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Yan Liu

Researcher at Rutgers University

Publications -  13
Citations -  644

Yan Liu is an academic researcher from Rutgers University. The author has contributed to research in topics: Calbindin & Calcitriol receptor. The author has an hindex of 8, co-authored 11 publications receiving 616 citations. Previous affiliations of Yan Liu include University of Medicine and Dentistry of New Jersey.

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Journal ArticleDOI

New insights into the mechanisms of vitamin D action.

TL;DR: A number of exciting discoveries have been made that have enhanced the understanding of mechanisms involved in the pleiotropic actions of 1,25(OH)2D3, including the epithelial calcium channel and in the distal nephron.
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Prevention of glucocorticoid-induced apoptosis in osteocytes and osteoblasts by calbindin-D28k.

TL;DR: It is shown for the first time that calbindin‐D28k can prevent glucocorticoid‐induced bone cell death and the anti‐apoptotic effect of cal bindin‐ D28k involves inhibition of glucose‐induced caspase 3 activation as well as ERK activation.
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Biological actions and mechanism of action of calbindin in the process of apoptosis

TL;DR: The findings suggest that calbindin is capable of directly inhibiting the activity of caspase-3, a common downstream effector of multiple apoptotic signaling pathways, and that this inhibition results in an inhibition of tumor necrosis factor (TNFalpha) and glucocorticoid induced apoptosis in bone cells.
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Calbindin-D28k decreases L-type calcium channel activity and modulates intracellular calcium homeostasis in response to K+ depolarization in a rat beta cell line RINr1046-38.

TL;DR: It is shown for the first time that the calcium binding protein calbindin-D(28k) acts by affecting calcium influx through voltage-dependent calcium channels in RIN pancreatic beta cells to regulate calcium influx via L-type calcium channels.
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Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.

TL;DR: Insight is provided into the role of highly conserved residues in the Crk-SH3-C, suggesting a mechanism for how the linker and the CrK-SH 3-C function in the transactivation of the Abl tyrosine kinase.