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5篇 您的检索式：作者名="Thermou"

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		题名	作者	年代	出处	被引量
	1	Seismic design and performance of composite frames显示文摘	Thermou G E Elnashai A S Plumier A Doneux C		0，，：	1
	2	Seismic Design and Performance of Composite Frames显示文摘	THERMOU G E ELNASHAI A S PLUMIER A	2004	Journal of Constructional Steel Research2004，60，1：	1
	3	Flexural be- havior of brittle RC members rehabilitated with concrete jacketing显示文摘	Thermou G E Pantazopoulou S J Elnashai A S	2007	Journal of StrucLural Engineering2007，133，10：	1
	4	Seismic design and performance of composite frames 显示文摘	Thermou G E Elnashai A S Plumier A	2004	Journal of Constructional Steel Research2004，60，：	1
	5	A single synonymous mutation determines the phosphorylation and stability of the nascent protein显示文摘p53 is an intrinsically disordered protein with a large number of post-translational modifications and interacting partners.The hierarchical order and subcellular location of these events are still poorly understood.The activation of p53 during the DNA damage response(DDR)requires a switch in the activity of the E3 ubiquitin ligase MDM2 from a negative to a positive regulator of p53.This is mediated by the ATM kinase that regulates the binding of MDM2 to the p53 mRNA facilitating an increase in p53 synthesis.Here we show that the binding of MDM2 to the p53 mRNA brings ATM to the p53 polysome where it phosphorylates the nascent p53 at serine 15 and prevents MDM2-mediated degradation of p53.A single synonymous mutation in p53 codon 22(L22L)prevents the phosphorylation of the nascent p53 protein and the stabilization of p53 following genotoxic stress.The ATM trafficking from the nucleus to the p53 polysome is mediated by MDM2,which requires its interaction with the ribosomal proteins RPL5 and RPL11.These results show how the ATM kinase phosphorylates the p53 protein while it is bang synthesized and offer a novel mechanism whereby a single synonymous mutation controls the stability and activity of the encoded protein.	Konstantinos Karakostis Sivakumar Vadivel Gnanasundram Ignacio Lopez Aikaterini Thermou Lixiao Wang Karin Nylander Vanesa Ollvares-Iliana Robin Fahraeus	2019	Journal of Molecular Cell Biology2019，11，3：	1

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