Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Yaoling Shu"'
Publikováno v:
JCI Insight, Vol 6, Iss 19 (2021)
The signaling mechanisms by which dietary fat and cholesterol signals regulate central pathways of glucose homeostasis are not completely understood. By using a hepatocyte-specific PKCβ-deficient (PKCβHep–/–) mouse model, we demonstrated the ro
Externí odkaz:
https://doaj.org/article/c4a0b39f28f34af4a669bb5d8f6e8633
Autor:
Yaoling Shu, Faizule Hassan, Vincenzo Coppola, Kedryn K. Baskin, Xianlin Han, Neil K. Mehta, Michael C. Ostrowski, Kamal D. Mehta
Publikováno v:
Molecular Metabolism, Vol 44, Iss , Pp 101133- (2021)
Objective: Nonalcoholic hepatic steatosis, also known as fatty liver, is a uniform response of the liver to hyperlipidic-hypercaloric diet intake. However, the post-ingestive signals and mechanistic processes driving hepatic steatosis are not well un
Externí odkaz:
https://doaj.org/article/2dd900419f04476babb5d35eeae3d29a
Autor:
Yaoling Shu1, Gumma, Nikhil1, Hassan, Faizule1, Branch, Daniel A.2, Baer, Lisa A.2, Ostrowski, Michael C.3, Stanford, Kristin I.2, Baskin, Kedryn K.2, Mehta, Kamal D.1,4 Mehta.80@osu.edu
Publikováno v:
Journal of Biological Chemistry. Aug2023, Vol. 299 Issue 8, p1-12. 12p.
Publikováno v:
JCI Insight
The signaling mechanisms by which dietary fat and cholesterol signals regulate central pathways of glucose homeostasis are not completely understood. By using a hepatocyte-specific PKCβ-deficient (PKCβHep-/-) mouse model, we demonstrated the role o
Autor:
Kamal D. Mehta, Xianlin Han, Vincenzo Coppola, Faizule Hassan, Kedryn K. Baskin, Michael C. Ostrowski, Yaoling Shu, Neil Mehta
Publikováno v:
Molecular Metabolism
Molecular Metabolism, Vol 44, Iss, Pp 101133-(2021)
Molecular Metabolism, Vol 44, Iss, Pp 101133-(2021)
Objective Nonalcoholic hepatic steatosis, also known as fatty liver, is a uniform response of the liver to hyperlipidic-hypercaloric diet intake. However, the post-ingestive signals and mechanistic processes driving hepatic steatosis are not well und
Publikováno v:
The FASEB Journal. 33
Publikováno v:
Heat Shock Proteins ISBN: 9783030022532
The major inducible 70 kDa heat shock protein (hsp70) is induced by and supports intracellular replication of viruses belonging to diverse families. Paradoxically, this virus-hsp70 interaction is protective in mouse models of viral neurovirulence, en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ff9044291bef60f0586f0ec0ffa5c6b
https://doi.org/10.1007/978-3-030-02254-9_2
https://doi.org/10.1007/978-3-030-02254-9_2
Publikováno v:
Journal of Virology. 87:10668-10678
The major inducible 70-kDa heat shock protein (hsp70) protects against measles virus (MeV) neurovirulence in the mouse that is caused by a cell-associated noncytolytic neuronal infection. Protection is type I interferon (IFN) dependent, and we have e
Autor:
Yuanzheng Gu, Yaoling Shu, Angela W. Corona, Kui Xu, Allen F. Yi, Shannon Chen, Man Luo, John G. Flanagan, Michel L. Tremblay, Gary E. Landreth, Randy J. Nelson, Jerry Silver, Yingjie Shen
Beta-amyloid accumulation and Tau aggregation are hallmarks of Alzheimer's disease, yet their underlying molecular mechanisms remain obscure, hindering therapeutic advances. Here we report that neuronal receptor PTPsigma; mediates both beta-amyloid a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::405b9bc16f6fbb9decd3dffcf3e55895
https://doi.org/10.1101/079806
https://doi.org/10.1101/079806
Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus
Autor:
Laurent Mamelli, Yaoling Shu, Johnny Habchi, Michael Oglesbee, Martin Blackledge, Stéphanie Blangy, Sonia Longhi, Hervé Darbon, Malene Ringkjøbing Jensen
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (15), pp.13583-13602. ⟨10.1074/jbc.M111.219857⟩
Journal of Biological Chemistry, 2011, 286 (15), pp.13583-13602. ⟨10.1074/jbc.M111.219857⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (15), pp.13583-13602. ⟨10.1074/jbc.M111.219857⟩
Journal of Biological Chemistry, 2011, 286 (15), pp.13583-13602. ⟨10.1074/jbc.M111.219857⟩
The Henipavirus genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid that recruits the polymerase complex via the phosphoprotein (P). In a previous study, we reported that in henipaviruses, the N-terminal domain of the phosph