메뉴 건너뛰기




Volumn 9, Issue 4, 2012, Pages 1024-1029

Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by 19F NMR

Author keywords

synuclein; 19F NMR; cell penetrating peptide; delivery system; eukaryotic cell

Indexed keywords

ALPHA SYNUCLEIN; CYTIDINE TRIPHOSPHATE; HYBRID PROTEIN;

EID: 84859329409     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp200615m     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospholipid-binding modes of α-synuclein revealed by solution NMR spectroscopy
    • Bodner, C. R.; Dobson, C. M.; Bax, A. Multiple tight phospholipid-binding modes of α-synuclein revealed by solution NMR spectroscopy J. Mol. Biol. 2009, 390 (4) 775-90
    • (2009) J. Mol. Biol. , vol.390 , Issue.4 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 2
    • 60549108729 scopus 로고    scopus 로고
    • Solid-state NMR and molecular dynamics simulations reveal the oligomeric ion-channels of TM2-GABA(A) stabilized by intermolecular hydrogen bonding
    • Kandasamy, S. K.; Lee, D. K.; Nanga, R. P.; Xu, J.; Santos, J. S.; Larson, R. G.; Ramamoorthy, A. Solid-state NMR and molecular dynamics simulations reveal the oligomeric ion-channels of TM2-GABA(A) stabilized by intermolecular hydrogen bonding Biochim. Biophys. Acta 2009, 1788 (3) 686-95
    • (2009) Biochim. Biophys. Acta , vol.1788 , Issue.3 , pp. 686-695
    • Kandasamy, S.K.1    Lee, D.K.2    Nanga, R.P.3    Xu, J.4    Santos, J.S.5    Larson, R.G.6    Ramamoorthy, A.7
  • 3
    • 34249081426 scopus 로고    scopus 로고
    • Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1
    • Henriques, S. T.; Quintas, A.; Bagatolli, L. A.; Homble, F.; Castanho, M. A. Energy-independent translocation of cell-penetrating peptides occurs without formation of pores. A biophysical study with pep-1 Mol. Membr. Biol. 2007, 24 (4) 282-93
    • (2007) Mol. Membr. Biol. , vol.24 , Issue.4 , pp. 282-293
    • Henriques, S.T.1    Quintas, A.2    Bagatolli, L.A.3    Homble, F.4    Castanho, M.A.5
  • 4
    • 0036052472 scopus 로고    scopus 로고
    • TAT peptide-modified liposomes for intracellular delivery of drugs and DNA
    • Torchilin, V. P. TAT peptide-modified liposomes for intracellular delivery of drugs and DNA Cell. Mol. Biol. Lett. 2002, 7 (2) 265-7
    • (2002) Cell. Mol. Biol. Lett. , vol.7 , Issue.2 , pp. 265-267
    • Torchilin, V.P.1
  • 5
    • 44849100942 scopus 로고    scopus 로고
    • The homeodomain derived peptide Penetratin induces curvature of fluid membrane domains
    • Lamaziere, A.; Wolf, C.; Lambert, O.; Chassaing, G.; Trugnan, G.; Ayala-Sanmartin, J. The homeodomain derived peptide Penetratin induces curvature of fluid membrane domains PLoS One 2008, 3 (4) e1938
    • (2008) PLoS One , vol.3 , Issue.4 , pp. 1938
    • Lamaziere, A.1    Wolf, C.2    Lambert, O.3    Chassaing, G.4    Trugnan, G.5    Ayala-Sanmartin, J.6
  • 7
    • 33646489207 scopus 로고    scopus 로고
    • Cytoplasmic transduction peptide (CTP): New approach for the delivery of biomolecules into cytoplasm in vitro and in vivo
    • Kim, D.; Jeon, C.; Kim, J. H.; Kim, M. S.; Yoon, C. H.; Choi, I. S.; Kim, S. H.; Bae, Y. S. Cytoplasmic transduction peptide (CTP): new approach for the delivery of biomolecules into cytoplasm in vitro and in vivo Exp. Cell Res. 2006, 312 (8) 1277-88
    • (2006) Exp. Cell Res. , vol.312 , Issue.8 , pp. 1277-1288
    • Kim, D.1    Jeon, C.2    Kim, J.H.3    Kim, M.S.4    Yoon, C.H.5    Choi, I.S.6    Kim, S.H.7    Bae, Y.S.8
  • 9
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • DOI 10.1038/nbt1201-1173
    • Morris, M. C.; Depollier, J.; Mery, J.; Heitz, F.; Divita, G. A peptide carrier for the delivery of biologically active proteins into mammalian cells Nat. Biotechnol. 2001, 19 (12) 1173-6 (Pubitemid 33115705)
    • (2001) Nature Biotechnology , vol.19 , Issue.12 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 10
    • 41549121011 scopus 로고    scopus 로고
    • TAT-mediated PRDX6 protein transduction protects against eye lens epithelial cell death and delays lens opacity
    • Kubo, E.; Fatma, N.; Akagi, Y.; Beier, D. R.; Singh, S. P.; Singh, D. P. TAT-mediated PRDX6 protein transduction protects against eye lens epithelial cell death and delays lens opacity Am. J. Physiol. 2008, 294 (3) C842-55
    • (2008) Am. J. Physiol. , vol.294 , Issue.3 , pp. 842-855
    • Kubo, E.1    Fatma, N.2    Akagi, Y.3    Beier, D.R.4    Singh, S.P.5    Singh, D.P.6
  • 12
    • 34447323868 scopus 로고    scopus 로고
    • High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA
    • DOI 10.1021/bi700416h
    • Ziegler, A.; Seelig, J. High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA Biochemistry 2007, 46 (27) 8138-45 (Pubitemid 47051649)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 8138-8145
    • Ziegler, A.1    Seelig, J.2
  • 13
  • 15
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • Vives, E.; Brodin, P.; Lebleu, B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 1997, 272 (25) 16010-7 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 17
    • 9444272812 scopus 로고    scopus 로고
    • Protective effect of TAT-delivered α-synuclein: Relevance of the C-terminal domain and involvement of HSP70
    • DOI 10.1096/fj.04-1621fje
    • Albani, D.; Peverelli, E.; Rametta, R.; Batelli, S.; Veschini, L.; Negro, A.; Forloni, G. Protective effect of TAT-delivered α-synuclein: relevance of the C-terminal domain and involvement of HSP70 FASEB J. 2004, 18 (14) 1713-5 (Pubitemid 39561660)
    • (2004) FASEB Journal , vol.18 , Issue.14 , pp. 1713-1715
    • Albani, D.1    Peverelli, E.2    Rametta, R.3    Batelli, S.4    Veschini, L.5    Negro, A.6    Forloni, G.7
  • 20
    • 77956373672 scopus 로고    scopus 로고
    • 19F NMR studies of α-synuclein-membrane interactions
    • 19F NMR studies of α-synuclein-membrane interactions Protein Sci. 2010, 19 (9) 1686-91
    • (2010) Protein Sci. , vol.19 , Issue.9 , pp. 1686-1691
    • Wang, G.F.1    Li, C.2    Pielak, G.J.3
  • 22
    • 77954755663 scopus 로고    scopus 로고
    • Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer
    • Buer, B. C.; Chugh, J.; Al-Hashimi, H. M.; Marsh, E. N. Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer Biochemistry 2010, 49 (27) 5760-5
    • (2010) Biochemistry , vol.49 , Issue.27 , pp. 5760-5765
    • Buer, B.C.1    Chugh, J.2    Al-Hashimi, H.M.3    Marsh, E.N.4
  • 24
    • 50849120027 scopus 로고    scopus 로고
    • Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1
    • Gottler, L. M.; de la Salud Bea, R.; Shelburne, C. E.; Ramamoorthy, A.; Marsh, E. N. Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1 Biochemistry 2008, 47 (35) 9243-50
    • (2008) Biochemistry , vol.47 , Issue.35 , pp. 9243-9250
    • Gottler, L.M.1    De La Salud Bea, R.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 25
    • 48849093330 scopus 로고    scopus 로고
    • Using fluorous amino acids to modulate the biological activity of an antimicrobial peptide
    • Gottler, L. M.; Lee, H. Y.; Shelburne, C. E.; Ramamoorthy, A.; Marsh, E. N. Using fluorous amino acids to modulate the biological activity of an antimicrobial peptide ChemBioChem 2008, 9 (3) 370-3
    • (2008) ChemBioChem , vol.9 , Issue.3 , pp. 370-373
    • Gottler, L.M.1    Lee, H.Y.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 26
    • 70349318199 scopus 로고    scopus 로고
    • Fluorine - A new element in the design of membrane-active peptides
    • Marsh, E. N.; Buer, B. C.; Ramamoorthy, A. Fluorine - a new element in the design of membrane-active peptides Mol. BioSyst. 2009, 5 (10) 1143-7
    • (2009) Mol. BioSyst. , vol.5 , Issue.10 , pp. 1143-1147
    • Marsh, E.N.1    Buer, B.C.2    Ramamoorthy, A.3
  • 28
    • 58149154666 scopus 로고    scopus 로고
    • α-Synuclein conformation affects its tyrosine-dependent oxidative aggregation
    • Ruf, R. A.; Lutz, E. A.; Zigoneanu, I. G.; Pielak, G. J. α-Synuclein conformation affects its tyrosine-dependent oxidative aggregation Biochemistry 2008, 47 (51) 13604-9
    • (2008) Biochemistry , vol.47 , Issue.51 , pp. 13604-13609
    • Ruf, R.A.1    Lutz, E.A.2    Zigoneanu, I.G.3    Pielak, G.J.4
  • 34
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg, B.; Ellis, R. J.; Dobson, C. M. Effects of macromolecular crowding on protein folding and aggregation EMBO J. 1999, 18 (24) 6927-33 (Pubitemid 30000446)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 35
    • 84862777869 scopus 로고    scopus 로고
    • Interaction of α-synuclein with vesicles that mimic mitochondrial membranes
    • Zigoneanu, I. G.; Yang, Y. J.; Krois, A. S.; Haque, M. E.; Pielak, G. J. Interaction of α-synuclein with vesicles that mimic mitochondrial membranes Biochim. Biophys. Acta 2012, 1818 (3) 512-519
    • (2012) Biochim. Biophys. Acta , vol.1818 , Issue.3 , pp. 512-519
    • Zigoneanu, I.G.1    Yang, Y.J.2    Krois, A.S.3    Haque, M.E.4    Pielak, G.J.5
  • 38
    • 71949090833 scopus 로고    scopus 로고
    • Mitochondrial trafficking of APP and α-synuclein: Relevance to mitochondrial dysfunction in Alzheimers and Parkinsons diseases
    • Devi, L.; Anandatheerthavarada, H. K. Mitochondrial trafficking of APP and α-synuclein: Relevance to mitochondrial dysfunction in Alzheimers and Parkinsons diseases Biochim. Biophys. Acta 2010, 1802 (1) 11-9
    • (2010) Biochim. Biophys. Acta , vol.1802 , Issue.1 , pp. 11-19
    • Devi, L.1    Anandatheerthavarada, H.K.2
  • 39
    • 44749085250 scopus 로고    scopus 로고
    • Mitochondrial translocation of α-synuclein is promoted by intracellular acidification
    • Cole, N. B.; Dieuliis, D.; Leo, P.; Mitchell, D. C.; Nussbaum, R. L. Mitochondrial translocation of α-synuclein is promoted by intracellular acidification Exp. Cell Res. 2008, 314 (10) 2076-89
    • (2008) Exp. Cell Res. , vol.314 , Issue.10 , pp. 2076-2089
    • Cole, N.B.1    Dieuliis, D.2    Leo, P.3    Mitchell, D.C.4    Nussbaum, R.L.5
  • 40
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: Membrane interactions and toxicity in Parkinsons disease
    • Auluck, P. K.; Caraveo, G.; Lindquist, S. α-Synuclein: membrane interactions and toxicity in Parkinsons disease Annu. Rev. Cell Dev. Biol. 2010, 26, 211-33
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.