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Biochemical and Biophysical Research Communications|December 5, 1998
TLE, the human homolog of groucho, interacts with AML1 and acts as a repressor of AML1-induced transactivationY Imai, M Kurokawa, K Tanaka, et al.Arteriosclerosis, Thrombosis, and Vascular Biology|February 12, 1999
Polymorphism of the methionine synthase gene : association with homocysteine metabolism and late-onset vascular diseases in the Japanese populationH Morita, H Kurihara, T Sugiyama, et al.Cancer Research|August 15, 1991
Expression of the GLUT1 glucose transporter increases thymidine uptake in Chinese hamster ovary cells at low glucose concentrationsT Asano, Y Shibasaki, J L Lin, et al.Biochemical and Biophysical Research Communications|May 29, 1992
Heterogeneity in smooth muscle cell population accumulating in the neointimas and the media of poststenotic dilatation of the rabbit carotid arteryE Okamoto, K Imataka, J Fujii, et al.The Journal of Clinical Investigation|August 1, 1984
Isozymic changes in myosin of human atrial myocardium induced by overload. Immunohistochemical study using monoclonal antibodiesH Tsuchimochi, M Sugi, M Kuro-o, et al.The American Journal of Physiology|February 1, 1993
Expression of GLUT-4 glucose transporter in unweighted soleus muscle of normal and STZ-induced diabetic ratsH Ishihara, T Asano, H Katagiri, et al.The Journal of Clinical Investigation|January 1, 1988
Heterogeneity of beta-type myosin isozymes in the human heart and regulational mechanisms in their expression. Immunohistochemical study using monoclonal antibodiesH Tsuchimochi, M Kuro-o, H Koyama, et al.The Biochemical Journal|February 1, 1992
Two glucose transporter isoforms are sorted differentially and are expressed in distinct cellular compartmentsY Shibasaki, T Asano, J L Lin, et al.FEBS Letters|February 24, 1992
Glucose binding enhances the papain susceptibility of the intracellular loop of the GLUT1 glucose transporterT Asano, H Katagiri, K Tsukuda, et al.Biochemical and Biophysical Research Communications|April 30, 1991
The glucose transport activity of GLUT1 is markedly decreased by substitution of a single amino acid with a different charge at residue 415H Ishihara, T Asano, H Katagiri, et al.Pageof 301