메뉴 건너뛰기




Volumn 27, Issue 5, 2009, Pages 485-494

Cosmeceuticals and peptides

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL HEXAPEPTIDE 3; ACETYL OCTAPEPTIDE 1; ACETYL TETRAPEPTIDE 2; ACETYL TETRAPEPTIDE 5; ACETYLPEPTIDE 1; ALPHA INTERMEDIN; ARGIRELINE; BOTULINUM TOXIN A; CALCIPOTRIOL; COSMETIC; DIPEPTIDE; DIPEPTIDE 2; DIPEPTIDE DIAMINOBUTYROYL BENZYLAMIDE DIACETATE; HEXAPEPTIDE 10; KOJIC ACID; MATRIXYL; NONAPEPTIDE 1; OLIGOPEPTIDE 10; OLIGOPEPTIDE 20; PALMITOYL HEXAPEPTIDE 6; PALMITOYL OLIGOPEPTIDE; PALMITOYL PENTAPEPTIDE 3; PALMITOYL TETRAPEPTIDE 7; PALMITOYL TRIPEPTIDE 5; PENTAPEPTIDE 3; PEPTIDE; RIGIN; SYNTHETIC PEPTIDE; TRIPEPTIDE; TRIPEPTIDE 1; TRIPEPTIDE 10 CITRULLINE; TRIPEPTIDE 2; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 68649106177     PISSN: 0738081X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clindermatol.2009.05.013     Document Type: Article
Times cited : (109)

References (100)
  • 1
    • 4243734507 scopus 로고    scopus 로고
    • EEMCO guidance to the in vivo assessment of tensile functional properties of the skin. Part 1: relevance to the structures and ageing of the skin and subcutaneous tissues
    • Pierard G.E. EEMCO guidance to the in vivo assessment of tensile functional properties of the skin. Part 1: relevance to the structures and ageing of the skin and subcutaneous tissues. Skin Pharmacol Appl Skin Physiol 12 (1999) 352-362
    • (1999) Skin Pharmacol Appl Skin Physiol , vol.12 , pp. 352-362
    • Pierard, G.E.1
  • 2
    • 0022001786 scopus 로고
    • Cutaneous wound healing: a model for cell-matrix interactions
    • Woodley D.T., O'Keefe E.J., and Prunieras M. Cutaneous wound healing: a model for cell-matrix interactions. J Am Acad Dermatol 12 (1985) 420-433
    • (1985) J Am Acad Dermatol , vol.12 , pp. 420-433
    • Woodley, D.T.1    O'Keefe, E.J.2    Prunieras, M.3
  • 3
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams J.C., and Watt F.M. Regulation of development and differentiation by the extracellular matrix. Development 117 (1993) 1183-1198
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.M.2
  • 4
    • 0022918931 scopus 로고
    • Collagen types I, III, and V in human embryonic and fetal skin
    • Smith L.T., Holbrook K.A., and Madri J.A. Collagen types I, III, and V in human embryonic and fetal skin. Am J Anat 175 (1986) 507-521
    • (1986) Am J Anat , vol.175 , pp. 507-521
    • Smith, L.T.1    Holbrook, K.A.2    Madri, J.A.3
  • 5
    • 1342279516 scopus 로고    scopus 로고
    • An introduction to matrikines: extracellular matrix-derived peptides which regulate cell activity. Implication in tumor invasion
    • Maquart F.X., Pasco S., Ramont L., Hornebeck W., and Monboisse J.C. An introduction to matrikines: extracellular matrix-derived peptides which regulate cell activity. Implication in tumor invasion. Crit Rev Oncol Hematol 49 (2004) 199-202
    • (2004) Crit Rev Oncol Hematol , vol.49 , pp. 199-202
    • Maquart, F.X.1    Pasco, S.2    Ramont, L.3    Hornebeck, W.4    Monboisse, J.C.5
  • 6
    • 0642283420 scopus 로고    scopus 로고
    • Cryptic sites and matrikines: cellular effects of fibronectin and laminin peptides
    • Labat-Robert J. Cryptic sites and matrikines: cellular effects of fibronectin and laminin peptides. J Soc Biol 197 (2003) 45-51
    • (2003) J Soc Biol , vol.197 , pp. 45-51
    • Labat-Robert, J.1
  • 7
    • 25644446962 scopus 로고    scopus 로고
    • Matrikines and matricryptins: Implications for cutaneous cancers and skin repair
    • Tran K.T., Lamb P., and Deng J.S. Matrikines and matricryptins: Implications for cutaneous cancers and skin repair. J Dermatol Sci 40 (2005) 11-20
    • (2005) J Dermatol Sci , vol.40 , pp. 11-20
    • Tran, K.T.1    Lamb, P.2    Deng, J.S.3
  • 8
    • 0035939665 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor
    • Swindle C.S., Tran K.T., Johnson T.D., et al. Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor. J Cell Biol 154 (2001) 459-468
    • (2001) J Cell Biol , vol.154 , pp. 459-468
    • Swindle, C.S.1    Tran, K.T.2    Johnson, T.D.3
  • 9
    • 0344953584 scopus 로고    scopus 로고
    • Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration
    • Pirila E., Sharabi A., Salo T., et al. Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration. Biochem Biophys Res Commun 303 (2003) 1012-1017
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 1012-1017
    • Pirila, E.1    Sharabi, A.2    Salo, T.3
  • 10
    • 33646258995 scopus 로고    scopus 로고
    • Role of matrikins in melanoma progression
    • Hornebeck W., and Maquart F.X. Role of matrikins in melanoma progression. Ann Pharm Fr 64 (2006) 83-86
    • (2006) Ann Pharm Fr , vol.64 , pp. 83-86
    • Hornebeck, W.1    Maquart, F.X.2
  • 11
    • 3042736423 scopus 로고    scopus 로고
    • Extracellular matrix signaling through growth factor receptors during wound healing
    • Tran K.T., Griffith L., and Wells A. Extracellular matrix signaling through growth factor receptors during wound healing. Wound Repair Regen 12 (2004) 262-268
    • (2004) Wound Repair Regen , vol.12 , pp. 262-268
    • Tran, K.T.1    Griffith, L.2    Wells, A.3
  • 12
    • 0023008543 scopus 로고
    • Post-transcriptional inhibition of collagen and fibronectin synthesis by a synthetic homolog of a portion of the carboxyl-terminal propeptide of human type I collagen
    • Aycock R.S., Raghow R., Stricklin G.P., Seyer J.M., and Kang A.H. Post-transcriptional inhibition of collagen and fibronectin synthesis by a synthetic homolog of a portion of the carboxyl-terminal propeptide of human type I collagen. J Biol Chem 261 (1986) 14355-14360
    • (1986) J Biol Chem , vol.261 , pp. 14355-14360
    • Aycock, R.S.1    Raghow, R.2    Stricklin, G.P.3    Seyer, J.M.4    Kang, A.H.5
  • 13
    • 0025827637 scopus 로고
    • Regulation of extracellular matrix production by chemically synthesized subfragments of type I collagen carboxy propeptide
    • Katayama K., Seyer J.M., Raghow R., and Kang A.H. Regulation of extracellular matrix production by chemically synthesized subfragments of type I collagen carboxy propeptide. Biochemistry 30 (1991) 7097-7104
    • (1991) Biochemistry , vol.30 , pp. 7097-7104
    • Katayama, K.1    Seyer, J.M.2    Raghow, R.3    Kang, A.H.4
  • 14
    • 0027289111 scopus 로고
    • Apentapeptide from type I procollagen promotes extracellular matrix production
    • Katayama K., Armendariz-Borunda J., Raghow R., Kang A.H., and Seyer J.M. Apentapeptide from type I procollagen promotes extracellular matrix production. J Biol Chem 268 (1993) 9941-9944
    • (1993) J Biol Chem , vol.268 , pp. 9941-9944
    • Katayama, K.1    Armendariz-Borunda, J.2    Raghow, R.3    Kang, A.H.4    Seyer, J.M.5
  • 15
    • 0027184575 scopus 로고
    • Valyl-alanyl-prolyl-glycine (VAPG) serves as a quantitative marker for human elastins
    • Price L.S., Roos P.J., Shively V.P., and Sandberg L.B. Valyl-alanyl-prolyl-glycine (VAPG) serves as a quantitative marker for human elastins. Matrix 13 (1993) 307-311
    • (1993) Matrix , vol.13 , pp. 307-311
    • Price, L.S.1    Roos, P.J.2    Shively, V.P.3    Sandberg, L.B.4
  • 16
    • 0027536583 scopus 로고
    • PGAIPG, a repeated hexapeptide of bovine tropoelastin, is a ligand for the 67-kDa bovine elastin receptor
    • Grosso L.E., and Scott M. PGAIPG, a repeated hexapeptide of bovine tropoelastin, is a ligand for the 67-kDa bovine elastin receptor. Matrix 13 (1993) 157-164
    • (1993) Matrix , vol.13 , pp. 157-164
    • Grosso, L.E.1    Scott, M.2
  • 17
    • 0022530366 scopus 로고
    • Quantitation of elastin through measurement of its pentapeptide content
    • Sandberg L.B., Wolt T.B., and Leslie J.G. Quantitation of elastin through measurement of its pentapeptide content. Biochem Biophys Res Commun 136 (1986) 672-678
    • (1986) Biochem Biophys Res Commun , vol.136 , pp. 672-678
    • Sandberg, L.B.1    Wolt, T.B.2    Leslie, J.G.3
  • 19
    • 0021884113 scopus 로고
    • Elastin fragment-induced monocyte chemotaxis. The role of desmosines
    • Kunitomo M., and Jay M. Elastin fragment-induced monocyte chemotaxis. The role of desmosines. Inflammation 9 (1985) 183-188
    • (1985) Inflammation , vol.9 , pp. 183-188
    • Kunitomo, M.1    Jay, M.2
  • 20
    • 0022883411 scopus 로고
    • Effect of elastin peptides on human monocytes: Ca2+ mobilization, stimulation of respiratory burst and enzyme secretion
    • Fulop Jr. T., Jacob M.P., Varga Z., Foris G., Leovey A., and Robert L. Effect of elastin peptides on human monocytes: Ca2+ mobilization, stimulation of respiratory burst and enzyme secretion. Biochem Biophys Res Commun 141 (1986) 92-98
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 92-98
    • Fulop Jr., T.1    Jacob, M.P.2    Varga, Z.3    Foris, G.4    Leovey, A.5    Robert, L.6
  • 21
    • 0021170197 scopus 로고
    • Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes
    • Senior R.M., Griffin G.L., Mecham R.P., Wrenn D.S., Prasad K.U., and Urry D.W. Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes. J Cell Biol 99 (1984) 870-874
    • (1984) J Cell Biol , vol.99 , pp. 870-874
    • Senior, R.M.1    Griffin, G.L.2    Mecham, R.P.3    Wrenn, D.S.4    Prasad, K.U.5    Urry, D.W.6
  • 22
    • 0030956837 scopus 로고    scopus 로고
    • Elastin-derived peptide induces monocyte chemotaxis by increasing intracellular cyclic GMP level and activating cyclic GMP dependent protein kinase
    • Uemura Y., and Okamoto K. Elastin-derived peptide induces monocyte chemotaxis by increasing intracellular cyclic GMP level and activating cyclic GMP dependent protein kinase. Biochem Mol Biol Int 41 (1997) 57-64
    • (1997) Biochem Mol Biol Int , vol.41 , pp. 57-64
    • Uemura, Y.1    Okamoto, K.2
  • 24
    • 0024429719 scopus 로고
    • Elastin repeat peptides as chemoattractants for bovine aortic endothelial cells
    • Long M.M., King V.J., Prasad K.U., Freeman B.A., and Urry D.W. Elastin repeat peptides as chemoattractants for bovine aortic endothelial cells. J Cell Physiol 140 (1989) 512-518
    • (1989) J Cell Physiol , vol.140 , pp. 512-518
    • Long, M.M.1    King, V.J.2    Prasad, K.U.3    Freeman, B.A.4    Urry, D.W.5
  • 25
    • 0024110163 scopus 로고
    • Identification of a tumor cell receptor for VGVAPG, an elastin-derived chemotactic peptide
    • Blood C.H., Sasse J., Brodt P., and Zetter B.R. Identification of a tumor cell receptor for VGVAPG, an elastin-derived chemotactic peptide. J Cell Biol 107 (1988) 1987-1993
    • (1988) J Cell Biol , vol.107 , pp. 1987-1993
    • Blood, C.H.1    Sasse, J.2    Brodt, P.3    Zetter, B.R.4
  • 26
    • 0024375589 scopus 로고
    • Membrane-bound protein kinase C modulates receptor affinity and chemotactic responsiveness of Lewis lung carcinoma sublines to an elastin-derived peptide
    • Blood C.H., and Zetter B.R. Membrane-bound protein kinase C modulates receptor affinity and chemotactic responsiveness of Lewis lung carcinoma sublines to an elastin-derived peptide. J Biol Chem 264 (1989) 10614-10620
    • (1989) J Biol Chem , vol.264 , pp. 10614-10620
    • Blood, C.H.1    Zetter, B.R.2
  • 27
    • 14044271602 scopus 로고    scopus 로고
    • Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP
    • Robinet A., Fahem A., Cauchard J.H., et al. Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP. J Cell Sci 118 (2005) 343-356
    • (2005) J Cell Sci , vol.118 , pp. 343-356
    • Robinet, A.1    Fahem, A.2    Cauchard, J.H.3
  • 28
    • 0029593563 scopus 로고
    • Growth stimulation of human skin fibroblasts by elastin-derived peptides
    • Kamoun A., Landeau J.M., Godeau G., et al. Growth stimulation of human skin fibroblasts by elastin-derived peptides. Cell Adhes Commun 3 (1995) 273-281
    • (1995) Cell Adhes Commun , vol.3 , pp. 273-281
    • Kamoun, A.1    Landeau, J.M.2    Godeau, G.3
  • 29
    • 0015927421 scopus 로고
    • Tripeptide in human serum which prolongs survival of normal liver cells and stimulates growth in neoplastic liver
    • Pickart L., and Thaler M.M. Tripeptide in human serum which prolongs survival of normal liver cells and stimulates growth in neoplastic liver. Nat New Biol 243 (1973) 85-87
    • (1973) Nat New Biol , vol.243 , pp. 85-87
    • Pickart, L.1    Thaler, M.M.2
  • 30
    • 0015908073 scopus 로고
    • Asynthetic tripeptide which increases survival of normal liver cells, and stimulates growth in hepatoma cells
    • Pickart L., Thayer L., and Thaler M.M. Asynthetic tripeptide which increases survival of normal liver cells, and stimulates growth in hepatoma cells. Biochem Biophys Res Commun 54 (1973) 562-566
    • (1973) Biochem Biophys Res Commun , vol.54 , pp. 562-566
    • Pickart, L.1    Thayer, L.2    Thaler, M.M.3
  • 31
    • 0023719508 scopus 로고
    • Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+
    • Maquart F.X., Pickart L., Laurent M., Gillery P., Monboisse J.C., and Borel J.P. Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS Lett 238 (1988) 343-346
    • (1988) FEBS Lett , vol.238 , pp. 343-346
    • Maquart, F.X.1    Pickart, L.2    Laurent, M.3    Gillery, P.4    Monboisse, J.C.5    Borel, J.P.6
  • 32
    • 18244403133 scopus 로고    scopus 로고
    • Biotinylated GHK peptide incorporated collagenous matrix: A novel biomaterial for dermal wound healing in rats
    • Arul V., Gopinath D., Gomathi K., and Jayakumar R. Biotinylated GHK peptide incorporated collagenous matrix: A novel biomaterial for dermal wound healing in rats. J Biomed Mater Res B Appl Biomater 73 (2005) 383-391
    • (2005) J Biomed Mater Res B Appl Biomater , vol.73 , pp. 383-391
    • Arul, V.1    Gopinath, D.2    Gomathi, K.3    Jayakumar, R.4
  • 33
    • 33845623411 scopus 로고    scopus 로고
    • Atherapeutic approach for diabetic wound healing using biotinylated GHK incorporated collagen matrices
    • Arul V., Kartha R., and Jayakumar R. Atherapeutic approach for diabetic wound healing using biotinylated GHK incorporated collagen matrices. Life Sci 80 (2007) 275-284
    • (2007) Life Sci , vol.80 , pp. 275-284
    • Arul, V.1    Kartha, R.2    Jayakumar, R.3
  • 34
    • 0027443057 scopus 로고
    • In vivo stimulation of connective tissue accumulation by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ in rat experimental wounds
    • Maquart F.X., Bellon G., Chaqour B., et al. In vivo stimulation of connective tissue accumulation by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ in rat experimental wounds. J Clin Invest 92 (1993) 2368-2376
    • (1993) J Clin Invest , vol.92 , pp. 2368-2376
    • Maquart, F.X.1    Bellon, G.2    Chaqour, B.3
  • 35
    • 0018763217 scopus 로고
    • Growth-modulating human plasma tripeptide: relationship between molecular structure and DNA synthesis in hepatoma cells
    • Pickart L., and Thaler M.M. Growth-modulating human plasma tripeptide: relationship between molecular structure and DNA synthesis in hepatoma cells. FEBS Lett 104 (1979) 119-122
    • (1979) FEBS Lett , vol.104 , pp. 119-122
    • Pickart, L.1    Thaler, M.M.2
  • 36
    • 0018826944 scopus 로고
    • Growth-modulating tripeptide (glycylhistidyllysine): association with copper and iron in plasma, and stimulation of adhesiveness and growth of hepatoma cells in culture by tripeptide-metal ion complexes
    • Pickart L., and Thaler M.M. Growth-modulating tripeptide (glycylhistidyllysine): association with copper and iron in plasma, and stimulation of adhesiveness and growth of hepatoma cells in culture by tripeptide-metal ion complexes. J Cell Physiol 102 (1980) 129-139
    • (1980) J Cell Physiol , vol.102 , pp. 129-139
    • Pickart, L.1    Thaler, M.M.2
  • 37
    • 0021068289 scopus 로고
    • Stimulation of rat peritoneal mast cell migration by tumor-derived peptides
    • Poole T.J., and Zetter B.R. Stimulation of rat peritoneal mast cell migration by tumor-derived peptides. Cancer Res 43 (1983) 5857-5861
    • (1983) Cancer Res , vol.43 , pp. 5857-5861
    • Poole, T.J.1    Zetter, B.R.2
  • 38
    • 0022118928 scopus 로고
    • An in vivo assay for chemoattractant activity
    • Zetter B.R., Rasmussen N., and Brown L. An in vivo assay for chemoattractant activity. Lab Invest 53 (1985) 362-368
    • (1985) Lab Invest , vol.53 , pp. 362-368
    • Zetter, B.R.1    Rasmussen, N.2    Brown, L.3
  • 39
    • 0019272157 scopus 로고
    • Experimental influence of pharmacological agents on the regeneration of nervous tissue in vitro
    • Grosse G., and Lindner G. Experimental influence of pharmacological agents on the regeneration of nervous tissue in vitro. Folia Morphol (Praha) 28 (1980) 345-347
    • (1980) Folia Morphol (Praha) , vol.28 , pp. 345-347
    • Grosse, G.1    Lindner, G.2
  • 41
    • 0028355889 scopus 로고
    • SPARC is a source of copper-binding peptides that stimulate angiogenesis
    • Lane T.F., Iruela-Arispe M.L., Johnson R.S., and Sage E.H. SPARC is a source of copper-binding peptides that stimulate angiogenesis. J Cell Biol 125 (1994) 929-943
    • (1994) J Cell Biol , vol.125 , pp. 929-943
    • Lane, T.F.1    Iruela-Arispe, M.L.2    Johnson, R.S.3    Sage, E.H.4
  • 42
    • 0026757171 scopus 로고
    • Stimulation of sulfated glycosaminoglycan synthesis by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+
    • Wegrowski Y., Maquart F.X., and Borel J.P. Stimulation of sulfated glycosaminoglycan synthesis by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. Life Sci 51 (1992) 1049-1056
    • (1992) Life Sci , vol.51 , pp. 1049-1056
    • Wegrowski, Y.1    Maquart, F.X.2    Borel, J.P.3
  • 43
    • 0023579695 scopus 로고
    • Biological activity of human plasma copper-binding growth factor glycyl-L-histidyl-L-lysine
    • Pickart L., and Lovejoy S. Biological activity of human plasma copper-binding growth factor glycyl-L-histidyl-L-lysine. Methods Enzymol 147 (1987) 314-328
    • (1987) Methods Enzymol , vol.147 , pp. 314-328
    • Pickart, L.1    Lovejoy, S.2
  • 44
    • 84989141943 scopus 로고
    • Enhanced healing of ulcers in patients with diabetes by topical treatment with glycyl-l-histidyl-l-lysine copper
    • Mulder G.D., Patt L.M., Sanders L., et al. Enhanced healing of ulcers in patients with diabetes by topical treatment with glycyl-l-histidyl-l-lysine copper. Wound Repair Regen 2 (1994) 259-269
    • (1994) Wound Repair Regen , vol.2 , pp. 259-269
    • Mulder, G.D.1    Patt, L.M.2    Sanders, L.3
  • 45
    • 0034703502 scopus 로고    scopus 로고
    • The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ stimulates matrix metalloproteinase-2 expression by fibroblast cultures
    • Simeon A., Emonard H., Hornebeck W., and Maquart F.X. The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ stimulates matrix metalloproteinase-2 expression by fibroblast cultures. Life Sci 67 (2000) 2257-2265
    • (2000) Life Sci , vol.67 , pp. 2257-2265
    • Simeon, A.1    Emonard, H.2    Hornebeck, W.3    Maquart, F.X.4
  • 46
    • 33645803815 scopus 로고    scopus 로고
    • Antimicrobial peptides: therapeutic potential
    • Zhang L., and Falla T.J. Antimicrobial peptides: therapeutic potential. Expert Opin Pharmacother 7 (2006) 653-663
    • (2006) Expert Opin Pharmacother , vol.7 , pp. 653-663
    • Zhang, L.1    Falla, T.J.2
  • 47
    • 33748094122 scopus 로고    scopus 로고
    • Antimicrobial peptides: an essential component of the skin defensive barrier
    • Braff M.H., and Gallo R.L. Antimicrobial peptides: an essential component of the skin defensive barrier. Curr Top Microbiol Immunol 306 (2006) 91-110
    • (2006) Curr Top Microbiol Immunol , vol.306 , pp. 91-110
    • Braff, M.H.1    Gallo, R.L.2
  • 48
    • 21344473480 scopus 로고    scopus 로고
    • Antimicrobial peptides in human skin
    • Harder J., and Schroder J.M. Antimicrobial peptides in human skin. Chem Immunol Allergy 86 (2005) 22-41
    • (2005) Chem Immunol Allergy , vol.86 , pp. 22-41
    • Harder, J.1    Schroder, J.M.2
  • 49
    • 20144367318 scopus 로고    scopus 로고
    • Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities
    • Braff M.H., Hawkins M.A., Di Nardo A., et al. Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities. J Immunol 174 (2005) 4271-4278
    • (2005) J Immunol , vol.174 , pp. 4271-4278
    • Braff, M.H.1    Hawkins, M.A.2    Di Nardo, A.3
  • 50
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K., Chen Q., Yarovinsky F., Oppenheim J.J., and Yang D. Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J Immunol 174 (2005) 6257-6265
    • (2005) J Immunol , vol.174 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 51
    • 27144468929 scopus 로고    scopus 로고
    • Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure
    • Shaykhiev R., Beisswenger C., Kandler K., et al. Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure. Am J Physiol Lung Cell Mol Physiol 289 (2005) L842-L848
    • (2005) Am J Physiol Lung Cell Mol Physiol , vol.289
    • Shaykhiev, R.1    Beisswenger, C.2    Kandler, K.3
  • 52
    • 25444468300 scopus 로고    scopus 로고
    • Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37
    • Tokumaru S., Sayama K., Shirakata Y., et al. Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. J Immunol 175 (2005) 4662-4668
    • (2005) J Immunol , vol.175 , pp. 4662-4668
    • Tokumaru, S.1    Sayama, K.2    Shirakata, Y.3
  • 53
    • 3042775937 scopus 로고    scopus 로고
    • HB-107, a nonbacteriostatic fragment of the antimicrobial peptide cecropin B, accelerates murine wound repair
    • Lee P.H., Rudisill J.A., Lin K.H., et al. HB-107, a nonbacteriostatic fragment of the antimicrobial peptide cecropin B, accelerates murine wound repair. Wound Repair Regen 12 (2004) 351-358
    • (2004) Wound Repair Regen , vol.12 , pp. 351-358
    • Lee, P.H.1    Rudisill, J.A.2    Lin, K.H.3
  • 54
    • 0036887517 scopus 로고    scopus 로고
    • Detection of dermcidin-derived peptides in sweat by ProteinChip technology
    • Flad T., Bogumil R., Tolson J., et al. Detection of dermcidin-derived peptides in sweat by ProteinChip technology. J Immunol Methods 270 (2002) 53-62
    • (2002) J Immunol Methods , vol.270 , pp. 53-62
    • Flad, T.1    Bogumil, R.2    Tolson, J.3
  • 56
    • 17044367481 scopus 로고    scopus 로고
    • Differential regulation of beta-defensin expression in human skin by microbial stimuli
    • Sorensen O.E., Thapa D.R., Rosenthal A., Liu L., Roberts A.A., and Ganz T. Differential regulation of beta-defensin expression in human skin by microbial stimuli. J Immunol 174 (2005) 4870-4879
    • (2005) J Immunol , vol.174 , pp. 4870-4879
    • Sorensen, O.E.1    Thapa, D.R.2    Rosenthal, A.3    Liu, L.4    Roberts, A.A.5    Ganz, T.6
  • 57
    • 26844567701 scopus 로고    scopus 로고
    • Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli
    • Chen X., Niyonsaba F., Ushio H., et al. Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli. J Dermatol Sci 40 (2005) 123-132
    • (2005) J Dermatol Sci , vol.40 , pp. 123-132
    • Chen, X.1    Niyonsaba, F.2    Ushio, H.3
  • 58
    • 22144453571 scopus 로고    scopus 로고
    • Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection
    • Lopez-Garcia B., Lee P.H., Yamasaki K., and Gallo R.L. Anti-fungal activity of cathelicidins and their potential role in Candida albicans skin infection. J Invest Dermatol 125 (2005) 108-115
    • (2005) J Invest Dermatol , vol.125 , pp. 108-115
    • Lopez-Garcia, B.1    Lee, P.H.2    Yamasaki, K.3    Gallo, R.L.4
  • 59
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet V., Ohtake T., Lauth X., et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414 (2001) 454-457
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3
  • 60
    • 14844351540 scopus 로고    scopus 로고
    • Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection
    • Lee P.H., Ohtake T., Zaiou M., et al. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc Natl Acad Sci U S A 102 (2005) 3750-3755
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3750-3755
    • Lee, P.H.1    Ohtake, T.2    Zaiou, M.3
  • 61
    • 33646482761 scopus 로고    scopus 로고
    • Cathelicidin deficiency predisposes to eczema herpeticum
    • Howell M.D., Wollenberg A., Gallo R.L., et al. Cathelicidin deficiency predisposes to eczema herpeticum. J Allergy Clin Immunol 117 (2006) 836-841
    • (2006) J Allergy Clin Immunol , vol.117 , pp. 836-841
    • Howell, M.D.1    Wollenberg, A.2    Gallo, R.L.3
  • 62
    • 20444384801 scopus 로고    scopus 로고
    • Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo
    • Rieg S., Steffen H., Seeber S., et al. Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo. J Immunol 174 (2005) 8003-8010
    • (2005) J Immunol , vol.174 , pp. 8003-8010
    • Rieg, S.1    Steffen, H.2    Seeber, S.3
  • 63
    • 30044433704 scopus 로고    scopus 로고
    • Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37
    • Mookherjee N., Brown K.L., Bowdish D.M., et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J Immunol 176 (2006) 2455-2464
    • (2006) J Immunol , vol.176 , pp. 2455-2464
    • Mookherjee, N.1    Brown, K.L.2    Bowdish, D.M.3
  • 64
    • 24344449113 scopus 로고    scopus 로고
    • Granulysin-derived peptides demonstrate antimicrobial and anti-inflammatory effects against Propionibacterium acnes
    • McInturff J.E., Wang S.J., Machleidt T., et al. Granulysin-derived peptides demonstrate antimicrobial and anti-inflammatory effects against Propionibacterium acnes. J Invest Dermatol 125 (2005) 256-263
    • (2005) J Invest Dermatol , vol.125 , pp. 256-263
    • McInturff, J.E.1    Wang, S.J.2    Machleidt, T.3
  • 66
    • 14644419658 scopus 로고    scopus 로고
    • Inflammation, gene mutation and photoimmunosuppression in response to UVR-induced oxidative damage contributes to photocarcinogenesis
    • Halliday G.M. Inflammation, gene mutation and photoimmunosuppression in response to UVR-induced oxidative damage contributes to photocarcinogenesis. Mutat Res 571 (2005) 107-120
    • (2005) Mutat Res , vol.571 , pp. 107-120
    • Halliday, G.M.1
  • 67
    • 0028048240 scopus 로고
    • Ultraviolet radiation-induced melanogenesis in human melanocytes. Effects of modulating protein kinase C
    • Carsberg C.J., Warenius H.M., and Friedmann P.S. Ultraviolet radiation-induced melanogenesis in human melanocytes. Effects of modulating protein kinase C. J Cell Sci 107 (1994) 2591-2597
    • (1994) J Cell Sci , vol.107 , pp. 2591-2597
    • Carsberg, C.J.1    Warenius, H.M.2    Friedmann, P.S.3
  • 68
    • 0024356985 scopus 로고
    • Regulation of tyrosinase synthesis and its processing in the hair follicular melanocytes of the mouse during eumelanogenesis and phaeomelanogenesis
    • Burchill S.A., Virden R., and Thody A.J. Regulation of tyrosinase synthesis and its processing in the hair follicular melanocytes of the mouse during eumelanogenesis and phaeomelanogenesis. J Invest Dermatol 93 (1989) 236-240
    • (1989) J Invest Dermatol , vol.93 , pp. 236-240
    • Burchill, S.A.1    Virden, R.2    Thody, A.J.3
  • 69
    • 0029863304 scopus 로고    scopus 로고
    • Binding of melanotropic hormones to the melanocortin receptor MC1R on human melanocytes stimulates proliferation and melanogenesis
    • Suzuki I., Cone R.D., Im S., Nordlund J., and Abdel-Malek Z.A. Binding of melanotropic hormones to the melanocortin receptor MC1R on human melanocytes stimulates proliferation and melanogenesis. Endocrinology 137 (1996) 1627-1633
    • (1996) Endocrinology , vol.137 , pp. 1627-1633
    • Suzuki, I.1    Cone, R.D.2    Im, S.3    Nordlund, J.4    Abdel-Malek, Z.A.5
  • 70
    • 33845698356 scopus 로고    scopus 로고
    • Melanoma prevention strategy based on using tetrapeptide alpha-MSH analogs that protect human melanocytes from UV-induced DNA damage and cytotoxicity
    • Abdel-Malek Z.A., Kadekaro A.L., Kavanagh R.J., et al. Melanoma prevention strategy based on using tetrapeptide alpha-MSH analogs that protect human melanocytes from UV-induced DNA damage and cytotoxicity. Faseb J 20 (2006) 1561-1563
    • (2006) Faseb J , vol.20 , pp. 1561-1563
    • Abdel-Malek, Z.A.1    Kadekaro, A.L.2    Kavanagh, R.J.3
  • 71
    • 0033870562 scopus 로고    scopus 로고
    • Inhibition of melanosome transfer results in skin lightening
    • Seiberg M., Paine C., Sharlow E., et al. Inhibition of melanosome transfer results in skin lightening. J Invest Dermatol 115 (2000) 162-167
    • (2000) J Invest Dermatol , vol.115 , pp. 162-167
    • Seiberg, M.1    Paine, C.2    Sharlow, E.3
  • 72
    • 0030970586 scopus 로고    scopus 로고
    • Agouti signaling protein inhibits melanogenesis and the response of human melanocytes to alpha-melanotropin
    • Suzuki I., Tada A., Ollmann M.M., et al. Agouti signaling protein inhibits melanogenesis and the response of human melanocytes to alpha-melanotropin. J Invest Dermatol 108 (1997) 838-842
    • (1997) J Invest Dermatol , vol.108 , pp. 838-842
    • Suzuki, I.1    Tada, A.2    Ollmann, M.M.3
  • 73
    • 0027314530 scopus 로고
    • The beta isoform of protein kinase C stimulates human melanogenesis by activating tyrosinase in pigment cells
    • Park H.Y., Russakovsky V., Ohno S., and Gilchrest B.A. The beta isoform of protein kinase C stimulates human melanogenesis by activating tyrosinase in pigment cells. J Biol Chem 268 (1993) 11742-11749
    • (1993) J Biol Chem , vol.268 , pp. 11742-11749
    • Park, H.Y.1    Russakovsky, V.2    Ohno, S.3    Gilchrest, B.A.4
  • 74
    • 0030601351 scopus 로고    scopus 로고
    • Alpha-melanocyte stimulating hormone-induced pigmentation is blocked by depletion of protein kinase C
    • Park H.Y., Russakovsky V., Ao Y., Fernandez E., and Gilchrest B.A. Alpha-melanocyte stimulating hormone-induced pigmentation is blocked by depletion of protein kinase C. Exp Cell Res 227 (1996) 70-79
    • (1996) Exp Cell Res , vol.227 , pp. 70-79
    • Park, H.Y.1    Russakovsky, V.2    Ao, Y.3    Fernandez, E.4    Gilchrest, B.A.5
  • 75
    • 0013587129 scopus 로고
    • Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus
    • Kwon B.S., Haq A.K., Pomerantz S.H., and Halaban R. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc Natl Acad Sci U S A 84 (1987) 7473-7477
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7473-7477
    • Kwon, B.S.1    Haq, A.K.2    Pomerantz, S.H.3    Halaban, R.4
  • 76
    • 1642534508 scopus 로고    scopus 로고
    • Topical application of a protein kinase C inhibitor reduces skin and hair pigmentation
    • Park H.Y., Lee J., Gonzalez S., et al. Topical application of a protein kinase C inhibitor reduces skin and hair pigmentation. J Invest Dermatol 122 (2004) 159-166
    • (2004) J Invest Dermatol , vol.122 , pp. 159-166
    • Park, H.Y.1    Lee, J.2    Gonzalez, S.3
  • 78
    • 2342586185 scopus 로고    scopus 로고
    • Solid-phase synthesis of kojic acid-tripeptides and their tyrosinase inhibitory activity, storage stability, and toxicity
    • Kim H., Choi J., Cho J.K., Kim S.Y., and Lee Y.S. Solid-phase synthesis of kojic acid-tripeptides and their tyrosinase inhibitory activity, storage stability, and toxicity. Bioorg Med Chem Lett 14 (2004) 2843-2846
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 2843-2846
    • Kim, H.1    Choi, J.2    Cho, J.K.3    Kim, S.Y.4    Lee, Y.S.5
  • 79
    • 34247486130 scopus 로고    scopus 로고
    • Kojic acid-tripeptide amide as a new tyrosinase inhibitor
    • Noh J.M., Kwak S.Y., Kim D.H., and Lee Y.S. Kojic acid-tripeptide amide as a new tyrosinase inhibitor. Biopolymers 88 (2007) 300-307
    • (2007) Biopolymers , vol.88 , pp. 300-307
    • Noh, J.M.1    Kwak, S.Y.2    Kim, D.H.3    Lee, Y.S.4
  • 80
    • 0035889713 scopus 로고    scopus 로고
    • Visualization of neuropeptide expression, transport, and exocytosis in Drosophila melanogaster
    • Rao S., Lang C., Levitan E.S., and Deitcher D.L. Visualization of neuropeptide expression, transport, and exocytosis in Drosophila melanogaster. J Neurobiol 49 (2001) 159-172
    • (2001) J Neurobiol , vol.49 , pp. 159-172
    • Rao, S.1    Lang, C.2    Levitan, E.S.3    Deitcher, D.L.4
  • 81
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino J.S., and Glick B.S. The mechanisms of vesicle budding and fusion. Cell 116 (2004) 153-166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 82
    • 0036876160 scopus 로고    scopus 로고
    • Neuromediators-a crucial component of the skin immune system
    • Luger T.A. Neuromediators-a crucial component of the skin immune system. J Dermatol Sci 30 (2002) 87-93
    • (2002) J Dermatol Sci , vol.30 , pp. 87-93
    • Luger, T.A.1
  • 83
    • 0032515962 scopus 로고    scopus 로고
    • Role of zinc in the structure and toxic activity of botulinum neurotoxin
    • Fu F.N., Lomneth R.B., Cai S., and Singh B.R. Role of zinc in the structure and toxic activity of botulinum neurotoxin. Biochemistry 37 (1998) 5267-5278
    • (1998) Biochemistry , vol.37 , pp. 5267-5278
    • Fu, F.N.1    Lomneth, R.B.2    Cai, S.3    Singh, B.R.4
  • 84
    • 0036435142 scopus 로고    scopus 로고
    • A synthetic hexapeptide (Argireline) with antiwrinkle activity
    • Blanes-Mira C., Clemente J., Jodas G., et al. A synthetic hexapeptide (Argireline) with antiwrinkle activity. Int J Cosmet Sci 24 (2002) 303
    • (2002) Int J Cosmet Sci , vol.24 , pp. 303
    • Blanes-Mira, C.1    Clemente, J.2    Jodas, G.3
  • 85
    • 0037172669 scopus 로고    scopus 로고
    • Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site
    • Molles B.E., Tsigelny I., Nguyen P.D., Gao S.X., Sine S.M., and Taylor P. Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site. Biochemistry 41 (2002) 7895-7906
    • (2002) Biochemistry , vol.41 , pp. 7895-7906
    • Molles, B.E.1    Tsigelny, I.2    Nguyen, P.D.3    Gao, S.X.4    Sine, S.M.5    Taylor, P.6
  • 86
    • 0036715979 scopus 로고    scopus 로고
    • DHEA treatment: myth or reality?
    • Allolio B., and Arlt W. DHEA treatment: myth or reality?. Trends Endocrinol Metab 13 (2002) 288-294
    • (2002) Trends Endocrinol Metab , vol.13 , pp. 288-294
    • Allolio, B.1    Arlt, W.2
  • 87
    • 33646380106 scopus 로고    scopus 로고
    • Effect of dehydroepiandrosterone on lipopolysaccharide-induced interleukin-6 production in DH82 cultured canine macrophage cells
    • Kim S.K., Shin M.S., Jung B.K., et al. Effect of dehydroepiandrosterone on lipopolysaccharide-induced interleukin-6 production in DH82 cultured canine macrophage cells. J Reprod Immunol 70 (2006) 71-81
    • (2006) J Reprod Immunol , vol.70 , pp. 71-81
    • Kim, S.K.1    Shin, M.S.2    Jung, B.K.3
  • 88
    • 33644792125 scopus 로고    scopus 로고
    • The sex steroid precursor DHEA accelerates cutaneous wound healing via the estrogen receptors
    • Mills S.J., Ashworth J.J., Gilliver S.C., Hardman M.J., and Ashcroft G.S. The sex steroid precursor DHEA accelerates cutaneous wound healing via the estrogen receptors. J Invest Dermatol 125 (2005) 1053-1062
    • (2005) J Invest Dermatol , vol.125 , pp. 1053-1062
    • Mills, S.J.1    Ashworth, J.J.2    Gilliver, S.C.3    Hardman, M.J.4    Ashcroft, G.S.5
  • 89
    • 0033159027 scopus 로고    scopus 로고
    • Study of immunosuppressive activity of a synthetic decapeptide corresponding to an ACTH-like sequence of human immunoglobulin G1
    • Navolotskaya E.V., Zargarova T.A., Lepikhova T.N., et al. Study of immunosuppressive activity of a synthetic decapeptide corresponding to an ACTH-like sequence of human immunoglobulin G1. Biochemistry (Mosc) 64 (1999) 758-764
    • (1999) Biochemistry (Mosc) , vol.64 , pp. 758-764
    • Navolotskaya, E.V.1    Zargarova, T.A.2    Lepikhova, T.N.3
  • 90
    • 0023130285 scopus 로고
    • Synthesis and biological activity of tuftsin and rigin derivatives containing monosaccharides or monosaccharide derivatives
    • Rocchi R., Biondi L., Cavaggion F., et al. Synthesis and biological activity of tuftsin and rigin derivatives containing monosaccharides or monosaccharide derivatives. Int J Pept Protein Res 29 (1987) 262-275
    • (1987) Int J Pept Protein Res , vol.29 , pp. 262-275
    • Rocchi, R.1    Biondi, L.2    Cavaggion, F.3
  • 91
    • 0042562053 scopus 로고    scopus 로고
    • Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco
    • Yang Y., Marczak E.D., Yokoo M., Usui H., and Yoshikawa M. Isolation and antihypertensive effect of angiotensin I-converting enzyme (ACE) inhibitory peptides from spinach Rubisco. J Agric Food Chem 51 (2003) 4897-4902
    • (2003) J Agric Food Chem , vol.51 , pp. 4897-4902
    • Yang, Y.1    Marczak, E.D.2    Yokoo, M.3    Usui, H.4    Yoshikawa, M.5
  • 93
    • 0042389815 scopus 로고    scopus 로고
    • New antihypertensive peptides isolated from rapeseed
    • Marczak E.D., Usui H., Fujita H., et al. New antihypertensive peptides isolated from rapeseed. Peptides 24 (2003) 791-798
    • (2003) Peptides , vol.24 , pp. 791-798
    • Marczak, E.D.1    Usui, H.2    Fujita, H.3
  • 94
    • 0346788748 scopus 로고    scopus 로고
    • Glucosyl hesperidin improves serum cholesterol composition and inhibits hypertrophy in vasculature
    • Ohtsuki K., Abe A., Mitsuzumi H., et al. Glucosyl hesperidin improves serum cholesterol composition and inhibits hypertrophy in vasculature. J Nutr Sci Vitaminol (Tokyo) 49 (2003) 447-450
    • (2003) J Nutr Sci Vitaminol (Tokyo) , vol.49 , pp. 447-450
    • Ohtsuki, K.1    Abe, A.2    Mitsuzumi, H.3
  • 95
    • 23344436043 scopus 로고    scopus 로고
    • Kinetics of radical-scavenging activity of hesperetin and hesperidin and their inhibitory activity on COX-2 expression
    • Hirata A., Murakami Y., Shoji M., Kadoma Y., and Fujisawa S. Kinetics of radical-scavenging activity of hesperetin and hesperidin and their inhibitory activity on COX-2 expression. Anticancer Res 25 (2005) 3367-3374
    • (2005) Anticancer Res , vol.25 , pp. 3367-3374
    • Hirata, A.1    Murakami, Y.2    Shoji, M.3    Kadoma, Y.4    Fujisawa, S.5
  • 96
    • 0034098046 scopus 로고    scopus 로고
    • The 500 Dalton rule for the skin penetration of chemical compounds and drugs
    • Bos J.D., and Meinardi M.M. The 500 Dalton rule for the skin penetration of chemical compounds and drugs. Exp Dermatol 9 (2000) 165-169
    • (2000) Exp Dermatol , vol.9 , pp. 165-169
    • Bos, J.D.1    Meinardi, M.M.2
  • 97
    • 0037073631 scopus 로고    scopus 로고
    • Applying peptide antigens onto bare skin: induction of humoral and cellular immune responses and potential for vaccination
    • Partidos C.D., Beignon A.S., Brown F., Kramer E., Briand J.P., and Muller S. Applying peptide antigens onto bare skin: induction of humoral and cellular immune responses and potential for vaccination. J Control Release 85 (2002) 27-34
    • (2002) J Control Release , vol.85 , pp. 27-34
    • Partidos, C.D.1    Beignon, A.S.2    Brown, F.3    Kramer, E.4    Briand, J.P.5    Muller, S.6
  • 98
    • 0037426686 scopus 로고    scopus 로고
    • Modeling skin permeability to hydrophilic and hydrophobic solutes based on four permeation pathways
    • Mitragotri S. Modeling skin permeability to hydrophilic and hydrophobic solutes based on four permeation pathways. J Control Release 86 (2003) 69-92
    • (2003) J Control Release , vol.86 , pp. 69-92
    • Mitragotri, S.1
  • 99
    • 20044388585 scopus 로고    scopus 로고
    • Comparative study of the skin penetration of protein transduction domains and a conjugated peptide
    • Lopes L.B., Brophy C.M., Furnish E., et al. Comparative study of the skin penetration of protein transduction domains and a conjugated peptide. Pharm Res 22 (2005) 750-757
    • (2005) Pharm Res , vol.22 , pp. 750-757
    • Lopes, L.B.1    Brophy, C.M.2    Furnish, E.3
  • 100
    • 17444372348 scopus 로고    scopus 로고
    • Topical delivery of cyclosporin A: an in vitro study using monoolein as a penetration enhancer
    • Lopes L.B., Collett J.H., and Bentley M.V. Topical delivery of cyclosporin A: an in vitro study using monoolein as a penetration enhancer. Eur J Pharm Biopharm 60 (2005) 25-30
    • (2005) Eur J Pharm Biopharm , vol.60 , pp. 25-30
    • Lopes, L.B.1    Collett, J.H.2    Bentley, M.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.