| [1] Pruessmeyer J, Ludwig A. The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer. Semin Cell Dev Biol, 2009, 20(2): 164-174.[2] Lichtenthaler SF. Alpha-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potential. J Neurochem, 2011, 116(1): 10-21.[3] Kuhn PH, Wang HH, Dislich B, Colombo A, Zeitschel U, Ellwart JW, Kremmer E, Roβner S, Lichtenthaler SF. ADAM10 is the physiologically relevant, constitutive α-secretase of the amyloid precursor protein in primary neurons. EMBO J, 2010, 29(17): 3020-3032.[4] Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, Snellinx A, Craessaerts K, Thathiah A, Tesseur I, Bartsch U, Weskamp G, Blobel CP, Glatzel M, De Strooper B, Saftig P. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci, 2010, 30(14): 4833-4844.[5] Kim M, Suh J, Romano D, Truong MH, Mullin K, Hooli B, Norton D, Tesco G, Elliott K, Wagner SL, Moir RD, Becker KD, Tanzi RE. Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate α-secretase activity. Hum Mol Genet, 2009, 18(20): 3987- 3996.[6] Prinzen C, Trümbach D, Wurst W, Endres K, Postina R, Fahrenholz F. Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice. BMC Genomics, 2009, 10: 66.[7] Parkin E, Harris B. A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10. J Neurochem, 2009, 108(6): 1464-1479.[8] Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Konietzko U, Reiss K, Maes E, Snellinx A, Serneels L, Nyabi O, Annaert W, Saftig P, Hartmann D, De Strooper B. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase. J Biol Chem, 2009, 284(17): 11738-11747.[9] 尹海芳, 李宁, 王秋菊. 基因敲除鼠疾病模型的研究进展. 遗传, 2002, 24(4): 463-469.[10] Altmeppen HC, Prox J, Puig B, Kluth MA, Bernreuther C, Thurm D, Jorissen E, Petrowitz B, Bartsch U, de Strooper B, Saftig P, Glatzel M. Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo. BMC Mol Neurodegener, 2011, 6: 36.[11] Weber S, Niessen MT, Prox J, Lüllmann-Rauch R, Schmitz A, Schwanbeck R, Blobel CP, Jorissen E, de Strooper B, Niessen CM, Saftig P. The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling. Development, 2011, 138(3): 495-505.[12] Zhang C, Tian L, Chi CW, Wu XH, Yang X, Han M, Xu T, Zhuang Y, Deng KJ. Adam10 is essential for early embryonic cardiovascular development. Dev Dyn, 2010, 239(10): 2594-2602.[13] Glomski K, Monette S, Manova K, de Strooper B, Saftig P, Blobel CP. Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures. Blood, 2011, 118(4): 1163-1174.[14] Gibb DR, El Shikh M, Kang DJ, Rowe WJ, El Sayed R, Cichy J, Yagita H, Tew JG, Dempsey PJ, Crawford HC, Conrad DH. ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo. J Exp Med, 2010, 207(3): 623-635.[15] Tian L, Wu XH, Chi CW, Han M, Xu T, Zhuang Y. ADAM10 is essential for proteolytic activation of Notch during thymocyte development. Int Immunol, 2008, 20(9): 1181-1187.[16] Hartmann D, de Strooper B, Serneels L, Craessaerts K, Herreman A, Annaert W, Umans L, Lübke T, Lena Illert A, von Figura K, Saftig P. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. Hum Mol Genet, 2002, 11(21): 2615-2624.[17] 徐瑛, 周常文, 林炤华, 柯琦. CaMKⅡα基因启动子的克隆和神经细胞特异性Cre表达载体的构建. 中国优生与遗传杂志, 2008, 1 |
