메뉴 건너뛰기




Volumn 11, Issue 8, 2014, Pages 861-867

Protein delivery into live cells by incubation with an endosomolytic agent

Author keywords

[No Author keywords available]

Indexed keywords

CELL PENETRATING PEPTIDE; DIMER; TETRAMETHYLRHODAMINE;

EID: 84905255035     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nMeth.2998     Document Type: Article
Times cited : (189)

References (39)
  • 1
    • 33746221130 scopus 로고    scopus 로고
    • Direct and rapid cytosolic delivery using cell-penetrating peptides mediated by pyrenebutyrate
    • Takeuchi, T. et al. Direct and rapid cytosolic delivery using cell-penetrating peptides mediated by pyrenebutyrate. ACS Chem. Biol. 1, 299-303 (2006).
    • (2006) ACS Chem. Biol. , vol.1 , pp. 299-303
    • Takeuchi, T.1
  • 2
    • 61949315876 scopus 로고    scopus 로고
    • Protein structure determination in living cells by in-cell NMR spectroscopy
    • Sakakibara, D. et al. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 458, 102-105 (2009).
    • (2009) Nature , vol.458 , pp. 102-105
    • Sakakibara, D.1
  • 3
    • 39749114895 scopus 로고    scopus 로고
    • Real-time fuorescence detection of protein transduction into live cells
    • Lee, Y.J., Datta, S. & Pellois, J.P. Real-time fuorescence detection of protein transduction into live cells. J. Am. Chem. Soc. 130, 2398-2399 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2398-2399
    • Lee, Y.J.1    Datta, S.2    Pellois, J.P.3
  • 4
    • 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. 10, 290-295 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 5
    • 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. 27, 85-131 (2004).
    • (2004) Mol. Cell. Neurosci. , vol.27 , pp. 85-131
    • Dietz, G.P.H.1    Bähr, M.2
  • 6
    • 77953175260 scopus 로고    scopus 로고
    • Reprogramming human fbroblasts using HIV-1 TAT recombinant proteins OCT4, SOX2, KLF4 and c-MYC
    • Pan, C., Lu, B., Chen, H. & Bishop, C. Reprogramming human fbroblasts using HIV-1 TAT recombinant proteins OCT4, SOX2, KLF4 and c-MYC. Mol. Biol. Rep. 37, 2117-2124 (2010).
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 2117-2124
    • Pan, C.1    Lu, B.2    Chen, H.3    Bishop, C.4
  • 7
    • 0037349932 scopus 로고    scopus 로고
    • Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-defcient viruses in cells and in vivo
    • Gratton, J.-P. et al. Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-defcient viruses in cells and in vivo. Nat. Med. 9, 357-362 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 357-362
    • Gratton, J.-P.1
  • 8
    • 77956275913 scopus 로고    scopus 로고
    • Enhanced fuorescence imaging of live cells by effective cytosolic delivery of probes
    • Massignani, M. et al. Enhanced fuorescence imaging of live cells by effective cytosolic delivery of probes. PLoS ONE 5, e10459 (2010).
    • (2010) PLoS ONE , vol.5
    • Massignani, M.1
  • 9
    • 84869236539 scopus 로고    scopus 로고
    • Improving the endosomal escape of cell-penetrating peptides and their cargos: Strategies and challenges
    • Erazo-Oliveras, A., Muthukrishnan, N., Baker, R., Wang, T.Y. & Pellois, J.P. Improving the endosomal escape of cell-penetrating peptides and their cargos: strategies and challenges. Pharmaceuticals (Basel.) 5, 1177-1209 (2012).
    • (2012) Pharmaceuticals (Basel.) , vol.5 , pp. 1177-1209
    • Erazo-Oliveras, A.1    Muthukrishnan, N.2    Baker, R.3    Wang, T.Y.4    Pellois, J.P.5
  • 10
    • 84867831150 scopus 로고    scopus 로고
    • Dimerization of a cell-penetrating peptide leads to enhanced cellular uptake and drug delivery
    • Hoyer, J., Schatzschneider, U., Schulz-Siegmund, M. & Neundorf, I. Dimerization of a cell-penetrating peptide leads to enhanced cellular uptake and drug delivery. Beilstein J. Org. Chem. 8, 1788-1797 (2012).
    • (2012) Beilstein J. Org. Chem. , vol.8 , pp. 1788-1797
    • Hoyer, J.1    Schatzschneider, U.2    Schulz-Siegmund, M.3    Neundorf, I.4
  • 11
    • 67149093390 scopus 로고    scopus 로고
    • Effcient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • Eguchi, A. et al. Effcient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat. Biotechnol. 27, 567-571 (2009).
    • (2009) Nat. Biotechnol. , vol.27 , pp. 567-571
    • Eguchi, A.1
  • 12
    • 29144496897 scopus 로고    scopus 로고
    • Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfde-based antibody-drug conjugates
    • Austin, C.D. et al. Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfde-based antibody-drug conjugates. Proc. Natl. Acad. Sci. USA 102, 17987-17992 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17987-17992
    • Austin, C.D.1
  • 13
    • 77951168054 scopus 로고    scopus 로고
    • Breaking down the barriers: SiRNA delivery and endosome escape
    • Dominska, M. & Dykxhoorn, D.M. Breaking down the barriers: siRNA delivery and endosome escape. J. Cell Sci. 123, 1183-1189 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1183-1189
    • Dominska, M.1    Dykxhoorn, D.M.2
  • 14
    • 0033203501 scopus 로고    scopus 로고
    • Cholesterol modulates membrane traffc along the endocytic pathway in sphingolipid-storage diseases
    • Puri, V. et al. Cholesterol modulates membrane traffc along the endocytic pathway in sphingolipid-storage diseases. Nat. Cell Biol. 1, 386-388 (1999).
    • (1999) Nat. Cell Biol. , vol.1 , pp. 386-388
    • Puri, V.1
  • 15
    • 77149129342 scopus 로고    scopus 로고
    • Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling
    • Koivusalo, M. et al. Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling. J. Cell Biol. 188, 547-563 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 547-563
    • Koivusalo, M.1
  • 16
    • 0027764386 scopus 로고
    • Endosome acidifcation and receptor traffcking: Baflomycin A1 slows receptor externalization by a mechanism involving the receptor's internalization motif
    • Johnson, L.S., Dunn, K.W., Pytowski, B. & McGraw, T.E. Endosome acidifcation and receptor traffcking: baflomycin A1 slows receptor externalization by a mechanism involving the receptor's internalization motif. Mol. Biol. Cell 4, 1251-1266 (1993).
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1251-1266
    • Johnson, L.S.1    Dunn, K.W.2    Pytowski, B.3    McGraw, T.E.4
  • 17
    • 77649272916 scopus 로고    scopus 로고
    • The use of inhibitors to study endocytic pathways of gene carriers: Optimization and pitfalls
    • Vercauteren, D. et al. The use of inhibitors to study endocytic pathways of gene carriers: optimization and pitfalls. Mol. Ther. 18, 561-569 (2010).
    • (2010) Mol. Ther. , vol.18 , pp. 561-569
    • Vercauteren, D.1
  • 18
    • 23844462026 scopus 로고    scopus 로고
    • Role of clathrin-and caveolae-mediated endocytosis in gene transfer mediated by lipo-and polyplexes
    • Rejman, J., Bragonzi, A. & Conese, M. Role of clathrin-and caveolae-mediated endocytosis in gene transfer mediated by lipo-and polyplexes. Mol. Ther. 12, 468-474 (2005).
    • (2005) Mol. Ther. , vol.12 , pp. 468-474
    • Rejman, J.1    Bragonzi, A.2    Conese, M.3
  • 19
    • 79952632412 scopus 로고    scopus 로고
    • Conjugation to the cell-penetrating peptide TAT potentiates the photodynamic effect of carboxytetramethylrhodamine
    • Srinivasan, D. et al. Conjugation to the cell-penetrating peptide TAT potentiates the photodynamic effect of carboxytetramethylrhodamine. PLoS ONE 6, e17732 (2011).
    • (2011) PLoS ONE , vol.6
    • Srinivasan, D.1
  • 20
    • 80052781568 scopus 로고    scopus 로고
    • Development of SNAP-tag fuorogenic probes for wash-free fuorescence imaging
    • Sun, X. et al. Development of SNAP-tag fuorogenic probes for wash-free fuorescence imaging. ChemBioChem 12, 2217-2226 (2011).
    • (2011) ChemBioChem , vol.12 , pp. 2217-2226
    • Sun, X.1
  • 21
    • 84866370878 scopus 로고    scopus 로고
    • Caspase-activated cell-penetrating peptides reveal temporal coupling between endosomal release and apoptosis in an RGC-5 cell model
    • Johnson, J.R., Kocher, B., Barnett, E.M., Marasa, J. & Piwnica-Worms, D. Caspase-activated cell-penetrating peptides reveal temporal coupling between endosomal release and apoptosis in an RGC-5 cell model. Bioconjug. Chem. 23, 1783-1793 (2012).
    • (2012) Bioconjug. Chem. , vol.23 , pp. 1783-1793
    • Johnson, J.R.1    Kocher, B.2    Barnett, E.M.3    Marasa, J.4    Piwnica-Worms, D.5
  • 22
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J.S., Stan, R.V. & Dowdy, S.F. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-315 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 23
    • 65549085650 scopus 로고    scopus 로고
    • An automated system for delivery of an unstable transcription factor to hematopoietic stem cell cultures
    • Csaszar, E. et al. An automated system for delivery of an unstable transcription factor to hematopoietic stem cell cultures. Biotechnol. Bioeng. 103, 402-412 (2009).
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 402-412
    • Csaszar, E.1
  • 24
    • 0345708270 scopus 로고    scopus 로고
    • Ex vivo expansion of human hematopoietic stem cells by direct delivery of the HOXB4 homeoprotein
    • Amsellem, S. et al. Ex vivo expansion of human hematopoietic stem cells by direct delivery of the HOXB4 homeoprotein. Nat. Med. 9, 1423-1427 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 1423-1427
    • Amsellem, S.1
  • 25
    • 0344413639 scopus 로고    scopus 로고
    • In vitro expansion of hematopoietic stem cells by recombinant TAT-HOXB4 protein
    • Krosl, J. et al. In vitro expansion of hematopoietic stem cells by recombinant TAT-HOXB4 protein. Nat. Med. 9, 1428-1432 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 1428-1432
    • Krosl, J.1
  • 26
    • 33645291810 scopus 로고    scopus 로고
    • HOXB4 inhibits cell growth in a dose-dependent manner and sensitizes cells towards extrinsic cues
    • Will, E. et al. HOXB4 inhibits cell growth in a dose-dependent manner and sensitizes cells towards extrinsic cues. Cell Cycle 5, 14-22 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 14-22
    • Will, E.1
  • 27
    • 84876795655 scopus 로고    scopus 로고
    • Synergy between cell-penetrating peptides and singlet oxygen generators leads to effcient photolysis of membranes
    • Muthukrishnan, N., Johnson, G.A., Erazo-Oliveras, A. & Pellois, J.P. Synergy between cell-penetrating peptides and singlet oxygen generators leads to effcient photolysis of membranes. Photochem. Photobiol. 89, 625-630 (2013).
    • (2013) Photochem. Photobiol. , vol.89 , pp. 625-630
    • Muthukrishnan, N.1    Johnson, G.A.2    Erazo-Oliveras, A.3    Pellois, J.P.4
  • 28
    • 84864535401 scopus 로고    scopus 로고
    • TAT-mediated photochemical internalization results in cell killing by causing the release of calcium into the cytosol of cells
    • Muthukrishnan, N., Johnson, G.A., Lim, J., Simanek, E.E. & Pellois, J.P. TAT-mediated photochemical internalization results in cell killing by causing the release of calcium into the cytosol of cells. Biochim. Biophys. Acta 1820, 1734-1743 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1734-1743
    • Muthukrishnan, N.1    Johnson, G.A.2    Lim, J.3    Simanek, E.E.4    Pellois, J.P.5
  • 29
    • 84859179165 scopus 로고    scopus 로고
    • Annexin A2 binds to endosomes following organelle destabilization by particulate wear debris
    • Scharf, B. et al. Annexin A2 binds to endosomes following organelle destabilization by particulate wear debris. Nat. Commun. 3, 755 (2012).
    • (2012) Nat. Commun. , vol.3 , pp. 755
    • Scharf, B.1
  • 30
    • 0036836978 scopus 로고    scopus 로고
    • Novel branching membrane translocational peptide as gene delivery vector
    • Tung, C.-H., Mueller, S. & Weissleder, R. Novel branching membrane translocational peptide as gene delivery vector. Bioorg. Med. Chem. 10, 3609-3614 (2002).
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3609-3614
    • Tung, C.-H.1    Mueller, S.2    Weissleder, R.3
  • 31
    • 11144229887 scopus 로고    scopus 로고
    • Tumor imaging by means of proteolytic activation of cell-penetrating peptides
    • Jiang, T. et al. Tumor imaging by means of proteolytic activation of cell-penetrating peptides. Proc. Natl. Acad. Sci. USA 101, 17867-17872 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17867-17872
    • Jiang, T.1
  • 32
    • 0037007121 scopus 로고    scopus 로고
    • Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: A tool for effcient genetic engineering of mammalian genomes
    • Peitz, M., Pfannkuche, K., Rajewsky, K. & Edenhofer, F. Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: a tool for effcient genetic engineering of mammalian genomes. Proc. Natl. Acad. Sci. USA 99, 4489-4494 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4489-4494
    • Peitz, M.1    Pfannkuche, K.2    Rajewsky, K.3    Edenhofer, F.4
  • 33
    • 24944434055 scopus 로고    scopus 로고
    • A ligation and photorelease strategy for the temporal and spatial control of protein function in living cells
    • Pellois, J.-P. & Muir, T.W. A ligation and photorelease strategy for the temporal and spatial control of protein function in living cells. Angew. Chem. Int. Ed. Engl. 44, 5713-5717 (2005).
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 5713-5717
    • Pellois, J.-P.1    Muir, T.W.2
  • 34
    • 0023852747 scopus 로고
    • Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line
    • Boukamp, P. et al. Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line. J. Cell Biol. 106, 761-771 (1988).
    • (1988) J. Cell Biol. , vol.106 , pp. 761-771
    • Boukamp, P.1
  • 35
    • 0018565733 scopus 로고
    • Comparison of four new cell lines from patients with adenocarcinoma of the ovary
    • Woods, L.K. et al. Comparison of four new cell lines from patients with adenocarcinoma of the ovary. Cancer Res. 39, 4449-4459 (1979).
    • (1979) Cancer Res. , vol.39 , pp. 4449-4459
    • Woods, L.K.1
  • 36
    • 0037484275 scopus 로고    scopus 로고
    • Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation
    • Jiang, N., Bénard, C.Y., Kébir, H., Shoubridge, E.A. & Hekimi, S. Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation. J. Biol. Chem. 278, 21678-21684 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 21678-21684
    • Jiang, N.1    Bénard, C.Y.2    Kébir, H.3    Shoubridge, E.A.4    Hekimi, S.5
  • 37
    • 0029791163 scopus 로고    scopus 로고
    • Lipoprotein and apolipoprotein secretion by a newborn piglet intestinal cell line (IPEC-1)
    • Gonzalez-Vallina, R. et al. Lipoprotein and apolipoprotein secretion by a newborn piglet intestinal cell line (IPEC-1). Am. J. Physiol. 271, 249-259 (1996).
    • (1996) Am. J. Physiol. , vol.271 , pp. 249-259
    • Gonzalez-Vallina, R.1
  • 38
    • 77955359913 scopus 로고    scopus 로고
    • Very bright green fuorescent proteins from the pontellid copepod Pontella mimocerami
    • Hunt, M.E., Scherrer, M.P., Ferrari, F.D. & Matz, M.V. Very bright green fuorescent proteins from the pontellid copepod Pontella mimocerami. PLoS ONE 5, e11517 (2010).
    • (2010) PLoS ONE , vol.5
    • Hunt, M.E.1    Scherrer, M.P.2    Ferrari, F.D.3    Matz, M.V.4
  • 39
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D. & Flügge, U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143 (1984).
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.