메뉴 건너뛰기




Volumn 15, Issue 2, 2005, Pages 153-166

Recent advances in therapeutic applications of human peptide transporters

Author keywords

Genetic variation; hPEPT1; hPEPT2; Molecular modelling; Peptide transporter; SLC15A1; SLC15A2; Substrate recognition; Valaciclovir; Valganciclovir

Indexed keywords

ACICLOVIR; ALAFOSFALIN; ANTINEOPLASTIC AGENT; BETA LACTAM ANTIBIOTIC; CARBONYL DERIVATIVE; CEFALEXIN; CYSTEINE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; EUDRAGIT; GABAPENTIN; GANCICLOVIR; LACTOSE PERMEASE; NEW DRUG; PEPTIDE TRANSPORTER 1; POLYMER; THIAZOLE DERIVATIVE; VALACICLOVIR;

EID: 14544273652     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.15.2.153     Document Type: Review
Times cited : (15)

References (81)
  • 3
    • 0030054574 scopus 로고    scopus 로고
    • Molecular modeling study of structural requirements for the oligopeptide transporter
    • LI J, HIDALGO IJ: Molecular modeling study of structural requirements for the oligopeptide transporter. J. Drug Target. (1996) 4:9-17.
    • (1996) J. Drug Target , vol.4 , pp. 9-17
    • Li, J.1    Hidalgo, I.J.2
  • 4
    • 4444338811 scopus 로고    scopus 로고
    • Dipeptidomimetic ketomethylene isosteres as pro-moieties for drug transport via the human intestinal di-/tripeptide transporter hPEPT1: Design, synthesis, stability, biological investigations
    • VÅBENØ J, NIELSEN CU, INGEBRIGTSEN T, LEJON T, STEFFANSEN B, LUTHMAN K: Dipeptidomimetic ketomethylene isosteres as pro-moieties for drug transport via the human intestinal di-/tripeptide transporter hPEPT1: design, synthesis, stability, biological investigations. J. Med. Chem. (2004) 47:4755-4765.
    • (2004) J. Med. Chem. , vol.47 , pp. 4755-4765
    • Våbenø, J.1    Nielsen, C.U.2    Ingebrigtsen, T.3    Lejon, T.4    Steffansen, B.5    Luthman, K.6
  • 5
    • 0842304421 scopus 로고    scopus 로고
    • Phe-Gly dipeptidomimetics designed for the di-/tripeptide transporters PEPT1 and PEPT2: Synthesis and biological investigations
    • VÅBENØ J, LEJON T, NIELSEN CU et al.: Phe-Gly dipeptidomimetics designed for the di-/tripeptide transporters PEPT1 and PEPT2: Synthesis and biological investigations. J. Med. Chem. (2004) 47:1060-1069.
    • (2004) J. Med. Chem. , vol.47 , pp. 1060-1069
    • Våbenø, J.1    Lejon, T.2    Nielsen, C.U.3
  • 6
    • 0242353755 scopus 로고    scopus 로고
    • Enhanced intestinal absorption of drugs by activation of peptide transporter PEPT1 using proton-releasing polymer
    • NOZAWA T, TOYOBUKU H, KOBAYASH D, KURUMA K, TSUJI A, TAMAI I: Enhanced intestinal absorption of drugs by activation of peptide transporter PEPT1 using proton-releasing polymer. J. Pharm. Sci. (2003) 92:2208-2216.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 2208-2216
    • Nozawa, T.1    Toyobuku, H.2    Kobayash, D.3    Kuruma, K.4    Tsuji, A.5    Tamai, I.6
  • 7
    • 3343020872 scopus 로고    scopus 로고
    • Genetic polymorphisms in human proton-dependent dipeptide transporter PEPT1: Implications for the functional role of Pro586
    • ZHANG EY, FU DJ, PAK YA et al.: Genetic polymorphisms in human proton-dependent dipeptide transporter PEPT1: Implications for the functional role of Pro586. J. Pharmacol. Exp. Ther. (2004) 310: 437-445.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 437-445
    • Zhang, E.Y.1    Fu, D.J.2    Pak, Y.A.3
  • 9
    • 0037530341 scopus 로고    scopus 로고
    • Di/tri-peptide transporters as drug delivery targets: Regulation of transport under physiological and patho-physiological conditions
    • NIELSEN CU, BRODIN B: Di/tri-peptide transporters as drug delivery targets: regulation of transport under physiological and patho-physiological conditions. Curr. Drug Targets (2003) 4 373-388.
    • (2003) Curr. Drug Targets , vol.4 , pp. 373-388
    • Nielsen, C.U.1    Brodin, B.2
  • 10
    • 2342644210 scopus 로고    scopus 로고
    • Molecular and integrative physiology of intestinal peptide transport
    • DANIEL H: Molecular and integrative physiology of intestinal peptide transport. Ann. Rev. Physiol. (2004) 66:361-384.
    • (2004) Ann. Rev. Physiol. , vol.66 , pp. 361-384
    • Daniel, H.1
  • 11
    • 1442351172 scopus 로고    scopus 로고
    • Peptide transporters: Structure, function, regulation and application for drug delivery
    • TERADA T, INUI K: Peptide transporters: structure, function, regulation and application for drug delivery. Curr. Drug Metab. (2004) 5:85-94.
    • (2004) Curr. Drug Metab. , vol.5 , pp. 85-94
    • Terada, T.1    Inui, K.2
  • 12
    • 1542345031 scopus 로고    scopus 로고
    • Molecular mechanisms of pulmonary peptidomimetic drug and peptide transport
    • GRONEBERG DA, FISCHER A, CHUNG KF, DANIEL H: Molecular mechanisms of pulmonary peptidomimetic drug and peptide transport. Am. J. Resp. Cell Mol. (2004) 30:251-260.
    • (2004) Am. J. Resp. Cell Mol. , vol.30 , pp. 251-260
    • Groneberg, D.A.1    Fischer, A.2    Chung, K.F.3    Daniel, H.4
  • 13
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • DANIEL H, KOTTRA G: The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch. (2004) 447:610-618.
    • (2004) Pflugers Arch. , vol.447 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 16
    • 0037380335 scopus 로고    scopus 로고
    • Current perspectives on established and putative mammalian oligopeptide transporters
    • HERRERA-RUIZ D, KNIPP GT: Current perspectives on established and putative mammalian oligopeptide transporters. J. Pharm. Sci. (2003) 92:691-714.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 691-714
    • Herrera-Ruiz, D.1    Knipp, G.T.2
  • 17
    • 2642602528 scopus 로고    scopus 로고
    • Delta-aminolevulinic acid transport by intestinal and renal peptide transporters and its physiological and clinical implications
    • DORING F, WALTER J, WILL J et al.: Delta-aminolevulinic acid transport by intestinal and renal peptide transporters and its physiological and clinical implications. J. Clin. Invest. (1998) 101:2761-2767.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2761-2767
    • Doring, F.1    Walter, J.2    Will, J.3
  • 18
    • 0347600965 scopus 로고    scopus 로고
    • Analysis of the transport properties of side chain modified dipeptides at the mammalian peptide transporter PEPT1
    • KNUTTER I, HARTRODT B, THEIS S et al.: Analysis of the transport properties of side chain modified dipeptides at the mammalian peptide transporter PEPT1. Eur. J. Pharm. Sci. (2004) 21 61-67.
    • (2004) Eur. J. Pharm. Sci. , vol.21 , pp. 61-67
    • Knutter, I.1    Hartrodt, B.2    Theis, S.3
  • 19
    • 0035836449 scopus 로고    scopus 로고
    • A novel inhibitor of the mammalian peptide transporter PEPT1
    • KNUTTER I, THEIS S, HARTRODT B et al.: A novel inhibitor of the mammalian peptide transporter PEPT1. Biochemistry (2001) 40: 4454-4458.
    • (2001) Biochemistry , vol.40 , pp. 4454-4458
    • Knutter, I.1    Theis, S.2    Hartrodt, B.3
  • 20
    • 84962464696 scopus 로고    scopus 로고
    • Minimal molecular determinants of substrates for recognition by the intestinal peptide transporter
    • DORING F, WILL J, AMASHEH S, CLAUSS W, AHLBRECHT H, DANIEL H: Minimal molecular determinants of substrates for recognition by the intestinal peptide transporter. J. Biol. Chem. (1998) 273 23211-23218.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23211-23218
    • Doring, F.1    Will, J.2    Amasheh, S.3    Clauss, W.4    Ahlbrecht, H.5    Daniel, H.6
  • 21
    • 0033938343 scopus 로고    scopus 로고
    • Modified amino acids and peptides as substrates for the intestinal peptide transporter PepT1
    • MEREDITH D, TEMPLE CS, GUHA N et al.: Modified amino acids and peptides as substrates for the intestinal peptide transporter PepT1. Eur. J. Biochem. (2000) 267:3723-3728.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3723-3728
    • Meredith, D.1    Temple, C.S.2    Guha, N.3
  • 22
    • 0030946942 scopus 로고    scopus 로고
    • Molecular determinants of recognition for the intestinal peptide carrier
    • SWAAN PW, TUKKER JJ: Molecular determinants of recognition for the intestinal peptide carrier. J. Pharm. Sci. (1997) 86 596-602.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 596-602
    • Swaan, P.W.1    Tukker, J.J.2
  • 23
    • 0032466466 scopus 로고    scopus 로고
    • Mapping the binding site of the small intestinal peptide carrier (PepT1) using comparative molecular field analysis
    • SWAAN PW, KOOPS BC, MORET EE, TUKKER JJ: Mapping the binding site of the small intestinal peptide carrier (PepT1) using comparative molecular field analysis. Recept. Channels (1998) 6:189-200.
    • (1998) Recept. Channels , vol.6 , pp. 189-200
    • Swaan, P.W.1    Koops, B.C.2    Moret, E.E.3    Tukker, J.J.4
  • 24
    • 0034603011 scopus 로고    scopus 로고
    • How to make drugs orally active: A substrate templete for peptide transporter PepT1
    • BAILEY PD, BOYD R, BRONK JR et al.: How to make drugs orally active: a substrate templete for peptide transporter PepT1. Angew. Chem. Int. Ed. (2000) 39:505-508.
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 505-508
    • Bailey, P.D.1    Boyd, R.2    Bronk, J.R.3
  • 25
    • 0035845726 scopus 로고    scopus 로고
    • Dipeptide model prodrugs for the intestinal oligopeptide transporter. Affinity to and transport via hPepT1 in the human intestinal Caco-2 cell line
    • NIELSEN CU, ANDERSEN R, BRODIN B, FROKJAER S, TAUB ME, STEFFANSEN B: Dipeptide model prodrugs for the intestinal oligopeptide transporter. Affinity to and transport via hPepT1 in the human intestinal Caco-2 cell line. J. Control. Rel. (2001) 76:129-138.
    • (2001) J. Control Rel. , vol.76 , pp. 129-138
    • Nielsen, C.U.1    Andersen, R.2    Brodin, B.3    Frokjaer, S.4    Taub, M.E.5    Steffansen, B.6
  • 26
    • 85069011228 scopus 로고    scopus 로고
    • Conformational restrictions in ligand binding to the human intestinal di-/tripeptide transporter: Implications for design of hPEPT1 targeted prodrugs
    • in press
    • VÅBENØ J, NIELSEN CU, STEFFANSEN B et al.: Conformational restrictions in ligand binding to the human intestinal di-/tripeptide transporter: Implications for design of hPEPT1 targeted prodrugs. Bioorg. Med. Chem. in press.
    • Bioorg. Med. Chem.
    • Våbenø, J.1    Nielsen, C.U.2    Steffansen, B.3
  • 27
    • 13944269270 scopus 로고    scopus 로고
    • A novel high-troughput PepT1 transporter assay differentiates between substrates and antagonists
    • FARIA T, TIMOSZYK JK, STOUCH TR et al.: A novel high-troughput PepT1 transporter assay differentiates between substrates and antagonists. Mol. Pharm. (2004) 1:67-76.
    • (2004) Mol. Pharm. , vol.1 , pp. 67-76
    • Faria, T.1    Timoszyk, J.K.2    Stouch, T.R.3
  • 28
    • 0032573036 scopus 로고    scopus 로고
    • Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions
    • COVITZ KMY, AMIDON GL, SADEE W: Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions. Biochemistry (1998) 37:15214-15221.
    • (1998) Biochemistry , vol.37 , pp. 15214-15221
    • Covitz, K.M.Y.1    Amidon, G.L.2    Sadee, W.3
  • 29
    • 0037087439 scopus 로고    scopus 로고
    • Importance of a small N-terminal region in mammalian peptide transporters for substrate affinity and function
    • DORING F, MARTINI C, WALTER J, DANIEL H: Importance of a small N-terminal region in mammalian peptide transporters for substrate affinity and function. J. Membr. Biol. (2002) 186:55-62.
    • (2002) J. Membr. Biol. , vol.186 , pp. 55-62
    • Doring, F.1    Martini, C.2    Walter, J.3    Daniel, H.4
  • 30
    • 0032495995 scopus 로고    scopus 로고
    • Identification of a potential substrate binding domain in the mammalian peptide transporters PEPT1 and PEPT2 using PEPT1-PEPT2 and PEPT2-PEPT1 chimeras
    • FEI YJ, LIU JC, FUJITA T, LIANG R, GANAPATHY V, LEIBACH FH: Identification of a potential substrate binding domain in the mammalian peptide transporters PEPT1 and PEPT2 using PEPT1-PEPT2 and PEPT2-PEPT1 chimeras. Biochem. Biophys. Res. Commun. (1998) 246:39-44.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 39-44
    • Fei, Y.J.1    Liu, J.C.2    Fujita, T.3    Liang, R.4    Ganapathy, V.5    Leibach, F.H.6
  • 32
    • 0032851715 scopus 로고    scopus 로고
    • Biopharmaceutics of transmucosal peptide and protein drug administration: Role of transport mechanisms with a focus on the involvement of PepT1
    • LEE VH, CHU C, MAHLIN ED et al.: Biopharmaceutics of transmucosal peptide and protein drug administration: role of transport mechanisms with a focus on the involvement of PepT1. J. Control Rel. (1999) 62:129-140.
    • (1999) J. Control Rel. , vol.62 , pp. 129-140
    • Lee, V.H.1    Chu, C.2    Mahlin, E.D.3
  • 33
    • 0032497316 scopus 로고    scopus 로고
    • Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton- coupled dipeptide transporter (hPepT1)
    • YEUNG AK, BASU SK, WU SK et al.: Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton- coupled dipeptide transporter (hPepT1). Biochem. Biophys. Res. Commun. (1998) 250: 103-107.
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 103-107
    • Yeung, A.K.1    Basu, S.K.2    Wu, S.K.3
  • 34
    • 18744431873 scopus 로고    scopus 로고
    • Structure, function, and molecular modeling approaches to the study of the intestinal dipeptide transporter PepT1
    • BOLGER MB, HAWORTH IS, YEUNG AK et al.: Structure, function, and molecular modeling approaches to the study of the intestinal dipeptide transporter PepT1. J. Pharm. Sci. (1998) 87 1286-1291.
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1286-1291
    • Bolger, M.B.1    Haworth, I.S.2    Yeung, A.K.3
  • 36
    • 0031037730 scopus 로고    scopus 로고
    • Identification of the histidyl residue obligatory for the catalytic activity of the human H+/peptide cotransporters PEPT1 and PEPT2
    • FEI YJ, LIU W, PRASAD PD et al.: Identification of the histidyl residue obligatory for the catalytic activity of the human H+/peptide cotransporters PEPT1 and PEPT2. Biochemistry (1997) 36:452-460.
    • (1997) Biochemistry , vol.36 , pp. 452-460
    • Fei, Y.J.1    Liu, W.2    Prasad, P.D.3
  • 38
    • 0037716534 scopus 로고    scopus 로고
    • Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway
    • KULKARNI AA, HAWORTH IS, LEE VH: Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway. Biochem. Biophys. Res. Commun. (2003) 306 177-185.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 177-185
    • Kulkarni, A.A.1    Haworth, I.S.2    Lee, V.H.3
  • 39
    • 0347064342 scopus 로고    scopus 로고
    • Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis
    • KULKARNI AA, HAWORTH IS, UCHIYAMA T, LEE VH: Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis. J. Biol. Chem. (2003) 278 51833-51840.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51833-51840
    • Kulkarni, A.A.1    Haworth, I.S.2    Uchiyama, T.3    Lee, V.H.4
  • 40
    • 0346846696 scopus 로고    scopus 로고
    • Biophysical evidence for His57 as a proton-binding site in the mammalian intestinal transporter hPepT1
    • UCHIYAMA T, KULKARNI AA, DAVIES DL, LEE VH: Biophysical evidence for His57 as a proton-binding site in the mammalian intestinal transporter hPepT1. Pharm. Res. (2003) 20:1911-1916.
    • (2003) Pharm. Res. , vol.20 , pp. 1911-1916
    • Uchiyama, T.1    Kulkarni, A.A.2    Davies, D.L.3    Lee, V.H.4
  • 41
    • 1942501812 scopus 로고    scopus 로고
    • Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PePT1
    • MEREDITH D: Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PePT1. J. Biol. Chem. (2004) 279 15795-15798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15795-15798
    • Meredith, D.1
  • 42
    • 0345307752 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Overall structure, the sugar-binding site and the alternating access model for transport
    • ABRAMSON J, SMIRNOVA I, KASHO V, VERNER G, IWATA S, KABACK HR: The lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport. FEBS Lett. (2003) 555:96-101.
    • (2003) FEBS Lett. , vol.555 , pp. 96-101
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Iwata, S.5    Kaback, H.R.6
  • 43
    • 85069016570 scopus 로고    scopus 로고
    • Oligopeptide transporter (PepT1) homology model based on lactose permease (LacY)
    • Abstracts of Papers, 227th ACS National Meeting: Anaheim, CA, USA
    • BOLGER MB: Oligopeptide transporter (PepT1) homology model based on lactose permease (LacY). Abstracts of Papers, 227th ACS National Meeting: Anaheim, CA, USA (2004).
    • (2004)
    • Bolger, M.B.1
  • 44
    • 85069016663 scopus 로고    scopus 로고
    • PepT1 substrate transport pharmacophore determinants: Refinement with data from a single consistent functional assay
    • Abstracts of Papers, 227th ACS National Meeting: Anaheim, CA, USA
    • STOUCH TR, FARIA T, TIMOSZYK J. PepT1 substrate transport pharmacophore determinants: Refinement with data from a single consistent functional assay. Abstracts of Papers, 227th ACS National Meeting: Anaheim, CA, USA (2004).
    • (2004)
    • Stouch, T.R.1    Faria, T.2    Timoszyk, J.3
  • 45
    • 3342901760 scopus 로고    scopus 로고
    • A rapid in vitro screening for delivery of peptide-derived peptidase inhibitors as potential drug candidates via epithelial peptide transporters
    • FOLTZ M, MEYER A, THEIS S, DEMUTH HU, DANIEL H: A rapid in vitro screening for delivery of peptide-derived peptidase inhibitors as potential drug candidates via epithelial peptide transporters. J. Pharmacol. Exp. Ther. (2004) 310:695-702.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 695-702
    • Foltz, M.1    Meyer, A.2    Theis, S.3    Demuth, H.U.4    Daniel, H.5
  • 46
    • 0038637117 scopus 로고    scopus 로고
    • Gene expression in the human intestine and correlation with oral valacyclovir pharmacokinetic parameters
    • LANDOWSKI CP, SUN DX, FOSTER DR et al.: Gene expression in the human intestine and correlation with oral valacyclovir pharmacokinetic parameters. J. Pharmacol. Exp. Ther. (2003) 306 778-786.
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 778-786
    • Landowski, C.P.1    Sun, D.X.2    Foster, D.R.3
  • 47
    • 0031022687 scopus 로고    scopus 로고
    • Oral absorption of β-lactams by intestinal peptide transport proteins
    • DANTZIG AH: Oral absorption of β-lactams by intestinal peptide transport proteins. Adv. Drug Deliv. Rev. (1998) 23 63-76.
    • (1998) Adv. Drug Deliv. Rev. , vol.23 , pp. 63-76
    • Dantzig, A.H.1
  • 49
    • 0037308045 scopus 로고    scopus 로고
    • Interactions of the dipeptide ester prodrugs of acyclovir with the intestinal oligopeptide transporter: Competitive inhibition of glycylsarcosine transport in human intestinal cell line Caco-2
    • ANAND BS, PATEL J, MITRA AK: Interactions of the dipeptide ester prodrugs of acyclovir with the intestinal oligopeptide transporter: Competitive inhibition of glycylsarcosine transport in human intestinal cell line Caco-2. J. Pharmacol. Exp. Ther. (2003) 304 781-791.
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 781-791
    • Anand, B.S.1    Patel, J.2    Mitra, A.K.3
  • 50
    • 6344288793 scopus 로고    scopus 로고
    • Pharmacokinetics of novel dipeptide ester prodrugs of acyclovir after oral administration: Intestinal absorption and liver metabolism
    • ANAND BS, KATRAGADDA S, MITRA AK: Pharmacokinetics of novel dipeptide ester prodrugs of acyclovir after oral administration: intestinal absorption and liver metabolism. J. Pharmacol. Exp. Ther. (2004) 311:659-667.
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 659-667
    • Anand, B.S.1    Katragadda, S.2    Mitra, A.K.3
  • 51
    • 3042558629 scopus 로고    scopus 로고
    • Antiepileptic drugs: Indications other than epilepsy
    • SPINA E, PERUGI G: Antiepileptic drugs: indications other than epilepsy. Epileptic Disord. (2004) 6:57-75.
    • (2004) Epileptic Disord. , vol.6 , pp. 57-75
    • Spina, E.1    Perugi, G.2
  • 52
    • 0018682364 scopus 로고
    • Phosphonopeptides as antibacterial agents: Metabolism and pharmacokinetics of alafosfalin in animals and humans
    • ALLEN JG, HAVAS L, LEICHT E, LENOX-SMITH I, NISBET LJ: Phosphonopeptides as antibacterial agents: metabolism and pharmacokinetics of alafosfalin in animals and humans. Antimicrob. Agents Chemother. (1979) 16:306-313.
    • (1979) Antimicrob. Agents Chemother. , vol.16 , pp. 306-313
    • Allen, J.G.1    Havas, L.2    Leicht, E.3    Lenox-Smith, I.4    Nisbet, L.J.5
  • 53
    • 0018887830 scopus 로고
    • Pharmacokinetics of alafosfalin, alone and in combination with cephalexin, in humans
    • ALLEN JG, LEES LJ: Pharmacokinetics of alafosfalin, alone and in combination with cephalexin, in humans. Antimicrob. Agents Chemother. (1980) 17:973-979.
    • (1980) Antimicrob. Agents Chemother. , vol.17 , pp. 973-979
    • Allen, J.G.1    Lees, L.J.2
  • 54
    • 0025638981 scopus 로고
    • Pharmacokinetic comparison between fosfomycin and other phosphonic acid derivatives
    • BERGAN T: Pharmacokinetic comparison between fosfomycin and other phosphonic acid derivatives. Chemotherapy (1990) 36 1):10-18.
    • (1990) Chemotherapy , vol.36 , Issue.1 , pp. 10-18
    • Bergan, T.1
  • 56
    • 0020616474 scopus 로고
    • Phosphonopeptides as substrates for peptide transport systems and peptidases of Escherichia coli
    • ATHERTON FR, HALL MJ, HASSALL CH et al.: Phosphonopeptides as substrates for peptide transport systems and peptidases of Escherichia coli. Antimicrob. Agents Chemother. (1983) 24:522-528.
    • (1983) Antimicrob. Agents Chemother. , vol.24 , pp. 522-528
    • Atherton, F.R.1    Hall, M.J.2    Hassall, C.H.3
  • 57
    • 2442688922 scopus 로고    scopus 로고
    • +/peptide cotransporters PEPT1 and PEPT2 in intestinal and renal epithelial cells
    • +/peptide cotransporters PEPT1 and PEPT2 in intestinal and renal epithelial cells. Eur. J. Biochem. (2004) 271:2012-2017.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2012-2017
    • Neumann, J.1    Bruch, M.2    Gebauer, S.3    Brandsch, M.4
  • 58
    • 0141569531 scopus 로고    scopus 로고
    • Metabolism and pharmacokinetics of a dipeptidyl peptidase IV inhibitor in rats, dogs, and monkeys with selective carbamoyl glucuronidation of the primary amine in dogs
    • BECONI MG, MAO A, LIU DQ et al.: Metabolism and pharmacokinetics of a dipeptidyl peptidase IV inhibitor in rats, dogs, and monkeys with selective carbamoyl glucuronidation of the primary amine in dogs. Drug Metab. Dispos. (2003) 31:1269-1277.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1269-1277
    • Beconi, M.G.1    Mao, A.2    Liu, D.Q.3
  • 59
    • 0036689265 scopus 로고    scopus 로고
    • Mechanism of corneal permeation of L-valyl ester of acyclovir: Targeting the oligopeptide transporter on the rabbit cornea
    • ANAND BS, MITRA AK: Mechanism of corneal permeation of L-valyl ester of acyclovir: targeting the oligopeptide transporter on the rabbit cornea. Pharm. Res. (2002) 19:1194-1202.
    • (2002) Pharm. Res. , vol.19 , pp. 1194-1202
    • Anand, B.S.1    Mitra, A.K.2
  • 60
    • 0013298520 scopus 로고    scopus 로고
    • Novel dipeptide prodrugs of acyclovir for ocular herpes infections: Bioreversion, antiviral activity and transport across rabbit cornea
    • ANAND B, NASHED Y, MITRA A: Novel dipeptide prodrugs of acyclovir for ocular herpes infections: Bioreversion, antiviral activity and transport across rabbit cornea. Curr. Eye Res. (2003) 26 151-163.
    • (2003) Curr. Eye Res. , vol.26 , pp. 151-163
    • Anand, B.1    Nashed, Y.2    Mitra, A.3
  • 61
    • 1342329731 scopus 로고    scopus 로고
    • + and expression of the transporter in tissues amenable for drug delivery
    • + and expression of the transporter in tissues amenable for drug delivery. J. Pharmacol. Exp. Ther. (2004) 308 1138-1147.
    • (2004) J. Pharmacol. Exp. Ther. , vol.308 , pp. 1138-1147
    • Hatanaka, T.1    Haramura, M.2    Fei, Y.J.3
  • 62
    • 0141567449 scopus 로고    scopus 로고
    • Preliminary investigation into the expression of proton-coupled oligopeptide transporters in neural retina and retinal pigment epithelium (RPE): Lack of functional activity in RPE plasma membranes
    • OCHELTREE SM, KEEP RF, SHEN H, YANG D, HUGHES BA, SMITH DE: Preliminary investigation into the expression of proton-coupled oligopeptide transporters in neural retina and retinal pigment epithelium (RPE): lack of functional activity in RPE plasma membranes. Pharm. Res. (2003) 20:1364-1372.
    • (2003) Pharm. Res. , vol.20 , pp. 1364-1372
    • Ocheltree, S.M.1    Keep, R.F.2    Shen, H.3    Yang, D.4    Hughes, B.A.5    Smith, D.E.6
  • 63
    • 1342329764 scopus 로고    scopus 로고
    • Mechanism of a model dipeptide transport across blood-ocular barriers following systemic administration
    • ATLURI H, ANAND BS, PATEL J, MITRA AK: Mechanism of a model dipeptide transport across blood-ocular barriers following systemic administration. Exp. Eye Res. (2004) 78:815-822.
    • (2004) Exp. Eye Res. , vol.78 , pp. 815-822
    • Atluri, H.1    Anand, B.S.2    Patel, J.3    Mitra, A.K.4
  • 64
    • 0013068816 scopus 로고    scopus 로고
    • Targeted disruption of the PEPT2 gene markedly reduces dipeptide uptake in choroid plexus
    • SHEN H, SMITH DE, KEEP RF, XIANG J, BROSIUS FC III: Targeted disruption of the PEPT2 gene markedly reduces dipeptide uptake in choroid plexus. J. Biol. Chem. (2003) 278:4786-4791.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4786-4791
    • Shen, H.1    Smith, D.E.2    Keep, R.F.3    Xiang, J.4    Brosius III, F.C.5
  • 65
    • 1942487737 scopus 로고    scopus 로고
    • Carnosine uptake in rat choroid plexus primary cell cultures and choroid plexus whole tissue from PEPT2 null mice
    • TEUSCHER NS, SHEN H, SHU C, XIANG J, KEEP RF, SMITH DE: Carnosine uptake in rat choroid plexus primary cell cultures and choroid plexus whole tissue from PEPT2 null mice. J. Neurochem. (2004) 89:375-382.
    • (2004) J. Neurochem. , vol.89 , pp. 375-382
    • Teuscher, N.S.1    Shen, H.2    Shu, C.3    Xiang, J.4    Keep, R.F.5    Smith, D.E.6
  • 66
    • 1542771649 scopus 로고    scopus 로고
    • Mechanisms of cefadroxil uptake in the choroid plexus: Studies in wild-type and PEPT2 knockout mice
    • OCHELTREE SM, SHEN H, HU Y, XIANG J, KEEP RF, SMITH DE: Mechanisms of cefadroxil uptake in the choroid plexus: studies in wild-type and PEPT2 knockout mice. J. Pharmacol. Exp. Ther. (2004) 308:462-467.
    • (2004) J. Pharmacol. Exp. Ther. , vol.308 , pp. 462-467
    • Ocheltree, S.M.1    Shen, H.2    Hu, Y.3    Xiang, J.4    Keep, R.F.5    Smith, D.E.6
  • 67
    • 0033047381 scopus 로고    scopus 로고
    • Distribution of peptide transporter PEPT2 mRNA in the rat nervous system
    • BERGER UV, HEDIGER MA: Distribution of peptide transporter PEPT2 mRNA in the rat nervous system. Anat. Embryol. (1999) 199 439-449.
    • (1999) Anat. Embryol. , vol.199 , pp. 439-449
    • Berger, U.V.1    Hediger, M.A.2
  • 68
    • 0032889671 scopus 로고    scopus 로고
    • The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative β-Ala-Lys-Nepsilon-AMCA in astrocytes
    • DIECK S T, HEUER H, EHRCHEN J, OTTO C, BAUER K: The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative β-Ala-Lys-Nepsilon-AMCA in astrocytes. Glia (1999) 25:10-20.
    • (1999) Glia , vol.25 , pp. 10-20
    • Dieck, S.T.1    Heuer, H.2    Ehrchen, J.3    Otto, C.4    Bauer, K.5
  • 69
    • 2942544305 scopus 로고    scopus 로고
    • Direct visualization of peptide uptake activity in the central nervous system of the rat
    • GRONEBERG DA, RUBIO-ALIAGA I, NICKOLAUS M, DORING F, DANIEL H: Direct visualization of peptide uptake activity in the central nervous system of the rat. Neurosci. Lett. (2004) 364:32-36.
    • (2004) Neurosci. Lett. , vol.364 , pp. 32-36
    • Groneberg, D.A.1    Rubio-Aliaga, I.2    Nickolaus, M.3    Doring, F.4    Daniel, H.5
  • 72
    • 1942452552 scopus 로고    scopus 로고
    • Peptide and peptide analog transport systems at the blood-CSF barrier
    • SMITH DE, JOHANSON CE, KEEP RF: Peptide and peptide analog transport systems at the blood-CSF barrier. Adv. Drug Deliv. Rev. (2004) 56:1765-1791.
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 1765-1791
    • Smith, D.E.1    Johanson, C.E.2    Keep, R.F.3
  • 73
    • 0037380039 scopus 로고    scopus 로고
    • Delta-aminolevulinic acid transport in cancer cells of the human extrahepatic biliary duct
    • NEUMANN J, BRANDSCH M: Delta-aminolevulinic acid transport in cancer cells of the human extrahepatic biliary duct. J. Pharmacol. Exp. Ther. (2003) 305:219-224.
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 219-224
    • Neumann, J.1    Brandsch, M.2
  • 75
    • 9444226965 scopus 로고    scopus 로고
    • Mutation screening of two candidate genes from 13q32 in families affected with Bipolar disorder: Human peptide transporter (SLC15A1) and human glypican5 (GPC5)
    • MAHESHWARI M, CHRISTIAN S, LIU C et al.: Mutation screening of two candidate genes from 13q32 in families affected with Bipolar disorder: human peptide transporter (SLC15A1) and human glypican5 (GPC5). BMC Genomics (2002) 3:30.
    • (2002) BMC Genomics , vol.3 , pp. 30
    • Maheshwari, M.1    Christian, S.2    Liu, C.3
  • 76
    • 0037636412 scopus 로고    scopus 로고
    • Intra- and interindividuall variabilities of valacyclovir oral bioavailability and effect of coadministration of an hPEPT1 inhibitor
    • PHAN DD, CHIN-HONG P, LIN ET, ERLE P, SADEE W, GUGLIELMO BJ: Intra- and interindividuall variabilities of valacyclovir oral bioavailability and effect of coadministration of an hPEPT1 inhibitor. Antimicrob. Agents Chemother. (2003) 47:2351-2353.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2351-2353
    • Phan, D.D.1    Chin-Hong, P.2    Lin, E.T.3    Erle, P.4    Sadee, W.5    Guglielmo, B.J.6
  • 78
    • 0029036084 scopus 로고
    • Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney
    • LIU W, LIANG R, RAMAMOORTHY S et al.: Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney. Biochim. Biophys. Acta. (1995) 1235:461-466.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 461-466
    • Liu, W.1    Liang, R.2    Ramamoorthy, S.3
  • 79
    • 0011896592 scopus 로고    scopus 로고
    • Human proton/oligopeptide transporter (POT) genes: Identification of putative genes using bioinformatics
    • BOTKA CW, WITTIG TW, GRAUL RC et al. Human proton/oligopeptide transporter (POT) genes: identification of putative genes using bioinformatics. AAPS Pharmsci. (2000) 2:16.
    • (2000) AAPS Pharmsci. , vol.2 , pp. 16
    • Botka, C.W.1    Wittig, T.W.2    Graul, R.C.3
  • 80
    • 0028322020 scopus 로고
    • Association of intestinal peptide transport with a protein related to the cadherin superfamily
    • DANTZIG AH, HOSKINS JA, TABAS LB, et al.: Association of intestinal peptide transport with a protein related to the cadherin superfamily. Science. (1994) 264:430-433.
    • (1994) Science , vol.264 , pp. 430-433
    • Dantzig, A.H.1    Hoskins, J.A.2    Tabas, L.B.3
  • 81
    • 0032005174 scopus 로고    scopus 로고
    • An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2
    • GONZALEZ DE, COVITZ KM SADEE W, MRSNY RJ: An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2. Cancer Res. (1998) 58:519-525.
    • (1998) Cancer Res. , vol.58 , pp. 519-525
    • Gonzalez, D.E.1    Covitz, K.M.2    Sadee, W.3    Mrsny, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.