@article{lin_leung_hsu_sheu_2009, title={Factors that influence the effectiveness of trail surfacing in minimizing recreational impact: A sudy in Yangmingshan National Park [in Chinese]}, volume={19}, number={4}, journal={Journal of National Parks (Taiwan)}, author={Lin, H.-C and Leung, Y.-F and Hsu, S.-I and Sheu, J.-E}, year={2009}, pages={65–79} }
 @article{lee_albanese_fu_m d'amico_lin_watanabe_haines_siegel_hung_yarden_et al._2000, title={Cyclin D1 is required for transformation by activated Neu and is induced through an E2F-dependent signaling pathway}, volume={20}, ISSN={["1098-5549"]}, DOI={10.1128/MCB.20.2.672-683.2000}, abstractNote={ABSTRACT The neu (c-erbB-2) proto-oncogene encodes a tyrosine kinase receptor that is overexpressed in 20 to 30% of human breast tumors. Herein, cyclin D1 protein levels were increased in mammary tumors induced by overexpression of wild-type Neu or activating mutants of Neu in transgenic mice and in MCF7 cells overexpressing transforming Neu. Analyses of 12 Neu mutants in MCF7 cells indicated important roles for specific C-terminal autophosphorylation sites and the extracellular domain in cyclin D1 promoter activation. Induction of cyclin D1 by NeuT involved Ras, Rac, Rho, extracellular signal-regulated kinase, c-Jun N-terminal kinase, and p38, but not phosphatidylinositol 3-kinase. NeuT induction of the cyclin D1 promoter required the E2F and Sp1 DNA binding sites and was inhibited by dominant negative E2F-1 or DP-1. Neu-induced transformation was inhibited by a cyclin D1 antisense or dominant negative E2F-1 construct in Rat-1 cells. Growth of NeuT-transformed mammary adenocarcinoma cells in nude mice was blocked by the cyclin D1 antisense construct. These results demonstrate that E2F-1 mediates a Neu-signaling cascade tocyclin D1 and identify cyclin D1 as a critical downstream target of neu-induced transformation.}, number={2}, journal={MOLECULAR AND CELLULAR BIOLOGY}, author={Lee, RJ and Albanese, C and Fu, MF and M D'Amico and Lin, B and Watanabe, G and Haines, GK and Siegel, PM and Hung, MC and Yarden, Y and et al.}, year={2000}, month={Jan}, pages={672–683} }
 @article{lin_heaton_1999, title={Mutational analyses of the putative calcium binding site and hinge of the turnip crinkle virus coat protein}, volume={259}, ISSN={["0042-6822"]}, DOI={10.1006/viro.1999.9742}, abstractNote={The turnip crinkle carmovirus (TCV) coat protein (CP) is folded into R (RNA-binding), S (shell), and P (protruding) domains. The S domain is an eight-stranded beta barrel common to the coat protein subunits of most RNA viruses. A five-amino-acid hinge connects the S and P domains. In assembled particles, each pair of CP subunits is thought to bind a single calcium ion through interactions with three residues of one subunit and two residues of a neighboring subunit. These five residues comprise the putative calcium-binding site (CBS). The putative CBS and hinge are adjacent to one another. Mutations were introduced into the putative CBS or hinge in an effort to further determine the biological functions of TCV CP. One putative CBS mutant, TCV-M32, exhibited wild-type cell-to-cell movement but failed to move systemically in Nicotiana benthamiana, and particles were not detected. Another putative CBS mutant, TCV-M23, exhibited deficient cell-to-cell movement but particles accumulated in isolated protoplasts. Two other putative CBS mutants, TCV-M22 and -M33, showed wild-type cell-to-cell and systemic movement but elicited mild systemic symptoms that were somewhat delayed. All of the hinge mutants exhibited wild-type movement but some elicited non-wild-type symptoms. Point mutations in the putative CBS or hinge appear to alter virus-ion interactions, secondary structure, or particle conformation, thereby affecting interactions between the CP and plant hosts.}, number={1}, journal={VIROLOGY}, author={Lin, B and Heaton, LA}, year={1999}, month={Jun}, pages={34–42} }