B. N. Giepmans, S. R. Adams, M. H. Ellisman, and R. Tsien, The Fluorescent Toolbox for Assessing Protein Location and Function, Science, vol.312, issue.5771, pp.217-224, 2006.
DOI : 10.1126/science.1124618

R. Yuste, Fluorescence microscopy today, Nature Methods, vol.8, issue.12, pp.902-904, 2005.
DOI : 10.1038/nmeth1205-902

T. A. Klar and S. W. Hell, Subdiffraction resolution in far-field fluorescence microscopy, Optics Letters, vol.24, issue.14, pp.954-956, 1999.
DOI : 10.1364/OL.24.000954

S. W. Hell, Far-Field Optical Nanoscopy, Science, vol.316, issue.5828, pp.1153-1158, 2007.
DOI : 10.1126/science.1137395

P. W. Winter and H. Shroff, Faster fluorescence microscopy: advances in high speed biological imaging, Current Opinion in Chemical Biology, vol.20, pp.46-53, 2014.
DOI : 10.1016/j.cbpa.2014.04.008

C. Bechara and S. Sagan, Cell-penetrating peptides: 20 years later, where do we stand?, FEBS Letters, vol.162, issue.12, pp.1693-1702, 2013.
DOI : 10.1016/j.febslet.2013.04.031

C. M. Brown, Fluorescence microscopy - avoiding the pitfalls, Journal of Cell Science, vol.120, issue.10, pp.1703-1705, 2007.
DOI : 10.1242/jcs.03433

L. Theodore, Intraneuronal delivery of protein kinase C pseudosubstrate leads to growth cone collapse, J. Neurosci, vol.15, pp.7158-7167, 1995.

S. R. Schwarze, A. Ho, A. Vocero-akbani, and S. F. Dowdy, In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse, Science, vol.285, issue.5433, pp.1569-1572, 1999.
DOI : 10.1126/science.285.5433.1569

S. Futaki, Stearylated Arginine-Rich Peptides:?? A New Class of Transfection Systems, Bioconjugate Chemistry, vol.12, issue.6, pp.1005-1011, 2001.
DOI : 10.1021/bc015508l

F. Burlina, S. Sagan, G. Bolbach, and G. Chassaing, Quantification of the Cellular Uptake of Cell-Penetrating Peptides by MALDI-TOF Mass Spectrometry, Angewandte Chemie, vol.279, issue.27, pp.4316-4319, 2005.
DOI : 10.1002/ange.200500477

C. Jiao, Translocation and Endocytosis for Cell-penetrating Peptide Internalization, Journal of Biological Chemistry, vol.284, issue.49, pp.33957-33965, 2009.
DOI : 10.1074/jbc.M109.056309
URL : https://hal.archives-ouvertes.fr/hal-00627026

D. Pisa, M. Chassaing, G. Swiecicki, and J. , Translocation Mechanism(s) of Cell-Penetrating Peptides: Biophysical Studies Using Artificial Membrane Bilayers, Biochemistry, vol.54, issue.2, pp.194-207, 2015.
DOI : 10.1021/bi501392n
URL : https://hal.archives-ouvertes.fr/hal-01093113

N. Nischan, Covalent Attachment of Cyclic TAT Peptides to GFP Results in Protein Delivery into Live Cells with Immediate Bioavailability, Angewandte Chemie International Edition, vol.189, issue.6, pp.1950-1953, 2015.
DOI : 10.1002/anie.201410006

J. R. Marks, J. Placone, K. Hristova, and W. Wimley, Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening, Journal of the American Chemical Society, vol.133, issue.23, pp.8995-9004, 2011.
DOI : 10.1021/ja2017416

J. Jo, S. Hong, W. Y. Choi, and D. R. Lee, Cell-penetrating peptide (CPP)-conjugated proteins is an efficient tool for manipulation of human mesenchymal stromal cells, Scientific Reports, vol.25, p.4378, 2014.
DOI : 10.1038/srep04378

C. M. Yamazaki, Collagen-like Cell-Penetrating Peptides, Angewandte Chemie International Edition, vol.22, issue.21, pp.5497-5500, 2013.
DOI : 10.1002/anie.201301266

J. P. Richard, Cell-penetrating Peptides. A REEVALUATION OF THE MECHANISM OF CELLULAR UPTAKE, Journal of Biological Chemistry, vol.278, issue.1, pp.585-590, 2003.
DOI : 10.1074/jbc.M209548200

S. Aubry, Cell-surface thiols affect cell entry of disulfide-conjugated peptides, The FASEB Journal, vol.23, issue.9, pp.2956-2967, 2009.
DOI : 10.1096/fj.08-127563
URL : https://hal.archives-ouvertes.fr/hal-00627354

I. M. Kaplan, J. S. Wadia, and S. F. Dowdy, Cationic TAT peptide transduction domain enters cells by macropinocytosis, Journal of Controlled Release, vol.102, issue.1, pp.247-253, 2005.
DOI : 10.1016/j.jconrel.2004.10.018

C. Bechara, Tryptophan within basic peptide sequences triggers glycosaminoglycan-dependent endocytosis, The FASEB Journal, vol.27, issue.2, pp.738-749, 2013.
DOI : 10.1096/fj.12-216176
URL : https://hal.archives-ouvertes.fr/hal-00744509

F. Duchardt, M. Fotin-mleczek, H. Schwarz, R. Fischer, and R. Brock, A Comprehensive Model for the Cellular Uptake of Cationic Cell-penetrating Peptides, Traffic, vol.14, issue.Suppl, pp.848-866, 2007.
DOI : 10.1111/j.1600-0854.2007.00572.x

C. A. Puckett and J. K. Barton, Fluorescein Redirects a Ruthenium???Octaarginine Conjugate to the Nucleus, Journal of the American Chemical Society, vol.131, issue.25, pp.8738-8739, 2009.
DOI : 10.1021/ja9025165

D. J. Mitchell, L. Steinman, D. T. Kim, C. G. Fathman, and J. B. Rothbard, Polyarginine enters cells more efficiently than other polycationic homopolymers, Journal of Peptide Research, vol.55, issue.5, pp.318-325, 2000.
DOI : 10.1139/bcb-76-2-3-235

R. I. Macdonald, Characteristics of self-quenching of the fluorescence of lipid-conjugated rhodamine in membranes, J. Biol. Chem, vol.265, pp.13533-13539, 1990.

M. M. Ribeiro, H. G. Franquelim, M. A. Castanho, and A. S. Veiga, Molecular interaction studies of peptides using steady-state fluorescence intensity. Static (de)quenching revisited, Journal of Peptide Science, vol.2, issue.4, pp.401-406, 2008.
DOI : 10.1002/psc.939

S. T. Henriques and M. A. Castanho, Environmental factors that enhance the action of the cell penetrating peptide pep-1, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1669, issue.2, pp.75-86, 2005.
DOI : 10.1016/j.bbamem.2004.11.017

L. W. Runnels and S. F. Scarlata, Theory and application of fluorescence homotransfer to melittin oligomerization, Biophysical Journal, vol.69, issue.4, pp.1569-1583, 1995.
DOI : 10.1016/S0006-3495(95)80030-5

T. A. Aguilera, E. S. Olson, M. M. Timmers, T. Jiang, and R. Y. Tsien, Systemic in vivo distribution of activatable cell penetrating peptides is superior to that of cell penetrating peptides, Integrative Biology, vol.126, issue.5-6, p.371, 2009.
DOI : 10.1039/b904890a

J. Lakowicz, Principles of fluorescence spectroscopy, 2006.
DOI : 10.1007/978-0-387-46312-4

J. E. Berlier, Quantitative Comparison of Long-wavelength Alexa Fluor Dyes to Cy Dyes: Fluorescence of the Dyes and Their Bioconjugates, Journal of Histochemistry & Cytochemistry, vol.51, issue.12, pp.1699-1712, 2003.
DOI : 10.1177/002215540305101214

N. G. Zhegalova, S. He, H. Zhou, D. M. Kim, and M. Y. Berezin, Minimization of self-quenching fluorescence on dyes conjugated to biomolecules with multiple labeling sites via asymmetrically charged NIR fluorophores, Contrast Media & Molecular Imaging, vol.84, issue.3, pp.355-362, 2014.
DOI : 10.1002/cmmi.1585

Y. Hong, J. W. Lam, and B. Tang, Aggregation-induced emission, Chemical Society Reviews, vol.9, issue.11, p.5361, 2011.
DOI : 10.1002/adfm.201002572

R. F. Chen and J. Knutson, Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes: Energy transfer to nonfluorescent dimers, Analytical Biochemistry, vol.172, issue.1, pp.61-77, 1988.
DOI : 10.1016/0003-2697(88)90412-5

T. Takeuchi, Direct and Rapid Cytosolic Delivery Using Cell-Penetrating Peptides Mediated by Pyrenebutyrate, ACS Chemical Biology, vol.1, issue.5, pp.299-303, 2006.
DOI : 10.1021/cb600127m

M. Kosuge, T. Takeuchi, I. Nakase, A. T. Jones, and S. Futaki, Cellular Internalization and Distribution of Arginine-Rich Peptides as a Function of Extracellular Peptide Concentration, Serum, and Plasma Membrane Associated Proteoglycans, Bioconjugate Chemistry, vol.19, issue.3, pp.656-664, 2008.
DOI : 10.1021/bc700289w

M. Rousset, Enterocytic differentiation and glucose utilization in the human colon tumor cell line Caco-2: Modulation by forskolin, Journal of Cellular Physiology, vol.32, issue.3, pp.377-385, 1985.
DOI : 10.1002/jcp.1041230313
URL : https://hal.archives-ouvertes.fr/hal-00814012

R. Jean and S. , Molecular Vehicles for Mitochondrial Chemical Biology and Drug Delivery, ACS Chemical Biology, vol.9, issue.2, pp.323-333, 2014.
DOI : 10.1021/cb400821p

M. F. Ross, A. Filipovska, R. A. Smith, M. J. Gait, and M. P. Murphy, Cell-penetrating peptides do not cross mitochondrial membranes even when conjugated to a lipophilic cation: evidence against direct passage through phospholipid bilayers, Biochemical Journal, vol.383, issue.3, pp.20237-20247, 2004.
DOI : 10.1042/BJ20041095

N. M. Zaki and N. Tirelli, Gateways for the intracellular access of nanocarriers: a review of receptor-mediated endocytosis mechanisms and of strategies in receptor targeting, Expert Opinion on Drug Delivery, vol.47, issue.4, pp.895-913, 2010.
DOI : 10.1083/jcb.92.2.425

S. R. Mujumdar, R. B. Mujumdar, C. M. Grant, and A. S. Waggoner, Cyanine-Labeling Reagents:?? Sulfobenzindocyanine Succinimidyl Esters, Bioconjugate Chemistry, vol.7, issue.3, pp.356-362, 1996.
DOI : 10.1021/bc960021b