Education
Ph.D in Polymer Chemistry, Polytechnic Institute, 1970
Current Position
Professor, Department of Chemistry, College of Staten Island, City University of New York, NY, USA
Publications
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Chill, J. H. and Naider, F. (2011). A solution NMR view of protein dynamics in the biological membrane. Curr Opin Struct Biol 21(5): 627-633.
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Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Guntert, P., Zerbe, O. and Naider, F. (2011). Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments. Biochim Biophys Acta 1808(11): 2674-2684.
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Schnur, E., Noah, E., Ayzenshtat, I., Sargsyan, H., Inui, T., Ding, F. X., Arshava, B., Sagi, Y., Kessler, N., Levy, R., Scherf, T., Naider, F. and Anglister, J. (2011). The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide. J Mol Biol 410(5): 778-797.
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Umanah, G. K., Huang, L. Y., Maccarone, J. M., Naider, F. and Becker, J. M. (2011). Changes in conformation at the cytoplasmic ends of the fifth and sixth transmembrane helices of a yeast G protein-coupled receptor in response to ligand binding. Biochemistry 50(32): 6841-6854.
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Mathew, E., Bajaj, A., Connelly, S. M., Sargsyan, H., Ding, F. X., Hajduczok, A. G., Naider, F. and Dumont, M. E. (2011). Differential interactions of fluorescent agonists and antagonists with the yeast G protein coupled receptor Ste2p. J Mol Biol 409(4): 513-528.
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Mullen, D. G., Kyro, K., Hauser, M., Gustavsson, M., Veglia, G., Becker, J. M., Naider, F. and Distefano, M. D. (2011). Synthesis of a-factor peptide from Saccharomyces cerevisiae and photoactive analogues via Fmoc solid phase methodology. Bioorg Med Chem 19(1): 490-497.
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Umanah, G. K., Huang, L., Ding, F. X., Arshava, B., Farley, A. R., Link, A. J., Naider, F. and Becker, J. M. (2010). Identification of residue-to-residue contact between a peptide ligand and its G protein-coupled receptor using periodate-mediated dihydroxyphenylalanine cross-linking and mass spectrometry. J Biol Chem 285(50): 39425-39436.
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Cohen, L. S., Becker, J. M. and Naider, F. (2010). Biosynthesis of peptide fragments of eukaryotic GPCRs in Escherichia coli by directing expression into inclusion bodies. J Pept Sci 16(5): 213-218.
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Tantry, S., Ding, F. X., Dumont, M., Becker, J. M. and Naider, F. (2010). Binding of fluorinated phenylalanine alpha-factor analogues to Ste2p: evidence for a cation-pi binding interaction between a peptide ligand and its cognate G protein-coupled receptor. Biochemistry 49(24): 5007-5015.
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Moseri, A., Tantry, S., Sagi, Y., Arshava, B., Naider, F. and Anglister, J. (2010). An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120. Virology 401(2): 293-304.
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Kim, H., Lee, B. K., Naider, F. and Becker, J. M. (2009). Identification of specific transmembrane residues and ligand-induced interface changes involved in homo-dimer formation of a yeast G protein-coupled receptor. Biochemistry 48(46): 10976-10987.
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Naider, F. and Anglister, J. (2009). Peptides in the treatment of AIDS. Curr Opin Struct Biol 19(4): 473-482.
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Mester, B., Manor, R., Mor, A., Arshava, B., Rosen, O., Ding, F. X., Naider, F. and Anglister, J. (2009). HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D. Biochemistry 48(33): 7867-7877.
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Neumoin, A., Cohen, L. S., Arshava, B., Tantry, S., Becker, J. M., Zerbe, O. and Naider, F. (2009). Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles. Biophys J 96(8): 3187-3196.
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Mor, A., Segal, E., Mester, B., Arshava, B., Rosen, O., Ding, F. X., Russo, J., Dafni, A., Schvartzman, F., Scherf, T., Naider, F. and Anglister, J. (2009). Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies. Biochemistry 48(15): 3288-3303.
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Umanah, G. K., Son, C., Ding, F., Naider, F. and Becker, J. M. (2009). Cross-linking of a DOPA-containing peptide ligand into its G protein-coupled receptor. Biochemistry 48(9): 2033-2044.
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Zou, C., Naider, F. and Zerbe, O. (2008). Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR. J Biomol NMR 42(4): 257-269.
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Naider, F. (2007). Synthesis, biosynthesis, and characterization of transmembrane domains of a G protein-coupled receptor. Methods Mol Biol 386: 95-121.
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Noah, E., Biron, Z., Naider, F., Arshava, B. and Anglister, J. (2008). The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N' peptide. Biochemistry 47(26): 6782-6792.
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Huang, L. Y., Umanah, G., Hauser, M., Son, C., Arshava, B., Naider, F. and Becker, J. M. (2008). Unnatural amino acid replacement in a yeast G protein-coupled receptor in its native environment. Biochemistry 47(20): 5638-5648.
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Neumoin, A., Arshava, B., Becker, J., Zerbe, O. and Naider, F. (2007). NMR studies in dodecylphosphocholine of a fragment containing the seventh transmembrane helix of a G-protein-coupled receptor from Saccharomyces cerevisiae. Biophys J 93(2): 467-482.
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Hauser, M., Kauffman, S., Lee, B. K., Naider, F. and Becker, J. M. (2007). The first extracellular loop of the Saccharomyces cerevisiae G protein-coupled receptor Ste2p undergoes a conformational change upon ligand binding. J Biol Chem 282(14): 10387-10397.
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Kier, R. and Kinder, B. (1992). Insulinomas: MR imaging with STIR sequences and motion suppression. AJR Am J Roentgenol 158(2): 457-458.
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Balambika, R., Inui, T., Sargsyan, H., Arshava, B., Cohen, L. S., Ding, F.X., Becker, J.M. and Naider, F. (2007). Synthesis of a Double Transmembrane Domain Fragment of Ste2p by Native Chemical Ligation. Int J Pept Res Ther 13: 251-263.
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Cano-Sanchez, P., Severino, B., Sureshbabu, V. V., Russo, J., Inui, T., Ding, F. X., Arshava, B., Becker, J. and Naider, F. (2006). Effects of N- and C-terminal addition of oligolysines or native loop residues on the biophysical properties of transmembrane domain peptides from a G-protein coupled receptor. J Pept Sci 12(12): 808-822.
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Bajaj, A., Connelly, S. M., Gehret, A. U., Naider, F. and Dumont, M. E. (2007). Role of extracellular charged amino acids in the yeast alpha-factor receptor. Biochim Biophys Acta 1773(6): 707-717.
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Englander, J., Cohen, L., Arshava, B., Estephan, R., Becker, J. M. and Naider, F. (2006). Selective labeling of a membrane peptide with 15N-amino acids using cells grown in rich medium. Biopolymers 84(5): 508-518.
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Gehret, A. U., Bajaj, A., Naider, F. and Dumont, M. E. (2006). Oligomerization of the yeast alpha-factor receptor: implications for dominant negative effects of mutant receptors. J Biol Chem 281(30): 20698-20714.
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Lee, Y. H., Naider, F. and Becker, J. M. (2006). Interacting residues in an activated state of a G protein-coupled receptor. J Biol Chem 281(4): 2263-2272.
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Biron, Z., Khare, S., Quadt, S. R., Hayek, Y., Naider, F. and Anglister, J. (2005). The 2F5 epitope is helical in the HIV-1 entry inhibitor T-20. Biochemistry 44(41): 13602-13611.
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Estephan, R., Englander, J., Arshava, B., Samples, K. L., Becker, J. M. and Naider, F. (2005). Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor. Biochemistry 44(35): 11795-11810.
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Naider, F., Khare, S., Arshava, B., Severino, B., Russo, J. and Becker, J. M. (2005). Synthetic peptides as probes for conformational preferences of domains of membrane receptors. Biopolymers 80(2-3): 199-213.
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Bajaj, A., Celic, A., Ding, F. X., Naider, F., Becker, J. M. and Dumont, M. E. (2004). A fluorescent alpha-factor analogue exhibits multiple steps on binding to its G protein coupled receptor in yeast. Biochemistry 43(42): 13564-13578.
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Son, C. D., Sargsyan, H., Naider, F. and Becker, J. M. (2004). Identification of ligand binding regions of the Saccharomyces cerevisiae alpha-factor pheromone receptor by photoaffinity cross-linking. Biochemistry 43(41): 13193-13203.
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Naider, F. and Becker, J. M. (2004). The alpha-factor mating pheromone of Saccharomyces cerevisiae: a model for studying the interaction of peptide hormones and G protein-coupled receptors. Peptides 25(9): 1441-1463.
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Naider, F., Ding, F. X., VerBerkmoes, N. C., Arshava, B. and Becker, J. M. (2003). Synthesis and biophysical characterization of a multidomain peptide from a Saccharomyces cerevisiae G protein-coupled receptor. J Biol Chem 278(52): 52537-52545.
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Celic, A., Martin, N. P., Son, C. D., Becker, J. M., Naider, F. and Dumont, M. E. (2003). Sequences in the intracellular loops of the yeast pheromone receptor Ste2p required for G protein activation. Biochemistry 42(10): 3004-3017.
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Lee, B. K., Lee, Y. H., Hauser, M., Son, C. D., Khare, S., Naider, F. and Becker, J. M. (2002). Tyr266 in the sixth transmembrane domain of the yeast alpha-factor receptor plays key roles in receptor activation and ligand specificity. Biochemistry 41(46): 13681-13689.
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Biron, Z., Khare, S., Samson, A. O., Hayek, Y., Naider, F. and Anglister, J. (2002). A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41. Biochemistry 41(42): 12687-12696.
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Akal-Strader, A., Khare, S., Xu, D., Naider, F. and Becker, J. M. (2002). Residues in the first extracellular loop of a G protein-coupled receptor play a role in signal transduction. J Biol Chem 277(34): 30581-30590.
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Henry, L. K., Khare, S., Son, C., Babu, V. V., Naider, F. and Becker, J. M. (2002). Identification of a contact region between the tridecapeptide alpha-factor mating pheromone of Saccharomyces cerevisiae and its G protein-coupled receptor by photoaffinity labeling. Biochemistry 41(19): 6128-6139.
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Ding, F. X., Schreiber, D., VerBerkmoes, N. C., Becker, J. M. and Naider, F. (2002). The chain length dependence of helix formation of the second transmembrane domain of a G protein-coupled receptor of Saccharomyces cerevisiae. J Biol Chem 277(17): 14483-14492.
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Lee, B. K., Khare, S., Naider, F. and Becker, J. M. (2001). Identification of residues of the Saccharomyces cerevisiae G protein-coupled receptor contributing to alpha-factor pheromone binding. J Biol Chem 276(41): 37950-37961.
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Ding, F. X., Lee, B. K., Hauser, M., Davenport, L., Becker, J. M. and Naider, F. (2001). Probing the binding domain of the Saccharomyces cerevisiae alpha-mating factor receptor with rluorescent ligands. Biochemistry 40(4): 1102-1108.
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Sommers, C. M., Martin, N. P., Akal-Strader, A., Becker, J. M., Naider, F. and Dumont, M. E. (2000). A limited spectrum of mutations causes constitutive activation of the yeast alpha-factor receptor. Biochemistry 39(23): 6898-6909.
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Beckerman, J. L., Naider, F. and Ebbole, D. J. (1997). Inhibition of pathogenicity of the rice blast fungus by Saccharomyces cerevisiae alpha-factor. Science 276(5315): 1116-1119.
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Xue, C. B., Eriotou-Bargiota, E., Miller, D., Becker, J. M. and Naider, F. (1989). A covalently constrained congener of the Saccharomyces cerevisiae tridecapeptide mating pheromone is an agonist. J Biol Chem 264(32): 19161-19168.
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Goodman, M., Ribeiro, A. A. and Naider, F. (1978). Protected homo-oligopeptide structure: Model for preferred conformation of a linear methionine heptapeptide in chloroform. Proc Natl Acad Sci U S A 75(10): 4647-4651.
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Naider, F., Becker, J. M. and Katzir-Katchalski, E. (1974). Utilization of methionine-containing peptides and their derivatives by a methionine-requiring auxotroph of Saccharomyces cerevisiae. J Biol Chem 249(1): 9-20.
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Naider, F., Benedetti, E. and Goodman, M. (1971). Conformation of cyclolinopeptide a observed by circular dichroism. Proc Natl Acad Sci U S A 68(6): 1195-1198.