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Relevant bibliographies by topics / Filensin

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Academic literature on the topic 'Filensin'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Filensin"

1

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.

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Filensin is a 100/110 kDa membrane-associated protein found in lens fiber cells. Previous studies have shown that this protein polymerizes in vitro and binds strongly to vimentin and to another 47 kDa lens membrane protein. Using cosedimentation assays, flotation assays and immunoelectron microscopy, we have examined the properties of purified filensin and measured its binding to lens membranes. Filensin behaves as a ureaextractable, hydrophilic protein which does not partition with Triton X-114 and is not affected by 1 M hydroxylamine at alkaline pH, an agent known to release fatty-acylated p

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2

Remington, 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.

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Filensin, a 100 kDa, membrane-associated, cytoskeletal protein, is uniquely expressed in the lens fiber cell (Merdes, A., Brunkener, M., Horstmann, H., and Georgatos, S. D. (1991) J. Cell Biol. 115, 397–410). I cloned and sequenced a full-length chicken lens cDNA encoding filensin, also known as CP95 (Ireland, M. and Maisel, H. (1989) Lens and Eye Toxicity Research 6, 623–638). The deduced amino acid sequence of 657 residues contained an internal 280 residue heptad repeat domain with sequence similarities to the rod domain of intermediate filament proteins. The putative filensin rod domain cou

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Goulielmos, 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.

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Filensin and phakinin constitute the subunits of a heteropolymeric, lens-specific intermediate filament (IF) system known as the beaded-chain filaments (BFs). Since the rod of filensin is four heptads shorter than the rods of all other IF proteins, we decided to examine the specific contribution of this protein in filament assembly. For these purposes, we constructed chimeric proteins in which regions of filensin were exchanged with the equivalent ones of vimentin, a self-polymerizing IF protein. Our in vitro studies show that the filensin rod domain does not allow homopolymeric filament elong

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Merdes, 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.

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We have studied the molecular properties of a 100-kD protein, termed filensin, which we have isolated from porcine lens membranes. Filensin represents a membrane-associated element, resistant to salt and nonionic detergent treatment, and extractable only by alkali or high concentrations of urea. By indirect immunofluorescence and immunoelectron microscopy, this protein can be localized at the periphery of the lens fiber cells. Immunochemical analysis suggests that filensin originates from a larger 110-kD component which is abundantly expressed in lens but not in other tissues. Purified filensi

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Gounari, 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.

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The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to intermediate filament (IF) proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various intermediate filament proteins and includes a p

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6

Merdes, 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.

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In previous studies we have characterized a lens-specific intermediate filament (IF) protein, termed filensin. Filensin does not self-assemble into regular IFs but is known to associate with another 47-kD lens-specific protein which has been suggested to represent its assembly partner. To address this possibility, we cloned and sequenced the cDNA coding for the bovine 47-kD protein which we have termed phakinin (from the greek phi alpha kappa omicron sigma = phakos = lens). The predicted sequence comprises 406 amino acids and shows significant similarity (31.3% identity over 358 residues) to t

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7

Goulielmos, 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.

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The fiber cells of the eye lens possess a unique cytoskeletal system known as the "beaded-chain filaments" (BFs). BFs consist of filensin and phakinin, two recently characterized intermediate filament (IF) proteins. To examine the organization and the assembly of these heteropolymeric IFs, we have performed a series of in vitro polymerization studies and transfection experiments. Filaments assembled from purified filensin and phakinin exhibit the characteristic 19-21-nm periodicity seen in many types of IFs upon low angle rotary shadowing. However, quantitative mass-per-length (MPL) measuremen

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Sandilands, 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.

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The cells of the eye lens contain the type III intermediate filament protein vimentin, as well as two other intermediate filament proteins, CP49 and filensin. These two proteins appear to be unique to the differentiated lens fibre cell. Immunoblotting and confocal microscopy were used to describe changes which occur in these three intermediate filament proteins and the networks they form during fibre cell differentiation and maturation. The vimentin network was present in both epithelial cells and some fibre cells. Fibre cells were vimentin positive up to a specific point 2–3 mm in from the le

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9

Fischer, 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.

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Georgatos, 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.

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For nearly three decades cytoplasmic intermediate filaments (IFs) have been described as 10 nm thick, unbranched ropes radiating from the cell nucleus and extending to the plasma membrane. This stereotype is now being challenged by the discovery and molecular characterization of the beaded filaments (BFs), a novel class of IFs composed of the lens-specific proteins filensin and phakinin. In contrast to ‘mainstream’ IFs, BFs have a distinctly nodular appearance and form a meshwork underneath the plasma membrane of the lens fiber cells. In vitro assembly studies, expression of filensin and phaki

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Dissertations / Theses on the topic "Filensin"

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Sandilands, Aileen. "Characterisation of the intermediate filament proteins filensin and CP49 within the eye lens." Thesis, University of Dundee, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.441633.

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McDermott, Joshua D. "The ovine lens cytoskeleton." Lincoln University, 2007. http://hdl.handle.net/10182/700.

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The lens of the eye is a vital tissue in the visual system, responsible for the collection and focusing of light on to the retina. Comprised of epithelial cells at differing stages of differentiation, the transparency of the lens is dependent on the highly ordered crystalline structure of lens proteins. The lens consists of several proteins including crystallins (α, β, γ) that make up 90% of the soluble protein, and the lens cytoskeletal proteins. Cytoskeletal proteins contribute only a fraction of the total lens protein, but are thought to play an important role in the establishment and maint

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Books on the topic "Filensin"

1

L'arco dei Fileni: [racconti]. Roma: Settimo sigillo, 2001.

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Franzolin, Ugo. L' arco dei Fileni: [racconti]. Roma: Settimo sigillo, 2001.

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Franzolin, Ugo. L' arco dei Fileni: [racconti]. Roma: Settimo sigillo, 2001.

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Conference papers on the topic "Filensin"

1

Nadgowda, Shripad. "Filenail." In Middleware '20: 21st International Middleware Conference. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3429885.3429961.

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