UV induces phosphorylation of protein kinase B (Akt) at Ser-473 and Thr-308 in mouse epidermal C1 41 cells through hydrogen peroxide (Q23911187)

HELD

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25 September 2023

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29 March 2020

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29 March 2020

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29 March 2020

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29 March 2020

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29 March 2020

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6

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Val Vallyathan

7

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Chuanshu Huang

C. Huang

1

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Xianglin Shi

8

X. Shi

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Liying Wang

5

L. Wang

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Jingxia Li

2

J. Li

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Min Ding

3

M. Ding

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Stephen S. Leonard

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full work available at URL

S. S. Leonard

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language of work or name

English

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publication date

26 October 2001

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http://www.jbc.org/cgi/content/full/276/43/40234

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29 March 2020

Journal of Biological Chemistry

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volume

276

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page(s)

40234-40240

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issue

43

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on focus list of Wikimedia project

Wikimedia–NIOSH collaboration

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2 February 2024

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p38 kinase mediates UV-induced phosphorylation of p53 protein at serine 389.

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NF-kappa B activation by ultraviolet light not dependent on a nuclear signal.

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Signal transduction through atypical PKCs, but not the EGF receptor, is necessary for UVC-induced AP-1 activation in immortal murine cells

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Cellular survival: a play in three Akts

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A putative modular domain present in diverse signaling proteins

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The PH domain: a common piece in the structural patchwork of signalling proteins

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Hydroxyl radical generation in the NADH/microsomal reduction of vanadate

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Requirement for generation of H2O2 for platelet-derived growth factor signal transduction

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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate

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A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain.

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