Academic literature on the topic 'Motility'
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Journal articles on the topic "Motility"
Boivin, M., M. Riberdy, M. C. Raymond, L. Trudel, and P. Poitras. "Motilin and the postprandial motility of the antrum." Canadian Journal of Physiology and Pharmacology 70, no. 11 (November 1, 1992): 1491–95. http://dx.doi.org/10.1139/y92-211.
Full textLayer, P., A. T. Chan, V. L. Go, and E. P. DiMagno. "Human pancreatic secretion during phase II antral motility of the interdigestive cycle." American Journal of Physiology-Gastrointestinal and Liver Physiology 254, no. 2 (February 1, 1988): G249—G253. http://dx.doi.org/10.1152/ajpgi.1988.254.2.g249.
Full textMalfertheiner, P., M. G. Sarr, M. P. Spencer, and 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, no. 3 (September 1, 1989): G415—G422. http://dx.doi.org/10.1152/ajpgi.1989.257.3.g415.
Full textMuller, E. L., P. A. Grace, R. L. Conter, J. J. Roslyn, and H. A. Pitt. "Influence of motilin and cholecystokinin on sphincter of Oddi and duodenal mobility." American Journal of Physiology-Gastrointestinal and Liver Physiology 253, no. 5 (November 1, 1987): G679—G683. http://dx.doi.org/10.1152/ajpgi.1987.253.5.g679.
Full textSakahara, Satoshi, Zuoyun Xie, Kanako Koike, Satoya Hoshino, Ichiro Sakata, Sen-ichi Oda, Toku Takahashi, and 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, no. 4 (October 2010): R1106—R1113. http://dx.doi.org/10.1152/ajpregu.00278.2010.
Full textAyutama, Wanodia, Tuty Rizkianti, and 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, no. 2 (October 29, 2020): 335. http://dx.doi.org/10.24912/jmstkik.v4i2.7788.
Full textChung, S. A., G. R. Greenberg, and 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, no. 8 (August 1, 1992): 1148–53. http://dx.doi.org/10.1139/y92-159.
Full textNahdiyah, Ayu Naila, Hari Santoso, and Hasan Zayadi. "Pengaruh Fraksi Ejakulasi terhadap Motilitas Spermatozoa Kambing Peranakan Etawa (Capra aegagrus)." BIOSAINTROPIS (BIOSCIENCE-TROPIC) 5, no. 2 (January 10, 2020): 72–76. http://dx.doi.org/10.33474/e-jbst.v5i2.288.
Full textKellow, John E., and Yiu-Kay Chan. "Advanced motility and motility disorders." Current Opinion in Gastroenterology 11, no. 2 (March 1995): 106–11. http://dx.doi.org/10.1097/00001574-199503000-00003.
Full textPeeters, T. L., J. Janssens, C. Plets, and G. Vantrappen. "Interdigestive Motility and Motilin in Hypophysectomized Patients." Scandinavian Journal of Gastroenterology 23, no. 1 (January 1988): 71–74. http://dx.doi.org/10.3109/00365528809093850.
Full textDissertations / Theses on the topic "Motility"
Cao, Luyan. "bases structurales de la motilité des kinésines." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS267/document.
Full textKinesins 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.
Full textPatankar, RoySuneel V. "Studies in gallbladder motility." Thesis, University of Southampton, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296188.
Full textUllah, Sana. "Factors governing gastrointestinal motility." Thesis, University of Hull, 2012. http://hydra.hull.ac.uk/resources/hull:7166.
Full textStanley, Hugh Gerard. "Neural mechanisms in abomasal motility." Thesis, University of Edinburgh, 1988. http://hdl.handle.net/1842/30009.
Full textRoss, Oliver N. "Algal motility in variable turbulence." Thesis, University of Southampton, 2004. https://eprints.soton.ac.uk/45995/.
Full textBiondini, Marco. "RALlying through cell motility and invasion." Thesis, Paris 11, 2014. http://www.theses.fr/2014PA11T042.
Full textMetastasis 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.
Full textThe 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/.
Full textWang, Qingqi. "Regulation of motility in Listeria monocytogenes." Thesis, University of Nottingham, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490996.
Full textBooks on the topic "Motility"
Bray, Dennis. Cell movements: From molecules to motility. 2nd ed. New York: Garland Pub., 2001.
Find full textRidley, Anne, Michelle Peckham, and Peter Clark, eds. Cell Motility. Chichester, UK: John Wiley & Sons, Ltd, 2004. http://dx.doi.org/10.1002/0470011742.
Full textGrundy, David. Gastrointestinal Motility. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-010-9355-2.
Full textRao, Satish S. C., Jeffrey L. Conklin, Frederick C. Johlin, Joseph A. Murray, Konrad S. Schulze-Delrieu, and Robert W. Summers, eds. Gastrointestinal Motility. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4803-4.
Full textW, Read N., ed. Gastrointestinal motility : which test? Peterfield: Wrightson Biomedical, 1989.
Find full textMelkonian, Michael, ed. Algal Cell Motility. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-9683-7.
Full textGoldberg, I. D., ed. Cell Motility Factors. Basel: Birkhäuser Basel, 1991. http://dx.doi.org/10.1007/978-3-0348-7494-6.
Full textCarlier, Marie-France, ed. Actin-based Motility. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9301-1.
Full textVerma, Navin Kumar, ed. T-Cell Motility. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9036-8.
Full textBardan, Eytan, and Reza Shaker, eds. Gastrointestinal Motility Disorders. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-59352-4.
Full textBook chapters on the topic "Motility"
Turnbull, Lynne, and Cynthia B. Whitchurch. "Motility Assay: Twitching Motility." In 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.
Full textAmils, Ricardo. "Motility." In Encyclopedia of Astrobiology, 1097–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1028.
Full textHuang, Cheng-Long. "Motility." In Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_3842-3.
Full textAmils, Ricardo. "Motility." In Encyclopedia of Astrobiology, 1644–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1028.
Full textHuang, Cheng-Long. "Motility." In Encyclopedia of Cancer, 2924–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-46875-3_3842.
Full textHuang, Cheng-Long. "Motility." In Encyclopedia of Cancer, 2374–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_3842.
Full textAnderson, O. Roger. "Motility." In Comparative Protozoology, 350–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-662-11340-0_18.
Full textAmils, Ricardo. "Motility." In Encyclopedia of Astrobiology, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1028-2.
Full textAmils, Ricardo. "Motility." In Encyclopedia of Astrobiology, 2029–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1028.
Full textGuraya, Sardul S. "Sperm Motility." In 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.
Full textConference papers on the topic "Motility"
"1st World Congress on Pediatric Neurogastroenterology and Motility." In 1st World Congress on Pediatric Neurogastroenterology and Motility. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88966-544-0.
Full textHidayatullah, Priyanto, Iwan Awaludin, Reyhan Damar Kusumo, and Muhammad Nuriyadi. "Automatic sperm motility measurement." In 2015 International Conference on Information Technology Systems and Innovation (ICITSI). IEEE, 2015. http://dx.doi.org/10.1109/icitsi.2015.7437674.
Full textVourc’h, Thomas, Julien Léopoldès, Annick Méjean, and Hassan Peerhossaini. "Motion of Active Fluids: Diffusion Dynamics of Cyanobacteria." In 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.
Full textYunardi, Riky Tri, Agung Budianto Achmad, and Qurrotul A'yun. "Imaging Motility Pattern Analyzer Based on Optical Flow on Mice Sperm Cells Motility." In 2020 10th Electrical Power, Electronics, Communications, Controls and Informatics Seminar (EECCIS). IEEE, 2020. http://dx.doi.org/10.1109/eeccis49483.2020.9263448.
Full textFadlallah, Hadi, Hassan Peerhossaini, Christopher De Groot, and Mojtaba Jarrahi. "Motility Response to Hydrodynamic Stress During the Growth Cycle in Active Fluid Suspensions." In 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.
Full textBiener, Gabriel, Emmanuel Vrotsos, Kiminogu Sugaya, and Aristide Dogariu. "Optical Torques Guide Cell Motility." In Conference on Lasers and Electro-Optics. Washington, D.C.: OSA, 2009. http://dx.doi.org/10.1364/cleo.2009.cmmm2.
Full textSmallwood, Nour, Mangnall, Smythe, and Brown. "Impedance Imaging and Gastric Motility." In 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.
Full textSmallwood, R. H., S. Nour, Y. Mangnall, A. Smythe, and B. H. Brown. "Impedance imaging and gastric motility." In 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.
Full textIglesias, Pablo A. "Excitable systems in cell motility." In 2013 IEEE 52nd Annual Conference on Decision and Control (CDC). IEEE, 2013. http://dx.doi.org/10.1109/cdc.2013.6759973.
Full textXiong, Yuan, and Pablo A. Iglesias. "Automated characterization of amoeboid motility." In 2009 43rd Annual Conference on Information Sciences and Systems (CISS). IEEE, 2009. http://dx.doi.org/10.1109/ciss.2009.5054747.
Full textReports on the topic "Motility"
Wells, Alan, Douglas A. Lauffenburger, and Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada428576.
Full textWells, Alan, Douglas A. Lauffenburger, and Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada410314.
Full textWells, Alan, Douglas A. Lauffenburger, and Timothy Turner. Cell Motility in Tumor Invasion. Fort Belvoir, VA: Defense Technical Information Center, July 2003. http://dx.doi.org/10.21236/ada417877.
Full textBodt, B. A., and R. J. Young. Hyperactivated Rabbit Sperm Cell Motility Parameters. Fort Belvoir, VA: Defense Technical Information Center, March 1995. http://dx.doi.org/10.21236/ada294502.
Full textChirgwin, John. Role of Autocrine Motility in Osteolytic Metastasis. Fort Belvoir, VA: Defense Technical Information Center, April 2000. http://dx.doi.org/10.21236/ada391901.
Full textBrackanbury, Robert W. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada403381.
Full textChirgwin, John M. Role of Autocrine Motility Factor in Osteolytic Metastasis. Fort Belvoir, VA: Defense Technical Information Center, April 2002. http://dx.doi.org/10.21236/ada408718.
Full textBrackenbury, Robert W. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada409404.
Full textBrackenbury, Robert. Control of Carcinoma Cell Motility by E-Cadherin. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada390725.
Full textBrackenbury, Robert. Control of Carcinoma Cell Motility by E-cadherin. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada393429.
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