Literatura académica sobre el tema "Motility"
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Artículos de revistas sobre el tema "Motility"
Boivin, M., M. Riberdy, M. C. Raymond, L. Trudel y P. Poitras. "Motilin and the postprandial motility of the antrum". Canadian Journal of Physiology and Pharmacology 70, n.º 11 (1 de noviembre de 1992): 1491–95. http://dx.doi.org/10.1139/y92-211.
Texto completoLayer, P., A. T. Chan, V. L. Go y E. P. DiMagno. "Human pancreatic secretion during phase II antral motility of the interdigestive cycle". American Journal of Physiology-Gastrointestinal and Liver Physiology 254, n.º 2 (1 de febrero de 1988): G249—G253. http://dx.doi.org/10.1152/ajpgi.1988.254.2.g249.
Texto completoMalfertheiner, P., M. G. Sarr, M. P. Spencer y E. P. DiMagno. "Effect of duodenectomy on interdigestive pancreatic secretion, gastrointestinal motility, and hormones in dogs". American Journal of Physiology-Gastrointestinal and Liver Physiology 257, n.º 3 (1 de septiembre de 1989): G415—G422. http://dx.doi.org/10.1152/ajpgi.1989.257.3.g415.
Texto completoMuller, E. L., P. A. Grace, R. L. Conter, J. J. Roslyn y H. A. Pitt. "Influence of motilin and cholecystokinin on sphincter of Oddi and duodenal mobility". American Journal of Physiology-Gastrointestinal and Liver Physiology 253, n.º 5 (1 de noviembre de 1987): G679—G683. http://dx.doi.org/10.1152/ajpgi.1987.253.5.g679.
Texto completoSakahara, Satoshi, Zuoyun Xie, Kanako Koike, Satoya Hoshino, Ichiro Sakata, Sen-ichi Oda, Toku Takahashi y Takafumi Sakai. "Physiological characteristics of gastric contractions and circadian gastric motility in the free-moving conscious house musk shrew (Suncus murinus)". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 299, n.º 4 (octubre de 2010): R1106—R1113. http://dx.doi.org/10.1152/ajpregu.00278.2010.
Texto completoAyutama, Wanodia, Tuty Rizkianti y Cut Fauziah. "HUBUNGAN JUMLAH LEUKOSIT DENGAN MOTILITAS SPERMATOZOA PADA ANALISIS SEMEN PRIA DI SAMMARIE FAMILY HEALTHCARE 2019". Jurnal Muara Sains, Teknologi, Kedokteran dan Ilmu Kesehatan 4, n.º 2 (29 de octubre de 2020): 335. http://dx.doi.org/10.24912/jmstkik.v4i2.7788.
Texto completoChung, S. A., G. R. Greenberg y N. E. Diamant. "Relationship of postprandial motilin, gastrin, and pancreatic polypeptide release to intestinal motility during vagal interruption". Canadian Journal of Physiology and Pharmacology 70, n.º 8 (1 de agosto de 1992): 1148–53. http://dx.doi.org/10.1139/y92-159.
Texto completoNahdiyah, Ayu Naila, Hari Santoso y Hasan Zayadi. "Pengaruh Fraksi Ejakulasi terhadap Motilitas Spermatozoa Kambing Peranakan Etawa (Capra aegagrus)". BIOSAINTROPIS (BIOSCIENCE-TROPIC) 5, n.º 2 (10 de enero de 2020): 72–76. http://dx.doi.org/10.33474/e-jbst.v5i2.288.
Texto completoKellow, John E. y Yiu-Kay Chan. "Advanced motility and motility disorders". Current Opinion in Gastroenterology 11, n.º 2 (marzo de 1995): 106–11. http://dx.doi.org/10.1097/00001574-199503000-00003.
Texto completoPeeters, T. L., J. Janssens, C. Plets y G. Vantrappen. "Interdigestive Motility and Motilin in Hypophysectomized Patients". Scandinavian Journal of Gastroenterology 23, n.º 1 (enero de 1988): 71–74. http://dx.doi.org/10.3109/00365528809093850.
Texto completoTesis sobre el tema "Motility"
Cao, Luyan. "bases structurales de la motilité des kinésines". Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS267/document.
Texto completoKinesins are a family of microtubule-interacting motor proteins that convert the chemical energy from ATP hydrolysis into mechanical work. Many kinesins are motile, walking along microtubules to fulfill different functions. Most kinesins are dimers, the monomer comprising a motor domain, a dimerizing stalk domain, and a tail domain. The motor domain contains both the nucleotide-binding site and the microtubule-binding site. I am interested in the molecular mechanism of kinesin's motility. In particular I want to establish the structural variations of the kinesin motor domain along with the mechanochemical cycle of this motor protein. During my thesis, I have focused my work on the human kinesin-1, also named conventional kinesin, which is the best characterized kinesin.I have studied two aspects of the kinesin mechanochemical cycle, by combining structural and mutational approaches. Both aspects rely on the binding of ADP-kinesin to a microtubule, which leads to the release of the nucleotide and to a tight kinesin-microtubule association. First I determined the crystal structure of nucleotide-free kinesin-1 motor domain in complex with a tubulin heterodimer, which is the building block of microtubule. This structure represented the main missing piece of the structural cycle of kinesin. Three subdomains in the kinesin motor domain can be identified through the comparison of my structure with ATP-analog kinesin-1-tubulin structure. The relative movements of these subdomains explain how ATP binding to apo-kinesin bound to microtubule triggers the opening of a hydrophobic cavity, 28 Å distant from the nucleotide-binding site. This cavity accommodates the first residue of the “neck linker”, a short peptide that is C-terminal to the motor domain, allowing the neck linker to dock on the motor domain. The docking of the neck linker is proposed to trigger the mechanical step, i.e. the displacement of the cargo and the stepping of the dimeric kinesin. By studying mutants of the neck linker, I have shown that, reciprocally, this peptide locks kinesin in the ATP state, which is also the conformation efficient for ATP hydrolysis. Doing so, it prevents the motor domain from switching back to the apo-state. It prevents also an untimely hydrolysis of ATP, before the mechanical step has occurred. These features are required for movement and processivity.Second, these structural data also suggest how the binding of ADP-kinesin to tubulin enhances nucleotide release from kinesin. To further study this step of the kinesin cycle, I studied the effect of kinesin-1 mutations. These mutations were designed in isolated kinesin to mimic the state when kinesin is bound to a microtubule. I identified two groups of mutations leading to a high spontaneous ADP dissociation rate, suggesting that there are two ways to interfere with ADP binding. Then I determined the crystal structures of the apo form of two mutants as well as that of the nucleotide-depleted wild type kinesin. It showed that apo-kinesin adopts either and ADP-like conformation or a tubulin-bound apo-like one. In the natural context, the second one is stabilized upon microtubule binding. Overall, the mutational and structural data suggest that microtubules accelerate ADP dissociation in kinesin by two main paths, by interfering with magnesium binding and by destabilizing the nucleotide-binding P-loop motif
Gholami, Azam. "Actin-based motility". Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-72151.
Texto completoPatankar, RoySuneel V. "Studies in gallbladder motility". Thesis, University of Southampton, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296188.
Texto completoUllah, Sana. "Factors governing gastrointestinal motility". Thesis, University of Hull, 2012. http://hydra.hull.ac.uk/resources/hull:7166.
Texto completoStanley, Hugh Gerard. "Neural mechanisms in abomasal motility". Thesis, University of Edinburgh, 1988. http://hdl.handle.net/1842/30009.
Texto completoRoss, Oliver N. "Algal motility in variable turbulence". Thesis, University of Southampton, 2004. https://eprints.soton.ac.uk/45995/.
Texto completoBiondini, Marco. "RALlying through cell motility and invasion". Thesis, Paris 11, 2014. http://www.theses.fr/2014PA11T042.
Texto completoMetastasis is a multistep process by which cancer cells migrate away from the primary neoplastic mass to give rise to secondary tumors at distant sites. Thus, the acquisition of motility and invasive traits by tumor cells is a crucial step for metastasis to occur. Depending on the cell type and the environment, cells can move collectively keeping stable cell-cell contacts or as individual cells, which translocate by exploiting either mesenchymal or amoeboid motility programs.Different molecules and pathways have been linked to the regulation of cell motility. Rho small GTPases (Rac1, Cdc42 and RhoA) control cell migration through their actions on actin assembly, actomyosin contractility and microtubules. Rac1 drives mesenchymal-type motility by promoting lamellipodia formation via the Wave Regulator Complex (WRC). On the contrary, amoeboid motility is governed by RhoA which promotes cell movement via the generation of actomyosin contractile force. Another family of small GTPases, the Ral proteins, was recently involved in the regulation of cell migration. RalB, through the mobilization of its main effector the Exocyst complex, was shown to play an essential role in cell motility. In this work of thesis we investigated the molecular mechanisms through which RalB/Exocyst pathway controls cell motility and invasion.In the first part of this manuscript we show that Exocyst interacts with the RacGAP SH3BP1 (project 1). In mesenchymal moving cells Exocyst/SH3BP1 interaction is required to organize membrane protrusion formation by spatially regulating the activity of Rac1 at the cellular front. In addition, in project 2, we show that the Exocyst binds to the wave regulator complex (WRC), a key promoter of actin polymerization. We provide evidences for Exocyst to be involved in driving the WRC to the leading edge of motile cells, where it can stimulate actin polymerization and membrane protrusions. Reactivation of a developmental program termed epithelial-mesenchymal transition (EMT) was recently shown to promote motility, invasion and metastasis of neoplastic cells. Tumor cells undergoing EMT loose cell-cell contacts acquire a fibroblastoid phenotype and invade the surrounding tissues as individual cells. In project 3 we characterized the invasion plasticity of cancer cells after EMT and we investigated the molecular contribution of Ral to post-EMT invasion. We showed that upon EMT cells disseminate individually in a Rho-driven fashion exploiting the generation of actomyosin force to deform the extracellular matrix. We document that RalB silencing severely impairs actomyosin contractility and dissemination of post-EMT cells. We hypothesize that RalB regulates invasion by controlling the dynamics of the Rho pathway via the Exocyst-associated RhoGEF GEF-H1 in post-EMT cells. Finally, in the last part of this thesis manuscript, we present the PIV-based “AVeMap” software which has been developed to quantify in a fully automated way cell migration and its parameters (Project 4).Taken together the results presented in this thesis manuscript point out the Ral/Exocyst pathway as a key molecular organizer of the execution of both Rac1- and Rho-driven motility programs
Chemeris, Angelina. "Régulation du suppresseur d'invasion Arpin par les Tankyrases". Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLX073.
Texto completoThe evolutionarily conserved Arp2/3 complex plays a central role in nucleating the branched actin filament arrays that drive cell migration, endocytosis, and other processes. Recently, an inactivator of the Arp2/3 complex at the lamellipodium tip, a small protein, Arpin, was discovered and characterized. On its C-terminus, Arpin possesses an acidic (A) motif, which is homologous to the A-motif of various Nucleation Promoting Factors (NPFs). It was predicted that Arpin can bind at two binding sites to the Arp2/3 complex, similar to VCA domains of NPFs. Here, we used single particle electron microscopy to obtain a 3D reconstruction of the Arp2/3 complex bound to Arpin at a 25Å resolution. We showed that the binding of Arpin causes the standard open conformational of the Arp2/3 complex. We confirmed that there are two binding sites on the Arp2/3 complex for Arpin: one on the back of the Arp3 subunit, and the second is located between Arp2 and ARPC1 subunits. The distance between the Arp2/3 complex and Arpin (5 nm) supports the view that Arpin interacts with its partner via its unstructured C-terminal acidic tail.Next, using the pull-down assay, we identified the new Arpin binding partners, Tankyrases1/2. Interestingly, Tankyrases and the Arp2/3 complex possess overlapping amino acid sequences at Arpin binding sites. Hence, we demonstrated a competition between the ARC4 domain of Tankyrase1 and the Arp2/3 complex in a dose-dependent manner.To understand the principles of Tankyrases-Arpin interaction, we created a mutant Arpin (ArpinG218D) that lacks its ability to interact with Tankyrases, but not with the Arp2/3 complex in vitro. Interestingly, ArpinG218D was not able to inhibit the Arp2/3 complex in vivo, suggesting that Tankyrase may be necessary for Arpin-Arp2/3 complex interaction. Arpin is the turning factor of migrating cells, so we performed a migration analysis of MCF10-A cells expressing either wild type Arpin (ArpinWT) or mutant ArpinG218D in parallel with the depletion of endogenous Arpin. Cells expressing ArpinG218D had higher directional persistence, similar to the cells where the endogenous Arpin was knocked down. Thus, we suggested that mutant ArpinG218D cannot inactivate the Arp2/3 complex since it is not present at the lamellipodial tip. We compared the amount of protein for both ArpinWT and ArpinG218D in the membrane fraction of the migrating cells. A significant difference (44%) in the amount of ArpinWT and Arpin G218D was consistent with our hypothesis.Tankyrases are therapeutic targets in a variety of cancers, but currently there is no structural model available for these large and flexible proteins. In this work, we obtained for the first time two 3D reconstructions of full-length Tankyrase1 and Tankyrase1 bound to Arpin using single particle electron microscopy. The achieved resolution (27Å) was enough to detect a dramatic conformational change in Tankyrase SAM and PARP domains upon binding of Arpin molecules. In our reconstruction, three Arpins were bound to the ARC1, ARC4 and ARC5 domains of Tankyrase1. ARC5 was shown to be the most flexible part of the ARC cluster.Based on the obtained data, we suggested a model of regulation of the activity of Arpin by Tankyrases. According to our model, Tankyrases bind Arpin in the cytoplasm, change their conformational state and bring Arpin closer to the membrane in the lamellipodia. Deciphering the extracellular signals, Rac GTPase activates Arpin, which sequentially inactivates the Arp2/3 complex, while Tankyrases are released
Macdonald, Julie. "Studies on motility in Rhodomicrobium vannielii". Thesis, University of Warwick, 1987. http://wrap.warwick.ac.uk/98453/.
Texto completoWang, Qingqi. "Regulation of motility in Listeria monocytogenes". Thesis, University of Nottingham, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490996.
Texto completoLibros sobre el tema "Motility"
Bray, Dennis. Cell movements: From molecules to motility. 2a ed. New York: Garland Pub., 2001.
Buscar texto completoRidley, Anne, Michelle Peckham y Peter Clark, eds. Cell Motility. Chichester, UK: John Wiley & Sons, Ltd, 2004. http://dx.doi.org/10.1002/0470011742.
Texto completoGrundy, David. Gastrointestinal Motility. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-010-9355-2.
Texto completoRao, Satish S. C., Jeffrey L. Conklin, Frederick C. Johlin, Joseph A. Murray, Konrad S. Schulze-Delrieu y Robert W. Summers, eds. Gastrointestinal Motility. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4803-4.
Texto completoW, Read N., ed. Gastrointestinal motility : which test? Peterfield: Wrightson Biomedical, 1989.
Buscar texto completoMelkonian, Michael, ed. Algal Cell Motility. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-9683-7.
Texto completoGoldberg, I. D., ed. Cell Motility Factors. Basel: Birkhäuser Basel, 1991. http://dx.doi.org/10.1007/978-3-0348-7494-6.
Texto completoCarlier, Marie-France, ed. Actin-based Motility. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9301-1.
Texto completoVerma, Navin Kumar, ed. T-Cell Motility. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9036-8.
Texto completoBardan, Eytan y Reza Shaker, eds. Gastrointestinal Motility Disorders. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-59352-4.
Texto completoCapítulos de libros sobre el tema "Motility"
Turnbull, Lynne y Cynthia B. Whitchurch. "Motility Assay: Twitching Motility". En Methods in Molecular Biology, 73–86. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0473-0_9.
Texto completoAmils, Ricardo. "Motility". En Encyclopedia of Astrobiology, 1097–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1028.
Texto completoHuang, Cheng-Long. "Motility". En Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_3842-3.
Texto completoAmils, Ricardo. "Motility". En Encyclopedia of Astrobiology, 1644–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1028.
Texto completoHuang, Cheng-Long. "Motility". En Encyclopedia of Cancer, 2924–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-46875-3_3842.
Texto completoHuang, Cheng-Long. "Motility". En Encyclopedia of Cancer, 2374–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_3842.
Texto completoAnderson, O. Roger. "Motility". En Comparative Protozoology, 350–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-662-11340-0_18.
Texto completoAmils, Ricardo. "Motility". En Encyclopedia of Astrobiology, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1028-2.
Texto completoAmils, Ricardo. "Motility". En Encyclopedia of Astrobiology, 2029–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1028.
Texto completoGuraya, Sardul S. "Sperm Motility". En Biology of Spermatogenesis and Spermatozoa in Mammals, 338–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71638-6_13.
Texto completoActas de conferencias sobre el tema "Motility"
"1st World Congress on Pediatric Neurogastroenterology and Motility". En 1st World Congress on Pediatric Neurogastroenterology and Motility. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88966-544-0.
Texto completoHidayatullah, Priyanto, Iwan Awaludin, Reyhan Damar Kusumo y Muhammad Nuriyadi. "Automatic sperm motility measurement". En 2015 International Conference on Information Technology Systems and Innovation (ICITSI). IEEE, 2015. http://dx.doi.org/10.1109/icitsi.2015.7437674.
Texto completoVourc’h, Thomas, Julien Léopoldès, Annick Méjean y Hassan Peerhossaini. "Motion of Active Fluids: Diffusion Dynamics of Cyanobacteria". En ASME 2016 Fluids Engineering Division Summer Meeting collocated with the ASME 2016 Heat Transfer Summer Conference and the ASME 2016 14th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2016. http://dx.doi.org/10.1115/fedsm2016-7526.
Texto completoYunardi, Riky Tri, Agung Budianto Achmad y Qurrotul A'yun. "Imaging Motility Pattern Analyzer Based on Optical Flow on Mice Sperm Cells Motility". En 2020 10th Electrical Power, Electronics, Communications, Controls and Informatics Seminar (EECCIS). IEEE, 2020. http://dx.doi.org/10.1109/eeccis49483.2020.9263448.
Texto completoFadlallah, Hadi, Hassan Peerhossaini, Christopher De Groot y Mojtaba Jarrahi. "Motility Response to Hydrodynamic Stress During the Growth Cycle in Active Fluid Suspensions". En ASME 2020 Fluids Engineering Division Summer Meeting collocated with the ASME 2020 Heat Transfer Summer Conference and the ASME 2020 18th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2020. http://dx.doi.org/10.1115/fedsm2020-20125.
Texto completoBiener, Gabriel, Emmanuel Vrotsos, Kiminogu Sugaya y Aristide Dogariu. "Optical Torques Guide Cell Motility". En Conference on Lasers and Electro-Optics. Washington, D.C.: OSA, 2009. http://dx.doi.org/10.1364/cleo.2009.cmmm2.
Texto completoSmallwood, Nour, Mangnall, Smythe y Brown. "Impedance Imaging and Gastric Motility". En Proceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1992. http://dx.doi.org/10.1109/iembs.1992.590125.
Texto completoSmallwood, R. H., S. Nour, Y. Mangnall, A. Smythe y B. H. Brown. "Impedance imaging and gastric motility". En 1992 14th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1992. http://dx.doi.org/10.1109/iembs.1992.5762022.
Texto completoIglesias, Pablo A. "Excitable systems in cell motility". En 2013 IEEE 52nd Annual Conference on Decision and Control (CDC). IEEE, 2013. http://dx.doi.org/10.1109/cdc.2013.6759973.
Texto completoXiong, Yuan y Pablo A. Iglesias. "Automated characterization of amoeboid motility". En 2009 43rd Annual Conference on Information Sciences and Systems (CISS). IEEE, 2009. http://dx.doi.org/10.1109/ciss.2009.5054747.
Texto completoInformes sobre el tema "Motility"
Wells, Alan, Douglas A. Lauffenburger y Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, julio de 2004. http://dx.doi.org/10.21236/ada428576.
Texto completoWells, Alan, Douglas A. Lauffenburger y Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, julio de 2002. http://dx.doi.org/10.21236/ada410314.
Texto completoWells, Alan, Douglas A. Lauffenburger y Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, julio de 2003. http://dx.doi.org/10.21236/ada417877.
Texto completoBodt, B. A. y R. J. Young. Hyperactivated Rabbit Sperm Cell Motility Parameters. Fort Belvoir, VA: Defense Technical Information Center, marzo de 1995. http://dx.doi.org/10.21236/ada294502.
Texto completoChirgwin, John. Role of Autocrine Motility in Osteolytic Metastasis. Fort Belvoir, VA: Defense Technical Information Center, abril de 2000. http://dx.doi.org/10.21236/ada391901.
Texto completoBrackanbury, Robert W. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2001. http://dx.doi.org/10.21236/ada403381.
Texto completoChirgwin, John M. Role of Autocrine Motility Factor in Osteolytic Metastasis. Fort Belvoir, VA: Defense Technical Information Center, abril de 2002. http://dx.doi.org/10.21236/ada408718.
Texto completoBrackenbury, Robert W. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2002. http://dx.doi.org/10.21236/ada409404.
Texto completoBrackenbury, Robert. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, agosto de 1999. http://dx.doi.org/10.21236/ada390725.
Texto completoBrackenbury, Robert. Control of Carcinoma Cell Motility by E-cadherin. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2000. http://dx.doi.org/10.21236/ada393429.
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