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The Crystal Structure of Human IRE1 Luminal Domain Reveals a Conserved Dimerization Interface Required for Activation of the Unfolded Protein Response
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Nitrogen Doped Graphene-Core/shell CdS@TiO2 for Direct Electrochemistry of Hemoglobin and Hydrogen Peroxide Biosensor Application
Shi, En-yong, She, Yu, Yao, Ji-ping, Zou, Xiao-jian, Liu, Chuan-yin
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electrochemical behavior of p-benzenediol on a self-assembled monolayers Pt electrode modified with N-(2-mercapto-1,3,4-thiadiazol-5-yl)-N′-(4-substituted-arylacetyl) urea
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Elucidating fluorination effect on benzodithiophene-based donor material in organic solar cells
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Non-compaction cardiomyopathy in a 5-generation Chinese family
Ding, Zhong-ru, Huang, Guo-ming, Wang, Hong-ru, Tu, Xiao-wen, Liu, Chuan-yin
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Structure and Intermolecular Interactions of the Luminal Dimerization Domain of Human IRE1α
Liu, Chuan Yin, Xu, Zhaohui, Kaufman, Randal J.
Published in The Journal of biological chemistry (16.05.2003)
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The Protein Kinase/Endoribonuclease IRE1α That Signals the Unfolded Protein Response Has a Luminal N-terminal Ligand-independent Dimerization Domain
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Published in The Journal of biological chemistry (24.05.2002)
Published in The Journal of biological chemistry (24.05.2002)
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