Search Results - "Keul, Nicholas D."

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  1. 1

    The entropic force generated by intrinsically disordered segments tunes protein function by Keul, Nicholas D., Oruganty, Krishnadev, Schaper Bergman, Elizabeth T., Beattie, Nathaniel R., McDonald, Weston E., Kadirvelraj, Renuka, Gross, Michael L., Phillips, Robert S., Harvey, Stephen C., Wood, Zachary A.

    Published in Nature (London) (01-11-2018)
    “…Protein structures are dynamic and can explore a large conformational landscape 1 , 2 . Only some of these structural substates are important for protein…”
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    Journal Article
  2. 2

    Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core by Beattie, Nathaniel R, Pioso, Brittany J, Sidlo, Andrew M, Keul, Nicholas D, Wood, Zachary A

    Published in Biochemistry (Easton) (18-12-2018)
    “…Human UDP-glucose dehydrogenase (hUGDH) oxidizes UDP-glucose to UDP-glucuronic acid, an essential substrate in the phase II metabolism of drugs. The activity…”
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  3. 3

    Conservation of Atypical Allostery in C. elegans UDP-Glucose Dehydrogenase by Beattie, Nathaniel R, Keul, Nicholas D, Hicks Sirmans, Tiffany N, McDonald, Weston E, Talmadge, Trevor M, Taujale, Rahil, Kannan, Natarajan, Wood, Zachary A

    Published in ACS omega (08-10-2019)
    “…Human UDP-glucose dehydrogenase (hUGDH) oxidizes uridine diphosphate (UDP)-glucose to UDP-glucuronic acid, an essential substrate in the phase II metabolism of…”
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    Journal Article
  4. 4

    1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY by LaMattina, Joseph W, Keul, Nicholas D, Reitzer, Pierre, Kapoor, Suraj, Galzerani, Felipe, Koch, Daniel J, Gouvea, Iuri E, Lanzilotta, William N

    Published in The Journal of biological chemistry (22-07-2016)
    “…Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical…”
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    Journal Article
  5. 5

    Anaerobic Heme Degradation: ChuY Is an Anaerobilin Reductase That Exhibits Kinetic Cooperativity by LaMattina, Joseph W, Delrossi, Michael, Uy, Katherine G, Keul, Nicholas D, Nix, David B, Neelam, Anudeep R, Lanzilotta, William N

    Published in Biochemistry (Easton) (14-02-2017)
    “…Heme catabolism is an important biochemical process that many bacterial pathogens utilize to acquire iron. However, tetrapyrrole catabolites can be reactive…”
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  6. 6
  7. 7

    Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase by Beattie, Nathaniel R, Keul, Nicholas D, Sidlo, Andrew M, Wood, Zachary A

    Published in Biochemistry (Easton) (10-01-2017)
    “…Human UDP-glucose dehydrogenase (hUGDH) is regulated by an atypical allosteric mechanism in which the feedback inhibitor UDP-xylose (UDP-Xyl) competes with the…”
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  8. 8

    The structural and biochemical impacts of monomerizing human acetylcholinesterase by Bester, Stephanie M., Adipietro, Kaylin A., Funk, Vanessa L., Myslinski, James M., Keul, Nicholas D., Cheung, Jonah, Wilder, Paul T., Wood, Zachary A., Weber, David J., Height, Jude J., Pegan, Scott D.

    Published in Protein science (01-06-2019)
    “…Serving a critical role in neurotransmission, human acetylcholinesterase (hAChE) is the target of organophosphate nerve agents. Hence, there is an active…”
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  9. 9

    Hysteresis in Human UDP-Glucose Dehydrogenase Is Due to a Restrained Hexameric Structure That Favors Feedback Inhibition by Kadirvelraj, Renuka, Custer, Gregory S, Keul, Nicholas D, Sennett, Nicholas C, Sidlo, Andrew M, Walsh, Richard M, Wood, Zachary A

    Published in Biochemistry (Easton) (30-12-2014)
    “…Human UDP-α-d-glucose-6-dehydrogenase (hUGDH) displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). Here we…”
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  10. 10
  11. 11

    1,2-Propanediol Dehydration in Roseburia inulinivorans by LaMattina, Joseph W., Keul, Nicholas D., Reitzer, Pierre, Kapoor, Suraj, Galzerani, Felipe, Koch, Daniel J., Gouvea, Iuri E., Lanzilotta, William N.

    Published in The Journal of biological chemistry (22-07-2016)
    “…Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical…”
    Get full text
    Journal Article
  12. 12
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