Journal articles on the topic 'Filensin'
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Brunkener, M., and S. D. Georgatos. "Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells." Journal of Cell Science 103, no. 3 (November 1, 1992): 709–18. http://dx.doi.org/10.1242/jcs.103.3.709.
Full textRemington, S. G. "Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins." Journal of Cell Science 105, no. 4 (August 1, 1993): 1057–68. http://dx.doi.org/10.1242/jcs.105.4.1057.
Full textGoulielmos, G., S. Remington, F. Schwesinger, S. D. Georgatos, and F. Gounari. "Contributions of the structural domains of filensin in polymer formation and filament distribution." Journal of Cell Science 109, no. 2 (February 1, 1996): 447–56. http://dx.doi.org/10.1242/jcs.109.2.447.
Full textMerdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. "Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell." Journal of Cell Biology 115, no. 2 (October 15, 1991): 397–410. http://dx.doi.org/10.1083/jcb.115.2.397.
Full textGounari, F., A. Merdes, R. Quinlan, J. Hess, P. G. FitzGerald, C. A. Ouzounis, and S. D. Georgatos. "Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins." Journal of Cell Biology 121, no. 4 (May 15, 1993): 847–53. http://dx.doi.org/10.1083/jcb.121.4.847.
Full textMerdes, A., F. Gounari, and S. D. Georgatos. "The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin." Journal of Cell Biology 123, no. 6 (December 15, 1993): 1507–16. http://dx.doi.org/10.1083/jcb.123.6.1507.
Full textGoulielmos, G., F. Gounari, S. Remington, S. Müller, M. Häner, U. Aebi, and S. D. Georgatos. "Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells." Journal of Cell Biology 132, no. 4 (February 15, 1996): 643–55. http://dx.doi.org/10.1083/jcb.132.4.643.
Full textSandilands, A., A. R. Prescott, J. M. Carter, A. M. Hutcheson, R. A. Quinlan, J. Richards, and P. G. FitzGerald. "Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation." Journal of Cell Science 108, no. 4 (April 1, 1995): 1397–406. http://dx.doi.org/10.1242/jcs.108.4.1397.
Full textFischer, R. S., R. A. Quinlan, and V. M. Fowler. "Tropomodulin binds to filensin intermediate filaments." FEBS Letters 547, no. 1-3 (June 26, 2003): 228–32. http://dx.doi.org/10.1016/s0014-5793(03)00711-7.
Full textGeorgatos, S. D., F. Gounari, G. Goulielmos, and U. Aebi. "To bead or not to bead? Lens-specific intermediate filaments revisited." Journal of Cell Science 110, no. 21 (November 1, 1997): 2629–34. http://dx.doi.org/10.1242/jcs.110.21.2629.
Full textMasaki, Shigeo, Yusuke Kamachi, Roy A. Quinlan, Satoshi Yonezawa, and Hisato Kondoh. "Identification and functional analysis of the mouse lens filensin gene promoter." Gene 214, no. 1-2 (July 1998): 77–86. http://dx.doi.org/10.1016/s0378-1119(98)00230-3.
Full textCarter, J. "Classification of CP49 and filensin: two lens specific intermediate filament proteins." Vision Research 35, no. 1 (October 1995): S196. http://dx.doi.org/10.1016/0042-6989(95)98757-z.
Full textWang, Zhen, Joy E. Obidike, and Kevin L. Schey. "Posttranslational Modifications of the Bovine Lens Beaded Filament Proteins Filensin and CP49." Investigative Opthalmology & Visual Science 51, no. 3 (March 1, 2010): 1565. http://dx.doi.org/10.1167/iovs.09-4565.
Full textAlizadeh, Azita, John Clark, Teri Seeberger, John Hess, Tom Blankenship, and Paul G. FitzGerald. "Targeted Deletion of the Lens Fiber Cell–Specific Intermediate Filament Protein Filensin." Investigative Opthalmology & Visual Science 44, no. 12 (December 1, 2003): 5252. http://dx.doi.org/10.1167/iovs.03-0224.
Full textGounari, Fotini, Niki Karagianni, Antoaneta Mincheva, Peter Lichter, Spyros D. Georgatos, and Volker Schirrmacher. "The mouse filensin gene: structure and evolutionary relation to other intermediate filament genes." FEBS Letters 413, no. 2 (August 18, 1997): 371–78. http://dx.doi.org/10.1016/s0014-5793(97)00937-x.
Full textCarter, J. M., S. V. Duff, W. H. I. McLean, A. R. Prescott, P. S. Wallace, and R. A. Quinlan. "P 218 Classification of CP49 and filensin: Two lens specific intermediate filament proteins." Vision Research 35 (October 1995): S196. http://dx.doi.org/10.1016/0042-6989(95)90534-0.
Full textChaves, Jose M., Ratna Gupta, Kiran Srivastava, and Om Srivastava. "Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin." Biochemical and Biophysical Research Communications 494, no. 1-2 (December 2017): 402–8. http://dx.doi.org/10.1016/j.bbrc.2017.09.088.
Full textRose, Kristie M. Lindsey, Robert G. Gourdie, Alan R. Prescott, Roy A. Quinlan, Rosalie K. Crouch, and Kevin L. Schey. "The C Terminus of Lens Aquaporin 0 Interacts with the Cytoskeletal Proteins Filensin and CP49." Investigative Opthalmology & Visual Science 47, no. 4 (April 1, 2006): 1562. http://dx.doi.org/10.1167/iovs.05-1313.
Full textWang, Zhen, and Kevin L. Schey. "Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin." Experimental Eye Research 159 (June 2017): 23–29. http://dx.doi.org/10.1016/j.exer.2017.02.012.
Full textMasaki, Shigeo, Satoshi Yonezawa, and Roy A. Quinlan. "Localization of Two Conserved Cis -acting Enhancer Regions for the Filensin Gene Promoter That Direct Lens-specific Expression." Experimental Eye Research 75, no. 3 (September 2002): 295–305. http://dx.doi.org/10.1006/exer.2002.2016.
Full textMasaki, S., and R. A. Quinlan. "Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: implications for protein classification and assembly." Gene 201, no. 1-2 (November 1997): 11–20. http://dx.doi.org/10.1016/s0378-1119(97)00419-8.
Full textLiu, Ke, Lei Lyu, David Chin, Junyuan Gao, Xiurong Sun, Fu Shang, Andrea Caceres, et al. "Altered ubiquitin causes perturbed calcium homeostasis, hyperactivation of calpain, dysregulated differentiation, and cataract." Proceedings of the National Academy of Sciences 112, no. 4 (January 12, 2015): 1071–76. http://dx.doi.org/10.1073/pnas.1404059112.
Full textHESS, JOHN F., JODI T. CASSELMAN, ALLEN P. KONG, and PAUL G. FITZGERALD. "Primary Sequence, Secondary Structure, Gene Structure, and Assembly Properties Suggests that the Lens-specific Cytoskeletal Protein Filensin Represents a Novel Class of Intermediate Filament Protein." Experimental Eye Research 66, no. 5 (May 1998): 625–44. http://dx.doi.org/10.1006/exer.1998.0478.
Full textde Iongh, Robbert U., Frank J. Lovicu, Paul A. Overbeek, Michael D. Schneider, Josephine Joya, Edna D. Hardeman, and John W. McAvoy. "Requirement for TGFβ receptor signaling during terminal lens fiber differentiation." Development 128, no. 20 (October 15, 2001): 3995–4010. http://dx.doi.org/10.1242/dev.128.20.3995.
Full textNakamuta, Ryoichi, Hiroyuki Ainobu, Masaya Wada, Taketsune Matsuzaki, Yushi Oishi, Mikako Oka, Makoto Takehana, Yozo Takasaki, and Shoji Ando. "2P-050 Morphological analysis of the intermediate filaments formed by lens-specific proteins filensin and phakinin in vitro(The 46th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 48, supplement (2008): S82—S83. http://dx.doi.org/10.2142/biophys.48.s82_6.
Full textLi, Yong, Dandan Qi, Baoli Zhu, and Xin Ye. "Analysis of m6A RNA Methylation-Related Genes in Liver Hepatocellular Carcinoma and Their Correlation with Survival." International Journal of Molecular Sciences 22, no. 3 (February 2, 2021): 1474. http://dx.doi.org/10.3390/ijms22031474.
Full textAgbamu, Samuel. "The Arco dei Fileni: A fascist reading of Sallust’s Bellum Iugurthinum." Classical Receptions Journal 11, no. 2 (January 28, 2019): 157–77. http://dx.doi.org/10.1093/crj/cly023.
Full textPARFITT, ROSE. "Fascism, Imperialism and International Law: An Arch Met a Motorway and the Rest is History . . ." Leiden Journal of International Law 31, no. 3 (July 2, 2018): 509–38. http://dx.doi.org/10.1017/s0922156518000304.
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