A. Deshpande, A.J. Bryer, J.R. Andino-Moncada, J. Shi, J. Hong, C. Torres, S. Harel, A.C. Francis, J.R. Perilla, C. Aiken and I. Rousso. Elasticity of the HIV-1 core facilitates nuclear entry and infection. PLos Pathog. 20(9), e1012537, (2024). Full text>>
S. Harel, Y. Altaras, D. Nachmias, N. Rotem-Dai, I. Dvilansky, N. Elia and I. Rousso. Analysis of individual HIV-1 budding event using fast AFM reveals a multiplexed role for VPS4. Biophys. J. 121, 4229-4238, (2022). Full text>>
I. Rousso and A. Deshpande. Application of Atomic Force Microscopy in HIV-1 Research. Viruses, 14, 648 (2022). Full text>>.
C. Aiken and I. Rousso. The HIV-1 Capsid and Reverse Transcription. Retrovirology, 18, 29 (2021). Full text>>.
E. Bergman, R. Goldbart, T. Traitel, E. Amar-Lewis, J. Zorea, K. Yagodayev, I. Allon, S. Rankovic, Y. Krieger, I. Rousso, M. Elkabets and J. Kost. Cell stiffness predicts cancer cell sensitivity to ultrasound as a selective superficial cancer therapy. Bioengineering & Translational Medicine, e10226, (2021). Full text>>
S. Rankovic, A. Deshpande, S. Harel, C. Aiken and I. Rousso. HIV-1 uncoating occurs via a series of rapid biomechanical changes in the core related to individual stages of reverse transcription. J. Virology, 95, e00166-21, (2021). Full text>>
C. Xu, D.K. Fischer, S. Rankovic, W. Li, RA Dick, B. Runge, R. Zadorozhnyi, J. Ahn, C. Aiken, T. Polenova, A.N. Engelman, Z. Ambrose, I. Rousso and J.R. Perilla. Permeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis. PLoS Biol. 18: e3001015, (2020). Full Text>>
S. Rankovic, R. Ramalho, C. Aiken, and I. Rousso. PF74 reinforces the HIV-1 capsid to impair reverse transcription-induced uncoating. J. Virology 92, e00845-18, (2018). Full Text>>
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S. Rankovic, J. Varadarajan, R. Ramalho, C. Aiken, and I. Rousso. Reverse transcription mechanically initiates HIV-1 capsid disassembly. J. Virology, e00289-17, (2017). Full Text>>
R. Ramalho, S. Rankovic, J. Zhou, C. Aiken and I. Rousso. Analysis of the mechanical properties of wild type and hyperstable mutants of the HIV-1 capsid. Retrovirology, 13, 17 (2016). Full Text>>
C. Liu, J.R. Perilla, J. Ning, M. Lu, G. Hou, R. Ramalho, B.A. Himes, G. Zhao, G.J. Bedwell, I. Byeon, J. Ahn, A.M. Gronenborn, P.E. Prevelige, I. Rousso, C. Aiken, T. Polenova, K. Schulten, and P. Zhang. 2016. Cyclophilin A Stabilizes the HIV-1 Capsid through a Novel Non-canonical Binding Site. Nature Comm. 7, 10714, (2016). Full Text>>
L. Karp-Boss, R. Gueta and I. Rousso. Judging diatoms by their cover: variability in local elasticity of Lithodesmium undulatum undergoing cell division. Plos One, 9, e109089, (2014). Full Text>>
H. Pang, L. Hevroni, N. Kol, D.M. Eckert, M. Tsvitov, M.S. Kay and I. Rousso. Virion stiffness regulates immature HIV-1 entry. Retrovirology, 10, 4, (2013). Full Text>>
R. Gueta, J. Levitt, A. Xia, O. Katz, J.S. Oghalai, and I. Rousso. Structural and Mechanical Analysis of Tectorial Membrane Tecta Mutants. Biophys. J. 100, 2530 – 2538, (2011). Full Text>>
L. Adler-Abramovich, N. Kol, I. Yanai, D. Barlam, R.Z. Shneck, E. Gazit and I. Rousso. SelfAssembled Organic Nanostructures with Metallic-like Tensile Strength. Angewandte Chemie Int Ed, 49, 9788, (2010). Full Text>>
N. Kol, M. Tsvitov, L. Hevroni, S.G. Wolf, H. Pang, M.S. Kay, and I. Rousso. The effects of purification method on the completeness of the immature HIV-1 gag shell. J. Virol. Methods, 169, 244-247, (2010). Full Text>>
M. Gladnikoff, E. Shimoni, N. Gov and I. Rousso. Retrovirus assembly and budding occur through an actin-driven mechanism. Biophys. J. 97, 2419-2428, (2009). Full Text>>
R. Gueta, D. Barlam, R.Z. Shneck and I. Rousso. Sound-evoked deflections of aural stereocilia arise from tectorial membrane anisotropy. Biophys. J. 94, 4570-4576, (2008). Full Text>>
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M. Gladnikoff and I. Rousso. Directly monitoring individual retrovirus budding events using atomic force microscopy. Biophys. J. 94, 320-326, (2008). Full Text>>
R. Gueta, E. Tal, Y. Silberberg, and I. Rousso. The 3D structure of the tectorial membrane determined by second-harmonic imaging microscopy. J. Struct. Biol. 159, 103-110, (2007). Full Text>>
N. Kol, Y. Shi, M. Tsvitov, D. Barlam, R.Z. Shneck, M.S. Kay, and I. Rousso. A stiffness switch in human immunodeficiency virus. Biophys. J. 92, 1777-1783, (2007). Full Text>>
R. Gueta, D. Barlam, R.Z. Shneck, and I. Rousso. Measurement of the mechanical properties of isolated tectorial membrane using atomic force microscopy. Proc. Natl. Acad. Sci. USA. 103, 14790-14795, (2006). Full Text>>
N. Kol, M. Gladnikoff, D. Barlam, R.Z. Shneck, A. Rein and I. Rousso. Mechanical properties of murine leukemia virus particles: Effect of maturation. Biophys. J. 91, 767-774, (2006). Full Text>>
N. Kol, L. Adler-Abramovich, D. Barlam, R.Z. Shneck, E. Gazit and I. Rousso. Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures. Nano Lett. 5, 1343-1346, (2005). Full Text>>
M. Anwar and I. Rousso. Atomic force microscopy with time resolution of microseconds. Appl. Phys. Lett. 86, 014101, (2005). Full Text>>
H. Taha, R.S. Marks, L.A. Gheber, I. Rousso, J. Newman, C. Sukenik and A. Lewis. Protein printing with an atomic force sensing NanoFountainPen. Appl. Phys. Lett. 83, 1041-1043, (2003). Full Text>>
B.K. Chen, I. Rousso, S. Shim, P.S. Kim. Efficient assembly of an HIV/MLV Gag-chimeric virus in murine cells. Proc. Natl. Acad. Sci. USA, 98, 15239-15244, (2001). Full Text>>
A. Aharoni, B. Hou, N. Friedman, M. Ottolenghi, I. Rousso, S. Ruhman, M. Sheves, T. Ye and Q. Zhong. Non-Isomerizable Artificial pigments: Implications to the Primary LightInduced Events in Bacteriorhodopsin. Biochemistry-Moscow, 60, 1210-1219, (2001). Full Text>>
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I. Rousso, M.B. Mixon, B.K. Chen and P.S. Kim. Palmitoylation of the HIV envelope glycoprotein is critical for viral infectivity. Proc. Natl. Acad. Sci. USA, 97, 13523-13525, (2000). Full Text>>
P. Kolodner, E.P. Lukashev, Y.C. Ching, I. Rousso and M. Sheves. Electric-field effects in 13-demethyl-11,14-epoxyretinal-bacteriorhodopsin films, Photochem. Photobiol., 70, 103-110, (1999).
C. Rodig, H. Georg, F. Siebert, I. Rousso and M. Sheves. Temperature effects of excitation laser pulses during step-scan FT-IR measurements, Laser Chem., 19, 169-172, (1999).
I. Rousso, Y. Gat, A. Lewis, M. Sheves and M. Ottolenghi. Effective light-induced hydroxylamine reactions occur with C13=C14 non-isomerizable Bacteriorhodopsin pigments, Biophys. J., 75, 413-417, (1998).
N. Friedman, I. Rousso, M. Sheves, X. Fu, S. Bressler and M. Ottolenghi. Time resolved titration of Asp-85 in bacteriorhodopsin: The multi-component kinetic mechanism. Biochemistry, 36, 11369-11380, (1997).
I. Rousso, E. Khachatryan, I. Brodsky, R. Nachustai, M. Ottolenghi, M. Sheves and A. Lewis. Atomic force sensing of light-induced protein dynamics with microsecond time resolution in Bacteriorhodopsin and Photosynthetic Reaction Centers. J. Struct. Biol., 119, 158-164, (1997).
I. Rousso, N. Friedman, A. Lewis and M. Sheves. Evidence for a controlling role of water in producing the native bacteriorhodopsin structure. Biophys. J., 73, 2081-2089, (1997).
I. Rousso, E. Khachatryan, Y. Gat, I. Brodsky, A. Lewis, M. Ottolenghi and M.Sheves. Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA, 94, 7937-7941, (1997).
I. Rousso, M. Sheves and A. Lewis. Protein structure alterations induced by light activated water absorption. A study with Bacteriorhodopsin. J. Am. Chem. Soc. Comm., 118, 11299-11300, (1996).
A. Lewis, I. Rousso, E. Khachatryan, I. Brodsky, K. Liebermann and M. Sheves. Directly Probing Rapid Membrane Protein Dynamics with an Atomic Force Microscope: A Study of Light-Induced Alterations in Bacteriorhodopsin. Biophys. J., 70, 2380-2384, (1996).
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S. Druckmann, M. Ottolenghi, I. Rousso, N. Friedman and M. Sheves. Time resolved titrations of the schiff base and of the Asp85 residue in artificial Bacteriorhodopsins. Biochemistry, 34, 12066-12074, (1995).
I. Rousso, N. Friedman, M. Sheves and M. Ottolenghi. The pKa of the protonated schiffBase and Aspartic 85 in the Bacteriorhodopsin binding site is controlled by a specific geometry between the two residues. Biochemistry, 34, 12059-12065, (1995).
I. Rousso, I. Brodsky, A. Lewis and M. Sheves. The role of water in retinal binding to Bacterio-opsin. J. Biol. Chem., 270, 13860-13868, (1995).
M. Portnoy, Y. Ben-David, I. Rousso and D. Milstein. Reactions of electron-rich arylpalladium complexes with olefins. Origin of the chelate effect in vinylation catalysis. Organometallics, 13, 3465-4379, (1994).