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The Shocks in the Interbank Market: An Analysis of China and the US
Jiangang Peng,Ziwei Fei,Xiaoquan Jiang,Li Zeng 한국증권학회 2015 Asia-Pacific Journal of Financial Studies Vol.44 No.6
We compare the contagion risk in the interbank market between China and the United States during the period from 2011 to 2013. Applying simulation method, we find that the conta- gion risk of an individual bank shock in the US interbank market is relatively lower than that in China during the period. For a group bank shock, we find that the group with the lowest capital adequacy ratio in China induces a serious contagion, while the group with the highest concentration degree in the US induces a mild contagion. One potential reason is that the additional capital of most commercial banks in China is relatively lower than that of the US and most banks in China highly depend on the interbank market for acquiring liquidity or income.
Wu, Jing,Tan, Xinyu,Peng, Xiaozhong,Yuan, Jiangang,Qiang, Boqin Korean Society for Biochemistry and Molecular Biol 2003 Journal of biochemistry and molecular biology Vol.36 No.4
For better understanding of functions of the Calcyclin Binding Protein (CacyBP) and exploring its possible roles in neuronal differentiation, the subcellular localization of human CacyBP was examined in retinoic acid(RA)-induced and uninduced neuroblastoma SH-SY5Y cells. Immunostaining indicated that CacyBP was present in the cytoplasm of uninduced SH-SY5Y cells, in which the resting $Ca^{2+}$ concentration was relatively lower than that of RA-induced cells. After the RA induction, immunostaining was seen in both the nucleus and cytoplasm. In the RA-induced differentiated SH-SY5Y cells, CacyBP was phosphorylated on serine residue(s), while it existed in a dephosphorylated form in normal (uninduced) cells. Thus, the phosphorylation of CacyBP occurs when it is translocated to the nuclear region. The translocation of CacyBP during the RA-induced differentiation of SH-SY5Y cells suggested that this protein might play a role in neuronal differentiation.
ShcD interacts with TrkB via its PTB and SH2 domains and regulates BDNF-induced MAPK activation
( Yuangang You ),( Weiqi Li ),( Yanhua Gong ),( Bin Yin ),( Boqin Qiang ),( Jiangang Yuan ),( Xiaozhong Peng ) 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.7
Neurotrophins regulate many aspects of neuronal function through activation of the high affinity Trk receptors. Shc family proteins are implicated in the coupling of RTK to the Ras/mitogen- activated protein kinase signaling cascade. Here we report that the fourth Shc family member, ShcD, associates with TrkB receptor and regulates BDNF-induced MAPK activation. Yeast two-hybrid assay and Co-IP experiments demonstrate ShcD interacts with TrkB in a kinase-activity-dependent manner. Confocal analysis shows ShcD cololizes well with TrkB in transfected 293T cells. Subsequent mapping experiments and mutational analysis indicate that both PTB and SH2 domains are capable of binding to TrkB and PTB domain binds to TrkB NPQY motif. Furthermore, ShcD is involved in BDNF-induced MAPK activation. In summary, we demonstrate that ShcD is a substrate of TrkB and mediates TrkB downstream signaling pathway. [BMB reports 2010; 43(7): 485-490]