J
Jeff L. Staudinger
Researcher at University of Kansas
Publications - 58
Citations - 7800
Jeff L. Staudinger is an academic researcher from University of Kansas. The author has contributed to research in topics: Pregnane X receptor & Nuclear receptor. The author has an hindex of 38, co-authored 57 publications receiving 7400 citations. Previous affiliations of Jeff L. Staudinger include GlaxoSmithKline & College of Osteopathic Medicine of the Pacific.
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Journal ArticleDOI
An Orphan Nuclear Receptor Activated by Pregnanes Defines a Novel Steroid Signaling Pathway
Steven A. Kliewer,John T. Moore,Laura E. Wade,Jeff L. Staudinger,Michael A. Watson,Stacey A. Jones,David D. McKee,Beverly B. Oliver,Timothy M. Willson,Rolf Zetterström,Thomas Perlmann,Jürgen M. Lehmann +11 more
TL;DR: The results provide evidence for the existence of a novel steroid hormone signaling pathway with potential implications in the regulation of steroid hormone and sterol homeostasis and the expression of the CYP3A family of steroid hydroxylases and modulates sterol and bile acid biosynthesis in vivo.
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The nuclear receptor PXR is a lithocholic acid sensor that protects against liver toxicity
Jeff L. Staudinger,Jeff L. Staudinger,Bryan Goodwin,Stacey A. Jones,Diane Hawkins-Brown,Kathleen I. MacKenzie,Anne M. Latour,Yaping Liu,Curtis D. Klaassen,Kathleen K. Brown,John F. Reinhard,Timothy M. Willson,Beverly H. Koller,Steven A. Kliewer +13 more
TL;DR: It is proposed that PXR serves as a physiological sensor of LCA, and coordinately regulates gene expression to reduce the concentrations of this toxic bile acid, and suggest that PxR agonists may prove useful in the treatment of human cholestatic liver disease.
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Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1.
TL;DR: PICK1 (protein interacting with C kinase), a PDZ domain-containing protein, interacts with the C termini of alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptors in vitro and in vivo and suggests that PICK1 may play an important role in the modulation of synaptic transmission by regulating the synaptic targeting of AMPA receptors.
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PDZ Proteins Bind, Cluster, and Synaptically Colocalize with Eph Receptors and Their Ephrin Ligands
Richard Torres,Bonnie L. Firestein,Hualing Dong,Jeff L. Staudinger,Eric N. Olson,Richard L. Huganir,David S. Bredt,Nicholas W. Gale,George D. Yancopoulos +8 more
TL;DR: PDZ proteins may play critical roles in localizing vertebrate receptor tyrosine kinases and/or their ligands and may be particularly important for Eph function in guidance or patterning or at the synapse.
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Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1.
Gonzalo E. Torres,Wei-Dong Yao,Amy R. Mohn,Hui Quan,Kyeong Man Kim,Allan I. Levey,Jeff L. Staudinger,Marc G. Caron +7 more
TL;DR: A role is indicated for PDZ-mediated protein interactions in the localization, expression, and function of monoamine transporters in mammalian cells and neurons in culture.