The Experts below are selected from a list of 15681 Experts worldwide ranked by ideXlab platform
Velia M Fowler - One of the best experts on this subject based on the ideXlab platform.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:To elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.We investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.F-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.These results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:Author(s): Cheng, Catherine; Nowak, Roberta B; Biswas, Sondip K; Lo, Woo-Kuen; FitzGerald, Paul G; Fowler, Velia M | Abstract: PurposeTo elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.MethodsWe investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.ResultsF-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.ConclusionsThese results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
Catherine Cheng - One of the best experts on this subject based on the ideXlab platform.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:To elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.We investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.F-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.These results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:Author(s): Cheng, Catherine; Nowak, Roberta B; Biswas, Sondip K; Lo, Woo-Kuen; FitzGerald, Paul G; Fowler, Velia M | Abstract: PurposeTo elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.MethodsWe investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.ResultsF-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.ConclusionsThese results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
Jozef L Kokini - One of the best experts on this subject based on the ideXlab platform.
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non newtonian fluid mixing in a twin screw mixer geometry three dimensional mesh development effect of fluid model and operating conditions
Journal of Food Process Engineering, 2015Co-Authors: Maureen L Rathod, Jozef L Kokini, Bharani Ashokan, Lindsay M FanningAbstract:Mixing was examined in a Readco continuous mixer (Readco Kurimoto, LLC, York, PA); a mesh was developed for three-dimensional (3D) finite element method simulation and validated against experimental Newtonian fluid results. The mesh was designed to ensure accuracy in areas with a high velocity gradient while minimizing computational cost. It was utilized for investigation of non-Newtonian fluids, including power-law and Bird-Carreau models. Simple shear flow is seen at high gamma in the center of the mixer; efficient dispersive mixing appears near the barrel wall at all flow rates. Both configurations experience increasing velocity and gamma with mixer speed. Efficient dispersive mixing is observed near the barrel center with parallel Paddles. Staggered Paddles cause areas of backflow, improving fluid retention time. Under the same operating conditions, the Bird-Carreau fluid shows the greater influence of Paddle motion, including less flow-through and significant backflow. Maximum gamma is higher than that seen for the power-law fluid, while mixing index maxima are similar for both fluids. Practical Applications This work evaluates mixing using complex fluids in a realistic geometry and explores the effect of different operating conditions. Previous work has been confined to mainly Newtonian fluids or simplified geometries. A major benefit of 3D numerical simulation is that it enables comprehensive, noninvasive fluid analysis and determination of mixing quality. The most valuable simulations are those that closely mimic existing equipment scenarios. This information will allow industry users to design more efficient mixers and develop better mixer configurations with lower capital cost. This is particularly important to the dough industry which needs a well-defined mixing profile for both product rheology and machinability.
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effect of mixer geometry and operating conditions on mixing efficiency of a non newtonian fluid in a twin screw mixer
Journal of Food Engineering, 2013Co-Authors: Maureen L Rathod, Jozef L KokiniAbstract:Abstract The effect of mixer speed, fluid inflow rate, and Paddle angle was examined in a shortened geometry. 3D FEM simulation of non-Newtonian 2 g/100 mL carboxymethyl cellulose aqueous solution in the mixing region of a Readco continuous mixer was performed. Data gathered included velocity vectors, shear rate, and mixing index. Increasing mixer speed increased velocity magnitudes in the horizontal and vertical directions. Fluid inflow rate had little impact on velocity in the horizontal and vertical directions, but increased velocity in the axial direction and elongational contribution to the mixing index. All configurations showed areas of simple shear flow where the fluid experienced high shear rates. Staggering Paddles increased the maximum axial velocity and shear rate. When successive Paddles on the same screw are parallel, a zone was seen between the center of the Paddle and the barrel wall which demonstrated efficient dispersive mixing.
Roberta B Nowak - One of the best experts on this subject based on the ideXlab platform.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:To elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.We investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.F-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.These results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:Author(s): Cheng, Catherine; Nowak, Roberta B; Biswas, Sondip K; Lo, Woo-Kuen; FitzGerald, Paul G; Fowler, Velia M | Abstract: PurposeTo elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.MethodsWe investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.ResultsF-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.ConclusionsThese results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
Paul G. Fitzgerald - One of the best experts on this subject based on the ideXlab platform.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:To elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.We investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.F-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.These results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
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tropomodulin 1 regulation of actin is required for the formation of large Paddle protrusions between mature lens fiber cells
Investigative Ophthalmology & Visual Science, 2016Co-Authors: Catherine Cheng, Roberta B Nowak, Paul G. Fitzgerald, Sondip K Biswas, Velia M FowlerAbstract:Author(s): Cheng, Catherine; Nowak, Roberta B; Biswas, Sondip K; Lo, Woo-Kuen; FitzGerald, Paul G; Fowler, Velia M | Abstract: PurposeTo elucidate the proteins required for specialized small interlocking protrusions and large Paddle domains at lens fiber cell tricellular junctions (vertices), we developed a novel method to immunostain single lens fibers and studied changes in cell morphology due to loss of tropomodulin 1 (Tmod1), an F-actin pointed end-capping protein.MethodsWe investigated F-actin and F-actin-binding protein localization in interdigitations of Tmod1+/+ and Tmod1-/- single mature lens fibers.ResultsF-actin-rich small protrusions and large Paddles were present along cell vertices of Tmod1+/+ mature fibers. In contrast, Tmod1-/- mature fiber cells lack normal Paddle domains, while small protrusions were unaffected. In Tmod1+/+ mature fibers, Tmod1, β2-spectrin, and α-actinin are localized in large puncta in valleys between Paddles; but in Tmod1-/- mature fibers, β2-spectrin was dispersed while α-actinin was redistributed at the base of small protrusions and rudimentary Paddles. Fimbrin and Arp3 (actin-related protein 3) were located in puncta at the base of small protrusions, while N-cadherin and ezrin outlined the cell membrane in both Tmod1+/+ and Tmod1-/- mature fibers.ConclusionsThese results suggest that distinct F-actin organizations are present in small protrusions versus large Paddles. Formation and/or maintenance of large Paddle domains depends on a β2-spectrin-actin network stabilized by Tmod1. α-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization. Formation of small protrusions is likely facilitated by Arp3-branched and fimbrin-bundled F-actin networks, which do not depend on Tmod1. This is the first work to reveal the F-actin-associated proteins required for the formation of Paddles between lens fibers.
