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Gotowe bibliografie tematyczne / Vimentin

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Gotowa bibliografia na temat „Vimentin”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 lipca 2025

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Artykuły w czasopismach na temat "Vimentin"

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Dent, J. A., R. B. Cary, J. B. Bachant, A. Domingo, and M. W. Klymkowsky. "Host cell factors controlling vimentin organization in the Xenopus oocyte." Journal of Cell Biology 119, no. 4 (1992): 855–66. http://dx.doi.org/10.1083/jcb.119.4.855.

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To study vimentin filament organization in vivo we injected Xenopus oocytes, which have no significant vimentin system of their own, with in vitro-synthesized RNAs encoding Xenopus vimentins. Exogenous vimentins were localized primarily to the cytoplasmic surface of the nucleus and to the subplasma membrane "cortex." In the cortex of the animal hemisphere, wild-type vimentin forms punctate structures and short filaments. In contrast, long anastomosing vimentin filaments are formed in the vegetal hemisphere cortex. This asymmetry in the organization of exogenous vimentin is similar to that of t

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Niazi Tabar, Amirreza, Hossein Azizi, Danial Hashemi Karoii, and Thomas Skutella. "Testicular Localization and Potential Function of Vimentin Positive Cells during Spermatogonial Differentiation Stages." Animals 12, no. 3 (2022): 268. http://dx.doi.org/10.3390/ani12030268.

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Vimentin is a type of intermediate filament (IF) and one of the first filaments expressed in spermatogenesis. Vimentin plays numerous roles, consisting of the determination of cell shape, differentiation, cell motility, the maintenance of cell junctions, intracellular trafficking, and assisting in keeping normal differentiating germ cell morphology. This study investigated the vimentin expression in two populations of undifferentiated and differentiated spermatogonia. We examined vimentin expression in vivo and in vitro by immunocytochemistry (ICC), immunohistochemistry (IMH), and Fluidigm rea

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Kohl, Tobias, Melanie von Brandenstein, Andreas Stog, et al. "Vimentin 3 and endothelin in prostate cancer." Journal of Clinical Oncology 36, no. 6_suppl (2018): 349. http://dx.doi.org/10.1200/jco.2018.36.6_suppl.349.

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349 Background: An upregulation of vimentin 3, a truncated version of the full length vimentin, with an unknown function, was previously described by our group, in a direct dependency of increased ET-1 levels. We analyzed now vimentin 3 in further genitourinary cancers. Here, we describe our findings how vimentin 3 is part of the signaling pathways from Endothelin-1 (ET-1) and the Endothelin-A-Receptor (ETAR) and how it correlates with aggressive tumor behavior in a PCa cell culture and in human tissue and serum samples from PCa patients. Methods: DU145 cells were cultured. We stimulated with

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Costigliola, Nancy, Liya Ding, Christoph J. Burckhardt, et al. "Vimentin fibers orient traction stress." Proceedings of the National Academy of Sciences 114, no. 20 (2017): 5195–200. http://dx.doi.org/10.1073/pnas.1614610114.

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The intermediate filament vimentin is required for cells to transition from the epithelial state to the mesenchymal state and migrate as single cells; however, little is known about the specific role of vimentin in the regulation of mesenchymal migration. Vimentin is known to have a significantly greater ability to resist stress without breaking in vitro compared with actin or microtubules, and also to increase cell elasticity in vivo. Therefore, we hypothesized that the presence of vimentin could support the anisotropic mechanical strain of single-cell migration. To study this, we fluorescent

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Wang, Ruping, Sakeeb Khan, Guoning Liao, Yidi Wu, and Dale D. Tang. "Nestin Modulates Airway Smooth Muscle Cell Migration by Affecting Spatial Rearrangement of Vimentin Network and Focal Adhesion Assembly." Cells 11, no. 19 (2022): 3047. http://dx.doi.org/10.3390/cells11193047.

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Airway smooth muscle cell migration plays a role in the progression of airway remodeling, a hallmark of allergic asthma. However, the mechanisms that regulate cell migration are not yet entirely understood. Nestin is a class VI intermediate filament protein that is involved in the proliferation/regeneration of neurons, cancer cells, and skeletal muscle. Its role in cell migration is not fully understood. Here, nestin knockdown (KD) inhibited the migration of human airway smooth muscle cells. Using confocal microscopy and the Imaris software, we found that nestin KD attenuated focal adhesion si

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Ivaska, Johanna. "Vimentin." Small GTPases 2, no. 1 (2011): 51–53. http://dx.doi.org/10.4161/sgtp.2.1.15114.

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Cary, R. B., M. W. Klymkowsky, R. M. Evans, A. Domingo, J. A. Dent, and L. E. Backhus. "Vimentin's tail interacts with actin-containing structures in vivo." Journal of Cell Science 107, no. 6 (1994): 1609–22. http://dx.doi.org/10.1242/jcs.107.6.1609.

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The tail domain of the intermediate filament (IF) protein vimentin is unnecessary for IF assembly in vitro. To study the role of vimentin's tail in vivo, we constructed a plasmid that directs the synthesis of a ‘myc-tagged’ version of the Xenopus vimentin-1 tail domain in bacteria. This polypeptide, mycVimTail, was purified to near homogeneity and injected into cultured Xenopus A6 cells. In these cells the tail polypeptide co-localized with actin even in the presence of cytochalasin. Two myc-tagged control polypeptides argue for the specificity of this interaction. First, a similarly myc-tagge

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Paramita, Paramita, Melva Louisa, and Nafrialdi Nafrialdi. "Increased vimentin mRNA expression in MCF-7 breast cancer cell line after repeated endoxifen-treatment." Medical Journal of Indonesia 25, no. 4 (2017): 207–13. http://dx.doi.org/10.13181/mji.v25i4.1397.

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Background: Epithelial mesenchymal transition (EMT) plays a significant role in the development of cancer cell resistance to drugs. Vimentin, a type III intermediate filament protein, is a marker of EMT. Vimentin's over-expression in cancer correlates well with increased tumor growth, change in cell shape and poor prognosis. Endoxifen is an active metabolite of tamoxifen and has become a new potent agent in the treatment of breast cancer. This is a study that aimed to investigate the effect of endoxifen exposure with or without estradiol on cell viability, cell morphology and EMT progression t

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Ngai, J., V. C. Bond, B. J. Wold, and E. Lazarides. "Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences." Molecular and Cellular Biology 7, no. 11 (1987): 3955–70. http://dx.doi.org/10.1128/mcb.7.11.3955-3970.1987.

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We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. Expression of vimentin in differentiating MEL cells reflects the disappearance of vimentin filaments during mammalian erythropoiesis in vivo. In contrast, chicken erythroid cells express high levels of vimentin mRNA and vimentin filaments during terminal differentiation. We demonstrate here that chicken vimentin mRNA

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Ngai, J., V. C. Bond, B. J. Wold, and E. Lazarides. "Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences." Molecular and Cellular Biology 7, no. 11 (1987): 3955–70. http://dx.doi.org/10.1128/mcb.7.11.3955.

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We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. Expression of vimentin in differentiating MEL cells reflects the disappearance of vimentin filaments during mammalian erythropoiesis in vivo. In contrast, chicken erythroid cells express high levels of vimentin mRNA and vimentin filaments during terminal differentiation. We demonstrate here that chicken vimentin mRNA

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Rozprawy doktorskie na temat "Vimentin"

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Besarani, Dler. "Anti-Vimentin Antibodies in Renal Transplantation." Thesis, Imperial College London, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.526360.

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Wong, Kai-lun, and 黃棨麟. "Nanomechanical studies of vimentin intermediate filaments." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hub.hku.hk/bib/B49799617.

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Intermediate filaments, microtubules and microfilaments are the major components of the cytoskeleton. Though it is known that intermediate filaments play an important role in the mechanical behaviour of cells, it is surprising that their mechanical properties are far from being fully understood. The morphology and assembly process of the vimentin intermediate filaments (IFs) were studied using transmission electron microscopy (TEM) and atomic force spectroscopy (AFM). The width of the vimentin was found to change as the assembly proceeded. This finding agrees with the literature about the

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Carter, D. Vaughan. "The role of vimentin antibodies in transplantation." Thesis, University of Newcastle Upon Tyne, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424154.

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Vechio, Aluana Maria da Costa Dal. "Expressão da vimentina em cultivo tridimensional de linhagens celulares derivadas de carcinoma epidermóide de boca." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/23/23141/tde-08042009-160336/.

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O carcinoma epidermóide representa mais de 90% das neoplasias malignas de cabeça e de pescoço, apresentando taxas elevadas de morbi-mortalidade. Proteínas relacionadas à invasão e proliferação celular estão em evidência devido ao seu envolvimento na carcinogênese, a exemplo da vimentina, encontrada em células de origem mesodérmica. Sua presença em células epiteliais neoplásicas contribui na transição epitélio mesenquimal e está associada à tumorigênese, à invasão celular e à metástase. O propósito deste estudo foi analisar através de métodos qualitativos (imunofluorescência e imunoistoquímica)

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Gianelo, Maikol Carlos Simões. "Estudo da resposta regenerativa do músculo sóleo de ratas bebês após procedimento de imobilização e reabilitação pelo alongamento." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/17/17152/tde-02072015-122858/.

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Modelos de desusos do músculo esquelético como imobilização gessada, suspensão são frequentemente utilizados em grupos de pesquisas experimentais. Esse tempo de desuso por período prolongado pode determinar alterações significativas na citoarquitetura muscular. Este estudo teve como objetivo avaliar os aspectos morfológicos do músculo sóleo de ratas em desenvolvimento pós-natal que tiveram seus membros posteriores direitos imobilizados, e posteriormente foram submetidas ao protocolo passivo de alongamento (alongamento manual passivo intermitente), por um período de sete dias. Utilizou-se 20 ra

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Pattabiraman, Sundararaghavan [Verfasser]. "Vimentin protects differentiating stem cells from stress / Sundararaghavan Pattabiraman." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2020. http://d-nb.info/1223171582/34.

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McGinn, Mary Catherine. "Interplay Between Keratin and Vimentin Expression in Oral Cancer." VCU Scholars Compass, 2010. http://scholarscompass.vcu.edu/etd/49.

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Previous research in our laboratory found that inhibiting expression of vimentin, a marker of epithelial-to mesenchymal transition, inhibited cell growth and motility in vitro and in vivo. Tumors derived from vimentin knockdown cells showed features of epithelial redifferentiation and increased expression of differentiation-specific keratins. It is unknown what causes re-expression of keratins when vimentin is inhibited. Although, canonical Wnt signaling may activate NF-κB and repress of keratin and/or induce vimentin expression through β-catenin. We hypothesize that downregulation of differen

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Kirmse, Robert. "Studium der Wachstumskinetik von Intermediärfilamenten mit Hilfe von Vimentin." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:16-opus-83413.

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Fay, Nikta. "Parvoviral interactions with the cytoskeleton : exposing vimentin – the forgotten player." Thesis, University of British Columbia, 2014. http://hdl.handle.net/2429/50672.

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There are three structurally and functionally distinct cytoskeleton components: actin filaments, microtubules, and intermediate filaments (IFs). Among the three cytoskeleton networks IFs are understudied; consequently, there is a lack of information about the role of IFs during early viral infection. IFs have long been known to serve structural functions within the cell, and recently, additional functions have been elucidated, including novel roles during infection by many viruses. During early infection with the parvovirus minute virus of mice (MVM), prior to viral replication, I have found t

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Rato, Leila Sofia Coelho. "Vimentin interacts with the Akt/mTOR pathway mediating cell growth." Master's thesis, Universidade de Aveiro, 2017. http://hdl.handle.net/10773/22372.

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Mestrado em Bioquímica - Bioquímica Clínica<br>A vimentina é uma proteína da classe III dos filamentos intermédios que promove processos tais como proliferação, migração e invasão celular através da interação com diferentes vias de sinalização. No entanto, o papel da vimentina no crescimento celular é ainda pouco conhecido. Neste estudo, observamos que fibroblastos isolados de embriões de ratinhos sem vimentina (Vim -/- MEFs) eram mais pequenos que o tipo normal (WT). Assim, o objetivo deste estudo era entender de que forma a vimentina regula o crescimento celular. Com recurso a modelos in vit

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Książki na temat "Vimentin"

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Roser, Florian. Expression der Differenzierungsantigene A2B5, O4 und Vimentin im normalen menschlichen Hirngewebe. [s.n.], 1999.

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Mello, Ramon Andrade de. Vimentin Concepts and Molecular Mechanisms. Nova Science Publishers, Incorporated, 2013.

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Hennekes, Hartwig. Clonierung und Charakterisierung des Mausgens für das Intermediärfilamentprotein Vimentin. 1990.

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Perides, Georg. Wechselwirkung von Vimentin-Intermediärfilamenten mit natürlichen und artifiziellen Lipidmembranen. 1986.

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Otano, Marta. Immunozytologische Untersuchungen zur Expression von Vimentin und Zytokeratin in Plasma- und Plasmozytomzellen. 1991.

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Bonn, Universität, ed. Expressionsmuster von Desmin und Vimentin in Skelettmuskulatur bei Central-core-Erkrankung und neurogenen Prozessen. 1996.

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Künzig, Barbara Maria. Licht- und elektronenmikroskopische Untersuchungen von Vimentin, Desmin und GFAP an normalen intrakraniellen Gefässen des Menschen. 1993.

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Malzahn, Karin. Expression von Cytokeratinen und Vimentin in invasiven duktalen Mammacarcinomen und ihre Beziehung zu Tumordifferenzierung und Prognose. 1994.

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Senner, Volker. Spezifische Intergration modifizierter vimentin-cDNA in das Genom eukaryotischer Zellen und Untersuchungen zur Expression der Proteinmutanten. 1996.

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Link, Markus Norbert. Uberexpression des Intermediärfilament-Proteins Vimentin und seiner Subdomänen in einem bakteriellen Expressionssystem: Sowie Charakterisierung der Expressionsprodukte in vivo und in vitro. 1997.

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Części książek na temat "Vimentin"

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Koch, Clarissa M., and Karen M. Ridge. "Vimentin." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101951.

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Holdenrieder, S., and P. Stieber. "Vimentin." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3253.

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Holdenrieder, S., and P. Stieber. "Vimentin." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_3253-1.

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Koch, Clarissa M., and Karen M. Ridge. "Vimentin." In Encyclopedia of Signaling Molecules. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101951-1.

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Wang, Ning, and Dimitrijie Stamenovic. "Mechanics of vimentin intermediate filaments." In Mechanics of Elastic Biomolecules. Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0147-2_13.

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Gierten, B. "Autoantikörper gegen mutiertes citrulliniertes Vimentin." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3698.

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Gierten, B. "Autoantikörper gegen mutiertes citrulliniertes Vimentin." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_3698-1.

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Leong, Anthony S.-Y. "The Expression of Vimentin in Epithelial Neoplasms." In Progress in Surgical Pathology. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-662-09515-7_2.

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Schepers, Anna V., Julia Kraxner, Charlotta Lorenz, and Sarah Köster. "Mechanics of Single Vimentin Intermediate Filaments Under Load." In Optical Tweezers. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2229-2_24.

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Quax, Wim, and Hans Bloemendal. "Organization and Expression of the Vimentin and Desmin Genes." In Cell and Molecular Biology of the Cytoskeleton. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2151-4_5.

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Streszczenia konferencji na temat "Vimentin"

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Muszbek, L., R. Adåny, M. A. Glukhova, M. G. Frid, A. E. Kabakov, and V. E. Kot-e-liansky. "THE IDENTIFICATION OF VIMENTIN, AN INTERMEDIATE,FILAMENT SUBUNIT PROTEIN IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643900.

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In platelets the presence of basic subunit proteins of microtubules as well as microfilaments has been verified a long time ago and it was also shown that both of these cytoskeletal systems go through a tremendous reorganization during the activation process. Surprisingly, none of the components of intermediate filaments has so far been identified in these cells, perhaps because platelets were considered too motile to have intermediate filaments, the most static structures among the three major cytoskeletal systems. By using two different monoclonal antibodies (II C4 and II D8) here we attempt

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Schmidt, G., M. Kasoha, EF Solomayer, and R. Bohle. "Vimentin als Prognosefaktor beim triple negativen Mammakarzinom." In 38. Jahrestagung der Deutschen Gesellschaft für Senologie. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1651796.

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Raveendran, V. V., S. AlQattan, A. Alaiya, et al. "Interaction of S100A13 With Vimentin in Pulmonary Fibrosis." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a2232.

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Buehler, Markus J., and Je´re´mie Bertaud. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13103.

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Intermediate filaments (often abbreviated as IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells (Figure 1). It has been suggested that intermediate filaments are crucial in defining key mechanical functions of cells such as cell migration, cell division and mechanotransduction, and have also been referred to as the “safety belts of cells” reflecting their role in preventing exceedingly large cell stretch [1, 2]. Vimentin is a specific type of this protein filament found in fibroblasts, leukocytes, and blood vessel

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Ackbarow, Theodor, and Markus J. Buehler. "Superelasticity of Vimentin Coiled-Coil Intermediate Filaments: Atomistic and Continuum Studies." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176471.

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Vimentin coiled-coil alpha-helical dimers are elementary protein building blocks of intermediate filaments (IFs), an important component of the cell’s cytoskeleton that has been shown to control the large-deformation behavior of eukaryotic cell [1].

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Thaiparambil, J., L. Bender, E. Kline, et al. "Vimentin: A Novel Chemopreventive Target for Breast Cancer Metastasis." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-5063.

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Buehler, Markus J., and Zhao Qin. "Hierarchical Structure Controls Nanomechanical Properties of Vimentin Intermediate Filaments." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13102.

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Intermediate filaments (IFs), in addition to microtubules and microfilaments, are one of the three major components of the cytoskeleton in eukaryotic cells, playing a vital role in mechanotransduction and in providing mechanical stability to cells (Figure 1) [1]. Despite the importance of IF mechanics for cell biology and cell mechanics, the structural basis for their mechanical properties remains unknown. Specifically, our understanding of fundamental filament properties, such as the basis for their great extensibility, stiffening properties, and their exceptional mechanical resilience remain

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Zhu, Quansheng, Guy Lahat, Svetlana Bolshakov, et al. "Abstract 642: Vimentin is a novel anticancer therapeutic target." In 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.am10-642.

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Wang Xiao-Wu, Ding Gui-Rong, Zhao Tao, et al. "Effects of electromagnetic pulse on the vimentin of mice testes." In 4th International Symposium on Electromagnetic Compatibility 2007. IEEE, 2007. http://dx.doi.org/10.1109/elmagc.2007.4413530.

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Kayyali, Usamah S., Tiegang Liu, Oscar Guevara, and Nicholas S. Hill. "Role Of Vimentin Intermediate Filaments In Endothelial Permeability Barrier Regulation." In 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.a4182.

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Raporty organizacyjne na temat "Vimentin"

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อัศวานนท์, ประวิตร, รัชต์ธร หมอนจันทร์ та ถนอม บรรณประเสริฐ. โครงการวิจัยเพื่อพัฒนาเซลล์ต้นกำเนิดเส้นผม. จุฬาลงกรณ์มหาวิทยาลัย, 2011. https://doi.org/10.58837/chula.res.2011.25.

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งานวิจัยนี้ได้ทำการศึกษา และพัฒนากระบวนการแยกเซลล์ต้นกำเนิดเส้นผมชนิด dermal papilla จากเนื้อเยื่อต่อมขนบริเวณหนัง โดยใช้เทคนิคใหม่ “One-Step Enzyme digestion and Simple dissection” โดยอาศัยการตัดแยกเซลล์และเนื้อเยื่อส่วนต่าง ๆ จากต่อมขน (surgical microdissection) ภายใต้กล้องจุลทรรศน์ ชนิด stereomicroscope ร่วมกับการย่อยด้วยเอนไซน์ (enzymatic Dissociation) ชนิดผสมระหว่าง Dispase และ collagenase (Liberase DH) เพื่อแยกเซลล์ต้นกำเนิด และสามารถเพาะเลี้ยงเซลล์โดยใช้อาหารเลี้ยงเซลล์ (Culture media) และสารเร่งการเจริญเติบโต (growth factors และ cytokines) ที่เหมาะสม ทำให้สามารถเพาะเลี้ยงและเพิ่มจำนวนเ

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