Lab Members Web

Publications

[1] S.S. Shah, C.N. Cultrara, J.A. Ramos, U. Samuni, J. Zilberberg, D. Sabatino, Bifunctional Au-templated RNA nanoparticles enable direct cell uptake detection and GRP75 knockdown in prostate cancer, J. Mater. Chem. B. 8 (2020) 2169–2176. https://doi.org/10.1039/c9tb02438g [HTML]

[2] C.N. Cultrara, S. Shah, G. Antuono, C.J. Heller, J.A. Ramos, U. Samuni, J. Zilberberg, D. Sabatino, Size Matters: Arginine-Derived Peptides Targeting the PSMA Receptor Can Efficiently Complex but Not Transfect siRNA, Mol. Ther. Acids. 18 (2019) 863–870. https://doi.org/10.1016/j.omtn.2019.10.013 [HTML]

[3] R. Pan, K. Hu, D. Jiang, U. Samuni, M. V Mirkin, Electrochemical Resistive-Pulse Sensing, J. Am. Chem. Soc. 141 (2019) 19555–19559. https://doi.org/10.1021/jacs.9b10329 [HTML]

[4] U. Samuni, E. Maimon, S. Goldstein, A kinetic study of the oxidation of hydroxamic acids by compounds I and II of horseradish peroxidase: Effect of transition metal ions, J. Coord. Chem. 71 (2018) 1728–1737. https://doi.org/10.1080/00958972.2018.1493200 [HTML]

[5] E. Maimon, U. Samuni, S. Goldstein, Studying mechanism of radical reactions: From radiation to nitroxides as research tools, Radiat. Phys. Chem. 143 (2018) 14–19. https://doi.org/10.1016/j.radphyschem.2017.07.012 [HTML]

[6] S.S. Shah, C.N. Cultrara, S.D. Kozuch, M.R. Patel, J.A. Ramos, U. Samuni, J. Zilberberg, D. Sabatino, Direct Transfection of Fatty Acid Conjugated siRNAs and Knockdown of the Glucose-Regulated Chaperones in Prostate Cancer Cells, Bioconjug. Chem. 29 (2018) 3638–3648. https://doi.org/10.1021/acs.bioconjchem.8b00580 [HTML]

[7] M.R. Patel, S.D. Kozuch, C.N. Cultrara, R. Yadav, S. Huang, U. Samuni, J. Koren, G. Chiosis, D. Sabatino, RNAi Screening of the Glucose-Regulated Chaperones in Cancer with Self-Assembled siRNA Nanostructures, Nano Lett. 16 (2016) 6099–6108. https://doi.org/10.1021/acs.nanolett.6b02274 [HTML]

[8] N. Rana, S.Y. Huang, P. Patel, U. Samuni, D. Sabatino, Synthesis, characterization and anti-cancer activity of a peptide nucleolipid bioconjugate, Bioorg. Med. Chem. Lett. 26 (2016) 3567–3571. https://doi.org/10.1016/j.bmcl.2016.06.020 [HTML]

[9] U. Samuni, G. Czapski, S. Goldstein, Nitroxide radicals as research tools: Elucidating the kinetics and mechanisms of catalase-like and “suicide inactivation” of metmyoglobin, Biochim. Biophys. Acta-General Subj. 1860 (2016) 1409–1416. https://doi.org/10.1016/j.bbagen.2016.04.002 [HTML]

[10] R. Yadav, S. Goldstein, M.O. Nasef, W. Lee, U. Samuni, Synergistic activity of acetohydroxamic acid on prokaryotes under oxidative stress: The role of reactive nitrogen species, Free Radic. Biol. Med. 77 (2014) 291–297. https://doi.org/10.1016/j.freeradbiomed.2014.09.020 [HTML]

[11] R. Yadav, Y. Samuni, A. Abramson, R. Zeltser, N. Casap, T.K. Kabiraj, M.L. Banach, U. Samuni, Pro-oxidative synergic bactericidal effect of NO: kinetics and inhibition by nitroxides, Free Radic. Biol. Med. 67 (2014) 248–254. https://doi.org/10.1016/j.freeradbiomed.2013.10.012 [HTML]

[12] P. Patel, E. Hanawa, R. Yadav, U. Samuni, C. Marzabadi, D. Sabatino, Synthesis, DNA binding and anti-leukemic activity of an aminoacyl nucleolipid, Bioorg. Med. Chem. Lett. 23 (2013) 5086–5090. https://doi.org/10.1016/j.bmcl.2013.07.030 [HTML]

[13] Y. Samuni, U. Samuni, S. Goldstein, The use of cyclic nitroxide radicals as HNO scavengers, J. Inorg. Biochem. 118 (2013) 155–161. https://doi.org/10.1016/j.jinorgbio.2012.10.002 [HTML]

[14] Y. Samuni, U. Samuni, S. Goldstein, The mechanism underlying nitroxyl and nitric oxide formation from hydroxamic acids, Biochim. Biophys. Acta-General Subj. 1820 (2012) 1560–1566. https://doi.org/10.1016/j.bbagen.2012.05.006 [HTML]

[15] U. Samuni, Y. Samuni, S. Goldstein, On the Distinction between Nitroxyl and Nitric Oxide Using Nitronyl Nitroxides, J. Am. Chem. Soc. 132 (2010) 8428–8432. https://doi.org/10.1021/ja101945j [HTML]

[16] Y. Samuni, H. Ishii, F. Hyodo, U. Samuni, M.C. Krishna, S. Goldstein, J.B. Mitchell, Reactive oxygen species mediate hepatotoxicity induced by the Hsp90 inhibitor geldanamycin and its analogs, Free Radic. Biol. Med. 48 (2010) 1559–1563. https://doi.org/10.1016/j.freeradbiomed.2010.03.001 [HTML]

[17] D. Giordano, L. Boechi, A. Vergara, M.A. Marti, U. Samuni, D. Dantsker, L. Grassi, D.A. Estrin, J.M. Friedman, L. Mazzarella, G. Di Prisco, C. Verde, The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - oxygen-binding equilibria, kinetics and molecular dynamics, FEBS J. 276 (2009) 2266–2277. https://doi.org/10.1111/j.1742-4658.2009.06954.x [HTML]

[18]. U. Samuni, C.J. Roche, D. Dantsker, J.M. Friedman, T- and R-state Tertiary Relaxations in Sol-gel Encapsulated Haemoglobin. In: Dioxygen binding and sensing proteins. Protein Reviews 9 (2008) 161-182.

[19] U. Samuni, D. Dantsker, C.J. Roche, J.M. Friedman, Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins, Gene. 398 (2007) 234–248. https://doi.org/10.1016/j.gene.2007.04.032 [HTML]

[20] U. Samuni, C.J. Roche, D. Dantsker, J.M. Friedman, Conformational dependence of hemoglobin reactivity under high viscosity conditions: The role of solvent slaved dynamics, J. Am. Chem. Soc. 129 (2007) 12756–12764. https://doi.org/10.1021/ja072342b [HTML]

[21] C.J. Roche, D. Dantsker, U. Samuni, J.M. Friedman, Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin - Influence of quaternary and tertiary structure, J. Biol. Chem. 281 (2006) 36874–36882. https://doi.org/10.1074/jbc.M603914200 [HTML]

[22] U. Samuni, C.J. Roche, D. Dantsker, L.J. Juszczak, J.M. Friedman, Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation, Biochemistry. 45 (2006) 2820–2835. https://doi.org/10.1021/bi050010i [HTML]

[23] U. Samuni, J.M. Friedman, Proteins in motion: resonance Raman spectroscopy as a probe of functional intermediates, Methods in Molecular Biology 305 (2005) 287-300. 10.1385/1-59259-912-5:287 [HTML]

[24] D. Dantsker, C. Roche, U. Samuni, G. Blouin, J.S. Olson, J.M. Friedman, The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities, J. Biol. Chem. 280 (2005) 38740–38755. https://doi.org/10.1074/jbc.M506333200 [HTML]

[25] D. Dantsker, U. Samuni, J.M. Friedman, N. Agmon, A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model, Biochim. Biophys. Acta-Proteins Proteomics. 1749 (2005) 234–251. https://doi.org/10.1016/j.bbapap.2005.04.002 [HTML]

[26] L. Juszczak, U. Samuni, J.M. Friedman, Conformational and functional significance of the alpha 140 side-chain in HbA: a UV and visible resonance Raman study of three alpha 140 mutants, J. Raman Spectrosc. 36 (2005) 350–358. https://doi.org/10.1002/jrs.1322 [HTML]

[27] D. Dantsker, U. Samuni, Y. Ouellet, B.A. Wittenberg, J.B. Wittenberg, M. Milani, M. Bolognesi, M. Guertin, J.M. Friedman, Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis, J Biol Chem. 279 (2004) 38844–53. https://doi.org/10.1074/jbc.M401513200 [HTML]

[28] T.K. Das, U. Samuni, Y. Lin, D.E. Goldberg, D.L. Rousseau, J.M. Friedman, Distal heme pocket conformers of carbonmonoxy derivatives of Ascaris hemoglobin - Evidence of conformational trapping in porous sol-gel matrices, J. Biol. Chem. 279 (2004) 10433–10441. doi:10.1074/jbc.M309590200 [HTML]

[29] U. Samuni, D. Dantsker, L.J. Juszczak, S. Bettati, L. Ronda, A. Mozzarelli, J.M. Friedman, Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels, Biochemistry. 43 (2004) 13674–13682. https://doi.org/10.1021/bi048531d [HTML]

[30] U. Samuni, Y. Ouellet, M. Guertin, J.M. Friedman, S.R. Yeh, The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis, J. Am. Chem. Soc. 126 (2004) 2682–2683. DOI: 10.1021/ja038093i [HTML]

[31] A. Tsuneshige, K. Kanaori, U. Samuni, D. Danstker, J.M. Friedman, S. Neya, L. Giangiacomo, T. Yonetani, Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers, J. Biol. Chem. 279 (2004) 48959–48967. https://doi.org/10.1074/jbc.M405909200 [HTML]

[32] M.S. Navati, U. Samuni, P. Aisen, J.M. Friedman, Binding and release of iron by gel-encapsulated human transferrin: Evidence for a conformational search, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 3832–3837. https://doi.org/10.1073/pnas.262526399 [HTML]

[33] H. Ouellet, L. Juszczak, D. Dantsker, U. Samuni, Y.H. Ouellet, P.Y. Savard, J.B. Wittenberg, B.A. Wittenberg, J.M. Friedman, M. Guertin, Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network, Biochemistry. 42 (2003) 5764–5774. DOI: 10.1021/bi0270337 [HTML]

[34] U. Samuni, D. Dantsker, A. Ray, J.B. Wittenberg, B.A. Wittenberg, S. Dewilde, L. Moens, Y. Ouellet, M. Guertin, J.M. Friedman, Kinetic modulation in carbonmonoxy derivatives of truncated hemoglobins - The role of distal heme pocket residues and extended apolar tunnel, J. Biol. Chem. 278 (2003) 27241–27250. doi:10.1074/jbc.M212634200 [HTML]

[35] U. Samuni, L. Juszczak, D. Dantsker, I. Khan, A.J. Friedman, J. Perez-Gonzalez-De-Apodaca, S. Bruno, H.L. Hui, J.E. Colby, E. Karasik, L.D. Kwiatkowski, A. Mozzarelli, R. Noble, J.M. Friedman, Functional and spectroscopic characterization of half-liganded iron-zinc hybrid hemoglobin: Evidence for conformational plasticity within the T state, Biochemistry. 42 (2003) 8272–8288. DOI: 10.1021/bi020648j [HTML]

[36] D. Dantsker, U. Samuni, A.J. Friedman, M. Yang, A. Ray, J.M. Friedman, Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories, J. Mol. Biol. 315 (2002) 239–251.

[37] U. Samuni, D. Dantsker, I. Khan, A.J. Friedman, E. Peterson, J.M. Friedman, Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin - A comparison with hemoglobin, J. Biol. Chem. 277 (2002) 25783–25790. https://doi.org/10.1074/jbc.M200301200 [HTML]

[38] I. Khan, D. Dantsker, U. Samuni, A.J. Friedman, C. Bonaventura, B. Manjula, S.A. Acharya, J.M. Friedman, beta 93 modified hemoglobin: Kinetic and conformational consequences, Biochemistry. 40 (2001) 7581–7592.

[39] U. Samuni, M.S. Navati, L.J. Juszczak, D. Dantsker, M. Yang, J.M. Friedman, Unfolding and refolding of sol-gel encapsulated carbonmonoxymyoglobin: An orchestrated spectroscopic study of intermediates and kinetics?, J. Phys. Chem. B. 104 (2000) 10802–10813. DOI: 10.1021/jp000802g [HTML]

[40] Y. Haas, U. Samuni, Reactions in rare gas matrices - Matrix and site effects, Prog. React. Kinet. Mech. 23 (1998) 211–280.

[41] U. Samuni, Y. Haas, R. Fajgar, J. Pola, Matrix effects in the low-temperature ozonation of ethylene, tetramethylethylene and 1-hexene, J. Mol. Struct. 449 (1998) 177–201.

[42] U. Samuni, S. Kahana, E. Haas, Matrix photochemistry of cycloheptatriene: Site effects, J. Phys. Chem. A. 102 (1998) 4758–4768. [HTML]

[43] R. Ponec, G. Yuzhakov, Y. Haas, U. Samuni, Theoretical analysis of the stereoselectivity in the ozonolysis of olefins. Evidence for a modified Criegee mechanism, J. Org. Chem. 62 (1997) 2757–2762. [HTML]

[44] U. Samuni, R. Fraenkel, Y. Haas, R. Fajgar, J. Pola, Environmental effects on the formation of the primary and secondary ozonides of ethylene at cryogenic temperatures, J. Am. Chem. Soc. 118 (1996) 3687–3693. [HTML]

[45] U. Samuni, Y. Haas, An ab-initio study of the normal modes of the primary and secondary ozonides of ethylene, Spectrochim. Acta Part a-Molecular Biomol. Spectrosc. 52 (1996) 1479–1492.

[46] U. Samuni, S. Kahana, R. Fraenkel, Y. Haas, D. Danovich, S. Shaik, The ICN-INC System - Experiment and Quantum-Chemical Calculations, Chem. Phys. Lett. 225 (1994) 391–397.

[47] S. Zilberg, U. Samuni, R. Fraenkel, Y. Haas, The Vibrational Structure of the S0- S1 Transition of Anthracene, Chem. Phys. 186 (1994) 303–316.

[48] R. Fraenkel, U. Samuni, Y. Haas, A matrix-isolation study of the fluorescence of anthracene and anthracene ammonia adducts in solid argon, Chem. Phys. Lett. 203 (1993) 523–530.

[49] A. Samuni, J.B. Mitchell, W. Degraff, C.M. Krishna, U. Samuni, A. Russo, Nitroxide Sod-Mimics - Modes of Action, Free Radic. Res. Commun. 12–3 (1991) 187–194.

[50] J.B. Mitchell, A. Samuni, M.C. Krishna, W.G. Degraff, M.S. Ahn, U. Samuni, A. Russo, Biologically-Active Metal-Independent Superoxide-Dismutase Mimics, Biochemistry. 29 (1990) 2802–2807.


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