Search Results - "Bilsel, Osman"

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  1. 1

    Engineering the Upconversion Nanoparticle Excitation Wavelength: Cascade Sensitization of Tri‐doped Upconversion Colloidal Nanoparticles at 800 nm by Shen, Jie, Chen, Guanying, Vu, Anne‐Marie, Fan, Wei, Bilsel, Osman S., Chang, Chun‐Chih, Han, Gang

    Published in Advanced optical materials (01-09-2013)
    “…Cascade‐sensitized 800 nm excited tri‐doped upconversion nanoparticles (UCNPs) are developed for the first time. This novel class of UCNPs employ Nd3+ as an…”
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  2. 2

    Tailoring dye-sensitized upconversion nanoparticle excitation bands towards excitation wavelength selective imaging by Wu, Xiang, Lee, Hyungseok, Bilsel, Osman, Zhang, Yuanwei, Li, Zhanjun, Chen, Teresa, Liu, Yi, Duan, Chunying, Shen, Jie, Punjabi, Amol, Han, Gang

    Published in Nanoscale (01-01-2015)
    “…One of the key roadblocks in UCNP development is its extremely limited choices of excitation wavelengths. We report a generic design to program UCNPs to…”
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  3. 3

    Transient Kinetic Analysis of SWR1C-Catalyzed H2A.Z Deposition Unravels the Impact of Nucleosome Dynamics and the Asymmetry of Histone Exchange by Singh, Raushan K., Fan, Jiayl, Gioacchini, Nathan, Watanabe, Shinya, Bilsel, Osman, Peterson, Craig L.

    Published in Cell reports (Cambridge) (09-04-2019)
    “…The SWR1C chromatin remodeling enzyme catalyzes ATP-dependent replacement of nucleosomal H2A with the H2A.Z variant, regulating key DNA-mediated processes such…”
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  4. 4

    Frustration and folding of a TIM barrel protein by Halloran, Kevin T., Wang, Yanming, Arora, Karunesh, Chakravarthy, Srinivas, Irving, Thomas C., Bilsel, Osman, Brooks, Charles L., Matthews, C. Robert

    “…Triosephosphate isomerase (TIM) barrel proteins have not only a conserved architecture that supports a myriad of enzymatic functions, but also a conserved…”
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  5. 5

    Computer design of microfluidic mixers for protein/RNA folding studies by Inguva, Venkatesh, Kathuria, Sagar V, Bilsel, Osman, Perot, Blair James

    Published in PloS one (20-06-2018)
    “…Kinetic studies of biological macromolecules increasingly use microfluidic mixers to initiate and monitor reaction progress. A motivation for using…”
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  6. 6

    Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes by Das, Sanchaita, Malaby, Andrew W., Nawrotek, Agata, Zhang, Wenhua, Zeghouf, Mahel, Maslen, Sarah, Skehel, Mark, Chakravarthy, Srinivas, Irving, Thomas C., Bilsel, Osman, Cherfils, Jacqueline, Lambright, David G.

    Published in Structure (London) (03-12-2019)
    “…Membrane dynamic processes require Arf GTPase activation by guanine nucleotide exchange factors (GEFs) with a Sec7 domain. Cytohesin family Arf GEFs function…”
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  7. 7

    Methods for analysis of size-exclusion chromatography-small-angle X-ray scattering and reconstruction of protein scattering by Malaby, Andrew W., Chakravarthy, Srinivas, Irving, Thomas C., Kathuria, Sagar V., Bilsel, Osman, Lambright, David G.

    Published in Journal of applied crystallography (01-08-2015)
    “…Size‐exclusion chromatography in line with small‐angle X‐ray scattering (SEC–SAXS) has emerged as an important method for investigation of heterogeneous and…”
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  8. 8

    Native State Conformational Heterogeneity of HP35 Revealed by Time-Resolved FRET by Serrano, Arnaldo L, Bilsel, Osman, Gai, Feng

    Published in The journal of physical chemistry. B (06-09-2012)
    “…The villin headpiece subdomain (HP35) has become one of the most widely used model systems in protein folding studies, due to its small size and ultrafast…”
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  9. 9

    Creating round focused micro-jets from rectangular nozzles by Inguva, Venkatesh, Graceffa, Rita, Schulz, Joachim, Bilsel, Osman, Perot, Blair J.

    “…A focused jet is an axisymmetric jet of liquid surrounded by an outer coaxial gas jet. The gas jet is typically used to compress the liquid jet in the radial…”
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  10. 10

    Microsecond Barrier-Limited Chain Collapse Observed by Time-Resolved FRET and SAXS by Kathuria, Sagar V., Kayatekin, Can, Barrea, Raul, Kondrashkina, Elena, Graceffa, Rita, Guo, Liang, Nobrega, R. Paul, Chakravarthy, Srinivas, Matthews, C. Robert, Irving, Thomas C., Bilsel, Osman

    Published in Journal of molecular biology (01-05-2014)
    “…It is generally held that random-coil polypeptide chains undergo a barrier-less continuous collapse when the solvent conditions are changed to favor the fully…”
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  11. 11

    Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam by Graceffa, Rita, Nobrega, R. Paul, Barrea, Raul A., Kathuria, Sagar V., Chakravarthy, Srinivas, Bilsel, Osman, Irving, Thomas C.

    Published in Journal of synchrotron radiation (01-11-2013)
    “…Small‐angle X‐ray scattering (SAXS) is a well established technique to probe the nanoscale structure and interactions in soft matter. It allows one to study…”
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  12. 12

    Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein by Wu, Ying, Kondrashkina, Elena, Kayatekin, Can, Matthews, C. Robert, Bilsel, Osman

    “…The earliest kinetic folding events for (βα)₈ barrels reflect the appearance of off-pathway intermediates. Continuous-flow microchannel mixing methods…”
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  13. 13

    Non-Native Structure Appears in Microseconds during the Folding of E. coli RNase H by Rosen, Laura E., Kathuria, Sagar V., Matthews, C. Robert, Bilsel, Osman, Marqusee, Susan

    Published in Journal of molecular biology (30-01-2015)
    “…The folding pathway of Escherichia coli RNase H is one of the best experimentally characterized for any protein. In spite of this, spectroscopic studies have…”
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  14. 14

    Microsecond Subdomain Folding in Dihydrofolate Reductase by Arai, Munehito, Iwakura, Masahiro, Matthews, C. Robert, Bilsel, Osman

    Published in Journal of molecular biology (08-07-2011)
    “…The characterization of microsecond dynamics in the folding of multisubdomain proteins has been a major challenge in understanding their often complex folding…”
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  15. 15

    Modulation of frustration in folding by sequence permutation by Nobrega, R. Paul, Arora, Karunesh, Kathuria, Sagar V., Graceffa, Rita, Barrea, Raul A., Guo, Liang, Chakravarthy, Srinivas, Bilsel, Osman, Irving, Thomas C., Brooks, Charles L., Matthews, C. Robert

    “…Folding of globular proteins can be envisioned as the contraction of a random coil unfolded state toward the native state on an energy surface rough with local…”
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  16. 16

    Metal Deficiency Increases Aberrant Hydrophobicity of Mutant Superoxide Dismutases That Cause Amyotrophic Lateral Sclerosis by Tiwari, Ashutosh, Liba, Amir, Sohn, Se Hui, Seetharaman, Sai V., Bilsel, Osman, Matthews, C.Robert, Hart, P.John, Valentine, Joan Selverstone, Hayward, Lawrence J.

    Published in The Journal of biological chemistry (02-10-2009)
    “…The mechanisms by which mutant variants of Cu/Zn-superoxide dismutase (SOD1) cause familial amyotrophic lateral sclerosis are not clearly understood. Evidence…”
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  17. 17

    Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species by Svensson, Anna-Karin E, Bilsel, Osman, Kayatekin, Can, Adefusika, Jessica A, Zitzewitz, Jill A, Matthews, C Robert

    Published in PloS one (09-04-2010)
    “…Amino acid replacements at dozens of positions in the dimeric protein human, Cu,Zn superoxide dismutase (SOD1) can cause amyotrophic lateral sclerosis (ALS)…”
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  18. 18

    Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells by Sainlos, Matthieu, Chitta, Sriram, Venkatraman, Prasanna, Imperiali, Barbara, Stern, Lawrence J, Bilsel, Osman, Nguyen, Tina T

    Published in Nature chemical biology (01-04-2007)
    “…A crucial step in the immune response is the binding of antigenic peptides to major histocompatibility complex (MHC) proteins. Class II MHC proteins present…”
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    Mapping the Folding Free Energy Surface for Metal-free Human Cu,Zn Superoxide Dismutase by Svensson, Anna-Karin E., Bilsel, Osman, Kondrashkina, Elena, Zitzewitz, Jill A., Matthews, C. Robert

    Published in Journal of molecular biology (15-12-2006)
    “…Mutations at many different sites in the gene encoding human Cu,Zn superoxide dismutase (SOD) are known to be causative agents in amyotrophic lateral sclerosis…”
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