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  1. 1.   The Relationship between Heart Rate Variability, Psychological Flexibility, and Pain in Neurofibromatosis Type 1
  2. Allen, Taryn; Struemph, Kari L; Tamula, Mary Anne; Wolters, Pamela L; Baldwin, Andrea; Widemann, Brigitte; Martin, Staci
  3. Pain practice : the official journal of World Institute of Pain. 2018, Nov; 18(8): 969-978.
  1. 2.   Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution
  2. Sathiyamoorthy, Karthik; Vijayalakshmi, J; Tirupati, Bhramara; Fan, Lixin; Saper, Mark A
  3. The Journal of Biological Chemistry. 2017, Oct 27; 292(43): 17626-17642.
  1. 3.   Use of RNA structure flexibility data in nanostructure modeling
  2. Kasprzak, W.; Bindewald, E.; Kim, T. J.; Jaeger, L.; Shapiro, B. A.
  3. Methods. 2011, Jun; 54(2): 239-250.
  1. 4.   An integrated suite of fast docking algorithms
  2. Mashiach, E.; Schneidman-Duhovny, D.; Peri, A.; Shavit, Y.; Nussinov, R.; Wolfson, H. J.
  3. Proteins-Structure Function and Bioinformatics. 2010, Nov; 78(15): 3197-3204.
  1. 5.   FiberDock: a web server for flexible induced-fit backbone refinement in molecular docking
  2. Mashiach, E.; Nussinov, R.; Wolfson, H. J.
  3. Nucleic Acids Research. 2010, Jul; 38: W457-W461.
  1. 6.   Fiber Dock: Flexible induced-fit backbone refinement in molecular docking
  2. Mashiach, E.; Nussinov, R.; Wolfson, H. J.
  3. Proteins-Structure Function and Bioinformatics. 2010, May; 78(6): 1503-1519.
  1. 7.   Light chain somatic mutations change thermodynamics of binding and water coordination in the HyHEL-10 family of antibodies
  2. Acchione, M.; Lipschultz, C. A.; DeSantis, M. E.; Shanmuganathan, A.; Li, M.; Wlodawer, A.; Tarasov, S.; Smith-Gill, S. J.
  3. Molecular Immunology. 2009, Dec; 47(2-3): 457-464.
  1. 8.   HingeProt: Automated prediction of hinges in protein structures
  2. Emekli, U.; Schneidman-Duhovny, D.; Wolfson, H. J.; Nussinov, R.; Haliloglu, T.
  3. Proteins-Structure Function and Bioinformatics. 2008 70(4): 1219-1227.
  1. 9.   Restricted mobility of conserved residues in protein-protein interfaces in molecular simulations
  2. Yogurtcu, O. N.; Erdemli, S. B.; Nussinov, R.; Turkay, M.; Keskin, O.
  3. Biophysical Journal. 2008 94(9): 3475-3485.
  1. 10.   Automatic prediction of protein interactions with large scale motion
  2. Schneidman-Duhovny, D.; Nussinov, R.; Wolfson, H. J.
  3. Proteins-Structure Function and Bioinformatics. 2007, Dec; 69(4): 764-773.
  1. 11.   FireDock: Fast interaction refinement in molecular docking
  2. Andrusier, N.; Nussinov, R.; Wolfson, H. J.
  3. Proteins-Structure Function and Bioinformatics. 2007, Oct; 69(1): 139-159.
  1. 13.   Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097
  2. Das, K.; Sarafianos, S. G.; Clark, A. D.; Boyer, P. L.; Hughes, S. H.; Arnold, E.
  3. Journal of Molecular Biology. 2007, Jan; 365(1): 77-89.
  1. 14.   Understanding antibody-antigen associations by molecular dynamics simulations: Detection of important intra- and inter-molecular salt bridges
  2. Sinha, N.; Li, Y. L.; Lipschultz, C. A.; Smith-Gill, S. J.
  3. Cell Biochemistry and Biophysics. 2007 47(3): 361-375.
  1. 15.   Structure by design: from single proteins and their building blocks to nanostructures
  2. Tsai, C. J.; Zheng, J.; Aleman, C.; Nussinov, R.
  3. Trends in Biotechnology. 2006, Oct; 24(10): 449-454.
  1. 16.   Crystallography and the design of anti-AIDS drugs: Conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors
  2. Das, K.; Lewi, P. J.; Hughes, S. H.; Arnold, E.
  3. Progress in Biophysics and Molecular Biology. 2005, JUN; 88(2): 209-231.
  1. 17.   Characterization of the conformational state and flexibility of HIV-1 gp120
  2. Pan, Y. P.; Ma, B. Y.; Keskin, O.; Nussinov, R.
  3. Biophysical Journal. 2005, JAN; 88(1, Part 2, Suppl. S): 34A-34A.
  1. 18.   A structural similarity analysis of double-helical DNA
  2. Gardiner, E. J.; Hunter, C. A.; Lu, X. J.; Willett, P.
  3. Journal of Molecular Biology. 2004, OCT 29; 343(4): 879-889.
  1. 19.   Predicting molecular interactions in silico: II. Protein- protein and protein-drug docking
  2. Schneidman-Duhovny, D.; Nussinov, R.; Wolfson, H. J.
  3. Current Medicinal Chemistry. 2004 11(1): 91-107.
  1. 20.   Small molecule toxins targeting tumor receptors
  2. Dyba, M.; Tarasova, N. I.; Michejda, C. J.
  3. Current Pharmaceutical Design. 2004 10(19): 2311-2334.
  1. 21.   Noncatalytic assembly of ribonuclease III with double-stranded RNA
  2. Blaszczyk, J.; Gan, J. H.; Tropea, J. E.; Court, D. L.; Waugh, D. S.; Ji, X. H.
  3. Structure. 2004 12(3): 457-466.
  1. 22.   Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (etravirine) and related non-nucleoside reverse transcriptase inhibitors that are highly potent and effective against wild-type and drug-resistant HIV-1 variants
  2. Das, K.; Clark, A. D.; Lewi, P. J.; Heeres, J.; de Jonge, M. R.; Koymans, L. M. H.; Vinkers, H. M.; Daeyaert, F.; Ludovici, D. W.; Kukla, M. J.; De Corte, B.; Kavash, R. W.; Ho, C. Y.; Ye, H.; Lichtenstein, M. A.; Andries, K.; Pauwels, R.; de Bethune, M. P.; Boyer, P. L.; Clark, P.; Hughes, S. H.; Janssen, P. A. J.; Arnold, E.
  3. Journal of Medicinal Chemistry. 2004 47(10): 2550-2560.
  1. 23.   Modulating functional loop movements: The role of highly conserved residues in the correlated loop motions
  2. Gunasekaran, K.; Nussinov, R.
  3. Chembiochem. 2004 5(2): 224-230.
  1. 24.   Different roles of electrostatics in heat and in cold: Adaptation by citrate synthase
  2. Kumar, S.; Nussinov, R.
  3. Chembiochem. 2004 5(3): 280-290.
  1. 25.   Nonnucleoside inhibitor binding affects the interactions of the fingers subdomain of human immunodeficiency virus type 1 reverse transcriptase with DNA
  2. Peletskaya, E. N.; Kogon, A. A.; Tuske, S.; Arnold, E.; Hughes, S. H.
  3. Journal of Virology. 2004 78(7): 3387-3397.
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