메뉴 건너뛰기




Volumn 161, Issue 3, 2012, Pages 835-842

Defeating Leishmania resistance to Miltefosine (hexadecylphosphocholine) by peptide-mediated drug smuggling: A proof of mechanism for trypanosomatid chemotherapy

Author keywords

Cell penetrating peptide; Leishmania; Miltefosine; Resistance reversion; Tat; Trypanosoma

Indexed keywords

CELL-PENETRATING PEPTIDE; LEISHMANIA; MILTEFOSINE; TAT; TRYPANOSOMA;

EID: 84864626959     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2012.05.023     Document Type: Article
Times cited : (24)

References (70)
  • 1
    • 79957596962 scopus 로고    scopus 로고
    • Control of the leishmaniases
    • (back cover)
    • Control of the leishmaniases World Health Organ. Tech. Rep. Ser. xii-xiii 2010 1 186 (back cover)
    • (2010) World Health Organ. Tech. Rep. Ser. , vol.12-13 , pp. 1-186
  • 5
    • 0041767590 scopus 로고    scopus 로고
    • Leishmania donovani resistance to miltefosine involves a defective inward translocation of the drug
    • DOI 10.1128/AAC.47.8.2397-2403.2003
    • F.J. Pérez-Victoria, S. Castanys, and F. Gamarro Leishmania donovani resistance to miltefosine involves a defective inward translocation of the drug Antimicrob. Agents Chemother. 47 2003 2397 2403 (Pubitemid 36919436)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.8 , pp. 2397-2403
    • Perez-Victoria, F.J.1    Castanys, S.2    Gamarro, F.3
  • 6
    • 34547337720 scopus 로고    scopus 로고
    • Inactivation of the miltefosine transporter, LdMT, causes miltefosine resistance that is conferred to the amastigote stage of Leishmania donovani and persists in vivo
    • DOI 10.1016/j.ijantimicag.2007.05.007, PII S092485790700252X
    • K. Seifert, F.J. Pérez-Victoria, M. Stettler, M.P. Sánchez-Cañete, S. Castanys, F. Gamarro, and S.L. Croft Inactivation of the miltefosine transporter, LdMT, causes miltefosine resistance that is conferred to the amastigote stage of Leishmania donovani and persists in vivo Int. J. Antimicrob. Agents 30 2007 229 235 (Pubitemid 47135625)
    • (2007) International Journal of Antimicrobial Agents , vol.30 , Issue.3 , pp. 229-235
    • Seifert, K.1    Perez-Victoria, F.J.2    Stettler, M.3    Sanchez-Canete, M.P.4    Castanys, S.5    Gamarro, F.6    Croft, S.L.7
  • 7
    • 80053395366 scopus 로고    scopus 로고
    • Tolerance to drug-induced cell death favours the acquisition of multidrug resistance in Leishmania
    • W. Moreira, P. Leprohon, and M. Ouellette Tolerance to drug-induced cell death favours the acquisition of multidrug resistance in Leishmania Cell Death Dis. 2 2011 e201
    • (2011) Cell Death Dis. , vol.2 , pp. 201
    • Moreira, W.1    Leprohon, P.2    Ouellette, M.3
  • 8
    • 59749105928 scopus 로고    scopus 로고
    • In vitro susceptibility of field isolates of Leishmania donovani to Miltefosine and amphotericin B: Correlation with sodium antimony gluconate susceptibility and implications for treatment in areas of endemicity
    • D. Kumar, A. Kulshrestha, R. Singh, and P. Salotra In vitro susceptibility of field isolates of Leishmania donovani to Miltefosine and amphotericin B: correlation with sodium antimony gluconate susceptibility and implications for treatment in areas of endemicity Antimicrob. Agents Chemother. 53 2009 835 838
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 835-838
    • Kumar, D.1    Kulshrestha, A.2    Singh, R.3    Salotra, P.4
  • 9
    • 0346118937 scopus 로고    scopus 로고
    • Functional cloning of the miltefosine transporter: A novel p-type phospholipid translocase from leishmania involved in drug resistance
    • DOI 10.1074/jbc.M308352200
    • F.J. Pérez-Victoria, F. Gamarro, M. Ouellette, and S. Castanys Functional cloning of the miltefosine transporter. A novel P-type phospholipid translocase from Leishmania involved in drug resistance J. Biol. Chem. 278 2003 49965 49971 (Pubitemid 37548832)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 49965-49971
    • Perez-Victoria, F.J.1    Gamarro, F.2    Ouellette, M.3    Castanys, S.4
  • 11
    • 65649096220 scopus 로고    scopus 로고
    • Low plasma membrane expression of the miltefosine transport complex renders Leishmania braziliensis refractory to the drug
    • M.P. Sánchez-Cañete, L. Carvalho, F.J. Pérez- Victoria, F. Gamarro, and S. Castanys Low plasma membrane expression of the miltefosine transport complex renders Leishmania braziliensis refractory to the drug Antimicrob. Agents Chemother. 53 2009 1305 1313
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1305-1313
    • Sánchez-Cañete, M.P.1    Carvalho, L.2    Pérez-Victoria, F.J.3    Gamarro, F.4    Castanys, S.5
  • 13
    • 77951144106 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Nanocarrier for macromolecule delivery in living cells
    • A. Chugh, F. Eudes, and Y.S. Shim Cell-penetrating peptides: nanocarrier for macromolecule delivery in living cells IUBMB Life 62 2010 183 193
    • (2010) IUBMB Life , vol.62 , pp. 183-193
    • Chugh, A.1    Eudes, F.2    Shim, Y.S.3
  • 14
    • 79952782063 scopus 로고    scopus 로고
    • The delivery of biologically active (therapeutic) peptides and proteins into cells
    • M. Grdisa The delivery of biologically active (therapeutic) peptides and proteins into cells Curr. Med. Chem. 18 2011 1373 1379
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1373-1379
    • Grdisa, M.1
  • 15
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • S.B. Fonseca, M.P. Pereira, and S.O. Kelley Recent advances in the use of cell-penetrating peptides for medical and biological applications Adv. Drug Deliv. 61 2009 953 964
    • (2009) Adv. Drug Deliv. , vol.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 16
    • 79952197259 scopus 로고    scopus 로고
    • Classes and prediction of cell-penetrating peptides
    • M. Lindgren, and U. Langel Classes and prediction of cell-penetrating peptides Methods Mol. Biol. 683 2011 3 19
    • (2011) Methods Mol. Biol. , vol.683 , pp. 3-19
    • Lindgren, M.1    Langel, U.2
  • 17
    • 79952197781 scopus 로고    scopus 로고
    • Nonclinical and clinical experiences with CPP-based self-assembling peptide systems in topical drug development
    • J.M. Waugh, J. Lee, M.D. Dake, and D. Browne Nonclinical and clinical experiences with CPP-based self-assembling peptide systems in topical drug development Methods Mol. Biol. 683 2011 553 572
    • (2011) Methods Mol. Biol. , vol.683 , pp. 553-572
    • Waugh, J.M.1    Lee, J.2    Dake, M.D.3    Browne, D.4
  • 18
    • 77956561675 scopus 로고    scopus 로고
    • CPP-ZFN: A potential DNA-targeting anti-malarial drug
    • V. Nain, S. Sahi, and A. Verma CPP-ZFN: a potential DNA-targeting anti-malarial drug Malar. J. 9 2010 258
    • (2010) Malar. J. , vol.9 , pp. 258
    • Nain, V.1    Sahi, S.2    Verma, A.3
  • 19
    • 67649268280 scopus 로고    scopus 로고
    • Amphibian antimicrobial peptides and Protozoa: Lessons from parasites
    • L. Rivas, J.R. Luque-Ortega, and D. Andreu Amphibian antimicrobial peptides and Protozoa: lessons from parasites Biochim. Biophys. Acta 1788 2009 1570 1581
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1570-1581
    • Rivas, L.1    Luque-Ortega, J.R.2    Andreu, D.3
  • 21
    • 56249122251 scopus 로고    scopus 로고
    • Synthesis of BODIPY-labeled alkylphosphocholines with leishmanicidal activity, as fluorescent analogues of miltefosine
    • V. Hornillos, E. Carrillo, L. Rivas, F. Amat-Guerri, and A.U. Acuña Synthesis of BODIPY-labeled alkylphosphocholines with leishmanicidal activity, as fluorescent analogues of miltefosine Bioorg. Med. Chem. Lett. 18 2008 6336 6339
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 6336-6339
    • Hornillos, V.1    Carrillo, E.2    Rivas, L.3    Amat-Guerri, F.4    Acuña, A.U.5
  • 23
    • 77950470234 scopus 로고    scopus 로고
    • Characterization of the leishmanicidal activity of antimicrobial peptides
    • J.R. Luque-Ortega, and L. Rivas Characterization of the leishmanicidal activity of antimicrobial peptides Methods Mol. Biol. 618 2010 393 420
    • (2010) Methods Mol. Biol. , vol.618 , pp. 393-420
    • Luque-Ortega, J.R.1    Rivas, L.2
  • 24
    • 0033561049 scopus 로고    scopus 로고
    • Trypanosoma brucei variant surface glycoprotein regulation involves coupled activation/inactivation and chromatin remodeling of expression sites
    • M. Navarro, G.A. Cross, and E. Wirtz Trypanosoma brucei variant surface glycoprotein regulation involves coupled activation/inactivation and chromatin remodeling of expression sites EMBO J. 18 1999 2265 2272 (Pubitemid 29179182)
    • (1999) EMBO Journal , vol.18 , Issue.8 , pp. 2265-2272
    • Navarro, M.1    Cross, G.A.M.2    Wirtz, E.3
  • 25
    • 2142695761 scopus 로고    scopus 로고
    • Fungus-Elicited Metabolites from Plants as an Enriched Source for New Leishmanicidal Agents: Antifungal Phenyl-Phenalenone Phytoalexins from the Banana Plant (Musa acuminata) Target Mitochondria of Leishmania donovani Promastigotes
    • DOI 10.1128/AAC.48.5.1534-1540.2004
    • J.R. Luque-Ortega, S. Martínez, J.M. Saugar, L.R. Izquierdo, T. Abad, J.G. Luis, J. Piñero, B. Valladares, and L. Rivas Fungus-elicited metabolites from plants as an enriched source for new leishmanicidal agents: antifungal phenyl-phenalenone phytoalexins from the banana plant (Musa acuminata) target mitochondria of Leishmania donovani promastigotes Antimicrob. Agents Chemother. 48 2004 1534 1540 (Pubitemid 38544356)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.5 , pp. 1534-1540
    • Luque-Ortega, J.R.1    Martinez, S.2    Saugar, J.M.3    Izquierdo, L.R.4    Abad, T.5    Luis, J.G.6    Pinero, J.7    Valladares, B.8    Rivas, L.9
  • 26
    • 0035077737 scopus 로고    scopus 로고
    • In vivo monitoring of intracellular ATP levels in Leishmania donovani promastigotes as a rapid method to screen drugs targeting bioenergetic metabolism
    • DOI 10.1128/AAC.45.4.1121-1125.2001
    • J.R. Luque-Ortega, O.M. Rivero-Lezcano, S.L. Croft, and L. Rivas In vivo monitoring of intracellular ATP levels in Leishmania donovani promastigotes as a rapid method to screen drugs targeting bioenergetic metabolism Antimicrob. Agents Chemother. 45 2001 1121 1125 (Pubitemid 32230992)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.4 , pp. 1121-1125
    • Luque-Ortega, J.R.1    Rivero-Lezcano, O.M.2    Croft, S.L.3    Rivas, L.4
  • 27
    • 0037572243 scopus 로고    scopus 로고
    • Endocytosis of a glycosylphosphatidylinositol-anchored protein via clathrin-coated vesicles, sorting by default in endosomes, and exocytosis via RAB11-positive carriers
    • DOI 10.1091/mbc.E02-10-0640
    • C.G. Grunfelder, M. Engstler, F. Weise, H. Schwarz, Y.D. Stierhof, G.W. Morgan, M.C. Field, and P. Overath Endocytosis of a glycosylphosphatidylinositol-anchored protein via clathrin-coated vesicles, sorting by default in endosomes, and exocytosis via RAB11-positive carriers Mol. Biol. Cell 14 2003 2029 2040 (Pubitemid 36583551)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.5 , pp. 2029-2040
    • Grunfelder, C.G.1    Engstler, M.2    Weise, F.3    Schwarz, H.4    Stierhof, Y.-D.5    Morgan, G.W.6    Field, M.C.7    Overath, P.8
  • 28
    • 37849043927 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of fluorescent leishmanicidal analogues of hexadecylphosphocholine (miltefosine) as probes of antiparasite mechanisms
    • J.M. Saugar, J. Delgado, V. Hornillos, J.R. Luque-Ortega, F. Amat-Guerri, A.U. Acuña, and L. Rivas Synthesis and biological evaluation of fluorescent leishmanicidal analogues of hexadecylphosphocholine (miltefosine) as probes of antiparasite mechanisms J. Med. Chem. 50 2007 5994 6003
    • (2007) J. Med. Chem. , vol.50 , pp. 5994-6003
    • Saugar, J.M.1    Delgado, J.2    Hornillos, V.3    Luque-Ortega, J.R.4    Amat-Guerri, F.5    Acuña, A.U.6    Rivas, L.7
  • 29
    • 0024396169 scopus 로고
    • Maintenance of cytoplasmic pH and proton motive force in promastigotes of Leishmania donovani
    • D. Zilberstein, H. Philosoph, and A. Gepstein Maintenance of cytoplasmic pH and proton motive force in promastigotes of Leishmania donovani Mol. Biochem. Parasitol. 36 1989 109 117
    • (1989) Mol. Biochem. Parasitol. , vol.36 , pp. 109-117
    • Zilberstein, D.1    Philosoph, H.2    Gepstein, A.3
  • 30
    • 0034863516 scopus 로고    scopus 로고
    • Alkyl-lysophospholipid resistance in multidrug-resistant Leishmania tropica and chemosensitization by a novel P-glycoprotein-like transporter modulator
    • DOI 10.1128/AAC.45.9.2468-2474.2001
    • J.M. Pérez-Victoria, F.J. Pérez-Victoria, A. Parodi-Talice, I.A. Jiménez, A.G. Ravelo, S. Castanys, and F. Gamarro Alkyl-lysophospholipid resistance in multidrug-resistant Leishmania tropica and chemosensitization by a novel P-glycoprotein-like transporter modulator Antimicrob. Agents Chemother. 45 2001 2468 2474 (Pubitemid 32801897)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.9 , pp. 2468-2474
    • Perez-Victoria, J.M.1    Perez-Victoria, F.J.2    Parodi-Talice, A.3    Jimenez, I.A.4    Ravelo, A.G.5    Castanys, S.6    Gamarro, F.7
  • 31
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: Back to basics
    • DOI 10.1016/j.addr.2004.12.001, PII S0169409X04002741
    • H. Brooks, B. Lebleu, and E. Vives Tat peptide-mediated cellular delivery: back to basics Adv. Drug Deliv. Rev. 57 2005 559 577 (Pubitemid 40255561)
    • (2005) Advanced Drug Delivery Reviews , vol.57 , Issue.4 SPEC. ISS. , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vives, E.3
  • 33
    • 0030481123 scopus 로고    scopus 로고
    • The activities of four anticancer alkyllysophospholipids against Leishmania donovani, Trypanosoma cruzi and Trypanosoma brucei
    • DOI 10.1093/jac/38.6.1041
    • S.L. Croft, D. Snowdon, and V. Yardley The activities of four anticancer alkyllysophospholipids against Leishmania donovani, Trypanosoma cruzi and Trypanosoma brucei J. Antimicrob. Chemother. 38 1996 1041 1047 (Pubitemid 27073283)
    • (1996) Journal of Antimicrobial Chemotherapy , vol.38 , Issue.6 , pp. 1041-1047
    • Croft, S.L.1    Snowdon, D.2    Yardley, V.3
  • 34
    • 60849108318 scopus 로고    scopus 로고
    • Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death
    • M. Delgado, P. Anderson, J.A. García-Salcedo, M. Caro, and E. González-Rey Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death Cell Death Differ. 16 2009 406 416
    • (2009) Cell Death Differ. , vol.16 , pp. 406-416
    • Delgado, M.1    Anderson, P.2    García-Salcedo, J.A.3    Caro, M.4    González-Rey, E.5
  • 35
    • 77957739105 scopus 로고    scopus 로고
    • The antitumoral depsipeptide IB-01212 kills Leishmania through an apoptosis-like process involving intracellular targets
    • J.R. Luque-Ortega, L.J. Cruz, F. Albericio, and L. Rivas The antitumoral depsipeptide IB-01212 kills Leishmania through an apoptosis-like process involving intracellular targets Mol. Pharm. 7 2010 1608 1617
    • (2010) Mol. Pharm. , vol.7 , pp. 1608-1617
    • Luque-Ortega, J.R.1    Cruz, L.J.2    Albericio, F.3    Rivas, L.4
  • 36
    • 44949133077 scopus 로고    scopus 로고
    • Human antimicrobial peptide histatin 5 is a cell-penetrating peptide targeting mitochondrial ATP synthesis in Leishmania
    • DOI 10.1096/fj.07-096081
    • J.R. Luque-Ortega, W. van't Hof, E.C. Veerman, J.M. Saugar, and L. Rivas Human antimicrobial peptide histatin 5 is a cell-penetrating peptide targeting mitochondrial ATP synthesis in Leishmania FASEB J. 22 2008 1817 1828 (Pubitemid 351811459)
    • (2008) FASEB Journal , vol.22 , Issue.6 , pp. 1817-1828
    • Luque-Ortega, J.R.1    Van't Hof, W.2    Veerman, E.C.I.3    Saugar, J.M.4    Rivas, L.5
  • 38
    • 0036847052 scopus 로고    scopus 로고
    • Novel peptide inhibitors of Leishmania gp63 based on the cleavage site of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein
    • DOI 10.1042/BJ20020386
    • S. Corradin, A. Ransijn, G. Corradin, J. Bouvier, M.B. Delgado, J. Fernández-Carneado, J.C. Mottram, G. Vergeres, and J. Mauel Novel peptide inhibitors of Leishmania gp63 based on the cleavage site of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein Biochem. J. 367 2002 761 769 (Pubitemid 35305715)
    • (2002) Biochemical Journal , vol.367 , Issue.3 , pp. 761-769
    • Corradin, S.1    Ransijn, A.2    Corradin, G.3    Bouvier, J.4    Delgado, M.B.5    Fernandez-Carneado, J.6    Mottram, J.C.7    Vergeres, G.8    Mauel, J.9
  • 41
    • 70349759756 scopus 로고    scopus 로고
    • Conjugation of doxorubicin to cell penetrating peptides sensitizes human breast MDA-MB 231 cancer cells to endogenous TRAIL-induced apoptosis
    • S. Aroui, S. Brahim, J. Hamelin, M. De Waard, J. Breard, and A. Kenani Conjugation of doxorubicin to cell penetrating peptides sensitizes human breast MDA-MB 231 cancer cells to endogenous TRAIL-induced apoptosis Apoptosis 14 2009 1352 1365
    • (2009) Apoptosis , vol.14 , pp. 1352-1365
    • Aroui, S.1    Brahim, S.2    Hamelin, J.3    De Waard, M.4    Breard, J.5    Kenani, A.6
  • 42
    • 77953238614 scopus 로고    scopus 로고
    • Reduction of doxorubicin resistance in P-glycoprotein overexpressing cells by hybrid cell-penetrating and drug-binding peptide
    • Z. Zheng, H. Aojula, and D. Clarke Reduction of doxorubicin resistance in P-glycoprotein overexpressing cells by hybrid cell-penetrating and drug-binding peptide J. Drug Target. 18 2010 477 487
    • (2010) J. Drug Target. , vol.18 , pp. 477-487
    • Zheng, Z.1    Aojula, H.2    Clarke, D.3
  • 43
    • 50249127636 scopus 로고    scopus 로고
    • Effective antibacterial action of tat (47-58) by increased uptake into bacterial cells in the presence of trypsin
    • H.J. Jung, K.S. Jeong, and D.G. Lee Effective antibacterial action of tat (47-58) by increased uptake into bacterial cells in the presence of trypsin J. Microbiol. Biotechnol. 18 2008 990 996
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 990-996
    • Jung, H.J.1    Jeong, K.S.2    Lee, D.G.3
  • 44
    • 33646402378 scopus 로고    scopus 로고
    • Biological activity of Tat (47-58) peptide on human pathogenic fungi
    • H.J. Jung, Y. Park, K.S. Hahm, and D.G. Lee Biological activity of Tat (47-58) peptide on human pathogenic fungi Biochem. Biophys. Res. Commun. 345 2006 222 228
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 222-228
    • Jung, H.J.1    Park, Y.2    Hahm, K.S.3    Lee, D.G.4
  • 45
    • 67649234630 scopus 로고    scopus 로고
    • Effects of dimerization of the cell-penetrating peptide Tat analog on antimicrobial activity and mechanism of bactericidal action
    • W.L. Zhu, and S.Y. Shin Effects of dimerization of the cell-penetrating peptide Tat analog on antimicrobial activity and mechanism of bactericidal action J. Pept. Sci. 15 2009 345 352
    • (2009) J. Pept. Sci. , vol.15 , pp. 345-352
    • Zhu, W.L.1    Shin, S.Y.2
  • 46
    • 33748887226 scopus 로고    scopus 로고
    • Endocytic portals in Trypanosoma cruzi epimastigote forms
    • DOI 10.1007/s00436-006-0189-9
    • M.J. Soares Endocytic portals in Trypanosoma cruzi epimastigote forms Parasitol. Res. 99 2006 321 322 (Pubitemid 44426717)
    • (2006) Parasitology Research , vol.99 , Issue.4 , pp. 321-322
    • Soares, M.J.1
  • 47
    • 0141530903 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis is essential in Trypanosoma brucei
    • DOI 10.1093/emboj/cdg481
    • C.L. Allen, D. Goulding, and M.C. Field Clathrin-mediated endocytosis is essential in Trypanosoma brucei EMBO J. 22 2003 4991 5002 (Pubitemid 37222020)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 4991-5002
    • Allen, C.L.1    Goulding, D.2    Field, M.C.3
  • 48
    • 3843103801 scopus 로고    scopus 로고
    • Endocytosis, membrane recycling and sorting of GPI-anchored proteins: Trypanosoma brucei as a model system
    • DOI 10.1111/j.1365-2958.2004.04224.x
    • P. Overäth, and M. Engstler Endocytosis, membrane recycling and sorting of GPI-anchored proteins: Trypanosoma brucei as a model system Mol. Microbiol. 53 2004 735 744 (Pubitemid 39036955)
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 735-744
    • Overath, P.1    Engstler, M.2
  • 49
    • 34548162679 scopus 로고    scopus 로고
    • Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells
    • G.M. Poon, and J. Gariepy Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells Biochem. Soc. Trans. 35 2007 788 793 (Pubitemid 47310369)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.4 , pp. 788-793
    • Poon, G.M.K.1    Gariepy, J.2
  • 50
    • 44049095595 scopus 로고    scopus 로고
    • Binding and clustering of glycosaminoglycans: A common property of mono- and multivalent cell-penetrating compounds
    • A. Ziegler, and J. Seelig Binding and clustering of glycosaminoglycans: a common property of mono- and multivalent cell-penetrating compounds Biophys. J. 94 2008 2142 2149
    • (2008) Biophys. J. , vol.94 , pp. 2142-2149
    • Ziegler, A.1    Seelig, J.2
  • 51
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • J.M. Gump, R.K. June, and S.F. Dowdy Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction J. Biol. Chem. 285 2010 1500 1507
    • (2010) J. Biol. Chem. , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 52
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles
    • P. Saalik, A. Niinep, J. Pae, M. Hansen, D. Lubenets, U. Langel, and M. Pooga Penetration without cells: membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles J. Control. Release 153 2011 117 125
    • (2011) J. Control. Release , vol.153 , pp. 117-125
    • Saalik, P.1    Niinep, A.2    Pae, J.3    Hansen, M.4    Lubenets, D.5    Langel, U.6    Pooga, M.7
  • 53
    • 33748648777 scopus 로고    scopus 로고
    • Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells
    • DOI 10.1096/fj.05-5523com
    • G. Tunnemann, R.M. Martin, S. Haupt, C. Patsch, F. Edenhofer, and M.C. Cardoso Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells FASEB J. 20 2006 1775 1784 (Pubitemid 44933791)
    • (2006) FASEB Journal , vol.20 , Issue.11 , pp. 1775-1784
    • Tunnemann, G.1    Martin, R.M.2    Haupt, S.3    Patsch, C.4    Edenhofer, F.5    Cardoso, M.C.6
  • 54
    • 77957865000 scopus 로고    scopus 로고
    • Disruption of the lipid-transporting LdMT-LdRos3 complex in Leishmania donovani affects membrane lipid asymmetry but not host cell invasion
    • A. Weingartner, B. Drobot, A. Herrmann, M.P. Sánchez-Cañete, F. Gamarro, S. Castanys, and T. Gunther Pomorski Disruption of the lipid-transporting LdMT-LdRos3 complex in Leishmania donovani affects membrane lipid asymmetry but not host cell invasion PLoS One 5 2010 e12443
    • (2010) PLoS One , vol.5 , pp. 12443
    • Weingartner, A.1    Drobot, B.2    Herrmann, A.3    Sánchez-Cañete, M.P.4    Gamarro, F.5    Castanys, S.6    Gunther Pomorski, T.7
  • 56
    • 2442546710 scopus 로고    scopus 로고
    • Biodistribution of intracellularly acting peptides conjugated reversibly to Tat
    • DOI 10.1016/j.bbrc.2004.04.121, PII S0006291X04008587
    • R. Begley, T. Liron, J. Baryza, and D. Mochly-Rosen Biodistribution of intracellularly acting peptides conjugated reversibly to Tat Biochem. Biophys. Res. Commun. 318 2004 949 954 (Pubitemid 38625866)
    • (2004) Biochemical and Biophysical Research Communications , vol.318 , Issue.4 , pp. 949-954
    • Begley, R.1    Liron, T.2    Baryza, J.3    Mochly-Rosen, D.4
  • 57
    • 0347926091 scopus 로고    scopus 로고
    • Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities
    • DOI 10.1016/S0169-409X(02)00179-5, PII S0169409X02001795
    • G. Saito, J.A. Swanson, and K.D. Lee Drug delivery strategy utilizing conjugation via reversible disulfide linkages: role and site of cellular reducing activities Adv. Drug Deliv. Rev. 55 2003 199 215 (Pubitemid 36135916)
    • (2003) Advanced Drug Delivery Reviews , vol.55 , Issue.2 , pp. 199-215
    • Saito, G.1    Swanson, J.A.2    Lee, K.-D.3
  • 58
    • 60849101051 scopus 로고    scopus 로고
    • Disulfide and thioether linked cytochrome c-oligoarginine conjugates in HeLa cells
    • M.P. Barnes, and W.C. Shen Disulfide and thioether linked cytochrome c-oligoarginine conjugates in HeLa cells Int. J. Pharm. 369 2009 79 84
    • (2009) Int. J. Pharm. , vol.369 , pp. 79-84
    • Barnes, M.P.1    Shen, W.C.2
  • 60
    • 0037325060 scopus 로고    scopus 로고
    • Antiprotozoal activities of phospholipid analogues
    • DOI 10.1016/S0166-6851(02)00283-9, PII S0166685102002839
    • S.L. Croft, K. Seifert, and M. Duchene Antiprotozoal activities of phospholipid analogues Mol. Biochem. Parasitol. 126 2003 165 172 (Pubitemid 36255615)
    • (2003) Molecular and Biochemical Parasitology , vol.126 , Issue.2 , pp. 165-172
    • Croft, S.L.1    Seifert, K.2    Duchene, M.3
  • 61
    • 34247164978 scopus 로고    scopus 로고
    • Miltefosine (hexadecylphosphocholine) inhibits cytochrome c oxidase in Leishmania donovani promastigotes
    • DOI 10.1128/AAC.01415-06
    • J.R. Luque-Ortega, and L. Rivas Miltefosine (hexadecylphosphocholine) inhibits cytochrome c oxidase in Leishmania donovani promastigotes Antimicrob. Agents Chemother. 51 2007 1327 1332 (Pubitemid 46586813)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.4 , pp. 1327-1332
    • Luque-Ortega, J.R.1    Rivas, L.2
  • 62
    • 77953493504 scopus 로고    scopus 로고
    • The essential neutral sphingomyelinase is involved in the trafficking of the variant surface glycoprotein in the bloodstream form of Trypanosoma brucei
    • S.A. Young, and T.K. Smith The essential neutral sphingomyelinase is involved in the trafficking of the variant surface glycoprotein in the bloodstream form of Trypanosoma brucei Mol. Microbiol. 76 2010 1461 1482
    • (2010) Mol. Microbiol. , vol.76 , pp. 1461-1482
    • Young, S.A.1    Smith, T.K.2
  • 63
    • 34249787648 scopus 로고    scopus 로고
    • A novel ATP-binding cassette transporter from Leishmania is involved in transport of phosphatidylcholine analogues and resistance to alkyl-phospholipids
    • DOI 10.1111/j.1365-2958.2007.05653.x
    • E. Castanys-Muñoz, N. Alder-Baerens, T. Pomorski, F. Gamarro, and S. Castanys A novel ATP-binding cassette transporter from Leishmania is involved in transport of phosphatidylcholine analogues and resistance to alkyl-phospholipids Mol. Microbiol. 64 2007 1141 1153 (Pubitemid 46849008)
    • (2007) Molecular Microbiology , vol.64 , Issue.5 , pp. 1141-1153
    • Castanys-Munoz, E.1    Alder-Baerens, N.2    Pomorski, T.3    Gamarro, F.4    Castanys, S.5
  • 64
    • 54049089634 scopus 로고    scopus 로고
    • Characterization of an ABCG-like transporter from the protozoan parasite Leishmania with a role in drug resistance and transbilayer lipid movement
    • E. Castanys-Munoz, J.M. Pérez-Victoria, F. Gamarro, and S. Castanys Characterization of an ABCG-like transporter from the protozoan parasite Leishmania with a role in drug resistance and transbilayer lipid movement Antimicrob. Agents Chemother. 52 2008 3573 3579
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3573-3579
    • Castanys-Munoz, E.1    Pérez-Victoria, J.M.2    Gamarro, F.3    Castanys, S.4
  • 65
    • 77958153239 scopus 로고    scopus 로고
    • In vivo biodistribution and efficacy of peptide mediated delivery
    • P. Jarver, I. Mager, and U. Langel In vivo biodistribution and efficacy of peptide mediated delivery Trends Pharmacol. Sci. 31 2010 528 535
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 528-535
    • Jarver, P.1    Mager, I.2    Langel, U.3
  • 67
    • 0036000128 scopus 로고    scopus 로고
    • Methotrexate conjugate with branched polypeptide influences Leishmania donovani infection in vitro and in experimental animals
    • DOI 10.1021/bc015530e
    • G. Koczan, A.C. Ghose, A. Mookerjee, and F. Hudecz Methotrexate conjugate with branched polypeptide influences Leishmania donovani infection in vitro and in experimental animals Bioconjug. Chem. 13 2002 518 524 (Pubitemid 34527513)
    • (2002) Bioconjugate Chemistry , vol.13 , Issue.3 , pp. 518-524
    • Koczan, G.1    Ghose, A.C.2    Mookerjee, A.3    Hudecz, F.4
  • 69
    • 77954199596 scopus 로고    scopus 로고
    • Efficient liposomal nanocarrier-mediated oligodeoxynucleotide delivery involving dual use of a cell-penetrating peptide as a packaging and intracellular delivery agent
    • P.E. Saw, Y.T. Ko, and S. Jon Efficient liposomal nanocarrier-mediated oligodeoxynucleotide delivery involving dual use of a cell-penetrating peptide as a packaging and intracellular delivery agent Macromol. Rapid Commun. 31 2010 1155 1162
    • (2010) Macromol. Rapid Commun. , vol.31 , pp. 1155-1162
    • Saw, P.E.1    Ko, Y.T.2    Jon, S.3
  • 70
    • 33847671358 scopus 로고    scopus 로고
    • TAT peptide-based micelle system for potential active targeting of anti-cancer agents to acidic solid tumors
    • DOI 10.1016/j.jconrel.2006.12.008, PII S016836590600705X
    • V.A. Sethuraman, and Y.H. Bae TAT peptide-based micelle system for potential active targeting of anti-cancer agents to acidic solid tumors J. Control. Release 118 2007 216 224 (Pubitemid 46350711)
    • (2007) Journal of Controlled Release , vol.118 , Issue.2 , pp. 216-224
    • Sethuraman, V.A.1    Bae, Y.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.