Relevant bibliographies by topics / Lp82

Academic literature on the topic 'Lp82'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "Lp82"

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Ma, H., M. Shih, I. Hata, C. Fukiage, M. Azuma, and T. R. Shearer. "Lp85 calpain is an enzymatically active rodent-specific isozyme of lens Lp82." Current Eye Research 20, no. 3 (January 2000): 183–89. http://dx.doi.org/10.1076/0271-3683(200003)2031-9ft183.

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Fukiage, Chiho, Emi Nakajima, Hong Ma, Mitsuyoshi Azuma, and Thomas R. Shearer. "Characterization and Regulation of Lens-specific Calpain Lp82." Journal of Biological Chemistry 277, no. 23 (March 19, 2002): 20678–85. http://dx.doi.org/10.1074/jbc.m200697200.

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Shearer, T. R., H. Ma, M. Shih, I. Hata, C. Fukiage, Y. Nakamura, and M. Azuma. "Lp82 calpain during rat lens maturation and cataract formation." Current Eye Research 17, no. 11 (January 1998): 1037–43. http://dx.doi.org/10.1076/ceyr.17.11.1037.5232.

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NAKAMURA, Y., C. FUKIAGE, H. MA, M. SHIH, M. AZUMA, and T. R. SHEARER. "Decreased Sensitivity of Lens-Specific Calpain Lp82 to Calpastatin Inhibitor." Experimental Eye Research 69, no. 2 (August 1999): 155–62. http://dx.doi.org/10.1006/exer.1998.0686.

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MA, H., I. HATA, M. SHIH, C. FUKIAGE, Y. NAKAMURA, M. AZUMA, and T. R. SHEARER. "Lp82 is the Dominant Form of Calpain in Young Mouse Lens." Experimental Eye Research 68, no. 4 (April 1999): 447–56. http://dx.doi.org/10.1006/exer.1998.0625.

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Ueda, Yoji, Ashley L. McCormack, Thomas R. Shearer, and Larry L. David. "Purification and Characterization of Lens Specific Calpain (Lp82) from Bovine Lens." Experimental Eye Research 73, no. 5 (November 2001): 625–37. http://dx.doi.org/10.1006/exer.2001.1071.

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Gao, Junyuan, Xiurong Sun, Francisco J. Martinez-Wittinghan, Xiaohua Gong, Thomas W. White, and Richard T. Mathias. "Connections Between Connexins, Calcium, and Cataracts in the Lens." Journal of General Physiology 124, no. 4 (September 27, 2004): 289–300. http://dx.doi.org/10.1085/jgp.200409121.

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There is a good deal of evidence that the lens generates an internal micro circulatory system, which brings metabolites, like glucose, and antioxidants, like ascorbate, into the lens along the extracellular spaces between cells. Calcium also ought to be carried into the lens by this system. If so, the only path for Ca2+ to get out of the lens is to move down its electrochemical gradient into fiber cells, and then move by electrodiffusion from cell to cell through gap junctions to surface cells, where Ca-ATPase activity and Na/Ca exchange can transport it back into the aqueous or vitreous humors. The purpose of the present study was to test this calcium circulation hypothesis by studying calcium homeostasis in connexin (Cx46) knockout and (Cx46 for Cx50) knockin mouse lenses, which have different degrees of gap junction coupling. To measure intracellular calcium, FURA2 was injected into fiber cells, and the gradient in calcium concentration from center to surface was mapped in each type of lens. In wild-type lenses the coupling conductance of the mature fibers was ∼0.5 S/cm2 of cell to cell contact, and the best fit to the calcium concentration data varied from 700 nM in the center to 300 nM at the surface. In the knockin lenses, the coupling conductance was ∼1.0 S/cm2 and calcium varied from ∼500 nM at the center to 300 nM at the surface. Thus, when the coupling conductance doubled, the concentration gradient halved, as predicted by the model. In knockout lenses, the coupling conductance was zero, hence the efflux path was knocked out and calcium accumulated to ∼2 μM in central fibers. Knockout lenses also had a dense central cataract that extended from the center to about half the radius. Others have previously shown that this cataract involves activation of a calcium-dependent protease, Lp82. We can now expand on this finding to provide a hypothesis on each step that leads to cataract formation: knockout of Cx46 causes loss of coupling of mature fiber cells; the efflux path for calcium is therefore blocked; calcium accumulates in the central cells; at concentrations above ∼1 μM (from the center to about half way out of a 3-wk-old lens) Lp82 is activated; Lp82 cleaves cytoplasmic proteins (crystallins) in central cells; and the cleaved proteins aggregate and scatter light.
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MA, H., M. SHIH, I. HATA, C. FUKIAGE, M. AZUMA, and T. R. SHEARER. "Protein for Lp82 Calpain Is Expressed and Enzymatically Active in Young Rat Lens." Experimental Eye Research 67, no. 2 (August 1998): 221–29. http://dx.doi.org/10.1006/exer.1998.0515.

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Inomata, Mitsushi, Masami Hayashi, Yoshimasa Ito, Yuko Matsubara, Makoto Takehana, Seiichi Kawashima, and Seigo Shumiya. "Comparison of Lp82- and m-calpain-mediated proteolysis during cataractogenesis in Shumiya cataract rat (SCR)." Current Eye Research 25, no. 4 (January 2002): 207–13. http://dx.doi.org/10.1076/ceyr.25.4.207.13486.

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Azuma, Mitsuyoshi, Yoshiyuki Tamada, Sayaka Kanaami, Emi Nakajima, Yoshikuni Nakamura, Chiho Fukiage, Neil E. Forsberg, Melinda K. Duncan, and Thomas R. Shearer. "Differential influence of proteolysis by calpain 2 and Lp82 on in vitro precipitation of mouse lens crystallins." Biochemical and Biophysical Research Communications 307, no. 3 (August 2003): 558–63. http://dx.doi.org/10.1016/s0006-291x(03)01194-x.

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Dissertations / Theses on the topic "Lp82"

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Shuyu, E. "Role of the LPA2 receptor in protecting against apoptosis." View the abstract Download the full-text PDF version, 2008. http://etd.utmem.edu/WORLD-ACCESS/E/2008-046-E.pdf.

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Thesis (Ph.D.)--University of Tennessee Health Science Center, 2008.
Title from title page screen (viewed on January 7, 2009). Research advisor: Gabor Tigyi, M.D., Ph.D. Document formatted into pages (xiv, 105 p. : ill.). Vita. Abstract. Includes bibliographical references (p. 90-105).
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Pequignot, Marc Bolliet Louis. "Étude et réalisation d'outil de programmation pour IRIS 80 mode C, LP80-metteur au point." S.l. : Université Grenoble 1, 2008. http://dumas.ccsd.cnrs.fr/dumas-00307037.

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Muir, Matthew Stewart. "Proteomics of the ovine cataract." Diss., Lincoln University, 2008. http://hdl.handle.net/10182/792.

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The lens of the eye needs to be completely transparent in order to allow all light entering the eye to reach the retina. This transparency is maintained by the highly ordered structure of the lens proteins the crystallins. Any disruption to the lens proteins can cause an opacity to develop which is known as cataract. During cortical cataract formation there is increased truncation of the lens crystallins. It is believed that overactivation of calcium-dependent cysteine proteases, the calpains, is responsible for the increased proteolysis of the crystallins seen during cataractogenesis. Within the ovine lens there are three calpains, calpain 1, 2 and the lens specific calpain Lp82. The aim of this thesis was to determine the changes in the lens proteins during ageing and cataractogenesis, and to establish the role of the calpains in these processes. Calpain 1 and 2 were purified from ovine lung and Lp82 was purified from lamb lenses using chromatography. Activity and presence of the calpains was determined by using the BODIPY-FL casein assay, gel electrophoresis, Western blot and casein zymography. Changes in the lens proteins, specifically the crystallins, were visualised using two-dimensional electrophoresis (2DE). Lenses from fetal, 6 month old and 8 year old sheep were collected, as well as stage 0, 1, 3 and 6 cataractous ovine lenses. The proteins from the lenses were separated into the water soluble and urea soluble fractions and analysed by 2DE. Mass spectrometry was used to determine the masses and therefore modifications of the crystallins. Finally, the individual crystallins were separated using gel filtration chromatography and incubated with the purified calpains in the presence of calcium. The extent of the proteolysis was visualised using 2DE and truncation sites determined by mass spectrometry. Purification of the calpains resulted in samples that were specific for each calpain and could be used in further experiments. 2DE analysis showed that there were changes to the crystallins during maturation of the lens. The α-crystallins become increasingly phosphorylated as the lens ages and a small amount becomes truncated. The β-crystallins were also modified during ageing by truncation and deamidation. When crystallins from cataractous lenses were compared using 2DE there were changes to both the α- and β-crystallins. The α-crystallins were found to be extensively truncated at their C-terminal tail. Four of the seven β-crystallins, βB1, βB3, βB2 and βA3, showed increased truncation of their N-terminal extensions during cataract formation. All three calpains truncated αA and αB-crystallin at their C-terminal ends after incubation. Calpain 2 and Lp82 each produced unique αA-crystallin truncations. All three calpains truncated βB1 and βA3 and calpain 2 also truncated βB3. When the truncations from the calpain incubations were compared to those seen during cataract formation, many of the truncations were found to be similar. Both the unique truncations from calpain 2 and Lp82 were found in cataractous lenses, with the Lp82 more obvious in the 2DE. The β-crystallin truncations found after incubation with the calpains were similar to those found during cataractogenesis. In conclusion this study documents the changes to the ovine lens during maturation and cataractogenesis and indicates a role for the calpain family in the increased proteolysis observed in the ovine cataract.
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Jones, Joanna L. "The involvement and regulation of ARF6 in agonist-induced internalization of the β₂-adrenoceptor and the LPA2 and LPA3 receptors." Thesis, University of Bristol, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422551.

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Nygård, Skalman Jonas. "Molnkopplade koldioxid sensorer : Prototypkonstruktion och strömmätningar." Thesis, Mittuniversitetet, Avdelningen för elektronikkonstruktion, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:miun:diva-30979.

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Dagens stora miljöutmaningar i form av förbränning av fossila bränslen och medföljande koldioxidutsläpp har också gjort att många individer blivit allt mer miljömedvetna. Avancerade sensor för att mäta koldioxid finns numera på marknaden i form av lågenergiförbrukande alternativ som Senseairs LP8. Att utveckla firmware och att bedriva utveckling med sådana avancerade sensorer är något som inte är speciellt enkelt för vanliga användare. I detta projekt har en plattform byggd på bluetooth och enkla gratis utvecklingsverktyg tagits fram. Denna prototyp ugör en grund för utvecklingen av ett klimatsmycke där CO2 skall rapporteras till en molntjänst via mobiltelefon. Med prototypen har det utförts mätningar av strömförbrukningen genom att mäta urladdningstid av superkondensatorer, spänningsfallmätningar av cr2032 batterier samt kompletterande kapacitansmätningar av superkondensatorerna. Dessa mätningar visar att strömförbrukningen för prototypen ligger i intervallet 1-2 mA, beroende av vilka inställningar som önskas. Metoderna är väldigt enkla men ger en relativt god uppskattning av den totala strömförbrukningen.
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Lin, Shih-Hung, and 林士閎. "The Roles of LPA2 during Erythrocyte and Megakaryocyte Differentiation in Zebrafish." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/91946306718005941980.

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碩士
國立臺灣大學
生命科學系
102
Lysophosphatidic acid (LPA) is a small lysophospholipid which regulates many cell behaviors, such as cell proliferation, migration, and survival. LPA binds to a family of G-protein-coupled receptor, LPA receptor 1-6, and activates its downstream pathways. Hematopoiesis is a developmental process that hematopoietic stem cells (HSCs) differentiate into all types of blood cells, including erythrocytes, lymphocytes, and megakaryocytes. In our previous study, we demonstrated that activation of LPA3 could enhance erythropoiesis processes. However, the roles of other LPA receptors in hematopoiesis remain unclear. Since erythrocyte and megakaryocyte share the common progenitor cell, we attempted to investigate the role of LPA receptors in megakaryopoiesis processes. To clarify the role of LPA2 in erythrocyte and megakaryocyte differentiation in zebrafish, we first injected anti-sense morpholino oligonucleotide of LPA2 into wild-type zebrafish embryos at one-cell-stage. O-dianisidine staining for hemoglobin and real-time PCR were used to determine the expression of erythrocyte and mRNA expression of erythropoietic markers, Hbae1 and GATA1, or megakaryocyte marker, CD41, respectively. Moreover, we also injected LPA2 morpholino into embryos of Tg(eGFP:CD41) transgenic line. Our results demonstrated that knockdown of LPA2 enhanced the staining at CHT and mRNA levels of Hbea1, GATA1, and CD41. In addition, the number of megakaryocyte in Tg(eGFP:CD41) zebrafish embryos was also increased. Furthermore, we performed pharmacological experiment to confirm these results by incubating embryos with the LPA2 agonist GRI977143 and RP-239. Results from staining of o-dianisidine and real-time PCR of Hbea1, and CD41 showed that both protein and mRNA levels were suppressed by LPA2 agonists. In conclusion, our results suggested that activation of LPA2 inhibit differentiation of erythrocyte and megakaryocyte in zebrafish.
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Vera, Rodriguez Arturo. "Novel export and import pathways in S. cerevisiae identified by an engineered SUMO system." Doctoral thesis, 2017. http://hdl.handle.net/11858/00-1735-0000-002E-E49F-0.

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Books on the topic "Lp82"

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Hse. Lp80 Driver Controlled Deliveries in Accordance with Part 3. Health and Safety Executive (HSE), 1999.

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Ar Lp02 Librarians Picks Middle Grades 2001: Grade 4-8. Renaissance Learning Inc, 2003.

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Book chapters on the topic "Lp82"

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Perović, Aleksandar, Dragan Doder, Nebojša Ikodinović, and Angelina Ilić Stepić. "Erratum to: Extensions of the Probability Logics LPP2 and LFOP1." In Probability Logics, E1. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-47012-2_8.

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Doskočil, J., J. Forstová, H. Štorchová, and J. Meyer. "Genomic Structure and Evolution of Bacillus Licheniformis ϑ and LP52 Phage Family." In Gene Manipulation and Expression, 3–21. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-011-6565-5_1.

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Hughes, G. E., and D. G. Londey. "LPC2 : Axiomatization." In The Elements of Formal Logic, 242–47. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-36.

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Hughes, G. E., and D. G. Londey. "The System LPC2 : Introductory." In The Elements of Formal Logic, 228–31. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-32.

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Hughes, G. E., and D. G. Londey. "LPC2 : Decision Procedure I." In The Elements of Formal Logic, 232–35. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-33.

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Hughes, G. E., and D. G. Londey. "LPC2: Decision Procedure II–Exposition." In The Elements of Formal Logic, 236–39. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-34.

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Hughes, G. E., and D. G. Londey. "LPC2 : Decision Procedure II -Justification." In The Elements of Formal Logic, 240–41. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-35.

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Hughes, G. E., and D. G. Londey. "LPC2 and the Logic of an Empty Universe." In The Elements of Formal Logic, 248–56. Routledge, 2019. http://dx.doi.org/10.4324/9780367854126-37.

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Conference papers on the topic "Lp82"

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Turnaturi, Rita, Carmela Parenti, Girolamo Calò, Santina Chiechio, Agostino Marrazzo, and Lorella Pasquinucci. "From LP2 to 2S-LP2: discovery of a biased dual-target mu/delta opioid receptor agonist for pain management." In 6th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07383.

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Lee, Jennifer H., Michael E. Durst, Demirhan Kobat, Chris Xu, and Lars Grüner-Nielsen. "Focusing of the LP02 Mode from a Higher Order Mode Fiber." In CLEO: Applications and Technology. Washington, D.C.: OSA, 2011. http://dx.doi.org/10.1364/cleo_at.2011.jwa103.

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Sharma, A., and R. Posey. "Multiwavelength LP02 - LP21 intermodal interferometric temperature sensing using stimulated Raman scattering." In Optical Fiber Sensors. Washington, D.C.: OSA, 1996. http://dx.doi.org/10.1364/ofs.1996.we317.

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Shen, Dongya, Chuan Ma, Changhui Wan, Hong Yuan, and Xiupu Zhang. "A new all-fiber LP01/LP02 mode converter in mode division multiplexing." In 2017 16th International Conference on Optical Communications and Networks (ICOCN). IEEE, 2017. http://dx.doi.org/10.1109/icocn.2017.8121388.

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Smith, C., S. Ghalmi, P. Balling, S. Ramachandran, and J. W. Nicholson. "Enhanced Resolution in Nonlinear Microscopy Using the LP02 mode of an optical fiber." In Conference on Lasers and Electro-Optics. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/cleo.2010.cwl5.

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Bock, Wojtek J., and Tinko A. Eftimov. "Strain sensor based on LP01-LP02 intermodal interference in highly birefringent optical fibers." In Optical Tools for Manufacturing and Advanced Automation, edited by Ramon P. DePaula. SPIE, 1994. http://dx.doi.org/10.1117/12.169951.

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Mori, T., T. Sakamoto, M. Wada, A. Urushibara, T. Yamamoto, and K. Nakajima. "Unrepeated LP02 Mode Transmission over 205 km Few-mode Fibre with Selective Mode Excitation." In 2017 European Conference on Optical Communication (ECOC). IEEE, 2017. http://dx.doi.org/10.1109/ecoc.2017.8346169.

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Jossent, M., E. Tartaret-Josnière, L. Kotov, A. Le Rouge, P. Di Bin, P. Roy, L. Bigot, and S. Février. "Pure and achromatic excitation of the LP02 mode in a dispersion-tailored optical fiber." In Specialty Optical Fibers. Washington, D.C.: OSA, 2016. http://dx.doi.org/10.1364/sof.2016.som4g.4.

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Xin, Ding, Gong Dao-lei, and Ming-Yang Chen. "Design of broadband LP01 < - > LP02 mode converter based on long period fiber grating." In First Optics Frontier Conference, edited by Shining Zhu, Tiejun Cui, Xiangang Luo, and Long Zhang. SPIE, 2021. http://dx.doi.org/10.1117/12.2599830.

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Kumar, Dablu, and Rakesh Ranjan. "Crosstalk analysis in homogeneous 12-core multicore fiber with different core layouts for LP01 and LP02 modes." In TENCON 2017 - 2017 IEEE Region 10 Conference. IEEE, 2017. http://dx.doi.org/10.1109/tencon.2017.8228264.

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