Search Results - "SUDMEIER, James L"

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    Pro-Soft Val-boroPro: A Strategy for Enhancing in Vivo Performance of Boronic Acid Inhibitors of Serine Proteases by Poplawski, Sarah E, Lai, Jack H, Sanford, David G, Sudmeier, Wengen Wu, James L, Bachovchin, William W

    Published in Journal of medicinal chemistry (14-04-2011)
    “…Val-boroPro, 1, is a potent, but relatively nonspecific inhibitor of the prolyl peptidases. It has antihyperglycemic activity from inhibition of DPPIV but also…”
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    A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases? Theory Versus Experiment by Ash, Elissa L., Sudmeier, James L., De Fabo, Edward C., Bachovchin, William W.

    “…Cleland and Kreevoy recently advanced the idea that a special type of hydrogen bond (H-bond), termed a low-barrier hydrogen bond (LBHB), may account for the…”
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    Identification of Selective and Potent Inhibitors of Fibroblast Activation Protein and Prolyl Oligopeptidase by Poplawski, Sarah E, Lai, Jack H, Li, Youhua, Jin, Zhiping, Liu, Yuxin, Wu, Wengen, Wu, Yong, Zhou, Yuhong, Sudmeier, James L, Sanford, David G, Bachovchin, William W

    Published in Journal of medicinal chemistry (09-05-2013)
    “…Fibroblast activation protein (FAP) is a serine protease selectively expressed on reactive stromal fibroblasts of epithelial carcinomas. It is widely believed…”
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    α-Lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities by Haddad, Kristin Coffman, Sudmeier, James L, Bachovchin, Daniel A, Bachovchin, William W

    “…α-Lytic protease is a bacterial serine protease widely studied as a model system of enzyme catalysis. Here we report that lyophilization induces a structural…”
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    Identification of Histidine Tautomers in Proteins by 2D 1H/13Cδ2 One-Bond Correlated NMR by Sudmeier, James L, Bradshaw, Elizabeth M, Haddad, Kristin E. Coffman, Day, Regina M, Thalhauser, Craig J, Bullock, Peter A, Bachovchin, William W

    Published in Journal of the American Chemical Society (16-07-2003)
    “…If the 13Cδ2 chemical shift of neutral (“high pH”) histidine is >122 ppm, primarily Nδ1−H tautomer (2) is indicated; if it is <122 ppm, primarily Nε2−H…”
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    Synthesis and Characterization of Constrained Peptidomimetic Dipeptidyl Peptidase IV Inhibitors:  Amino-Lactam boroAlanines by Lai, Jack H, Wu, Wengen, Zhou, Yuhong, Maw, Hlaing H, Liu, Yuxin, Milo, Lawrence J, Poplawski, Sarah E, Henry, Gillian D, Sudmeier, James L, Sanford, David G, Bachovchin, William W

    Published in Journal of medicinal chemistry (17-05-2007)
    “…We describe here the epimerization-free synthesis and characterization of a new class of conformationally constrained lactam aminoboronic acid inhibitors of…”
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    Tautomerism, acid‐base equilibria, and H‐bonding of the six histidines in subtilisin BPN′ by NMR by Day, Regina M., Thalhauser, Craig J., Sudmeier, James L., Vincent, Matthew P., Torchilin, Ekaterina V., Sanford, David G., Bachovchin, Christopher W., Bachovchin, William W.

    Published in Protein science (01-04-2003)
    “…We have determined by 15N, 1H, and 13C NMR, the chemical behavior of the six histidines in subtilisin BPN′ and their PMSF and peptide boronic acid complexes in…”
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    Autochelation in Dipeptide Boronic Acids:  pH-Dependent Structures and Equilibria of Asp-boroPro and His-boroPro by NMR Spectroscopy by Sudmeier, James L., Zhou, Yuhong, Lai, Jack H., Maw, Hlaing H., Wu, Wengen, Bachovchin, William W.

    Published in Journal of the American Chemical Society (08-06-2005)
    “…Many dipeptide boronic acids of the type H2N-X − Y-B(OH)2 are potent protease inhibitors. Interest in these compounds as drugs for cancer, diabetes, and other…”
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    T Antigen Origin-Binding Domain of Simian Virus 40:  Determinants of Specific DNA Binding by Bradshaw, Elizabeth M., Sanford, David G., Luo, Xuelian, Sudmeier, James L., Gurard-Levin, Zachary A., Bullock, Peter A., Bachovchin, William W.

    Published in Biochemistry (Easton) (08-06-2004)
    “…To better understand origin recognition and initiation of DNA replication, we have examined by NMR complexes formed between the origin-binding domain of SV40 T…”
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