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Osman S Bilsel PhD

TitleAssociate Professor
InstitutionUniversity of Massachusetts Medical School
DepartmentBiochemistry and Molecular Pharmacology
AddressUniversity of Massachusetts Medical School
364 Plantation Street, LRB
Worcester MA 01605
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    Other Positions
    InstitutionUMMS - School of Medicine
    DepartmentBiochemistry and Molecular Pharmacology

    InstitutionUMMS - Graduate School of Biomedical Sciences
    DepartmentBiochemistry and Molecular Pharmacology


    Collapse Biography 
    Collapse education and training
    University of Rochester, Rochester, NY, United StatesBAPhysics & Chemistry
    Washington University in St Louis, Saint Louis, MO, United StatesPHDPhysical Chemistry

    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    1. Inguva V, Kathuria SV, Bilsel O, Perot BJ. Computer design of microfluidic mixers for protein/RNA folding studies. PLoS One. 2018; 13(6):e0198534. PMID: 29924842.
      View in: PubMed
    2. Malaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG. Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors. Structure. 2018 Jan 02; 26(1):106-117.e6. PMID: 29276036.
      View in: PubMed
    3. Shi J, Nobrega RP, Schwantes C, Kathuria SV, Bilsel O, Matthews CR, Lane TJ, Pande VS. Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY. Sci Rep. 2017 Mar 08; 7:44116. PMID: 28272524.
      View in: PubMed
    4. Watson MD, Peran I, Zou J, Bilsel O, Raleigh DP. Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure. Biochemistry. 2017 Feb 28; 56(8):1085-1094. PMID: 28124899.
      View in: PubMed
    5. Peran I, Watson MD, Bilsel O, Raleigh DP. Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure. Chem Commun (Camb). 2016 Feb 04; 52(10):2055-8. PMID: 26686928.
      View in: PubMed
    6. Wu X, Zhang Y, Takle K, Bilsel O, Li Z, Lee H, Zhang Z, Li D, Fan W, Duan C, Chan EM, Lois C, Xiang Y, Han G. Dye-Sensitized Core/Active Shell Upconversion Nanoparticles for Optogenetics and Bioimaging Applications. ACS Nano. 2016 Jan 26; 10(1):1060-6. PMID: 26736013.
      View in: PubMed
    7. Orevi T, Rahamim G, Amir D, Kathuria S, Bilsel O, Matthews CR, Haas E. Sequential Closure of Loop Structures Forms the Folding Nucleus during the Refolding Transition of the Escherichia coli Adenylate Kinase Molecule. Biochemistry. 2016 Jan 12; 55(1):79-91. PMID: 26666584.
      View in: PubMed
    8. Wu X, Lee H, Bilsel O, Zhang Y, Li Z, Chen T, Liu Y, Duan C, Shen J, Punjabi A, Han G. Tailoring dye-sensitized upconversion nanoparticle excitation bands towards excitation wavelength selective imaging. Nanoscale. 2015 Nov 28; 7(44):18424-8. PMID: 26499208.
      View in: PubMed
    9. Malaby AW, Chakravarthy S, Irving TC, Kathuria SV, Bilsel O, Lambright DG. Methods for analysis of size-exclusion chromatography-small-angle X-ray scattering and reconstruction of protein scattering. J Appl Crystallogr. 2015 Aug 1; 48(Pt 4):1102-1113. PMID: 26306089.
      View in: PubMed
    10. Rosen LE, Kathuria SV, Matthews CR, Bilsel O, Marqusee S. Non-native structure appears in microseconds during the folding of E. coli RNase H. J Mol Biol. 2015 Jan 30; 427(2):443-53. PMID: 25311861.
      View in: PubMed
    11. Nobrega RP, Arora K, Kathuria SV, Graceffa R, Barrea RA, Guo L, Chakravarthy S, Bilsel O, Irving TC, Brooks CL, Matthews CR. Modulation of frustration in folding by sequence permutation. Proc Natl Acad Sci U S A. 2014 Jul 22; 111(29):10562-7. PMID: 25002512.
      View in: PubMed
    12. Kathuria SV, Kayatekin C, Barrea R, Kondrashkina E, Graceffa R, Guo L, Nobrega RP, Chakravarthy S, Matthews CR, Irving TC, Bilsel O. Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS. J Mol Biol. 2014 May 1; 426(9):1980-94. PMID: 24607691.
      View in: PubMed
    13. Zhou HX, Bilsel O. SAXS/SANS probe of intermolecular interactions in concentrated protein solutions. Biophys J. 2014 Feb 18; 106(4):771-3. PMID: 24559977.
      View in: PubMed
    14. Kathuria SV, Chan A, Graceffa R, Paul Nobrega R, Robert Matthews C, Irving TC, Perot B, Bilsel O. Advances in turbulent mixing techniques to study microsecond protein folding reactions. Biopolymers. 2013 Nov; 99(11):888-96. PMID: 23868289.
      View in: PubMed
    15. Graceffa R, Nobrega RP, Barrea RA, Kathuria SV, Chakravarthy S, Bilsel O, Irving TC. Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam. J Synchrotron Radiat. 2013 Nov; 20(Pt 6):820-5. PMID: 24121320.
      View in: PubMed
    16. Serrano AL, Bilsel O, Gai F. Native state conformational heterogeneity of HP35 revealed by time-resolved FRET. J Phys Chem B. 2012 Sep 6; 116(35):10631-8. PMID: 22891809.
      View in: PubMed
    17. Arai M, Iwakura M, Matthews CR, Bilsel O. Microsecond subdomain folding in dihydrofolate reductase. J Mol Biol. 2011 Jul 8; 410(2):329-42. PMID: 21554889.
      View in: PubMed
    18. Kathuria SV, Guo L, Graceffa R, Barrea R, Nobrega RP, Matthews CR, Irving TC, Bilsel O. Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering. Biopolymers. 2011 Aug; 95(8):550-8. PMID: 21442608.
      View in: PubMed
    19. Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR. Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species. PLoS One. 2010 Apr 09; 5(4):e10064. PMID: 20404910.
      View in: PubMed
    20. Tiwari A, Liba A, Sohn SH, Seetharaman SV, Bilsel O, Matthews CR, Hart PJ, Valentine JS, Hayward LJ. Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis. J Biol Chem. 2009 Oct 02; 284(40):27746-58. PMID: 19651777.
      View in: PubMed
    21. Noel AF, Bilsel O, Kundu A, Wu Y, Zitzewitz JA, Matthews CR. The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors. J Mol Biol. 2009 Apr 10; 387(4):1002-16. PMID: 19150359.
      View in: PubMed
    22. Wu Y, Kondrashkina E, Kayatekin C, Matthews CR, Bilsel O. Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proc Natl Acad Sci U S A. 2008 Sep 9; 105(36):13367-72. PMID: 18757725.
      View in: PubMed
    23. Forsyth WR, Bilsel O, Gu Z, Matthews CR. Topology and sequence in the folding of a TIM barrel protein: global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (betaalpha)8 barrel of unknown function from B. subtilis. J Mol Biol. 2007 Sep 7; 372(1):236-53. PMID: 17619021.
      View in: PubMed
    24. Venkatraman P, Nguyen TT, Sainlos M, Bilsel O, Chitta S, Imperiali B, Stern LJ. Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells. Nat Chem Biol. 2007 Apr; 3(4):222-8. PMID: 17351628.
      View in: PubMed
    25. Arai M, Kondrashkina E, Kayatekin C, Matthews CR, Iwakura M, Bilsel O. Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein. J Mol Biol. 2007 Apr 20; 368(1):219-29. PMID: 17331539.
      View in: PubMed
    26. Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR. Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. J Mol Biol. 2006 Dec 15; 364(5):1084-102. PMID: 17046019.
      View in: PubMed
    27. Bilsel O, Matthews CR. Molecular dimensions and their distributions in early folding intermediates. Curr Opin Struct Biol. 2006 Feb; 16(1):86-93. PMID: 16442277.
      View in: PubMed
    28. Doyle SM, Bilsel O, Teschke CM. SecA folding kinetics: a large dimeric protein rapidly forms multiple native states. J Mol Biol. 2004 Jul 30; 341(1):199-214. PMID: 15312773.
      View in: PubMed
    29. Bilsel O, Matthews CR. Barriers in protein folding reactions. Adv Protein Chem. 2000; 53:153-207. PMID: 10751945.
      View in: PubMed
    30. Gualfetti PJ, Iwakura M, Lee JC, Kihara H, Bilsel O, Zitzewitz JA, Matthews CR. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry. 1999 Oct 5; 38(40):13367-78. PMID: 10529212.
      View in: PubMed
    31. Gualfetti PJ, Bilsel O, Matthews CR. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Sci. 1999 Aug; 8(8):1623-35. PMID: 10452606.
      View in: PubMed
    32. Bilsel O, Yang L, Zitzewitz JA, Beechem JM, Matthews CR. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry. 1999 Mar 30; 38(13):4177-87. PMID: 10194334.
      View in: PubMed
    33. Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 1999 Jan 19; 38(3):1018-29. PMID: 9893998.
      View in: PubMed
    34. Zitzewitz JA, Bilsel O, Luo J, Jones BE, Matthews CR. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry. 1995 Oct 3; 34(39):12812-9. PMID: 7548036.
      View in: PubMed
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