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6篇 您的检索式:作者名="QZHANG"
    题名 作者 年代 出处 被引量
1A Fully Integrated CMOS Readout Circuit for Particle Detectors 显示文摘QZhang Yacong Chen Zhongjian Lu Wengao 2007Chinese Journal of Semiconductors2007,28,2:1
2Usingfunctionalmagneticresonanceima-gingtoexplorethepossiblemechanismoftheactionofacupunctureatDazhong(KI4)onthefunctionalcerebralregionsofhealthyvolun-teers显示文摘QZhang ALi JYue etal 2015Internalmedicinejournal2015,45,6:1
3Theshapleyfunctionforfuzzycooperativegames with multilinearextensionform显示文摘FY MENG QZHANG 2010AppliedMathematicsLetters2010,23,5:1
4Ludemarin poly- meraseehain reaction am plification for the detection of portion parvovirus显示文摘Molitor T W oraveerakul K Qzhang Q 1991Journal of Rologieal Methods1991,32,:1
5Tn5-FISH,a novel cytogenetic method to image chromatin interactions with sub-kilobase resolution显示文摘There is an increasing interest in understanding how three-dimensional(3D)organization of the genome is regulated.Different strategies have been employed to identify genome-wide chromatin interactions.However,due to current limitations in resolving genomic contacts,visualization and validation of these genomic loci with sub-kilobase resolution remain unsolved to date.Here,we describe Tn5 transposase-based Fluorescencein situhybridization(Tn5-FISH),a PCR-based,cost-effective imaging method,which can co-localize the genomic loci with sub-kilobase resolution,dissect genome architecture,and verify chromatin interactions detected by chromatin configuration capture(3C)-derived methods.To validate this method,short-range interactions in keratin-encoding gene(KRT)locus in topologically associated domain(TAD)were imaged by triple-color Tn5-FISH,indicating that Tn5-FISH is very useful to verify short-range chromatin interactions inside the contact domain and TAD.Therefore,Tn5-FISH can be a powerful molecular tool for the clinical detection of cytogenetic changes in numerous genetic diseases such as cancers.Jing Niu Xu Zhang Li Guipeng Pixi Yan Qing Yan Qionghai Dai Dayong Jin Xiaohua Shen Jichang Wang Michael QZhang Juntao Gao 2020Journal of Genetics and Genomics2020,47,12:0
6Ttm50 facilitates calpain activation by anchoring it to calcium stores and increasing its sensitivity to calcium显示文摘Calcium-dependent proteolytic calpains are implicated in a variety of physiological processes,as well as pathologies associated with calcium overload.However,the mechanism by which calpain is activated remains elusive since intracellular calcium levels under physiological conditions do not reach the high concentration range required to trigger calpain activation.From a candidate screening using the abundance of the calpain target glutamate receptor GluRIIA at the Drosophila neuromuscular junction as a readout,we uncovered that calpain activity was inhibited upon knockdown of Ttm50,a subunit of the Tim23 complex known to be involved in the import of proteins across the mitochondrial inner membrane.Unexpectedly,Ttm50 and calpain are co-localized at calcium stores Golgi and endoplasmic reticulum(ER),and Ttm50 interacts with calpain via its C-terminal domain.This interaction is required for calpain localization at Golgi/ER,and increases calcium sensitivity of calpain by roughly an order of magnitude.Our findings reveal the regulation of calpain activation by Ttm50,and shed new light on calpain-associated pathologies.Elsayed Metwally Guoli Zhao Qifu Wang Yong QZhang 2021Cell Research2021,31,4:0
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