1 , Issue.5 , pp. 319-324
    • Pollaro, L.1    Heinis, C.2
  • 75
    • 77951571813 scopus 로고    scopus 로고
    • Delivery of therapeutic proteins
    • COI: 1:CAS:528:DC%2BC3cXkvVOkurY%3D, PID: 20049941
    • Pisal DS, Kosloski MP, Balu-Iyer SV. Delivery of therapeutic proteins. J Pharm Sci. 2010;99(6):2557–75.
    • (2010) J Pharm Sci , vol.99 , Issue.6 , pp. 2557-2575
    • Pisal, D.S.1    Kosloski, M.P.2    Balu-Iyer, S.V.3
  • 76
    • 33751218547 scopus 로고    scopus 로고
    • Therapeutic peptides: technological advances driving peptides into development
    • COI: 1:CAS:528:DC%2BD28Xht1eqs7zL, PID: 17049837
    • Sato AK, Viswanathan M, Kent RB, Wood CR. Therapeutic peptides: technological advances driving peptides into development. Curr Opin Biotechnol. 2006;17(6):638–42.
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.6 , pp. 638-642
    • Sato, A.K.1    Viswanathan, M.2    Kent, R.B.3    Wood, C.R.4
  • 77
    • 40749110680 scopus 로고    scopus 로고
    • N-terminal acetylation protects glucagon-like peptide GLP-1-(7–34)-amide from DPP-IV-mediated degradation retaining cAMP-and insulin releasing capacity
    • COI: 1:CAS:528:DC%2BD1cXlsV2qu7c%3D, PID: 18424366
    • John H, Maronde E, Forssmann W-G, Meyer M, Adermann K. N-terminal acetylation protects glucagon-like peptide GLP-1-(7–34)-amide from DPP-IV-mediated degradation retaining cAMP-and insulin releasing capacity. Eur J Med Res. 2008;13(2):73–8.
    • (2008) Eur J Med Res , vol.13 , Issue.2 , pp. 73-78
    • John, H.1    Maronde, E.2    Forssmann, W.-G.3    Meyer, M.4    Adermann, K.5
  • 78
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37
    • COI: 1:CAS:528:DC%2BD1MXhslenuro%3D
    • Stroemstedt AA, Pasupuleti M, Schmidtchen A, Malmsten M. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob Agents Chemother. 2009;53(2):593–602.
    • (2009) Antimicrob Agents Chemother , vol.53 , Issue.2 , pp. 593-602
    • Stroemstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 79
    • 33846009834 scopus 로고    scopus 로고
    • Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue
    • COI: 1:CAS:528:DC%2BD2sXivVOrsrg%3D, PID: 17214611
    • Ferdinandi ES, Brazeau P, High K, Procter B, Fennell S, Dubreuil P. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue. Basic Clin Pharmacol Toxicol. 2007;100(1):49–58.
    • (2007) Basic Clin Pharmacol Toxicol , vol.100 , Issue.1 , pp. 49-58
    • Ferdinandi, E.S.1    Brazeau, P.2    High, K.3    Procter, B.4    Fennell, S.5    Dubreuil, P.6
  • 81
    • 4744337511 scopus 로고    scopus 로고
    • Pharmacokinetics and renal excretion of desmopressin after intravenous administration to healthy subjects and renally impaired patients
    • COI: 1:CAS:528:DC%2BD2cXpsVSiu70%3D, PID: 15373927
    • Agerso H, Larsen LS, Riis A, Lovgren U, Karlsson MO, Senderovitz T. Pharmacokinetics and renal excretion of desmopressin after intravenous administration to healthy subjects and renally impaired patients. Br J Clin Pharmacol. 2004;58(4):352–8.
    • (2004) Br J Clin Pharmacol , vol.58 , Issue.4 , pp. 352-358
    • Agerso, H.1    Larsen, L.S.2    Riis, A.3    Lovgren, U.4    Karlsson, M.O.5    Senderovitz, T.6
  • 82
    • 0028306217 scopus 로고
    • Somatostatin and somatostatin analogues: pharmacokinetics and pharmacodynamic effects
    • COI: 1:CAS:528:DyaK2cXkvF2qtL4%3D, PID: 7911441
    • Harris AG. Somatostatin and somatostatin analogues: pharmacokinetics and pharmacodynamic effects. Gut. 1994;35(3 Suppl):S1–4.
    • (1994) Gut , vol.35 , Issue.3 , pp. S1-S4
    • Harris, A.G.1
  • 83
    • 84880639988 scopus 로고    scopus 로고
    • Improving binding affinity and stability of peptide ligands by substituting glycines with D-amino acids
    • COI: 1:CAS:528:DC%2BC3sXhtVGku7vL, PID: 23828687
    • Chen S, Gfeller D, Buth SA, Michielin O, Leiman PG, Heinis C. Improving binding affinity and stability of peptide ligands by substituting glycines with D-amino acids. Chem Bio Chem. 2013;14(11):1316–22.
    • (2013) Chem Bio Chem , vol.14 , Issue.11 , pp. 1316-1322
    • Chen, S.1    Gfeller, D.2    Buth, S.A.3    Michielin, O.4    Leiman, P.G.5    Heinis, C.6
  • 84
    • 12244310801 scopus 로고    scopus 로고
    • Partial D-amino acid substitution: improved enzymatic stability and preserved Ab recognition of a MUC2 epitope peptide
    • COI: 1:CAS:528:DC%2BD2MXptFSkuw%3D%3D, PID: 15630090
    • Tugyi R, Uray K, Ivan D, Fellinger E, Perkins A, Hudecz F. Partial D-amino acid substitution: improved enzymatic stability and preserved Ab recognition of a MUC2 epitope peptide. Proc Natl Acad Sci U S A. 2005;102(2):413–8.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.2 , pp. 413-418
    • Tugyi, R.1    Uray, K.2    Ivan, D.3    Fellinger, E.4    Perkins, A.5    Hudecz, F.6
  • 85
    • 0023686915 scopus 로고
    • Dermorphin analogs: resistance to in vitro enzymatic degradation is not always increased by additional D-amino acid substitutions
    • COI: 1:CAS:528:DyaL1MXhvVKhsQ%3D%3D, PID: 2902857
    • Darlak K, Benovitz DE, Spatola AF, Grzonka Z. Dermorphin analogs: resistance to in vitro enzymatic degradation is not always increased by additional D-amino acid substitutions. Biochem Biophys Res Commun. 1988;156(1):125–30.
    • (1988) Biochem Biophys Res Commun , vol.156 , Issue.1 , pp. 125-130
    • Darlak, K.1    Benovitz, D.E.2    Spatola, A.F.3    Grzonka, Z.4
  • 86
    • 0023873458 scopus 로고
    • Pharmacokinetic evaluation of superactive analogues of growth hormone-releasing factor (1–29)-amide
    • COI: 1:CAS:528:DyaL1cXhsVers74%3D, PID: 2896343
    • Rafferty B, Coy DH, Poole S. Pharmacokinetic evaluation of superactive analogues of growth hormone-releasing factor (1–29)-amide. Peptides. 1988;9(1):207–9.
    • (1988) Peptides , vol.9 , Issue.1 , pp. 207-209
    • Rafferty, B.1    Coy, D.H.2    Poole, S.3
  • 87
    • 33751527644 scopus 로고    scopus 로고
    • Innovative approaches to anti-arrhythmic drug therapy
    • COI: 1:CAS:528:DC%2BD28Xht1Kju7vJ, PID: 17139288
    • Nattel S, Carlsson L. Innovative approaches to anti-arrhythmic drug therapy. Nat Rev Drug Discov. 2006;5(12):1034–49.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.12 , pp. 1034-1049
    • Nattel, S.1    Carlsson, L.2
  • 88
    • 77957942154 scopus 로고    scopus 로고
    • Design of a potent D-peptide HIV-1 entry inhibitor with a strong barrier to resistance
    • COI: 1:CAS:528:DC%2BC3cXhsVeisb7E, PID: 20719956
    • Welch BD, Francis JN, Redman JS, Paul S, Weinstock MT, Reeves JD, et al. Design of a potent D-peptide HIV-1 entry inhibitor with a strong barrier to resistance. J Virol. 2010;84(21):11235–44.
    • (2010) J Virol , vol.84 , Issue.21 , pp. 11235-11244
    • Welch, B.D.1    Francis, J.N.2    Redman, J.S.3    Paul, S.4    Weinstock, M.T.5    Reeves, J.D.6
  • 89
    • 0141940302 scopus 로고    scopus 로고
    • Phase II study of cetrorelix, a luteinizing hormone-releasing hormone antagonist in patients with platinum-resistant ovarian cancer
    • COI: 1:CAS:528:DC%2BD3sXnt1antbo%3D, PID: 13678723
    • Verschraegen CF, Westphalen S, Hu W, Loyer E, Kudelka A, Volker P, et al. Phase II study of cetrorelix, a luteinizing hormone-releasing hormone antagonist in patients with platinum-resistant ovarian cancer. Gynecol Oncol. 2003;90(3):552–9.
    • (2003) Gynecol Oncol , vol.90 , Issue.3 , pp. 552-559
    • Verschraegen, C.F.1    Westphalen, S.2    Hu, W.3    Loyer, E.4    Kudelka, A.5    Volker, P.6
  • 90
    • 33750701113 scopus 로고    scopus 로고
    • Is IGnRH-III the most potent GnRH analog containing only natural amino acids that specifically inhibits the growth of human breast cancer cells?
    • COI: 1:CAS:528:DC%2BD28Xht1WhtbvM, PID: 16967433
    • Heredi-Szabo K, Murphy RF, Lovas S. Is IGnRH-III the most potent GnRH analog containing only natural amino acids that specifically inhibits the growth of human breast cancer cells? J Pept Sci. 2006;12(11):714–20.
    • (2006) J Pept Sci , vol.12 , Issue.11 , pp. 714-720
    • Heredi-Szabo, K.1    Murphy, R.F.2    Lovas, S.3
  • 91
    • 0031792717 scopus 로고    scopus 로고
    • Ipamorelin, the first selective growth hormone secretagogue
    • COI: 1:CAS:528:DyaK1cXnvFyhur0%3D, PID: 9849822
    • Raun K, Hansen BS, Johansen NL, Thogersen H, Madsen K, Ankersen M, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998;139(5):552–61.
    • (1998) Eur J Endocrinol , vol.139 , Issue.5 , pp. 552-561
    • Raun, K.1    Hansen, B.S.2    Johansen, N.L.3    Thogersen, H.4    Madsen, K.5    Ankersen, M.6
  • 92
    • 0032872444 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers
    • COI: 1:CAS:528:DyaK1MXmtVKktbg%3D, PID: 10496658
    • Gobburu JVS, Agerso H, Jusko WJ, Ynddal L. Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers. Pharm Res. 1999;16(9):1412–6.
    • (1999) Pharm Res , vol.16 , Issue.9 , pp. 1412-1416
    • Gobburu, J.V.S.1    Agerso, H.2    Jusko, W.J.3    Ynddal, L.4
  • 93
    • 0027005949 scopus 로고
    • Whole body and brain distribution of [3H]cyclic [D-Pen2, D-Pen5]enkephalin after intraperitoneal, intravenous, oral and subcutaneous administration
    • COI: 1:CAS:528:DyaK3sXhtFOjs7k%3D, PID: 1469637
    • Weber SJ, Greene DL, Hruby VJ, Yamamura HI, Porreca F, Davis TP. Whole body and brain distribution of [3H]cyclic [D-Pen2, D-Pen5]enkephalin after intraperitoneal, intravenous, oral and subcutaneous administration. J Pharmacol Exp Ther. 1992;263(3):1308–16.
    • (1992) J Pharmacol Exp Ther , vol.263 , Issue.3 , pp. 1308-1316
    • Weber, S.J.1    Greene, D.L.2    Hruby, V.J.3    Yamamura, H.I.4    Porreca, F.5    Davis, T.P.6
  • 94
    • 27144548864 scopus 로고    scopus 로고
    • The effect of cyclization on the enzymatic degradation of herpes simplex virus glycoprotein D derived epitope peptide
    • COI: 1:CAS:528:DC%2BD2MXhtFygsL3F, PID: 15864815
    • Tugyi R, Mezo G, Fellinger E, Andreu D, Hudecz F. The effect of cyclization on the enzymatic degradation of herpes simplex virus glycoprotein D derived epitope peptide. J Pept Sci. 2005;11(10):642–9.
    • (2005) J Pept Sci , vol.11 , Issue.10 , pp. 642-649
    • Tugyi, R.1    Mezo, G.2    Fellinger, E.3    Andreu, D.4    Hudecz, F.5
  • 96
    • 34247492473 scopus 로고    scopus 로고
    • Reactivation of the p53 tumor suppressor pathway by a stapled p53 peptide [Erratum to document cited in CA146:397011]
    • COI: 1:CAS:528:DC%2BD2sXjsVOrsL8%3D
    • Bernal F, Tyler AF, Korsmeyer SJ, Walensky LD, Verdine GL. Reactivation of the p53 tumor suppressor pathway by a stapled p53 peptide [Erratum to document cited in CA146:397011]. J Am Chem Soc. 2007;129(16):5298.
    • (2007) J Am Chem Soc , vol.129 , Issue.16 , pp. 5298
    • Bernal, F.1    Tyler, A.F.2    Korsmeyer, S.J.3    Walensky, L.D.4    Verdine, G.L.5
  • 97
    • 77956294635 scopus 로고    scopus 로고
    • Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
    • COI: 1:CAS:528:DC%2BC3cXhtVCktrfJ, PID: 20660316, S/1-S/8
    • Bird GH, Madani N, Perry AF, Princiotto AM, Supko JG, He X, et al. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. Proc Natl Acad Sci U S A. 2010;107(32):14093–8. S/1-S/8.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.32 , pp. 14093-14098
    • Bird, G.H.1    Madani, N.2    Perry, A.F.3    Princiotto, A.M.4    Supko, J.G.5    He, X.6
  • 98
    • 84876316258 scopus 로고    scopus 로고
    • Stapled peptide to enter human testing, but affinity questions remain
    • COI: 1:CAS:528:DC%2BC3sXitVGgtbo%3D
    • Grigoryev Y. Stapled peptide to enter human testing, but affinity questions remain. Nat Med (N Y, NY, U S). 2013;19(2):120.
    • (2013) Nat Med (N Y, NY, U S) , vol.19 , Issue.2 , pp. 120
    • Grigoryev, Y.1
  • 99
    • 84862118560 scopus 로고    scopus 로고
    • Pharmacokinetic predictions for patients with renal impairment: focus on peptides and protein drugs
    • COI: 1:CAS:528:DC%2BC38Xht1Klur7F, PID: 22242561
    • Czock D, Keller F, Seidling HM. Pharmacokinetic predictions for patients with renal impairment: focus on peptides and protein drugs. Br J Clin Pharmacol. 2012;74(1):66–74.
    • (2012) Br J Clin Pharmacol , vol.74 , Issue.1 , pp. 66-74
    • Czock, D.1    Keller, F.2    Seidling, H.M.3
  • 100
    • 70349603042 scopus 로고    scopus 로고
    • Pharmacokinetics and dosage adjustment in patients with renal dysfunction
    • COI: 1:CAS:528:DC%2BD1MXptVaqtLk%3D, PID: 19543887
    • Verbeeck RK, Musuamba FT. Pharmacokinetics and dosage adjustment in patients with renal dysfunction. Eur J Clin Pharmacol. 2009;65(8):757–73.
    • (2009) Eur J Clin Pharmacol , vol.65 , Issue.8 , pp. 757-773
    • Verbeeck, R.K.1    Musuamba, F.T.2
  • 101
    • 0027493822 scopus 로고
    • Clinical pharmacokinetics of octreotide. Therapeutic applications in patients with pituitary tumours
    • COI: 1:STN:280:DyaK2c7hs1amtw%3D%3D, PID: 8287633
    • Chanson P, Timsit J, Harris AG. Clinical pharmacokinetics of octreotide. Therapeutic applications in patients with pituitary tumours. Clin Pharmacokinet. 1993;25(5):375–91.
    • (1993) Clin Pharmacokinet , vol.25 , Issue.5 , pp. 375-391
    • Chanson, P.1    Timsit, J.2    Harris, A.G.3
  • 102
    • 0022445443 scopus 로고
    • Pharmacokinetics of SMS 201–995 in healthy subjects
    • COI: 1:STN:280:DyaL2s%2FhvVKgtg%3D%3D, PID: 2876508
    • Kutz K, Nuesch E, Rosenthaler J. Pharmacokinetics of SMS 201–995 in healthy subjects. Scand J Gastroenterol Suppl. 1986;119:65–72.
    • (1986) Scand J Gastroenterol Suppl , vol.119 , pp. 65-72
    • Kutz, K.1    Nuesch, E.2    Rosenthaler, J.3
  • 103
    • 78049365082 scopus 로고    scopus 로고
    • Metabolism and excretion of the once-daily human glucagon-like peptide-1 analog liraglutide in healthy male subjects and its in vitro degradation by dipeptidyl peptidase IV and neutral endopeptidase
    • COI: 1:CAS:528:DC%2BC3cXhsVWqurrK, PID: 20709939
    • Malm-Erjefalt M, Bjoernsdottir I, Vanggaard J, Helleberg H, Larsen U, Oosterhuis B, et al. Metabolism and excretion of the once-daily human glucagon-like peptide-1 analog liraglutide in healthy male subjects and its in vitro degradation by dipeptidyl peptidase IV and neutral endopeptidase. Drug Metab Dispos. 2010;38(11):1944–53.
    • (2010) Drug Metab Dispos , vol.38 , Issue.11 , pp. 1944-1953
    • Malm-Erjefalt, M.1    Bjoernsdottir, I.2    Vanggaard, J.3    Helleberg, H.4    Larsen, U.5    Oosterhuis, B.6
  • 104
    • 84870609729 scopus 로고    scopus 로고
    • Liraglutide, a long-acting GLP-1 mimetic, and its metabolite attenuate inflammation after intracerebral hemorrhage
    • COI: 1:CAS:528:DC%2BC38XhslKrsb3N, PID: 22968320
    • Hou J, Manaenko A, Hakon J, Hansen-Schwartz J, Tang J, Zhang JH. Liraglutide, a long-acting GLP-1 mimetic, and its metabolite attenuate inflammation after intracerebral hemorrhage. J Cereb Blood Flow Metab. 2012;32(12):2201–10.
    • (2012) J Cereb Blood Flow Metab , vol.32 , Issue.12 , pp. 2201-2210
    • Hou, J.1    Manaenko, A.2    Hakon, J.3    Hansen-Schwartz, J.4    Tang, J.5    Zhang, J.H.6
  • 105
    • 84895198774 scopus 로고    scopus 로고
    • Novel exenatide analogs with peptidic albumin binding domains: potent anti-diabetic agents with extended duration of action
    • COI: 1:STN:280:DC%2BC2cvivFCjsw%3D%3D, PID: 24503632
    • Levy Odile E, Jodka Carolyn M, Ren Shijun S, Mamedova L, Sharma A, Samant M, et al. Novel exenatide analogs with peptidic albumin binding domains: potent anti-diabetic agents with extended duration of action. PLoS One. 2014;9(2):e87704.
    • (2014) PLoS One , vol.9 , Issue.2 , pp. e87704
    • Levy Odile, E.1    Jodka Carolyn, M.2    Ren Shijun, S.3    Mamedova, L.4    Sharma, A.5    Samant, M.6
  • 106
    • 84922005237 scopus 로고    scopus 로고
    • A GLP-1 receptor agonist conjugated to an albumin-binding domain for extended half-life
    • COI: 1:CAS:528:DC%2BC2cXhs1Knt7vK, PID: 24549714
    • Lindgren J, Refai E, Zaitsev Sergei V, Abrahmsen L, Berggren P-O, Karlstrom AE. A GLP-1 receptor agonist conjugated to an albumin-binding domain for extended half-life. Biopolymers. 2014;102(3):252–9.
    • (2014) Biopolymers , vol.102 , Issue.3 , pp. 252-259
    • Lindgren, J.1    Refai, E.2    Zaitsev Sergei, V.3    Abrahmsen, L.4    Berggren, P.-O.5    Karlstrom, A.E.6
  • 107
    • 84870015800 scopus 로고    scopus 로고
    • Bicyclization and tethering to albumin yields long-acting peptide antagonists
    • COI: 1:CAS:528:DC%2BC38XhsFChsrbE, PID: 23088498
    • Angelini A, Morales-Sanfrutos J, Diderich P, Chen S, Heinis C. Bicyclization and tethering to albumin yields long-acting peptide antagonists. J Med Chem. 2012;55(22):10187–97.
    • (2012) J Med Chem , vol.55 , Issue.22 , pp. 10187-10197
    • Angelini, A.1    Morales-Sanfrutos, J.2    Diderich, P.3    Chen, S.4    Heinis, C.5
  • 109
    • 41349098117 scopus 로고    scopus 로고
    • An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis
    • COI: 1:CAS:528:DC%2BD1cXls1Gls7s%3D, PID: 18313669
    • Baggio LL, Huang Q, Cao X, Drucker DJ. An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis. Gastroenterology. 2008;134(4):1137–47.
    • (2008) Gastroenterology , vol.134 , Issue.4 , pp. 1137-1147
    • Baggio, L.L.1    Huang, Q.2    Cao, X.3    Drucker, D.J.4
  • 111
    • 84899585635 scopus 로고    scopus 로고
    • Once-weekly albiglutide versus once-daily liraglutide in patients with type 2 diabetes inadequately controlled on oral drugs (HARMONY 7): a randomised, open-label, multicentre, non-inferiority phase 3 study
    • COI: 1:CAS:528:DC%2BC2cXosFSktro%3D, PID: 24703047
    • Pratley RE, Nauck MA, Barnett AH, Feinglos MN, Ovalle F, Harman-Boehm I, et al. Once-weekly albiglutide versus once-daily liraglutide in patients with type 2 diabetes inadequately controlled on oral drugs (HARMONY 7): a randomised, open-label, multicentre, non-inferiority phase 3 study. Lancet Diabetes Endocrinol. 2014;2(4):289–97.
    • (2014) Lancet Diabetes Endocrinol , vol.2 , Issue.4 , pp. 289-297
    • Pratley, R.E.1    Nauck, M.A.2    Barnett, A.H.3    Feinglos, M.N.4    Ovalle, F.5    Harman-Boehm, I.6
  • 113
    • 0031765907 scopus 로고    scopus 로고
    • Role of P-glycoprotein and cytochrome P450 3A in limiting oral absorption of peptides and peptidomimetics
    • COI: 1:CAS:528:DyaK1cXltlyhsb0%3D, PID: 9811484
    • Wacher VJ, Silverman JA, Zhang Y, Benet LZ. Role of P-glycoprotein and cytochrome P450 3A in limiting oral absorption of peptides and peptidomimetics. J Pharm Sci. 1998;87(11):1322–30.
    • (1998) J Pharm Sci , vol.87 , Issue.11 , pp. 1322-1330
    • Wacher, V.J.1    Silverman, J.A.2    Zhang, Y.3    Benet, L.Z.4
  • 114
    • 18844383217 scopus 로고    scopus 로고
    • Human metabolism of the proteasome inhibitor bortezomib: identification of circulating metabolites
    • COI: 1:CAS:528:DC%2BD2MXksleksrg%3D, PID: 15764713
    • Pekol T, Daniels JS, Labutti J, Parsons I, Nix D, Baronas E, et al. Human metabolism of the proteasome inhibitor bortezomib: identification of circulating metabolites. Drug Metab Dispos. 2005;33(6):771–7.
    • (2005) Drug Metab Dispos , vol.33 , Issue.6 , pp. 771-777
    • Pekol, T.1    Daniels, J.S.2    Labutti, J.3    Parsons, I.4    Nix, D.5    Baronas, E.6
  • 115
    • 84888632710 scopus 로고    scopus 로고
    • A perspective on the prediction of drug pharmacokinetics and disposition in drug research and development
    • COI: 1:CAS:528:DC%2BC3sXhvVCjtbrF, PID: 24065860
    • Di L, Feng B, Goosen TC, Lai Y, Steyn SJ, Varma MV, et al. A perspective on the prediction of drug pharmacokinetics and disposition in drug research and development. Drug Metab Dispos. 2013;41(12):1975–93.
    • (2013) Drug Metab Dispos , vol.41 , Issue.12 , pp. 1975-1993
    • Di, L.1    Feng, B.2    Goosen, T.C.3    Lai, Y.4    Steyn, S.J.5    Varma, M.V.6
  • 116
    • 77955297665 scopus 로고    scopus 로고
    • Prediction of human clearance of therapeutic proteins: simple allometric scaling method revisited
    • PID: 20437464
    • Wang W, Prueksaritanont T. Prediction of human clearance of therapeutic proteins: simple allometric scaling method revisited. Biopharm Drug Dispos. 2010;31(4):253–63.
    • (2010) Biopharm Drug Dispos , vol.31 , Issue.4 , pp. 253-263
    • Wang, W.1    Prueksaritanont, T.2
  • 117
    • 0026063359 scopus 로고
    • Interspecies scaling of clearance and volume of distribution data for five therapeutic proteins
    • COI: 1:CAS:528:DyaK3MXms12qsbk%3D, PID: 1798669
    • Mordenti J, Chen SA, Moore JA, Ferraiolo BL, Green JD. Interspecies scaling of clearance and volume of distribution data for five therapeutic proteins. Pharm Res. 1991;8(11):1351–9.
    • (1991) Pharm Res , vol.8 , Issue.11 , pp. 1351-1359
    • Mordenti, J.1    Chen, S.A.2    Moore, J.A.3    Ferraiolo, B.L.4    Green, J.D.5
  • 118
    • 0033044866 scopus 로고    scopus 로고
    • Animal pharmacokinetics of the tumor necrosis factor receptor-immunoglobulin fusion protein lenercept and their extrapolation to humans
    • COI: 1:CAS:528:DyaK1MXktFymtA%3D%3D, PID: 9884305
    • Richter WF, Gallati H, Schiller C-D. Animal pharmacokinetics of the tumor necrosis factor receptor-immunoglobulin fusion protein lenercept and their extrapolation to humans. Drug Metab Dispos. 1999;27(1):21–5.
    • (1999) Drug Metab Dispos , vol.27 , Issue.1 , pp. 21-25
    • Richter, W.F.1    Gallati, H.2    Schiller, C.-D.3
  • 119
    • 0029951502 scopus 로고    scopus 로고
    • Interspecies scaling of clearance and volume of distribution for digoxin-specific Fab
    • COI: 1:CAS:528:DyaK28XivVOnsL8%3D, PID: 8658517
    • Grene-Lerouge NAM, Bazin-Redureau MI, Debray M, Scherrmann JMG. Interspecies scaling of clearance and volume of distribution for digoxin-specific Fab. Toxicol Appl Pharmacol. 1996;138(1):84–9.
    • (1996) Toxicol Appl Pharmacol , vol.138 , Issue.1 , pp. 84-89
    • Grene-Lerouge, N.A.M.1    Bazin-Redureau, M.I.2    Debray, M.3    Scherrmann, J.M.G.4
  • 120
    • 0347755132 scopus 로고    scopus 로고
    • Interspecies scaling of protein drugs: prediction of clearance from animals to humans
    • COI: 1:CAS:528:DC%2BD2cXjvFWntw%3D%3D, PID: 14648647
    • Mahmood I. Interspecies scaling of protein drugs: prediction of clearance from animals to humans. J Pharm Sci. 2004;93(1):177–85.
    • (2004) J Pharm Sci , vol.93 , Issue.1 , pp. 177-185
    • Mahmood, I.1
  • 121
    • 84878825564 scopus 로고    scopus 로고
    • Interspecies modeling and prediction of human exenatide pharmacokinetics
    • COI: 1:CAS:528:DC%2BC38Xhs1Olu7fO, PID: 23229855
    • Chen T, Mager DE, Kagan L. Interspecies modeling and prediction of human exenatide pharmacokinetics. Pharm Res. 2013;30(3):751–60.
    • (2013) Pharm Res , vol.30 , Issue.3 , pp. 751-760
    • Chen, T.1    Mager, D.E.2    Kagan, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.