Littérature scientifique sur le sujet « Non muscle myosin II A »
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Articles de revues sur le sujet "Non muscle myosin II A"
Watanabe, T., H. Hosoya et S. Yonemura. « 1P205 Live imaging of Non-muscle myosin II in epithelial cells ». Seibutsu Butsuri 45, supplement (2005) : S83. http://dx.doi.org/10.2142/biophys.45.s83_1.
Texte intégralUbukawa, Kumi, Yong-Mei Guo, Masayuki Takahashi, Makoto Hirokawa, Yoshihiro Michishita, Miho Nara, Hiroyuki Tagawa et al. « Enucleation of human erythroblasts involves non-muscle myosin IIB ». Blood 119, no 4 (26 janvier 2012) : 1036–44. http://dx.doi.org/10.1182/blood-2011-06-361907.
Texte intégralDasbiswas, Kinjal, Shiqiong Hu, Frank Schnorrer, Samuel A. Safran et Alexander D. Bershadsky. « Ordering of myosin II filaments driven by mechanical forces : experiments and theory ». Philosophical Transactions of the Royal Society B : Biological Sciences 373, no 1747 (9 avril 2018) : 20170114. http://dx.doi.org/10.1098/rstb.2017.0114.
Texte intégralWrighton, Katharine H. « Non-muscle myosin II in kidney morphogenesis ». Nature Reviews Nephrology 13, no 7 (30 mai 2017) : 384. http://dx.doi.org/10.1038/nrneph.2017.77.
Texte intégralLevinson, Howard, Blaine Mischen, Bruce Klitzman, Detlev Erdmann et L. Scott Levin. « Non muscle myosin II regulates contractile phenotypes ». Journal of the American College of Surgeons 205, no 3 (septembre 2007) : S60—S61. http://dx.doi.org/10.1016/j.jamcollsurg.2007.06.148.
Texte intégralMaciver, Sutherland K. « Myosin II function in non-muscle cells ». BioEssays 18, no 3 (mars 1996) : 179–82. http://dx.doi.org/10.1002/bies.950180304.
Texte intégralPorro, Chiara, Antonio Pennella, Maria Antonietta Panaro et Teresa Trotta. « Functional Role of Non-Muscle Myosin II in Microglia : An Updated Review ». International Journal of Molecular Sciences 22, no 13 (22 juin 2021) : 6687. http://dx.doi.org/10.3390/ijms22136687.
Texte intégralTakubo, T., S. Wakui, K. Daigo, K. Kurokata, T. Ohashi, K. Katayama et M. Hino. « Expression of non-muscle type myosin heavy polypeptide 9 (MYH9) in mammalian cells ». European Journal of Histochemistry 47, no 4 (26 juin 2009) : 345. http://dx.doi.org/10.4081/845.
Texte intégralJuanes-García, Alba, Clara Llorente-González et Miguel Vicente-Manzanares. « Molecular control of non-muscle myosin II assembly ». Oncotarget 7, no 5 (18 janvier 2016) : 5092–93. http://dx.doi.org/10.18632/oncotarget.6936.
Texte intégralWan, Xiaohu. « Counting Molecules in Non-Muscle Myosin II Filaments ». Biophysical Journal 108, no 2 (janvier 2015) : 322a. http://dx.doi.org/10.1016/j.bpj.2014.11.1750.
Texte intégralThèses sur le sujet "Non muscle myosin II A"
Frei, Ryan. « Regulatory Elements of Drosophila Non-Muscle Myosin II ». Thesis, University of Oregon, 2013. http://hdl.handle.net/1794/12954.
Texte intégral2015-07-11
Swailes, Nathan. « Actin and non-muscle myosin II in pre-fusion myoblasts ». Thesis, University of Leeds, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.416842.
Texte intégralPicariello, Hannah Stubbs. « The Diverse Roles of Non-muscle Myosin II in Tumorigenesis ». Case Western Reserve University School of Graduate Studies / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=case1562680454131993.
Texte intégralKhan, Protiti. « The Role of Myosin Light Chain Kinase and Non Muscle Myosin II In Ras Signaling to ERK ». Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_theses/177.
Texte intégralSankara, Narayana Gautham Hari Narayana. « Role of non-muscle myosin-II isoforms in adherens junction biogenesis and collective migration ». Thesis, Université de Paris (2019-....), 2019. https://theses.md.univ-paris-diderot.fr/SANKARA_NARAYANA_Gautham_Hari_Naryana_va.pdf.
Texte intégralAdherens junction formation and remodeling is essential for many biological processes like embryo compaction, tissue morphogenesis and wound healing. It is now well described that non-muscle myosin II (NMII) acts as a mechanical support and force-generator for E-cadherin junctions during collective migration and morphogenesis. However, the contribution of NMII during early steps of junction formation remains obscure, probably because of the technical difficulty to catch such a transient event. In this work, we investigate the role of non-muscle myosin II isoforms (NMIIA and NMIIB) during adherens junction biogenesis in MDCK cells, using an in vitro reductionist approach. This system, based on chemically switchable micropatterns allows a spatio-temporal control of adherens junction formation. Our observations on MDCK cells show that the cells form irreversible E-cadherin based contacts, junction elongation is accompanied by the repolarization of actin cytoskeleton and nucleus-centrosome axis. Using isoform-specific ShRNA for NMIIA and IIB, we show that they have distinct contributions to junction formation and dynamics. NMIIA and NMIIB differentially regulate biogenesis of AJ through association with distinct actin networks. Analysis of junction dynamics, actin organization, and mechanical forces of control and knockdown cells for myosins revealed that NMIIA provides the mechanical tugging force necessary for cell-cell junction reinforcement and maintenance. NMIIB is involved in E-cadherin clustering, maintenance of a branched actin layer connecting E-cadherin complexes and perijunctional actin fibres leading to the building-up of anisotropic stress. These data reveal unanticipated complementary functions of NMIIA and NMIIB in the biogenesis and integrity of AJ
Ricketson, Derek Lee. « Drosophila non-muscle myosin II bipolar filament formation : importance of charged residues and specific domains for self-assembly / ». Connect to title online (Scholars' Bank) Connect to title online (ProQuest), 2009. http://hdl.handle.net/1794/10285.
Texte intégralDing, Siyu Serena. « Elucidating the role of non-muscle myosin II in Caenorhabditis elegans stem-like seam cell divisions ». Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:5b5cb805-327a-4a58-b3db-3787f5264efc.
Texte intégralRicketson, Derek Lee 1980. « Drosophila non-muscle myosin II bipolar filament formation : Importance of charged residues and specific domains for self-assembly ». Thesis, University of Oregon, 2009. http://hdl.handle.net/1794/10285.
Texte intégralNon-muscle myosin II generates contractile forces for processes such as cytokinesis, motility, and polarity. Contractility requires assembly of myosin molecules into bipolar mini-filaments through electrostatic interactions between coiled-coil tail domains of the heavy chains. Analyses of myosin II from various organisms have revealed "assembly domains" within the C-terminal portion of the tail domain that mediate filament formation. However, it has been unclear precisely how assembly domains interact with one another, or otherwise contribute to tail-tail interactions, to form the bipolar mini-filament structure. To understand tail domain interactions, we first identified a 90-residue region (1849-1940) of the Drosophila non-muscle myosin II tail domain that was necessary and sufficient for filament formation, using salt-dependent solubility and a novel fluorescence energy transfer assay. We identified residues within this "assembly domain" that were critical for filament assembly by analyzing the effect of point mutations. We found that single point mutations in specific positively charged regions completely disrupt filament assembly. Surprisingly, none of the negatively charged regions within the assembly domain are required for assembly. Most of the mutations in positively charged residues that disrupted filament assembly clustered within a 15-residue segment (1880-1894) that appears to form a critical interaction surface. Using this information, along with known geometrical constraints and electrostatic calculations, we constructed a structural model of the bipolar mini-filament. This model features one favored anti-parallel tail overlap and multiple slightly less stable alternative overlaps. The ability of the positive segment to interact with multiple negative regions explains the lack of required negatively charged residues in the assembly domain. To our knowledge, this structural model of the non- muscle myosin II bipolar filament is consistent with all physical observations and provides a framework for understanding the detailed mechanism by which this fundamental cellular structure is generated. This dissertation contains previously published and unpublished co-authored material.
Committee in charge: Tom Stevens, Chairperson, Chemistry; Kenneth Prehoda, Advisor, Chemistry; J. Andrew Berglund, Member, Chemistry; Christopher Doe, Member, Biology; Karen Guillemin, Outside Member, Biology
Sarkar, Saheli. « Combined Experimental and Mathematical Approach for Development of a Microfabrication-Based Model to Investigate Cell-Cell Interaction during Migration ». Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1301420667.
Texte intégralMessineo, Stefania. « Development of a gene targeting strategy (Recombinase-Mediated CAssette Exchange) to generate cellular models of MYH9-related disease ». Doctoral thesis, Università degli studi di Trieste, 2011. http://hdl.handle.net/10077/4603.
Texte intégralLa malattia MYH9-correlata (MYH9-RD) è una malattia autosomica dominante, caratterizzata da trombocitopenia congenita con piastrine di grandi dimensioni, aggregati nei neutrofili, sordità progressiva, cataratta e nefropatia. La MYH9-RD è causata da mutazioni nel gene MYH9 che codifica per la catena pesante della miosina non muscolare di classe II (miosina-9). I meccanismi patogenetici che causano questa malattia non sono ancora stati chiaramente identificati e il loro studio è complicato dalla mancanza di adeguati modelli cellulari e animali. Lo scopo di questo progetto è stato di generare un modello in vitro per studiare la funzione della miosina-9 e il ruolo di due mutazioni che incorrono nel gene MYH9: la R702C e la R1933X, che correlano rispettivamente con un fenotipo grave e lieve. Per questo motivo abbiamo deciso di manipolare le cellule staminali embrionali murine (ES), che sono pluripotenti e possono essere differenziate in diversi linee cellulari, compresa la linea megacariocitica. Per ingegnerizzare queste cellule ad alta efficienza abbiamo messo a punto una strategia nota come "scambio di cassette mediato da ricombinasi" (RMCE). Dopo l'integrazione di una cassetta fiancheggiata da siti FRT (sequenze di riconoscimento per l'enzima flippasi), il sistema ci ha permesso di scambiare diverse sequenze di DNA in presenza dell'enzima flippasi. Quindi il primo esone codificante del gene Myh9 è stato distrutto dall'inserimento, mediante ricombinazione omologa, di una cassetta fiancheggiata da due siti FRT contenente il gene reporter Beta-galattosidasi. Successivamente abbiamo scambiato questa cassetta con altre tre contenenti il cDNA Myh9 murino wild-type e i due mutati, generando i cloni ES che esprimono queste sequenze esogene sotto il controllo del promotore Myh9 endogeno. La caratterizzazione a livello dell'RNA e delle proteine di questi cloni ci ha portato a stabilire che gli alleli mutati e wild-type sono espressi allo stesso livello, suggerendo che le manipolazioni genetiche non interferiscono con i corretti meccanismi fisiologici di trascrizione e traduzione del gene Myh9. Tuttavia, mediante Western Blot abbiamo mostrato che la proteina miosina-9 è espressa a livello inferiore nei cloni mutati rispetto ai wild-type. Le analisi di immunofluorescenza per indagare la presenza di aggregati di miosina-9, che sono sempre presenti nei neutrofili di pazienti, non hanno rilevato alcuna variazione nella distribuzione della miosina-9, fatta eccezione per un segnale di intensità minore. Questi risultati indicano che, nonostante l'espressione dell'allele ingegnerizzato sia normale, la proteina mutata sembra essere degradata, almeno nelle cellule ES murine, determinando un effetto di aploinsufficienza delle mutazioni R702C e R1933X. Per accertare la loro pluripotenza, abbiamo differenziato dei cloni ES in corpi embrioidi e cardiomiociti, senza rivelare alcuna differenza tra i cloni mutanti e i wild-type. Dal momento che una caratteristica congenita dei pazienti MYH9-RD è la macrotrombocitopenia, abbiamo sviluppato un protocollo per differenziare i cloni mutati ES in megacariociti per indagare come le mutazioni in MYH9 portino a una impropria produzione di piastrine. In conclusione, per studiare la MYH9-RD abbiamo sviluppato una strategia che ci ha permesso di esprimere sequenze di interesse in cellule ES di topo sotto il controllo del promotore Myh9 endogeno. La differenziazione in vitro di queste cellule ci permetterà di studiare l'effetto delle mutazioni nel corso della megacariocitopoiesi. Inoltre, poiché le cellule ES possono anche essere usate per generare modelli animali, questa strategia ci permetterà di testare diverse ipotesi patogenetiche in vitro, prima di passare a studi in vivo.
XXIII Ciclo
1982
Livres sur le sujet "Non muscle myosin II A"
Turner, Neil, et Bertrand Knebelmann. MYH9 and renal disease. Sous la direction de Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0342_update_001.
Texte intégralBarker, Alan R., et Neil Armstrong. Pulmonary oxygen uptake kinetics. Sous la direction de Neil Armstrong et Willem van Mechelen. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198757672.003.0013.
Texte intégralChapitres de livres sur le sujet "Non muscle myosin II A"
Betapudi, Venkaiah. « Non-muscle Myosin II Motor Proteins in Human Health and Diseases ». Dans Genome Analysis and Human Health, 79–107. Singapore : Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-4298-0_5.
Texte intégralGoonewardene, Sanchia S., Raj Persad, Hanif Motiwala et David Albala. « NMIBC and Intravesical Chemotherapy—HIVEC I and HIVEC II ». Dans Management of Non-Muscle Invasive Bladder Cancer, 223–24. Cham : Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-28646-0_43.
Texte intégralBandman, E., D. L. Bourke et M. Wick. « Regulation of Myosin Heavy Chain Expression during Development, Maturation, and Regeneration in Avian Muscles : The Role of Myogenic and Non-Myogenic Factors ». Dans The Dynamic State of Muscle Fibers, sous la direction de Dirk Pette, 127–38. Berlin, Boston : De Gruyter, 1990. http://dx.doi.org/10.1515/9783110884784-013.
Texte intégralZolty, Ronald. « The Role of Neurohormonal Systems, Inflammatory Mediators and Oxydative Stress in Cardiomyopathy ». Dans Cardiomyopathy - Disease of the Heart Muscle. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97345.
Texte intégralLee-Gannon, Theo, Hannah Lehrenbaum, Rahul Sheth et Pradeep P.A. Mammen. « Clinical Management of DMD-Associated Cardiomyopathy ». Dans Cardiomyopathy - Disease of the Heart Muscle. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98919.
Texte intégralPartanen, Juhani, Urho Sompa et Miguel Muñoz-Ruiz. « Recording of Proprioceptive Muscle Reflexes in the Lower Extremity ». Dans Proprioception [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.95575.
Texte intégralActes de conférences sur le sujet "Non muscle myosin II A"
Zhang, Wenwu, Yidi Wu et Susan J. Gunst. « The Small GTPase RhoA Regulates Non-Muscle Myosin II Activity During Contractile Stimulation In Canine Tracheal Smooth Muscle ». Dans American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4131.
Texte intégralLi, Xiaona, Meiwen An, Li Wang et Wenzhou Wu. « The Experimental Study on the Functions of Non-Muscle Myosin II in Dividing Mammalian Cells ». Dans 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE 2009). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5163614.
Texte intégralHsu, Hui-Ju, Andrea Locke, Susan Q. Vanderzyl et Roland Kaunas. « Stretch-Induced Stress Fiber Remodeling and MAPK Activations Depend on Mechanical Strain Rate ». Dans ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53464.
Texte intégralSiegler, Jessica, Biji Mathew, Ting Wang, Tong Zhou, Michael S. Wade, Ralph Weichselbaum, Liliana Moreno-Vinasco et Joe G. Garcia. « Non-Muscle Myosin Light Chain Kinase Participates In Tumor Metastasis In Mice ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5084.
Texte intégralAprodu, Iuliana, Alberto Redaelli, Franco Maria Montevecchi et Monica Soncini. « Mechanical Characterization of Myosin II, Actin and Their Complexes by Molecular Mechanics Approach ». Dans ASME 8th Biennial Conference on Engineering Systems Design and Analysis. ASMEDC, 2006. http://dx.doi.org/10.1115/esda2006-95670.
Texte intégralSiegler, Jessica, Biji Mathew, Frances Lennon, Lynnette Gerhold, Chin-tu Chen, Patrick La Riviere, Christian Wietholt et al. « Non-Muscle Myosin Light Chain Kinase Promotes The Development Of Non-Small-Cell Lung Cancer ». Dans American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2062.
Texte intégralAlanazi, Samar M., Rosalin Mishra, Long Yuan, Hima Patel et Joan Garrett. « Abstract 4205 : The role of non-muscle myosin IIA in HER2+ breast cancers ». Dans Proceedings : AACR Annual Meeting 2020 ; April 27-28, 2020 and June 22-24, 2020 ; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4205.
Texte intégralMartin, Ryan D., Jayashree Banerjee, Meenakshi Lakshminarayanan, Yuxia Cao et Maria I. Ramirez. « T1± Interacts With Myh9, A Non-Muscle Myosin, In Type I Lung Epithelial Cells ». Dans American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6310.
Texte intégralBowers, Robert, Danyelle M. Townsend, Yefim Manevich et Kenneth D. Tew. « Abstract 5136 : Sulfiredoxin promotes cell migration through direct interaction with non muscle myosin IIa ». Dans Proceedings : AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010 ; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5136.
Texte intégralMoreno-Vinasco, Liliana, Syed R. Zaidi, Saad Sammani, Tamara Mirzapoiazova, Roberto F. Machado et Joe G. N. Garcia. « Role Of Non-muscle Myosin Light Chain Kinase In Hypoxia-induced Murine Pulmonary Hypertension ». Dans American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5245.
Texte intégralRapports d'organisations sur le sujet "Non muscle myosin II A"
Kanner, Joseph, Edwin Frankel, Stella Harel et Bruce German. Grapes, Wines and By-products as Potential Sources of Antioxidants. United States Department of Agriculture, janvier 1995. http://dx.doi.org/10.32747/1995.7568767.bard.
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