S. Manley, High-density mapping of single-molecule trajectories with photoactivated localization microscopy, Nat. methods, vol.5, pp.155-157, 2008.

E. Betzig, Imaging intracellular fluorescent proteins at nanometer resolution, vol.313, pp.1642-1645, 2006.

, Scientific REPORtS |, vol.8, 2018.

J. Sibarita, High-density single-particle tracking: quantifying molecule organization and dynamics at the nanoscale, Histochem. Cell Biol, vol.141, pp.587-595, 2014.

E. O. Freed, HIV-1 assembly, release and maturation, Nat. reviews. Microbiol, vol.13, pp.484-496, 2015.

D. Gheysen, Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells, Cell, vol.59, pp.103-112, 1989.

M. D. Resh, Intracellular trafficking of HIV-1 Gag: how Gag interacts with cell membranes and makes viral particles, AIDS reviews, vol.7, pp.84-91, 2005.

V. Chukkapalli and A. Ono, Molecular determinants that regulate plasma membrane association of HIV-1 Gag, J. Mol. Biol, vol.410, pp.512-524, 2011.

C. Mariani, M. Desdouits, C. Favard, P. Benaroch, and D. M. Muriaux, Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages, Front. Microbiol, vol.5, 2014.

S. A. Datta, Conformation of the HIV-1 Gag protein in solution, J Mol Biol, vol.365, pp.812-824, 2007.

N. Yandrapalli, Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P2/Cholesterol nanoclusters, Sci. Reports, vol.6, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02139122

H. S. Tanwar, The thermodynamics of Pr55gag-RNA interaction regulate the assembly of HIV, PLoS pathogens, vol.13, pp.1006221-1006221, 2017.

A. Rein, S. A. Datta, C. P. Jones, and K. Musier-forsyth, Diverse interactions of retroviral Gag proteins with RNAs, Trends Biochem. Sci, vol.36, pp.373-380, 2011.

D. Muriaux and J. Darlix, Properties and functions of the nucleocapsid protein in virus assembly, RNA biology, vol.7, pp.744-753, 2010.

H. De-rocquigny, Role of the nucleocapsid region in HIV-1 Gag assembly as investigated by quantitative fluorescence-based microscopy, Virus Res, vol.193, pp.78-88, 2014.
URL : https://hal.archives-ouvertes.fr/inserm-02154966

U. K. Von-schwedler, The protein network of HIV budding, Cell, vol.114, pp.701-713, 2003.

J. Prescher, Super-resolution imaging of escrt-proteins at hiv-1 assembly sites, PLoS pathogens, vol.11, 2015.
DOI : 10.1371/journal.ppat.1004677
URL : https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1004677&type=printable

S. A. Datta, On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch?, J. Virol, vol.85, pp.4111-4121, 2011.

N. Jouvenet, P. D. Bieniasz, and S. M. Simon, Imaging the biogenesis of individual HIV-1 virions in live cells, Nat, vol.454, pp.236-240, 2008.

S. Ivanchenko, Dynamics of HIV-1 assembly and release, PLoS pathogens, vol.5, pp.1000652-1000652, 2009.
DOI : 10.1371/journal.ppat.1000652
URL : https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000652&type=printable

N. Jouvenet, S. M. Simon, and P. D. Bieniasz, Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles, Proc. Natl. Acad. Sci. United States Am, vol.106, 2009.

J. T. Becker and N. M. Sherer, Subcellular Localization of HIV-1 gag-pol mRNAs Regulates Sites of Virion Assembly, J. virology, vol.91, 2017.

L. Sardo, Dynamics of HIV-1 RNA Near the Plasma Membrane during Virus Assembly, J. Virol, vol.89, pp.10832-10840, 2015.

K. A. Dilley, Interactions Between HIV-1 Gag and Viral RNA Genome Enhance Virion Assembly, J. virology, 2017.
DOI : 10.1128/jvi.02319-16
URL : http://europepmc.org/articles/pmc5533913?pdf=render

M. El-beheiry, M. Dahan, and J. Masson, InferenceMAP: mapping of single-molecule dynamics with Bayesian inference, Nat. methods, vol.12, pp.594-595, 2015.

M. El-beheiry, A Primer on the Bayesian Approach to High-Density Single-Molecule Trajectories Analysis, Biophys. journal, vol.110, pp.1209-1215, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01421582

J. Chojnacki and B. M¨uller, Investigation of HIV-1 assembly and release using modern fluorescence imaging techniques, Traffic, vol.14, pp.15-24, 2013.
DOI : 10.1111/tra.12006
URL : https://onlinelibrary.wiley.com/doi/pdf/10.1111/tra.12006

A. K. Chen, MicroRNA binding to the HIV-1 Gag protein inhibits Gag assembly and virus production, Proc. Natl. Acad. Sci. United States Am, vol.111, pp.2676-2683, 2014.
DOI : 10.1073/pnas.1408037111
URL : http://www.pnas.org/content/111/26/E2676.full.pdf

A. Thomas, Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells, J. virology, vol.89, pp.8162-8181, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01911482

A. Ono, D. Demirov, and E. O. Freed, Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding, J. Virol, vol.74, pp.5142-5150, 2000.
DOI : 10.1128/jvi.74.11.5142-5150.2000
URL : https://jvi.asm.org/content/74/11/5142.full.pdf

J. Gunzenhäuser, N. Olivier, T. Pengo, and S. Manley, Quantitative super-resolution imaging reveals protein stoichiometry and nanoscale morphology of assembling HIV-Gag virions, Nano Lett, vol.12, pp.4705-4710, 2012.

D. Orsogna, M. R. Zhao, B. Berenji, B. Chou, and T. , Combinatoric analysis of heterogeneous stochastic self-assembly, The J. Chem. Phys, vol.139, 2013.

R. Hu, Seed-Induced Heterogeneous Cross-Seeding Self-Assembly of Human and Rat Islet Polypeptides, ACS Omega, vol.2, pp.784-792, 2017.

B. R. Novak, E. J. Maginn, and M. J. Mccready, Comparison of heterogeneous and homogeneous bubble nucleation using molecular simulations, Phys. Rev. B, vol.75, 2007.

P. Ku, Identification of pauses during formation of HIV-1 virus like particles, Biophys. J, vol.105, pp.2262-2272, 2013.

B. A. Robinson, J. C. Reed, C. D. Geary, J. V. Swain, and J. R. Lingappa, A temporospatial map that defines specific steps at which critical surfaces in the gag ma and ca domains act during immature hiv-1 capsid assembly in cells, J. virology, vol.88, pp.5718-5741, 2014.

F. K. Schur, An atomic model of hiv-1 capsid-sp1 reveals structures regulating assembly and maturation, vol.353, pp.506-508, 2016.

S. A. Datta, Dimerization of the sp1 region of hiv-1 gag induces a helical conformation and association into helical bundles: Implications for particle assembly, J. virology, vol.90, pp.1773-1787, 2016.

M. J. Bayro, B. K. Ganser-pornillos, K. K. Zadrozny, M. Yeager, and R. Tycko, Helical conformation in the ca-sp1 junction of the immature hiv-1 lattice determined from solid-state nmr of virus-like particles, J. Am. Chem. Soc, vol.138, pp.12029-12032, 2016.

N. Jouvenet, S. M. Simon, and P. D. Bieniasz, Visualizing HIV-1 assembly, J. molecular biology, vol.410, pp.501-511, 2011.
DOI : 10.1016/j.jmb.2011.04.062
URL : http://europepmc.org/articles/pmc3144478?pdf=render

J. Masson, Mapping the energy and diffusion landscapes of membrane proteins at the cell surface using high-density singlemolecule imaging and Bayesian inference: application to the multiscale dynamics of glycine receptors in the neuronal membrane, Biophys. journal, vol.106, pp.74-83, 2014.

A. J. Pak, Immature HIV-1 lattice assembly dynamics are regulated by scaffolding from nucleic acid and the plasma membrane, Proc. Natl. Acad. Sci. United States Am, vol.114, pp.10056-10065, 2017.

W. Pezeshkian, Mechanism of shiga toxin clustering on membranes, ACS nano, vol.11, pp.314-324, 2017.

, Scientific REPORtS |, vol.8, 2018.

A. R. Evans, M. S. Turner, and P. Sens, Interactions between proteins bound to biomembranes, Phys. Rev. E, Stat. Nonlinear, Soft Matter Phys, vol.67, p.41907, 2003.
DOI : 10.1103/physreve.67.041907
URL : http://arxiv.org/pdf/cond-mat/0301144

P. Sens and M. S. Turner, Theoretical model for the formation of caveolae and similar membrane invaginations, Biophys. J, vol.86, pp.74266-74272, 2004.

D. Muriaux, J. Mirro, D. Harvin, and A. Rein, RNA is a structural element in retrovirus particles, Proc. Natl. Acad. Sci. United States Am, vol.98, pp.5246-5251, 2001.

C. Faivre-moskalenko, RNA Control of HIV-1 Particle Size Polydispersity, PLoS ONE, vol.9, 2014.
URL : https://hal.archives-ouvertes.fr/ensl-00947571

S. B. Kutluay and P. D. Bieniasz, Analysis of the initiating events in HIV-1 particle assembly and genome packaging, PLoS pathogens, vol.6, 2010.

J. Hendrix, Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers, The J. cell biology, vol.210, pp.629-646, 2015.

B. Grigorov, F. Arcanger, P. Roingeard, J. Darlix, and D. Muriaux, Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines, J. Mol. Biol, vol.359, pp.848-862, 2006.

I. Izeddin, Super-resolution dynamic imaging of dendritic spines using a low-affinity photoconvertible actin probe, PloS One, vol.6, 2011.
URL : https://hal.archives-ouvertes.fr/pasteur-02081263

A. Kechkar, D. Nair, M. Heilemann, D. Choquet, and J. Sibarita, Real-time analysis and visualization for single-molecule based super-resolution microscopy, PloS One, vol.8, 2013.

A. Sergé, N. Bertaux, H. Rigneault, and D. Marguet, Dynamic multiple-target tracing to probe spatiotemporal cartography of cell membranes, Nat. Methods, vol.5, pp.687-694, 2008.

H. L. Harney, Form Invariance II: Natural x, Bayesian Inference, pp.95-108, 2003.

F. Persson, M. Lindén, C. Unoson, and J. Elf, Extracting intracellular diffusive states and transition rates from single-molecule tracking data, Nat. Methods, vol.10, pp.265-269, 2013.

J. Van-de-meent, J. E. Bronson, C. H. Wiggins, and R. L. Gonzalez, Empirical Bayes methods enable advanced population-level analyses of single-molecule FRET experiments, Biophys. J, vol.106, pp.1327-1337, 2014.

J. C. Chang, P. Fok, and T. Chou, Bayesian Uncertainty Quantification for Bond Energies and Mobilities Using Path Integral Analysis, Biophys. J, vol.109, pp.966-974, 2015.