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Volumn 11, Issue 2, 2010, Pages 167-174

Cell-penetrating peptide technology to deliver chaperones and associated factors in diseases and basic research

Author keywords

Antennapedia (penetratin); Arginine rich peptide; HIV Tat; Ischemia; Pep 1; Protein delivery; Stroke; Trojan horse

Indexed keywords

ALPHA SYNUCLEIN; BAG 1 PROTEIN; CELL PENETRATING PEPTIDE; CHAPERONE; CHOLINE ACETYLTRANSFERASE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; HYBRID PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PENETRATIN; SOMATOMEDIN C; TRANSACTIVATOR PROTEIN; VASOPRESSIN RECEPTOR;

EID: 77949885837     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/138920110790909731     Document Type: Review
Times cited : (71)

References (104)
  • 1
    • 0014430496 scopus 로고
    • Uptake of protein by mammalian cells: An underdeveloped area
    • Ryser, H.J.P. Uptake of protein by mammalian cells: an underdeveloped area. Science, 1968, 159(813), 390-396.
    • (1968) Science , vol.159 , Issue.813 , pp. 390-396
    • Ryser, H.J.P.1
  • 2
    • 0026784945 scopus 로고
    • Antennapedia homeobox as a signal for the cellular internalization and nuclear addressing of a small exogenous peptide
    • Perez, F.; Joliot, A.; Bloch-Gallego, E.; Zahraoui, A.; Triller, A.; Prochiantz, A. Antennapedia homeobox as a signal for the cellular internalization and nuclear addressing of a small exogenous peptide. J. Cell Sci., 1992, 102(Pt 4), 717-722.
    • (1992) J. Cell Sci , vol.102 , Issue.PART 4 , pp. 717-722
    • Perez, F.1    Joliot, A.2    Bloch-Gallego, E.3    Zahraoui, A.4    Triller, A.5    Prochiantz, A.6
  • 4
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • Elliott, G.; O'Hare, P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell, 1997, 88(2), 223-233.
    • (1997) Cell , vol.88 , Issue.2 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 5
    • 2642680830 scopus 로고    scopus 로고
    • Cell penetration by transportan
    • Pooga, M.; Hallbrink, M.; Zorko, M.; Langel, U. Cell penetration by transportan. FASEB J., 1998, 12(1), 67-77.
    • (1998) FASEB J , vol.12 , Issue.1 , pp. 67-77
    • Pooga, M.1    Hallbrink, M.2    Zorko, M.3    Langel, U.4
  • 6
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze, S.R.; Ho, A.; Vocero-Akbani, A.; Dowdy, S.F. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science, 1999, 285(5433), 1569-1572.
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 7
    • 0033106072 scopus 로고    scopus 로고
    • High-efficiency intracellular magnetic labeling with novel superparamagnetic-Tat peptide conjugates
    • Josephson, L.; Tung, C.H.; Moore, A.; Weissleder, R. High-efficiency intracellular magnetic labeling with novel superparamagnetic-Tat peptide conjugates. Bioconjug. Chem., 1999, 10(2), 186-191.
    • (1999) Bioconjug. Chem , vol.10 , Issue.2 , pp. 186-191
    • Josephson, L.1    Tung, C.H.2    Moore, A.3    Weissleder, R.4
  • 8
    • 0033678653 scopus 로고    scopus 로고
    • Conjugation of arginine oligomers to cyclosporin A facilitates topical delivery and inhibition of inflammation
    • Rothbard, J.B.; Garlington, S.; Lin, Q.; Kirschberg, T.; Kreider, E.; McGrane, P.L.; Wender, P.A.; Khavari, P.A. Conjugation of arginine oligomers to cyclosporin A facilitates topical delivery and inhibition of inflammation. Nat. Med., 2000, 6(11), 1253-1257.
    • (2000) Nat. Med , vol.6 , Issue.11 , pp. 1253-1257
    • Rothbard, J.B.1    Garlington, S.2    Lin, Q.3    Kirschberg, T.4    Kreider, E.5    McGrane, P.L.6    Wender, P.A.7    Khavari, P.A.8
  • 9
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • 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.
    • (2001) Nat. Biotechnol , vol.19 , Issue.12 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 10
    • 0036395238 scopus 로고    scopus 로고
    • Inhibition of neuronal apoptosis in vitro and in vivo using TAT-mediated protein transduction
    • Dietz, G.P.H.; Kilic, E.; Bähr, M. Inhibition of neuronal apoptosis in vitro and in vivo using TAT-mediated protein transduction. Mol. Cell Neurosci., 2002, 21(1), 29-37.
    • (2002) Mol. Cell Neurosci , vol.21 , Issue.1 , pp. 29-37
    • Dietz, G.P.H.1    Kilic, E.2    Bähr, M.3
  • 12
    • 0036829818 scopus 로고    scopus 로고
    • Intravenous TAT-Bcl-xL is protective after middle cerebral artery occlusion in mice
    • Kilic, E.; Dietz, G.P.H.; Hermann, D.M.; Bähr, M. Intravenous TAT-Bcl-xL is protective after middle cerebral artery occlusion in mice. Ann Neurol., 2002, 52(5), 617-622.
    • (2002) Ann Neurol , vol.52 , Issue.5 , pp. 617-622
    • Kilic, E.1    Dietz, G.P.H.2    Hermann, D.M.3    Bähr, M.4
  • 14
    • 5644276383 scopus 로고    scopus 로고
    • Delivery of bioactive molecules into the cell: The Trojan horse approach
    • Dietz, G.P.H.; Bähr, M. Delivery of bioactive molecules into the cell: the Trojan horse approach. Mol. Cell Neurosci., 2004, 27(2), 85-131.
    • (2004) Mol. Cell Neurosci , vol.27 , Issue.2 , pp. 85-131
    • Dietz, G.P.H.1    Bähr, M.2
  • 15
    • 33947240257 scopus 로고    scopus 로고
    • Dual localization: Proteins in extracellular and intracellular compartments
    • Arnoys, E.J.; Wang, J.L. Dual localization: proteins in extracellular and intracellular compartments. Acta Histochem., 2007, 109(2), 89-110.
    • (2007) Acta Histochem , vol.109 , Issue.2 , pp. 89-110
    • Arnoys, E.J.1    Wang, J.L.2
  • 16
    • 46149125267 scopus 로고    scopus 로고
    • Membrane-associated stress proteins: More than simply chaperones 2
    • Horvath, I.; Multhoff, G.; Sonnleitner, A.; Vigh, L. Membrane-associated stress proteins: more than simply chaperones 2. Biochim. Biophys. Acta, 2008, 1778(7-8), 1653-1664.
    • (2008) Biochim. Biophys. Acta , vol.1778 , Issue.7-8 , pp. 1653-1664
    • Horvath, I.1    Multhoff, G.2    Sonnleitner, A.3    Vigh, L.4
  • 18
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • Multhoff, G.; Hightower, L.E. Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones, 1996, 1(3), 167-176.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.3 , pp. 167-176
    • Multhoff, G.1    Hightower, L.E.2
  • 19
    • 34848899804 scopus 로고    scopus 로고
    • Engineering secretable forms of chaperones for immune modulation and vaccine development
    • Beachy, S.H.; Kisailus, A.J.; Repasky, E.A.; Subjeck, J.R.; Wang, X.Y.; Kazim, A.L. Engineering secretable forms of chaperones for immune modulation and vaccine development. Methods, 2007, 43(3), 184-193.
    • (2007) Methods , vol.43 , Issue.3 , pp. 184-193
    • Beachy, S.H.1    Kisailus, A.J.2    Repasky, E.A.3    Subjeck, J.R.4    Wang, X.Y.5    Kazim, A.L.6
  • 23
    • 23344453615 scopus 로고    scopus 로고
    • Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues
    • Tytell, M. Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues. Int. J. Hyperthermia, 2005, 21(5), 445-455.
    • (2005) Int. J. Hyperthermia , vol.21 , Issue.5 , pp. 445-455
    • Tytell, M.1
  • 24
    • 77949881941 scopus 로고    scopus 로고
    • Tytell, M.; Robinson, M.B.; Milligan, C.E. Release of heat shock proteins and their effects when in the extracellular space in the nervous system. In: Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection; ed. Asea, A.A.A., Brown, I.R., Eds.; Springer Science+Business Media B.V. 2009, pp. 257-272.
    • Tytell, M.; Robinson, M.B.; Milligan, C.E. Release of heat shock proteins and their effects when in the extracellular space in the nervous system. In: Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection; ed. Asea, A.A.A., Brown, I.R., Eds.; Springer Science+Business Media B.V. 2009, pp. 257-272.
  • 25
    • 0022637881 scopus 로고
    • Heat shock-like protein is transferred from glia to axon
    • Tytell, M.; Greenberg, S.G.; Lasek, R.J. Heat shock-like protein is transferred from glia to axon. Brain Res., 1986, 363(1), 161-164.
    • (1986) Brain Res , vol.363 , Issue.1 , pp. 161-164
    • Tytell, M.1    Greenberg, S.G.2    Lasek, R.J.3
  • 26
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • Hightower, L.E.; Guidon, P.T., Jr. Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J. Cell Physiol., 1989, 138(2), 257-266.
    • (1989) J. Cell Physiol , vol.138 , Issue.2 , pp. 257-266
    • Hightower, L.E.1    Guidon Jr., P.T.2
  • 27
    • 0030225159 scopus 로고    scopus 로고
    • Exogenous heat shock cognate protein Hsc 70 prevents axotomy-induced death of spinal sensory neurons
    • Houenou, L.J.; Li, L.; Lei, M.; Kent, C.R.; Tytell, M. Exogenous heat shock cognate protein Hsc 70 prevents axotomy-induced death of spinal sensory neurons. Cell Stress Chaperones, 1996, 1(3), 161-6.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.3 , pp. 161-166
    • Houenou, L.J.1    Li, L.2    Lei, M.3    Kent, C.R.4    Tytell, M.5
  • 28
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • Guzhova, I.; Kislyakova, K.; Moskaliova, O.; Fridlanskaya, I.; Tytell, M.; Cheetham, M.; Margulis, B. In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Res., 2001, 914(1-2), 66-73.
    • (2001) Brain Res , vol.914 , Issue.1-2 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 29
    • 0035789135 scopus 로고    scopus 로고
    • Retinal uptake of intravitreally injected Hsc/Hsp70 and its effect on susceptibility to light damage
    • Yu, Q.; Kent, C.R.; Tytell, M. Retinal uptake of intravitreally injected Hsc/Hsp70 and its effect on susceptibility to light damage. Mol. Vis., 2001, 7, 48-56.
    • (2001) Mol. Vis , vol.7 , pp. 48-56
    • Yu, Q.1    Kent, C.R.2    Tytell, M.3
  • 30
    • 1842562325 scopus 로고    scopus 로고
    • Administration of Hsp70 in vivo inhibits motor and sensory neuron degeneration
    • Tidwell, J.L.; Houenou, L.J.; Tytell, M. Administration of Hsp70 in vivo inhibits motor and sensory neuron degeneration. Cell Stress Chaperones, 2004, 9(1), 88-98.
    • (2004) Cell Stress Chaperones , vol.9 , Issue.1 , pp. 88-98
    • Tidwell, J.L.1    Houenou, L.J.2    Tytell, M.3
  • 33
    • 38149065825 scopus 로고    scopus 로고
    • Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress
    • Robinson, M.B.; Taylor, A.R.; Gifondorwa, D.J.; Tytell, M.; Milligan, C.E. Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress. Dev. Neurobiol., 2008, 68(1), 1-17.
    • (2008) Dev. Neurobiol , vol.68 , Issue.1 , pp. 1-17
    • Robinson, M.B.1    Taylor, A.R.2    Gifondorwa, D.J.3    Tytell, M.4    Milligan, C.E.5
  • 35
    • 0033555665 scopus 로고    scopus 로고
    • Intranuclear targeted delivery of functional NF-kappaB by 70 kDa heat shock protein
    • Fujihara, S.M.; Nadler, S.G. Intranuclear targeted delivery of functional NF-kappaB by 70 kDa heat shock protein. EMBO J., 1999, 18(2), 411-419.
    • (1999) EMBO J , vol.18 , Issue.2 , pp. 411-419
    • Fujihara, S.M.1    Nadler, S.G.2
  • 36
    • 33750040895 scopus 로고    scopus 로고
    • Characterization of a novel cell penetrating peptide derived from Bag-1 protein
    • Niarchos, D.K.; Perez, S.A.; Papamichail, M. Characterization of a novel cell penetrating peptide derived from Bag-1 protein. Peptides, 2006, 27(11), 2661-2669.
    • (2006) Peptides , vol.27 , Issue.11 , pp. 2661-2669
    • Niarchos, D.K.1    Perez, S.A.2    Papamichail, M.3
  • 37
    • 85177150741 scopus 로고    scopus 로고
    • Takenaka, I.M.; Leung, S.M.; McAndrew, S.J.; Brown, J.P.; High-tower, L.E. Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences3. J. Biol. Chem., 1995, 270(34), 19839-19844.
    • Takenaka, I.M.; Leung, S.M.; McAndrew, S.J.; Brown, J.P.; High-tower, L.E. Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences3. J. Biol. Chem., 1995, 270(34), 19839-19844.
  • 38
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • Eguchi, A.; Meade, B.R.; Chang, Y.C.; Fredrickson, C.T.; Willert, K.; Puri, N.; Dowdy, S.F. Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat. Biotechnol., 2009, 27(6), 567-571.
    • (2009) Nat. Biotechnol , vol.27 , Issue.6 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.C.3    Fredrickson, C.T.4    Willert, K.5    Puri, N.6    Dowdy, S.F.7
  • 39
    • 77949892140 scopus 로고    scopus 로고
    • Lai, Y.; Du, L.; Wong, H.R.; Kochanek, P.M.; Jenkins, L.W.; Dunsmore, K.; Graham, S.H.; Clark, R.S.B. Tat-HSP70 protects neurons from peroxynitrite and glutamate-induced cell death. Society for Neuroscience Abstracts, 2002, Program No. 225.1. 2002.
    • Lai, Y.; Du, L.; Wong, H.R.; Kochanek, P.M.; Jenkins, L.W.; Dunsmore, K.; Graham, S.H.; Clark, R.S.B. Tat-HSP70 protects neurons from peroxynitrite and glutamate-induced cell death. Society for Neuroscience Abstracts, 2002, Program No. 225.1. 2002.
  • 40
    • 22244440491 scopus 로고    scopus 로고
    • Selectively increasing inducible heat shock protein 70 via TAT-protein transduction protects neurons from nitrosative stress and excitotoxicity
    • Lai, Y.; Du, L.; Dunsmore, K.E.; Jenkins, L.W.; Wong, H.R.; Clark, R.S. Selectively increasing inducible heat shock protein 70 via TAT-protein transduction protects neurons from nitrosative stress and excitotoxicity. J. Neurochem., 2005, 94(2), 360-366.
    • (2005) J. Neurochem , vol.94 , Issue.2 , pp. 360-366
    • Lai, Y.1    Du, L.2    Dunsmore, K.E.3    Jenkins, L.W.4    Wong, H.R.5    Clark, R.S.6
  • 41
    • 0037474523 scopus 로고    scopus 로고
    • Intracellular delivery of HSP70 using HIV-1 Tat protein transduction domain
    • Wheeler, D.S.; Dunsmore, K.E.; Wong, H.R. Intracellular delivery of HSP70 using HIV-1 Tat protein transduction domain. Biochem. Biophys. Res. Commun., 2003, 301(1), 54-59.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , Issue.1 , pp. 54-59
    • Wheeler, D.S.1    Dunsmore, K.E.2    Wong, H.R.3
  • 43
    • 34748850676 scopus 로고    scopus 로고
    • Protective effect of heat shock protein 27 using protein transduction domain-mediated delivery on ischemia/reperfusion heart injury
    • Kwon, J.H.; Kim, J.B.; Lee, K.H.; Kang, S.M.; Chung, N.; Jang, Y.; Chung, J.H. Protective effect of heat shock protein 27 using protein transduction domain-mediated delivery on ischemia/reperfusion heart injury. Biochem. Biophys. Res. Commun., 2007, 363(2), 399-404.
    • (2007) Biochem. Biophys. Res. Commun , vol.363 , Issue.2 , pp. 399-404
    • Kwon, J.H.1    Kim, J.B.2    Lee, K.H.3    Kang, S.M.4    Chung, N.5    Jang, Y.6    Chung, J.H.7
  • 44
    • 66649105782 scopus 로고    scopus 로고
    • The heat shock protein 27 (Hsp27) operates predominantly by blocking the mitochondrialin-dependent/ extrinsic pathway of cellular apoptosis
    • Tan, C.Y.; Ban, H.; Kim, Y.H.; Lee, S.K. The heat shock protein 27 (Hsp27) operates predominantly by blocking the mitochondrialin-dependent/ extrinsic pathway of cellular apoptosis. Mol. Cells., 2009, 27(5), 533-538.
    • (2009) Mol. Cells , vol.27 , Issue.5 , pp. 533-538
    • Tan, C.Y.1    Ban, H.2    Kim, Y.H.3    Lee, S.K.4
  • 45
    • 67649236178 scopus 로고    scopus 로고
    • Controlled delivery of heat shock protein using an injectable microsphere/ hydrogel combination system for the treatment of myocardial infarction
    • Lee, J.; Tan, C.Y.; Lee, S.K.; Kim, Y.H.; Lee, K.Y. Controlled delivery of heat shock protein using an injectable microsphere/ hydrogel combination system for the treatment of myocardial infarction. J. Control. Release, 2009, 137(3), 196-202.
    • (2009) J. Control. Release , vol.137 , Issue.3 , pp. 196-202
    • Lee, J.1    Tan, C.Y.2    Lee, S.K.3    Kim, Y.H.4    Lee, K.Y.5
  • 46
    • 39649104548 scopus 로고    scopus 로고
    • TAT-Hsp40 inhibits oxidative stress-mediated cytotoxicity via the inhibition of Hsp70 ubiquitination
    • Kim, S.A.; Chang, S.; Yoon, J.H.; Ahn, S.G. TAT-Hsp40 inhibits oxidative stress-mediated cytotoxicity via the inhibition of Hsp70 ubiquitination. FEBS Lett., 2008, 582(5), 734-740.
    • (2008) FEBS Lett , vol.582 , Issue.5 , pp. 734-740
    • Kim, S.A.1    Chang, S.2    Yoon, J.H.3    Ahn, S.G.4
  • 48
    • 43449122435 scopus 로고    scopus 로고
    • Quantitative evaluation of chaperone activity and neuroprotection by different preparations of a cell-penetrating Hsp70
    • Nagel, F.; Dohm, C.P.; Bahr, M.; Wouters, F.S.; Dietz, G.P.H. Quantitative evaluation of chaperone activity and neuroprotection by different preparations of a cell-penetrating Hsp70. J. Neurosci., Methods, 2008, 171(2), 226-232.
    • (2008) J. Neurosci., Methods , vol.171 , Issue.2 , pp. 226-232
    • Nagel, F.1    Dohm, C.P.2    Bahr, M.3    Wouters, F.S.4    Dietz, G.P.H.5
  • 50
    • 42249103388 scopus 로고    scopus 로고
    • Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease
    • Nagel, F.; Falkenburger, B.H.; Tonges, L.; Kowsky, S.; Poppelmeyer, C.; Schulz, J.B.; Bähr, M.; Dietz, G.P.H. Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease. J. Neurochem., 2008, 105(3), 853-864.
    • (2008) J. Neurochem , vol.105 , Issue.3 , pp. 853-864
    • Nagel, F.1    Falkenburger, B.H.2    Tonges, L.3    Kowsky, S.4    Poppelmeyer, C.5    Schulz, J.B.6    Bähr, M.7    Dietz, G.P.H.8
  • 51
    • 9444272812 scopus 로고    scopus 로고
    • Protective effect of TAT-delivered alpha-synuclein: Relevance of the C-terminal domain and involvement of HSP70
    • Albani, D.; Peverelli, E.; Rametta, R.; Batelli, S.; Veschini, L.; Negro, A.; Forloni, G. Protective effect of TAT-delivered alpha-synuclein: relevance of the C-terminal domain and involvement of HSP70. FASEB J., 2004, 18(14), 1713-1715.
    • (2004) FASEB J , 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
  • 52
    • 44849093321 scopus 로고    scopus 로고
    • DJ-1 modulates alpha-synuclein aggregation state in a cellular model of oxidative stress: Relevance for Parkinson's disease and involvement of HSP70
    • Batelli, S.; Albani, D.; Rametta, R.; Polito, L.; Prato, F.; Pesaresi, M.; Negro, A.; Forloni, G. DJ-1 modulates alpha-synuclein aggregation state in a cellular model of oxidative stress: relevance for Parkinson's disease and involvement of HSP70. PLoS ONE, 2008, 3(4), e1884.
    • (2008) PLoS ONE , vol.3 , Issue.4
    • Batelli, S.1    Albani, D.2    Rametta, R.3    Polito, L.4    Prato, F.5    Pesaresi, M.6    Negro, A.7    Forloni, G.8
  • 53
    • 67349287017 scopus 로고    scopus 로고
    • TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice
    • Doeppner, T.R.; Nagel, F.; Dietz, G.P.H.; Weise, J.; Tonges, L.; Schwarting, S.; Bahr, M. TAT-Hsp70-mediated neuroprotection and increased survival of neuronal precursor cells after focal cerebral ischemia in mice. J. Cereb. Blood Flow. Metab., 2009, 29(6), 1187-1196.
    • (2009) J. Cereb. Blood Flow. Metab , vol.29 , Issue.6 , pp. 1187-1196
    • Doeppner, T.R.1    Nagel, F.2    Dietz, G.P.H.3    Weise, J.4    Tonges, L.5    Schwarting, S.6    Bahr, M.7
  • 57
    • 1842850740 scopus 로고    scopus 로고
    • Sildenafil-induced vasorelaxation is associated with increases in the phosphorylation of the heat shock-related protein 20 (HSP20)
    • Tessier, D.J.; Komalavilas, P.; McLemore, E.; Thresher, J.; Brophy, C.M. Sildenafil-induced vasorelaxation is associated with increases in the phosphorylation of the heat shock-related protein 20 (HSP20). J. Surg. Res., 2004, 118(1), 21-25.
    • (2004) J. Surg. Res , vol.118 , Issue.1 , pp. 21-25
    • Tessier, D.J.1    Komalavilas, P.2    McLemore, E.3    Thresher, J.4    Brophy, C.M.5
  • 64
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • Schwarze, S.R.; Hruska, K.A.; Dowdy, S.F. Protein transduction: unrestricted delivery into all cells? Trends Cell Biol., 2000, 10(7), 290-295.
    • (2000) Trends Cell Biol , vol.10 , Issue.7 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 65
    • 0038048992 scopus 로고    scopus 로고
    • Wadia, J.S.; Dowdy, S.F. Modulation of cellular function by TAT mediated transduction of full length proteins. Curr. Protein Pept. Sci., 2003, 4(2), 97-104. [66] Nagahara, H.; Vocero-Akbani, A.M.; Snyder, E.L.; Ho, A.; Latham, D.G.; Lissy, N.A.; Becker-Hapak, M.; Ezhevsky, S.A.; Dowdy, S.F. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat. Med., 1998, 4(12), 1449-1452. [67] Derossi, D.; Calvet, S.; Trembleau, A.; Brunissen, A.; Chassaing, G.; Prochiantz, A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem., 1996, 271(30), 18188-18193.
    • Wadia, J.S.; Dowdy, S.F. Modulation of cellular function by TAT mediated transduction of full length proteins. Curr. Protein Pept. Sci., 2003, 4(2), 97-104. [66] Nagahara, H.; Vocero-Akbani, A.M.; Snyder, E.L.; Ho, A.; Latham, D.G.; Lissy, N.A.; Becker-Hapak, M.; Ezhevsky, S.A.; Dowdy, S.F. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat. Med., 1998, 4(12), 1449-1452. [67] Derossi, D.; Calvet, S.; Trembleau, A.; Brunissen, A.; Chassaing, G.; Prochiantz, A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem., 1996, 271(30), 18188-18193.
  • 66
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S.; Suzuki, T.; Ohashi, W.; Yagami, T.; Tanaka, S.; Ueda, K.; Sugiura, Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem., 2001, 276(8), 5836-5840.
    • (2001) J. Biol. Chem , vol.276 , Issue.8 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 67
    • 28144440865 scopus 로고    scopus 로고
    • Peptide-enhanced cellular internalization of proteins in neuroscience
    • Dietz, G.P.H.; Bähr, M. Peptide-enhanced cellular internalization of proteins in neuroscience. Brain Res. Bull., 2005, 68(1-2), 103-114.
    • (2005) Brain Res. Bull , vol.68 , Issue.1-2 , pp. 103-114
    • Dietz, G.P.H.1    Bähr, M.2
  • 68
    • 57149110011 scopus 로고    scopus 로고
    • CNS delivery via adsorptive transcytosis
    • Herve, F.; Ghinea, N.; Scherrmann, J.M. CNS delivery via adsorptive transcytosis. AAPS J., 2008, 10(3), 455-472.
    • (2008) AAPS J , vol.10 , Issue.3 , pp. 455-472
    • Herve, F.1    Ghinea, N.2    Scherrmann, J.M.3
  • 69
    • 67349230238 scopus 로고    scopus 로고
    • Cellular siRNA delivery using cellpenetrating peptides modified for endosomal escape
    • Endoh, T.; Ohtsuki, T. Cellular siRNA delivery using cellpenetrating peptides modified for endosomal escape. Adv. Drug Deliv. Rev., 2009, 61(9), 704-709.
    • (2009) Adv. Drug Deliv. Rev , vol.61 , Issue.9 , pp. 704-709
    • Endoh, T.1    Ohtsuki, T.2
  • 70
    • 39149093340 scopus 로고    scopus 로고
    • Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides
    • Meade, B.R.; Dowdy, S.F. Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides. Adv. Drug Deliv. Rev., 2008, 60(4-5), 530-536.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 530-536
    • Meade, B.R.1    Dowdy, S.F.2
  • 71
    • 34248680739 scopus 로고    scopus 로고
    • Exogenous siRNA delivery using peptide transduction domains/cell penetrating peptides
    • Meade, B.R.; Dowdy, S.F. Exogenous siRNA delivery using peptide transduction domains/cell penetrating peptides. Adv. Drug Deliv. Rev., 2007, 59(2-3), 134-140.
    • (2007) Adv. Drug Deliv. Rev , vol.59 , Issue.2-3 , pp. 134-140
    • Meade, B.R.1    Dowdy, S.F.2
  • 72
    • 45249112836 scopus 로고    scopus 로고
    • Delivery of small interfering RNA. A review and an example of application to a junction oncogene
    • Ramon, A.L.; Bertrand, J.R.; Malvy, C. Delivery of small interfering RNA. A review and an example of application to a junction oncogene. Tumori, 2008, 94(2), 254-263.
    • (2008) Tumori , vol.94 , Issue.2 , pp. 254-263
    • Ramon, A.L.1    Bertrand, J.R.2    Malvy, C.3
  • 73
    • 48749084702 scopus 로고    scopus 로고
    • Recent developments in Peptide-based nucleic Acid delivery
    • Veldhoen, S.; Laufer, S.D.; Restle, T. Recent developments in Peptide-based nucleic Acid delivery. Int. J. Mol. Sci., 2008, 9(7), 1276-1320.
    • (2008) Int. J. Mol. Sci , vol.9 , Issue.7 , pp. 1276-1320
    • Veldhoen, S.1    Laufer, S.D.2    Restle, T.3
  • 75
    • 52949148197 scopus 로고    scopus 로고
    • Cell penetrating peptides for in vivo molecular imaging applications
    • Kersemans, V.; Kersemans, K.; Cornelissen, B. Cell penetrating peptides for in vivo molecular imaging applications. Curr. Pharm. Des., 2008, 14(24), 2415-2447.
    • (2008) Curr. Pharm. Des , vol.14 , Issue.24 , pp. 2415-2447
    • Kersemans, V.1    Kersemans, K.2    Cornelissen, B.3
  • 76
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones, A.T. Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell Mol. Med., 2007, 11(4), 670-684.
    • (2007) J. Cell Mol. Med , vol.11 , Issue.4 , pp. 670-684
    • Jones, A.T.1
  • 77
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • Duchardt, F.; Fotin-Mleczek, M.; Schwarz, H.; Fischer, R.; Brock, R. A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic, 2007, 8(7), 848-866.
    • (2007) Traffic , vol.8 , Issue.7 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 78
    • 59849102702 scopus 로고    scopus 로고
    • Protein transduction revisited: Novel insights into the mechanism underlying intracellular delivery of proteins
    • Edenhofer, F. Protein transduction revisited: novel insights into the mechanism underlying intracellular delivery of proteins. Curr. Pharm. Des., 2008, 14(34), 3628-3636.
    • (2008) Curr. Pharm. Des , vol.14 , Issue.34 , pp. 3628-3636
    • Edenhofer, F.1
  • 79
    • 0038387344 scopus 로고    scopus 로고
    • Vives, E.; Richard, J.P.; Rispal, C.; Lebleu, B. TAT Peptide Internalization: Seeking the Mechanism of Entry. Curr. Protein Pept. Sci., 2003, 4(2), 125-132.
    • Vives, E.; Richard, J.P.; Rispal, C.; Lebleu, B. TAT Peptide Internalization: Seeking the Mechanism of Entry. Curr. Protein Pept. Sci., 2003, 4(2), 125-132.
  • 80
    • 38049092119 scopus 로고    scopus 로고
    • Reviewing biophysical and cell biological methodologies in cell-penetrating peptide (CPP) research
    • Herbig, M.E.; Weller, K.M.; Merkle, H.P. Reviewing biophysical and cell biological methodologies in cell-penetrating peptide (CPP) research. Crit. Rev. Ther. Drug Carr. Syst., 2007, 24(3), 203-255.
    • (2007) Crit. Rev. Ther. Drug Carr. Syst , vol.24 , Issue.3 , pp. 203-255
    • Herbig, M.E.1    Weller, K.M.2    Merkle, H.P.3
  • 81
    • 50849144942 scopus 로고    scopus 로고
    • Cell penetrating peptide-modified pharmaceutical nanocarriers for intracellular drug and gene delivery
    • Torchilin, V.P. Cell penetrating peptide-modified pharmaceutical nanocarriers for intracellular drug and gene delivery. Biopolymers, 2008, 90(5), 604-610.
    • (2008) Biopolymers , vol.90 , Issue.5 , pp. 604-610
    • Torchilin, V.P.1
  • 82
    • 38949192863 scopus 로고    scopus 로고
    • Tat peptide-mediated intracellular delivery of pharmaceutical nanocarriers
    • Torchilin, V.P. Tat peptide-mediated intracellular delivery of pharmaceutical nanocarriers. Adv. Drug Deliv. Rev., 2008, 60(4-5), 548-558.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 548-558
    • Torchilin, V.P.1
  • 83
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • Morris, M.C.; Deshayes, S.; Heitz, F.; Divita, G. Cell-penetrating peptides: from molecular mechanisms to therapeutics. Biol. Cell, 2008, 100(4), 201-217.
    • (2008) Biol. Cell , vol.100 , Issue.4 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 84
    • 33749656235 scopus 로고    scopus 로고
    • Molecular transporters: Synthesis of oligoguanidinium transporters and their application to drug delivery and real-time imaging 1
    • Goun, E.A.; Pillow, T.H.; Jones, L.R.; Rothbard, J.B.; Wender, P.A. Molecular transporters: synthesis of oligoguanidinium transporters and their application to drug delivery and real-time imaging 1. Chembiochem., 2006, 7(10), 1497-1515.
    • (2006) Chembiochem , vol.7 , Issue.10 , pp. 1497-1515
    • Goun, E.A.1    Pillow, T.H.2    Jones, L.R.3    Rothbard, J.B.4    Wender, P.A.5
  • 85
    • 42149194279 scopus 로고    scopus 로고
    • Arginine-rich cell penetrating peptides: Design, structure-activity, and applications to alter pre-mRNA splicing by steric-block oligonucleotides
    • Abes, R.; Arzumanov, A.; Moulton, H.; Abes, S.; Ivanova, G.; Gait, M.J.; Iversen, P.; Lebleu, B. Arginine-rich cell penetrating peptides: design, structure-activity, and applications to alter pre-mRNA splicing by steric-block oligonucleotides. J. Pept. Sci., 2008, 14(4), 455-460.
    • (2008) J. Pept. Sci , vol.14 , Issue.4 , pp. 455-460
    • Abes, R.1    Arzumanov, A.2    Moulton, H.3    Abes, S.4    Ivanova, G.5    Gait, M.J.6    Iversen, P.7    Lebleu, B.8
  • 87
    • 39149127301 scopus 로고    scopus 로고
    • Proline-rich, amphipathic cell-penetrating peptides
    • Pujals, S.; Giralt, E. Proline-rich, amphipathic cell-penetrating peptides. Adv. Drug Deliv. Rev., 2008, 60(4-5), 473-484.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 473-484
    • Pujals, S.1    Giralt, E.2
  • 88
    • 42149177168 scopus 로고    scopus 로고
    • Translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity
    • Henriques, S.T.; Castanho, M.A. Translocation or membrane disintegration? Implication of peptide-membrane interactions in pep-1 activity. J. Pept. Sci., 2008, 14(4), 482-487.
    • (2008) J. Pept. Sci , vol.14 , Issue.4 , pp. 482-487
    • Henriques, S.T.1    Castanho, M.A.2
  • 89
    • 38949213664 scopus 로고    scopus 로고
    • Predicting cell-penetrating peptides
    • Hansen, M.; Kilk, K.; Langel, U. Predicting cell-penetrating peptides. Adv. Drug Deliv. Rev., 2008, 60(4-5), 572-579.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 572-579
    • Hansen, M.1    Kilk, K.2    Langel, U.3
  • 90
    • 38949168425 scopus 로고    scopus 로고
    • Homeoproteins as natural Penetratin cargoes with signaling properties
    • Joliot, A.; Prochiantz, A. Homeoproteins as natural Penetratin cargoes with signaling properties. Adv. Drug Deliv. Rev., 2008, 60(4-5), 608-613.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 608-613
    • Joliot, A.1    Prochiantz, A.2
  • 91
    • 39149092665 scopus 로고    scopus 로고
    • PTD-mediated delivery of anti-cell death proteins/ peptides and therapeutic enzymes
    • Asoh, S.; Ohta, S. PTD-mediated delivery of anti-cell death proteins/ peptides and therapeutic enzymes. Adv. Drug Deliv. Rev., 2008, 60(4-5), 499-516.
    • (2008) Adv. Drug Deliv. Rev , vol.60 , Issue.4-5 , pp. 499-516
    • Asoh, S.1    Ohta, S.2
  • 92
    • 38049179255 scopus 로고    scopus 로고
    • Synthesis of cell penetrating peptides and their application in neurobiology
    • Borsello, T, Ed, Totowa, N.J, The Humana Press Inc
    • Dietz, G.P.H.; Bähr, M. Synthesis of cell penetrating peptides and their application in neurobiology. in: Neuroprotection; Borsello, T., Ed.; Totowa, N.J.: The Humana Press Inc., 2007, pp. 181-198.
    • (2007) Neuroprotection , pp. 181-198
    • Dietz, G.P.H.1    Bähr, M.2
  • 94
    • 51349113842 scopus 로고    scopus 로고
    • Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia
    • Sun, F.; Mi, Z.; Condliffe, S.B.; Bertrand, C.A.; Gong, X.; Lu, X.; Zhang, R.; Latoche, J.D.; Pilewski, J.M.; Robbins, P.D.; Frizzell, R.A. Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia. FASEB J., 2008, 22(9), 3255-3263.
    • (2008) FASEB J , vol.22 , Issue.9 , pp. 3255-3263
    • Sun, F.1    Mi, Z.2    Condliffe, S.B.3    Bertrand, C.A.4    Gong, X.5    Lu, X.6    Zhang, R.7    Latoche, J.D.8    Pilewski, J.M.9    Robbins, P.D.10    Frizzell, R.A.11
  • 95
    • 24344450713 scopus 로고    scopus 로고
    • Complementary remedy of aged-related learning and memory deficits via exogenous choline acetyltransferase
    • Fu, A.L.; Huang, S.J.; Sun, M.J. Complementary remedy of aged-related learning and memory deficits via exogenous choline acetyltransferase. Biochem. Biophys. Res. Commun., 2005, 336(1), 268-273.
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , Issue.1 , pp. 268-273
    • Fu, A.L.1    Huang, S.J.2    Sun, M.J.3
  • 98
    • 60349091880 scopus 로고    scopus 로고
    • A dual-functional E. coli vector for expressing recombinant protein with high solubility and antigen presentation ability
    • Chuang, C.K.; Su, Y.S.; Fan, C.T.; Lee, W.C.; Chen, M.Y. A dual-functional E. coli vector for expressing recombinant protein with high solubility and antigen presentation ability. Protein. Expr. Purif., 2009, 65(1), 51-56.
    • (2009) Protein. Expr. Purif , vol.65 , Issue.1 , pp. 51-56
    • Chuang, C.K.1    Su, Y.S.2    Fan, C.T.3    Lee, W.C.4    Chen, M.Y.5
  • 102
    • 65749109505 scopus 로고    scopus 로고
    • Tyrosine hydroxylase-positive amacrine interneurons in the mouse retina are resistant against the application of various parkinsonian toxins
    • Nagel, F.; Bähr, M.; Dietz, G.P.H. Tyrosine hydroxylase-positive amacrine interneurons in the mouse retina are resistant against the application of various parkinsonian toxins. Brain Res. Bull., 2009, 79(5), 303-309.
    • (2009) Brain Res. Bull , vol.79 , Issue.5 , pp. 303-309
    • Nagel, F.1    Bähr, M.2    Dietz, G.P.H.3
  • 103
    • 70350341973 scopus 로고    scopus 로고
    • Delivery of HSF1(+) protein using HIV-1 TAT protein transduction domain
    • Hou, Y.; Zou, J. Delivery of HSF1(+) protein using HIV-1 TAT protein transduction domain. Mol. Biol. Rep., 2009, 36(8), 2271-2277.
    • (2009) Mol. Biol. Rep , vol.36 , Issue.8 , pp. 2271-2277
    • Hou, Y.1    Zou, J.2
  • 104
    • 38049170908 scopus 로고    scopus 로고
    • A heat shock protein 90 binding domain in endothelial nitric-oxide synthase influences enzyme function
    • Xu, H.; Shi, Y.; Wang, J.; Jones, D.; Weilrauch, D.; Ying, R.; Wakim, B.; Pritchard, K.A., Jr. A heat shock protein 90 binding domain in endothelial nitric-oxide synthase influences enzyme function. J. Biol. Chem., 2007, 282(52), 37567-37574.
    • (2007) J. Biol. Chem , vol.282 , Issue.52 , pp. 37567-37574
    • Xu, H.1    Shi, Y.2    Wang, J.3    Jones, D.4    Weilrauch, D.5    Ying, R.6    Wakim, B.7    Pritchard Jr., K.A.8


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