Difference between revisions of "Team:Tuebingen/References"
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<h2> References</h2> | <h2> References</h2> | ||
| − | <p>< | + | <p>Ando, R., Mizuno, H., & Miyawaki, A. (2004). Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting. Science, 306(5700), 1370-1373. doi: 10.1126/science.1102506</p> |
| − | <p>< | + | <p>Andresen, M., Stiel, A. C., Trowitzsch, S., Weber, G., Eggeling, C., Wahl, M. C., . . . Jakobs, S. (2007). Structural basis for reversible photoswitching in Dronpa. Proc Natl Acad Sci U S A, 104(32), 13005-13009. doi: 10.1073/pnas.0700629104</p> |
| − | <p> | + | <p>Appleby, J. H., Zhou, K., Volkmann, G., & Liu, X. Q. (2009). Novel split intein for trans-splicing synthetic peptide onto C terminus of protein. J Biol Chem, 284(10), 6194-6199. doi: 10.1074/jbc.M805474200</p> |
| − | <p>< | + | <p>Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., . . . Kaplan, J. (1994). The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell, 76(2), 403-410. </p> |
| − | <p>< | + | <p>Bennetzen, J. L., & Hall, B. D. (1982). The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem, 257(6), 3018-3025. </p> |
| − | + | <p>Bolanos-Garcia, V. M., & Davies, O. R. (2006). Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography. Biochim Biophys Acta, 1760(9), 1304-1313. doi: 10.1016/j.bbagen.2006.03.027</p> | |
| + | <p>Entian, K. D., Meurer, B., Kohler, H., Mann, K. H., & Mecke, D. (1987). Studies on the regulation of enolases and compartmentation of cytosolic enzymes in Saccharomyces cerevisiae. Biochim Biophys Acta, 923(2), 214-221. </p> | ||
| + | <p>Hall, M. P., Unch, J., Binkowski, B. F., Valley, M. P., Butler, B. L., Wood, M. G., . . . Wood, K. V. (2012). Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate. ACS Chem Biol, 7(11), 1848-1857. doi: 10.1021/cb3002478</p> | ||
| + | <p>Hippler, M. (2003). Photochemical kinetics: Reaction orders and analogies with molecular beam scattering and cavity ring-down experiments. Journal of chemical education, 80(9), 1074.</p> | ||
| + | <p>Kim, H., & Gelenbe, E. (2012). Stochastic gene expression modeling with Hill function for switch-like gene responses. IEEE/ACM Trans Comput Biol Bioinform, 9(4), 973-979. doi: 10.1109/TCBB.2011.153</p> | ||
| + | <p>Kolodziej, E. P., Gray, J. L., & Sedlak, D. L. (2003). Quantification of steroid hormones with pheromonal properties in municipal wastewater effluent. Environ Toxicol Chem, 22(11), 2622-2629. </p> | ||
| + | <p>Kupchak, B. R., Garitaonandia, I., Villa, N. Y., Mullen, M. B., Weaver, M. G., Regalla, L. M., . . . Lyons, T. J. (2007). Probing the mechanism of FET3 repression by Izh2p overexpression. Biochim Biophys Acta, 1773(7), 1124-1132. doi: 10.1016/j.bbamcr.2007.04.003</p> | ||
| + | <p>Liu, Z., & Patino, R. (1993). High-affinity binding of progesterone to the plasma membrane of Xenopus oocytes: characteristics of binding and hormonal and developmental control. Biol Reprod, 49(5), 980-988.</p> | ||
| + | <p>Lutfiyya, L. L., & Johnston, M. (1996). Two zinc-finger-containing repressors are responsible for glucose repression of SUC2 expression. Mol Cell Biol, 16(9), 4790-4797. </p> | ||
| + | <p>Lyons, T. J., Villa, N. Y., Regalla, L. M., Kupchak, B. R., Vagstad, A., & Eide, D. J. (2004). Metalloregulation of yeast membrane steroid receptor homologs. Proc Natl Acad Sci U S A, 101(15), 5506-5511. doi: 10.1073/pnas.0306324101</p> | ||
| + | <p>Mizuno, H., Dedecker, P., Ando, R., Fukano, T., Hofkens, J., & Miyawaki, A. (2010). Higher resolution in localization microscopy by slower switching of a photochromic protein. Photochem Photobiol Sci, 9(2), 239-248. doi: 10.1039/b9pp00124g</p> | ||
| + | <p>Mizuno, H., Mal, T. K., Walchli, M., Kikuchi, A., Fukano, T., Ando, R., . . . Miyawaki, A. (2008). Light-dependent regulation of structural flexibility in a photochromic fluorescent protein. Proc Natl Acad Sci U S A, 105(27), 9227-9232. doi: 10.1073/pnas.0709599105</p> | ||
| + | <p>Nagy, A. (2000). Cre recombinase: the universal reagent for genome tailoring. Genesis, 26(2), 99-109. </p> | ||
| + | <p>Sikorski, R. S., & Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122(1), 19-27.</p> | ||
| + | <p>Smith, J. L., Kupchak, B. R., Garitaonandia, I., Hoang, L. K., Maina, A. S., Regalla, L. M., & Lyons, T. J. (2008). Heterologous expression of human mPRα, mPRβ and mPRγ in yeast confirms their ability to function as membrane progesterone receptors. steroids, 73(11), 1160-1173. </p> | ||
| + | <p>Tang, Y. T., Hu, T., Arterburn, M., Boyle, B., Bright, J. M., Emtage, P. C., & Funk, W. D. (2005). PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif. J Mol Evol, 61(3), 372-380. doi: 10.1007/s00239-004-0375-2</p> | ||
| + | <p>Zhou, X. X., Chung, H. K., Lam, A. J., & Lin, M. Z. (2012). Optical control of protein activity by fluorescent protein domains. Science, 338(6108), 810-814. doi: 10.1126/science.1226854</p> | ||
</div> | </div> | ||
</html> | </html> | ||
Revision as of 01:56, 19 September 2015
References
Ando, R., Mizuno, H., & Miyawaki, A. (2004). Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting. Science, 306(5700), 1370-1373. doi: 10.1126/science.1102506
Andresen, M., Stiel, A. C., Trowitzsch, S., Weber, G., Eggeling, C., Wahl, M. C., . . . Jakobs, S. (2007). Structural basis for reversible photoswitching in Dronpa. Proc Natl Acad Sci U S A, 104(32), 13005-13009. doi: 10.1073/pnas.0700629104
Appleby, J. H., Zhou, K., Volkmann, G., & Liu, X. Q. (2009). Novel split intein for trans-splicing synthetic peptide onto C terminus of protein. J Biol Chem, 284(10), 6194-6199. doi: 10.1074/jbc.M805474200
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., . . . Kaplan, J. (1994). The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell, 76(2), 403-410.
Bennetzen, J. L., & Hall, B. D. (1982). The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem, 257(6), 3018-3025.
Bolanos-Garcia, V. M., & Davies, O. R. (2006). Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography. Biochim Biophys Acta, 1760(9), 1304-1313. doi: 10.1016/j.bbagen.2006.03.027
Entian, K. D., Meurer, B., Kohler, H., Mann, K. H., & Mecke, D. (1987). Studies on the regulation of enolases and compartmentation of cytosolic enzymes in Saccharomyces cerevisiae. Biochim Biophys Acta, 923(2), 214-221.
Hall, M. P., Unch, J., Binkowski, B. F., Valley, M. P., Butler, B. L., Wood, M. G., . . . Wood, K. V. (2012). Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate. ACS Chem Biol, 7(11), 1848-1857. doi: 10.1021/cb3002478
Hippler, M. (2003). Photochemical kinetics: Reaction orders and analogies with molecular beam scattering and cavity ring-down experiments. Journal of chemical education, 80(9), 1074.
Kim, H., & Gelenbe, E. (2012). Stochastic gene expression modeling with Hill function for switch-like gene responses. IEEE/ACM Trans Comput Biol Bioinform, 9(4), 973-979. doi: 10.1109/TCBB.2011.153
Kolodziej, E. P., Gray, J. L., & Sedlak, D. L. (2003). Quantification of steroid hormones with pheromonal properties in municipal wastewater effluent. Environ Toxicol Chem, 22(11), 2622-2629.
Kupchak, B. R., Garitaonandia, I., Villa, N. Y., Mullen, M. B., Weaver, M. G., Regalla, L. M., . . . Lyons, T. J. (2007). Probing the mechanism of FET3 repression by Izh2p overexpression. Biochim Biophys Acta, 1773(7), 1124-1132. doi: 10.1016/j.bbamcr.2007.04.003
Liu, Z., & Patino, R. (1993). High-affinity binding of progesterone to the plasma membrane of Xenopus oocytes: characteristics of binding and hormonal and developmental control. Biol Reprod, 49(5), 980-988.
Lutfiyya, L. L., & Johnston, M. (1996). Two zinc-finger-containing repressors are responsible for glucose repression of SUC2 expression. Mol Cell Biol, 16(9), 4790-4797.
Lyons, T. J., Villa, N. Y., Regalla, L. M., Kupchak, B. R., Vagstad, A., & Eide, D. J. (2004). Metalloregulation of yeast membrane steroid receptor homologs. Proc Natl Acad Sci U S A, 101(15), 5506-5511. doi: 10.1073/pnas.0306324101
Mizuno, H., Dedecker, P., Ando, R., Fukano, T., Hofkens, J., & Miyawaki, A. (2010). Higher resolution in localization microscopy by slower switching of a photochromic protein. Photochem Photobiol Sci, 9(2), 239-248. doi: 10.1039/b9pp00124g
Mizuno, H., Mal, T. K., Walchli, M., Kikuchi, A., Fukano, T., Ando, R., . . . Miyawaki, A. (2008). Light-dependent regulation of structural flexibility in a photochromic fluorescent protein. Proc Natl Acad Sci U S A, 105(27), 9227-9232. doi: 10.1073/pnas.0709599105
Nagy, A. (2000). Cre recombinase: the universal reagent for genome tailoring. Genesis, 26(2), 99-109.
Sikorski, R. S., & Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122(1), 19-27.
Smith, J. L., Kupchak, B. R., Garitaonandia, I., Hoang, L. K., Maina, A. S., Regalla, L. M., & Lyons, T. J. (2008). Heterologous expression of human mPRα, mPRβ and mPRγ in yeast confirms their ability to function as membrane progesterone receptors. steroids, 73(11), 1160-1173.
Tang, Y. T., Hu, T., Arterburn, M., Boyle, B., Bright, J. M., Emtage, P. C., & Funk, W. D. (2005). PAQR proteins: a novel membrane receptor family defined by an ancient 7-transmembrane pass motif. J Mol Evol, 61(3), 372-380. doi: 10.1007/s00239-004-0375-2
Zhou, X. X., Chung, H. K., Lam, A. J., & Lin, M. Z. (2012). Optical control of protein activity by fluorescent protein domains. Science, 338(6108), 810-814. doi: 10.1126/science.1226854