Search Results - "Steavenson, Shirley"

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  1. 1

    A fully human anti-hepcidin antibody modulates iron metabolism in both mice and nonhuman primates by Cooke, Keegan S., Hinkle, Beth, Salimi-Moosavi, Hossein, Foltz, Ian, King, Chadwick, Rathanaswami, Palaniswami, Winters, Aaron, Steavenson, Shirley, Begley, C. Glenn, Molineux, Graham, Sasu, Barbra J.

    Published in Blood (24-10-2013)
    “…Iron maldistribution has been implicated in the etiology of many diseases including the anemia of inflammation (AI), atherosclerosis, diabetes, and…”
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    Journal Article
  2. 2

    FGF21 N- and C-termini play different roles in receptor interaction and activation by Yie, Junming, Hecht, Randy, Patel, Jennifer, Stevens, Jennitte, Wang, Wei, Hawkins, Nessa, Steavenson, Shirley, Smith, Steve, Winters, Dwight, Fisher, Seth, Cai, Ling, Belouski, Ed, Chen, Ching, Michaels, Mark L., Li, Yue-Sheng, Lindberg, Richard, Wang, Minghan, Véniant, Murielle, Xu, Jing

    Published in FEBS letters (05-01-2009)
    “…Fibroblast growth factor-21 (FGF21) signaling requires the presence of β-Klotho, a co-receptor with a very short cytoplasmic domain. Here we show that FGF21…”
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    An acyl-ghrelin-specific neutralizing antibody inhibits the acute ghrelin-mediated orexigenic effects in mice by Lu, Shu-Chen, Xu, Jing, Chinookoswong, Narumol, Liu, Shuying, Steavenson, Shirley, Gegg, Colin, Brankow, David, Lindberg, Richard, Véniant, Murielle, Gu, Wei

    Published in Molecular pharmacology (01-04-2009)
    “…Ghrelin is a 28-amino acid peptide secreted mainly by the stomach. Acyl-ghrelin, which binds to and activates the growth hormone secretagogue receptor type 1a…”
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    alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease by Wood, S J, Wypych, J, Steavenson, S, Louis, J C, Citron, M, Biere, A L

    Published in The Journal of biological chemistry (09-07-1999)
    “…Parkinson's disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major…”
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  7. 7

    Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation by Narhi, L, Wood, S J, Steavenson, S, Jiang, Y, Wu, G M, Anafi, D, Kaufman, S A, Martin, F, Sitney, K, Denis, P, Louis, J C, Wypych, J, Biere, A L, Citron, M

    Published in The Journal of biological chemistry (02-04-1999)
    “…Parkinson's disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major…”
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    Journal Article
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    α-Synuclein Fibrillogenesis Is Nucleation-dependent by Stephen J. Wood, Jette Wypych, Shirley Steavenson, Jean-Claude Louis, Martin Citron, Anja Leona Biere

    Published in The Journal of biological chemistry (09-07-1999)
    “…Parkinson’s disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major…”
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    Journal Article
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    Both Familial Parkinson’s Disease Mutations Accelerate α-Synuclein Aggregation by Linda Narhi, Stephen J. Wood, Shirley Steavenson, Yijia Jiang, Gay May Wu, Dan Anafi, Stephen A. Kaufman, Francis Martin, Karen Sitney, Paul Denis, Jean-Claude Louis, Jette Wypych, Anja Leona Biere, Martin Citron

    Published in The Journal of biological chemistry (02-04-1999)
    “…Parkinson’s disease (PD) is a neurodegenerative disorder that is pathologically characterized by the presence of intracytoplasmic Lewy bodies, the major…”
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    Journal Article
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    The use of glucose dehydrogenase to monitor the integrity of microsomes by Bublitz, C, Steavenson, S

    Published in Biochimica et biophysica acta (14-04-1988)
    “…Various concentrations of Tergitol NP-10 stimulate mannose-6-phosphatase and glucose dehydrogenase to the same extent in untreated rat liver microsomes. Thus,…”
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  16. 16

    The topology of phosphogluconate dehydrogenases in rat liver microsomes by Bublitz, C, Lawler, C A, Steavenson, S

    Published in Archives of biochemistry and biophysics (15-11-1987)
    “…Rat liver microsomes are known to contain a 6-phosphogluconate dehydrogenase which differs from the 6-phosphogluconate dehydrogenase in the soluble fraction…”
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    Journal Article