Biology Reference
In-Depth Information
Spiotto, M.T., Banh, A., Papandreou, I., Cao, H., Galvez, M.G., Gurtner, G.C., Denko, N.C.,
Le, Q.T., Koong, A.C., 2010. Imaging the unfolded protein response in primary tumors
reveals microenvironments with metabolic variations that predict tumor growth. Cancer
Res. 70, 78-88.
Spruce, B.A., Campbell, L.A., McTavish, N., Cooper, M.A., Appleyard, M.V., O'Neill, M.,
Howie, J., Samson, J., Watt, S., Murray, K., et al., 2004. Small molecule antagonists of the
sigma-1 receptor cause selective release of the death program in tumor and self-reliant
cells and inhibit tumor growth in vitro and in vivo. Cancer Res. 64, 4875-4886.
Sriburi, R., Bommiasamy, H., Buldak, G.L., Robbins, G.R., Frank, M., Jackowski, S., Brewer,
J.W., 2007. Coordinate regulation of phospholipid biosynthesis and secretory pathway
gene expression in XBP-1(S)-induced endoplasmic reticulum biogenesis. J. Biol. Chem.
282, 7024-7034.
Sriburi, R., Jackowski, S., Mori, K., Brewer, J.W., 2004. XBP1: a link between the unfolded
protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell
Biol. 167, 35-41.
Steele, A.D., Hetz, C., Yi, C.H., Jackson, W.S., Borkowski, A.W., Yuan, J., Wollmann,
R.H., Lindquist, S., 2007. Prion pathogenesis is independent of caspase-12. Prion
1, 243-247.
Stefan, C.J., Manford, A.G., Baird, D., Yamada-Hanff, J., Mao, Y., Emr, S.D., 2011. Osh pro-
teins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell.
144, 389-401.
Sterz, J., von Metzler, I., Hahne, J.C., Lamottke, B., Rademacher, J., Heider, U., Terpos, E.,
Sezer, O., 2008. The potential of proteasome inhibitors in cancer therapy. Expert Opin.
Investig. Drugs 17, 879-895.
Stokin, G.B., Lillo, C., Falzone, T.L., Brusch, R.G., Rockenstein, E., Mount, S.L., Raman, R.,
Davies, P., Masliah, E., Williams, D.S., et al., 2005. Axonopathy and transport deficits early
in the pathogenesis of Alzheimer's disease. Science 307, 1282-1288.
Strehler, E.E., Treiman, M., 2004. Calcium pumps of plasma membrane and cell interior.
Curr. Mol. Med. 4, 323-335.
Strøm, C.C., Aplin, M., Ploug, T., Christoffersen, T.E.H., Langfort, J., Viese, M., Galbo, H.,
Haunsø, S., Sheikh, S.P., 2005. Expression profiling reveals differences in metabolic gene
expression between exercise-induced cardiac effects and maladaptive cardiac hypertro-
phy. FEBS J. 272, 2684-2695.
Støy, J., Edghill, E.L., Flanagan, S.E.,Ye, H., Paz,V.P., Pluzhnikov, A., Below, J.E., Hayes, M.G.,
Cox, N.J., Lipkind, G.M., et al., 2007. Insulin gene mutations as a cause of permanent
neonatal diabetes. Proc. Natl. Acad. Sci. U.S.A. 104, 15040-15044.
Sun, J., Yamaguchi, N., Xu, L., Eu, J.P., Stamler, J.S., Meissner, G., 2008. Regulation of the
cardiac muscle ryanodine receptor by O(2) tension and S-nitrosoglutathione. Biochem-
istry 47, 13985-13990.
Sutendra, G., Dromparis, P., Wright, P., Bonnet, S., Haromy, A., Hao, Z., McMurtry, M.S.,
Michalak, M., Vance, J.E., Sessa, W.C., et al., 2011. The role of Nogo and the mito-
chondria-endoplasmic reticulum unit in pulmonary hypertension. Sci. Transl. Med. 3
(88ra55).
Swanson, R., Locher, M., Hochstrasser, M., 2001. A conserved ubiquitin ligase of the nuclear
envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2
repressor degradation. Genes Dev. 15, 2660-2674.
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M.R., Cavagna, D., Nagy,
A.I., Balla, T., Rizzuto, R., 2006. Chaperone-mediated coupling of endoplasmic reticu-
lum and mitochondrial Ca2+ channels. J. Cell Biol. 175, 901-911.
Tabas, I., Ron, D., 2011. Integrating the mechanisms of apoptosis induced by endoplasmic
reticulum stress. Nat. Cell Biol. 13, 184-190.
Tao, J., Zhu, W., Li, Y., Xin, P., Li, J., Liu, M., Li, J., Redington, A.N., Wei, M., 2011. Ape-
lin-13 protects the heart against ischemia-reperfusion injury through inhibition of
Search WWH ::




Custom Search