Relevant bibliographies by topics / Matrice de collagène

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Matrice de collagène'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "Matrice de collagène"

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Van der Rest, M. "Biologie du collagène et maladies héréditaires de la matrice extracellulaire." médecine/sciences 3, no. 7 (1987): 411. http://dx.doi.org/10.4267/10608/3707.

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Gonçalves-Neto, Joaquim, S. S. Witzel, W. R. Teodoro, A. E. Carvaho-Junior, T. D. Fernandes, and N. H. Yoshinari. "Modifications de la composition de la matrice de collagène dans les tendinopathies du jambier postérieur." Revue du Rhumatisme 69, no. 3 (2002): 280–85. http://dx.doi.org/10.1016/s1169-8330(02)00286-7.

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Grosjean, Guillaume, Frédéric Sailhan, Mohamed Mezghani, and Jean-Pierre Courpied. "82 Efficacité de la rh-BMP-7/matrice collagène (OP-1) dans la consolidation des pseudarthroses post-fracturaires." Revue de Chirurgie Orthopédique et Réparatrice de l'Appareil Moteur 93, no. 7 (2007): 67. http://dx.doi.org/10.1016/s0035-1040(07)79455-2.

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Idoux, Romane, Sandrine Bretaud, Christine Berthier, Vincent Jacquemond, Florence Ruggiero, and Bruno Allard. "Étude physiopathologique de la myopathie de Bethlem à l’aide d’un modèle de poisson zèbre." médecine/sciences 35 (November 2019): 39–42. http://dx.doi.org/10.1051/medsci/2019182.

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La myopathie de Bethlem (BM) est une maladie caractérisée par des rétractions et une faiblesse musculaires. Cette pathologie résulte de mutations dans un des gènes codant l’une des trois chaînes α du collagène VI (COLVI), un composant de la matrice extracellulaire musculaire squelettique. Aujourd’hui, une question non résolue est de comprendre comment l’altération de COLVI présent à l’extérieur des cellules musculaires conduit à des modifications fonctionnelles dans les fibres musculaires. Le modèle poisson zèbre col6a1Δex14 est actuellement un modèle animal unique de la BM puisqu’il est le se
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Goldberg, A. J., D. A. Lee, D. L. Bader, and G. Bentley. "Un facteur de croissance durant la période de culture pourrait normaliser les capacités de synthèse (matrice et collagène) des chondrocytes autologues transplantés." Revue de Chirurgie Orthopédique et Réparatrice de l'Appareil Moteur 92, no. 7 (2006): 730. http://dx.doi.org/10.1016/s0035-1040(06)77669-3.

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PASTOUREAU, P. "Physiologie du développement du tissu osseux." INRAE Productions Animales 3, no. 4 (1990): 265–73. http://dx.doi.org/10.20870/productions-animales.1990.3.4.4385.

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Le tissu osseux est un tissu conjonctif qui a la particularité de se minéraliser. Ceci confère à l’os ses propriétés de banque minérale et de soutien mécanique de l’organisme. De son bon développement dépend celui de tous les autres tissus. Il est ainsi mis en place très tôt au cours de la période foetale et reste sous étroit contrôle, notamment endocrinien (GH et IGF-1), pendant toute la croissance mais aussi chez l’adulte dont le tissu osseux est le siège d’un remodelage permanent. La physiologie du développement du tissu osseux est bien connue, en particulier lorsqu’elle concerne l’ostéogen
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Atlan, M., M. Naouri, G. Lorette, E. Estève, and G. Zakine. "Traitement original des callosités plantaires douloureuses constitutionnelles par exérèse, matrice de collagène et d’élastine (MatriDerm®) et greffe de peau mince en un temps, associée à une thérapie par pression négative." Annales de Chirurgie Plastique Esthétique 56, no. 2 (2011): 163–69. http://dx.doi.org/10.1016/j.anplas.2009.11.013.

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Musiime, Moses, Joan Chang, Uwe Hansen, Karl E. Kadler, Cédric Zeltz, and Donald Gullberg. "Collagen Assembly at the Cell Surface: Dogmas Revisited." Cells 10, no. 3 (2021): 662. http://dx.doi.org/10.3390/cells10030662.

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With the increased awareness about the importance of the composition, organization, and stiffness of the extracellular matrix (ECM) for tissue homeostasis, there is a renewed need to understand the details of how cells recognize, assemble and remodel the ECM during dynamic tissue reorganization events. Fibronectin (FN) and fibrillar collagens are major proteins in the ECM of interstitial matrices. Whereas FN is abundant in cell culture studies, it is often only transiently expressed in the acute phase of wound healing and tissue regeneration, by contrast fibrillar collagens form a persistent r
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Koide, Takaki. "Designed triple-helical peptides as tools for collagen biochemistry and matrix engineering." Philosophical Transactions of the Royal Society B: Biological Sciences 362, no. 1484 (2007): 1281–91. http://dx.doi.org/10.1098/rstb.2007.2115.

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Collagens, characterized by a unique triple-helical structure, are the predominant component of extracellular matrices (ECMs) existing in all multicellular animals. Collagens not only maintain structural integrity of tissues and organs, but also regulate a number of biological events, including cell attachment, migration and differentiation, tissue regeneration and animal development. The specific functions of collagens are generally triggered by specific interactions of collagen-binding molecules (membrane receptors, soluble factors and other ECM components) with certain structures displayed
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Lee, Jung-Seok, Goran Mitulović, Layla Panahipour, and Reinhard Gruber. "Proteomic Analysis of Porcine-Derived Collagen Membrane and Matrix." Materials 13, no. 22 (2020): 5187. http://dx.doi.org/10.3390/ma13225187.

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Collagen membranes and matrices being widely used in guided bone regeneration and soft tissue augmentation have characteristic properties based on their composition. The respective proteomic signatures have not been identified. Here, we performed a high-resolution shotgun proteomic analysis on two porcine collagen-based biomaterials designed for guided bone regeneration and soft tissue augmentation. Three lots each of a porcine-derived collagen membrane and a matrix derived from peritoneum and/or skin were digested and separated by nano-reverse-phase high-performance liquid chromatography. The
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Dissertations / Theses on the topic "Matrice de collagène"

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Manuel, Rachel. "Propriétés anti-angiogéniques d'un fragment dérivé du collagène V : mécanismes moléculaires et perspectives thérapeutiques." Thesis, Lyon 1, 2013. http://www.theses.fr/2013LYO10001.

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La matrice extracellulaire joue un rôle très important dans la régulation de l’angiogenèse en procurant un support dans la formation des vaisseaux, en délivrant des facteurs endogènes pro- ou anti-angiogéniques. Nous avons montré que l’hypoxie induit une surexpression du gène COL5A1 dans les cellules endothéliales. Le laboratoire a identifié un fragment issu du collagène V, noté HEPV, qui contient un site de liaison à l’héparine, et qui montre des propriétés anti-angiogéniques remarquables. En effet, ce fragment est capable d’inhiber la prolifération et la migration des cellules endothéliales
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Cluzel-Grangeasse, Caroline. "Caractérisation et fonctions des domaines moléculaires de l'aminopropeptide d'un collagène fibrillaire d'oursin." Lyon 1, 2000. http://www.theses.fr/2000LYO1T220.

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Carisey, Alexandre. "Rôle d’une protéine de la matrice extracellulaire, la ténascine-X, sur l’étalement des cellules sur un substrat de collagène I." Lyon 1, 2008. http://www.theses.fr/2008LYO10283.

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La ténascine-X (TNX) est une glycoprotéine de la matrice extracellulaire capable d’interagir avec certains collagènes ainsi que des protéoglycanes. Elle possède la structure modulaire caractéristique des membres de la famille des ténascines avec 3 types de domaines : des motifs de type EGF, des domaines similaires au FNIII et, enfin, une extrémité globulaire similaire au fibrinogène. La déficience en TNX chez l’homme conduit à une forme récessive du syndrome d’Ehlers-Danlos caractérisée par une hypermobilité articulaire et une peau fragile très extensible. Elle est également corrélée à un phén
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Strupler, Mathias. "Imagerie du collagène par microscopie multiphotonique." Phd thesis, Ecole Polytechnique X, 2008. http://pastel.archives-ouvertes.fr/pastel-00004540.

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Le développement de nouveaux outils et de nouvelles techniques pour la biologie et la médecine a toujours été un moteur pour la recherche en microscopie. Les premiers microscopes permirent à Antoine Von Leeuwenhoek en 1677 de découvrir les bactéries, les spermatozoïdes et les globules rouges et aujourd'hui nous cherchons à visualiser les processus intracellulaires, l'interaction des protéines, l'interaction des cellules dans les tissus... Chaque année de nouvelles techniques apparaissent pour voir plus petit, plus spécifique, plus physiologique. Le laboratoire d'optique et biosciences dans lequ
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Terreau-Haftek, Zofia. "Rôle des collagènes XV et XVIII dans le développement de vertébrés : étude préliminaire chez le poisson zèbre (Danio rerio)." Lyon 1, 2004. http://www.theses.fr/2004LYO10269.

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Les collagènes sont des protéines multimodulaires dont la fonction principale est de maintenir la cohésion des tissus et des organes. Depuis les dernières années, un nombre croissant de données mettent en évidence la multifonctionnalité de ces molécules qui ont un rôle actif dans le comportement cellulaire. Les collagènes XV et XVIII possèdent des domaines respectifs restine et endostatine qui ont des propriétés anti-angiogéniques et anti-tumorales et dont la fonction reste encore inconnue. Aussi, l'objectif de cette thèse a été d'obtenir les outils et les concepts nécessaires afin de débuter
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Petit, Béatrice. "Etude de l'organisation et des fonctions des collagènes de type IX et XI dans la matrice extracellulaire du cartilage articulaire bovin fœtal." Lyon 1, 1992. http://www.theses.fr/1992LYO10010.

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L'organisation du reseau collagenique de la matrice extracellulaire du cartilage articulaire ftal bovin et des cultures de chondrocytes ftaux bovins a ete etudiee par immunomarquage en microscopie photonique et electronique. Les resultats montrent que le reseau fibreux du cartilage est compose des collagenes de type ii, ix et xi arranges de la facon suivante: le collagene de type ii forme la majorite de la fibrille alors que le collagene de type xi en forme le cur. Le collagene de type ix est situe a la surface de la fibrille avec son domaine amino-terminal no collagenique oriente vers l'exter
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Benazzoug, Yasmina. "Vieillissement et biosynthèse de la matrice extracellulaire : effet du glucose et des polysaccharides anioniques." Paris 12, 1993. http://www.theses.fr/1993PA120070.

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Lors du vieillissement, la matrice extracellulaire subit de nombreuses modifications qualitatives et quantitatives qui, s'observent egalement dans certains etats pathologiques tels le diabete et l'atherosclerose. Le diabete, facteur de risque majeur de l'atherosclerose, est assimile a un vieillissement accelere. Des travaux anterieurs realises dans notre laboratoire, sur des fibroblastes et des cellules musculaires lisses, ont montre les effets benefiques des fragments d'heparine de faible poids moleculaire sur la biosynthese des macromolecules de la matrice extracellulaire dans le diabete et
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Faye, Clément. "Le réseau d'interactions de l'endostatine, une matricryptine du collagène XVIII." Thesis, Lyon 1, 2009. http://www.theses.fr/2009LYO10176.

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L’endostatine est le fragment C-terminal du collagène XVIII libéré dans la matrice extracellulaire par clivage enzymatique. C'est un inhibiteur endogène de l’angiogenèse et de la croissance tumorale. L'endostatine inhibe la prolifération et la migration des cellules endothéliales induite par le Fibroblast Growth Factor-2 ou le Vascular Endothelial Growth Factor et elle inhibe la croissance de 65 types de cellules tumorales. L’endostatine fait actuellement l’objet d’essais cliniques pour le traitement de différents cancers son mécanisme d’action est encore mal connu. Nous avons caractérisé par
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Peres, de Sá Peixoto Júnior Paulo Eduardo. "Physico-Chimie des phases cristal-liquides du collagène I et fibrillogenèse." Paris 6, 2010. http://www.theses.fr/2010PA066663.

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L’étude des propriétés d’auto assemblage du collagène a comme objectif principal d’acquérir les connaissances nécessaires pour la production des matrices modèles, mimant les tissus du vivant. Le but de ces études est de réaliser des implants ou d’apporter des supports tridimensionnels (3D) pour les études du comportement cellulaire. Elle a également pour objectif de comprendre les mécanismes de formation de structures complexes par les macromolécules biologiques. Le collagène I est la protéine la plus répandue du règne animal. C’est la protéine majoritaire des tissus conjonctifs tels : le derm
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Gonçalves, Tristan. "Implication du collagène XXV dans la myogenèse chez la souris Collagen XXV regulates myogenic differentiation and muscle formation Non-coding RNAs in skeletal muscle regeneration." Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCB117.

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La matrice extracellulaire (MEC) est impliquée dans les mécanismes de prolifération, migration, différenciation et d’adhésion cellulaire. La membrane basale (MB), MEC entourant le muscle, sert de soutien aux fibres musculaires durant la contraction donnant ainsi une élasticité aux fibres musculaires. La MB est composée de collagènes dont majoritairement le collagène IV, de laminines, de nidogène (entactine), de perlecan (heparan sulphate proteoglycan), et de protéoglycans. Au cours de la myogenèse, la modulation de la MEC est indispensable au bon déroulement des processus de délamination, migr
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Books on the topic "Matrice de collagène"

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Gage, J. P. Collagen and dental matrices. Wright, 1989.

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Borchert, Monika. Characterization of p34, a human collagen-binding membrane protein in the annexin family. H. Gertner, 1990.

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P, Mecham Robert, ed. Regulation of matrix accumulation. Academic Press, 1986.

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(Editor), Bjorn Reino Olsen, Yoshifumi Ninomiya (Editor), and Toshiro Ooyama (Editor), eds. Extracellular Matrix-Cell Interaction: Molecules to Diseases. Japan Scientific Societies Press, 1998.

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Yoshifumi, Ninomiya, Olsen Bjørn Reino, and Ooyama Toshiro, eds. Extracellular matrix-cell interaction: Molecules to diseases. Japan Scientific Societies Press, 1998.

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Mahboubeh, Eghbali-Webb, ed. Molecular biology of collagen matrix in the heart. R.G. Landes Co., 1995.

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Hay, Elizabeth D. Cell Biology of Extracellular Matrix. Springer, 2012.

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Hay, Elizabeth D. Cell Biology of Extracellular Matrix. Springer, 2011.

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D, Hay Elizabeth, ed. Cell biology of extracellular matrix. 2nd ed. Plenum Press, 1991.

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Lennon, Rachel, and Neil Turner. The molecular basis of glomerular basement membrane disorders. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0320_update_001.

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The glomerular basement membrane (GBM) is a condensed network of extracellular matrix molecules which provides a scaffold and niche to support the function of the overlying glomerular cells. Within the glomerulus, the GBM separates the fenestrated endothelial cells, which line capillary walls from the epithelial cells or podocytes, which cover the outer aspect of the capillaries. In common with basement membranes throughout the body, the GBM contains core components including collagen IV, laminins, nidogens, and heparan sulphate proteoglycans. However, specific isoforms of these proteins are r
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Book chapters on the topic "Matrice de collagène"

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Birk, David E., and Peter Brückner. "Collagens, Suprastructures, and Collagen Fibril Assembly." In The Extracellular Matrix: an Overview. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-16555-9_3.

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Linsenmayer, T. F. "Collagen." In Cell Biology of Extracellular Matrix. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3770-0_2.

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Zimmermann, Ralf, Jens Friedrichs, Babette Lanfer, Uwe Freudenberg, and Carsten Werner. "Aligned Fibrillar Collagen Matrices." In Encyclopedia of Biocolloid and Biointerface Science 2V Set. John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119075691.ch27.

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Olsen, Bjorn Reino. "Collagen Biosynthesis." In Cell Biology of Extracellular Matrix. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3770-0_7.

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Exposito, Jean-Yves, and Claire Lethias. "Invertebrate and Vertebrate Collagens." In Evolution of Extracellular Matrix. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36002-2_3.

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McDaniel, H. E. "Tissue Engineered Collagen Nerve Guidance Channels." In Biological Matrices and Tissue Reconstruction. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-60309-9_28.

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Raspanti, Mario, Marcella Reguzzoni, Petra Rita Basso, Marina Protasoni, and Désirée Martini. "Visualizing the Supramolecular Assembly of Collagen." In The Extracellular Matrix. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9133-4_3.

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Li, Fengfu, David J. Carlsson, Chris Lohmann, Donna Bueckert, Rejean Munger, and May Griffith. "Corneal Implantation with Collagen-Copolymer Matrices." In Advanced Biomaterials VI. Trans Tech Publications Ltd., 2005. http://dx.doi.org/10.4028/0-87849-967-9.389.

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Pedchenko, Vadim, and Ambra Pozzi. "Basement Membrane Collagens and Cancer." In Cell-Extracellular Matrix Interactions in Cancer. Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0814-8_4.

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Bugge, Thomas H., and Niels Behrendt. "Cooperation Between Proteolysis and Endocytosis in Collagen Turnover." In Extracellular Matrix Degradation. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_3.

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Conference papers on the topic "Matrice de collagène"

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Lai, Victor K., Edward A. Sander, Spencer P. Lake, Robert T. Tranquillo, and Victor H. Barocas. "Collagen Network Topology is Influenced by Collagen Concentration, But Not by Co-Gelation With Fibrin." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53239.

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Extracellular matrix (ECM) proteins (e.g. collagen, elastin) play an important role in biological tissues. In addition to conferring mechanical strength to a tissue, the ECM provides a biochemical environment essential for modulation of cellular responses such as growth and migration. Collagens are the dominant protein of the ECM, with collagen type I being most abundant. Our group and others have shown that the mechanical properties of a collagen I matrix change with collagen concentration, and when formed in the presence of a secondary fibril network such as fibrin [1]. We are interested in
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Hindriks, G. A., H. C. de Boer, H. K. Nieuwenhuis, J. J. Sixma, and P. H. G. de Groot. "ADHESION OF BLOOD PLATELETS TO THE EXTRACELLULAR MATRIX OF CULTURED CELLS IN WHICH COLLAGEN SYNTHESIS IS IMPAIRED OR INDUCED." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643561.

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One of the first phenomena in the hemostatic plug formation is adhesion of platelets to the subendothelium or to the perivascular connective tissue. With a rectangular perfusion chamber (Sakariassen et al., J.Lab.Clin.Med.(1983) 102, 522-535) it is possible to study platelet adhesion in flowing blood to extracellular matrix (ECM) of cultured cells.Collegen type I and III play an important role in the adhesion of platelets. To study their role in more detail, cultured cells with changed collagen synthesis were used. For this purpose, we used fibroblasts of a patient with Osteogenesis Imperfecta
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Kraning-Rush, Casey M., Shawn P. Carey, and Cynthia A. Reinhart-King. "Molded Collagen Microchannels for the Study of Cancer Cell Invasion." In ASME 2012 10th International Conference on Nanochannels, Microchannels, and Minichannels collocated with the ASME 2012 Heat Transfer Summer Conference and the ASME 2012 Fluids Engineering Division Summer Meeting. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/icnmm2012-73093.

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Metastasis is the cause of 90% of cancer-related deaths and yet the precise mechanism of metastasis is poorly understood[1]. To metastasize, cells break free from the primary tumor, migrate through the surrounding tissue, and enter the vascular system to move to a secondary site. To migrate through the stroma, cell can both degrade the tissue and use physical force to move the tissue from its path. However, the relative roles of matrix degradation and cellular force are not well-understood. Previous work has shown that as cell move through the matrix, they create channels that other cells can
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David, Geta, and Rodica Diaconescu. "Collagen-based hybrid 3-D matrices." In 2015 E-Health and Bioengineering Conference (EHB). IEEE, 2015. http://dx.doi.org/10.1109/ehb.2015.7391595.

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Maistrenko, Lesia, Olga Iungin, Oleksii Savchuk, and Olena Okhmat. "Collagen matrices from leather industry wastes for biomedical application." In The 8th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2020. http://dx.doi.org/10.24264/icams-2020.ii.15.

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Modern biomedical science is challenged to develop new wound healing drugs. The collagen-containing wastes of leather industry could be the rich source of collagen products for further use in biomedical science. The aim of this research was to find the best source of collagen between limed pelt, delimed pelt and fleshings of cattle hides, and to prepare it for the use as a matrix for further microbiological studies. Collagen was extracted with 0.5 M acetic acid and 5 mM EDTA. The purity of the extracted collagen was checked by gel-electophoresis (SDS-PAGE). The rate of growth and crystal viole
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Lake, Spencer P., Sadie Doggett, and Victor H. Barocas. "Collagen-Agarose Co-Gels as a Model for Collagen-Matrix Interaction in Soft Tissue." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53640.

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Connective soft tissues have complex mechanical properties that are determined by their collagen fiber network and surrounding non-fibrillar material. The mechanical role of non-fibrillar material and the nature of its interaction with the collagen network remain poorly understood, in part because of the lack of a simple experimental model system to examine and quantify these properties. The development of a simple but representational experimental system will allow for greater insight into the interaction between fibers and the non-fibrillar matrix. Reconstituted Type I collagen gels are an a
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Foolen, Jasper, and Frank Baaijens. "A Novel 3D Model System to Study Deformation-Induced Cytoskeletal Remodeling." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53510.

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Native fibrous tissues contain complex anisotropic matrices. This results in essential direction-dependent mechanical properties, primarily originating from the fibrillar collagen. When engineering fibrous tissues in vitro, matrix anisotropy is crucial for in vivo functionality and durability. However, it is not fully understood how to guide, maintain and control matrix anisotropy. Cell traction and associated cell orientation may contribute significantly to collagen orientation. Therefore, the ability to manipulate cell orientation may be essential to develop a preferred matrix anisotropy for
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Baker, Brendon M., Colin K. Choi, Britta Trappmann, and Christopher S. Chen. "Engineered Fibrillar Extracellular Matrices for the Study of Directed Cell Migration." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80943.

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The biology of cell adhesion and migration has traditionally been studied on 2D glass or plastic surfaces. While such studies have shed light on the molecular mechanisms governing these processes [1], current knowledge is limited by the dissimilarity between the flat surfaces conventionally employed and the topographically complex extracellular matrix (ECM) cells routinely navigate within the body. On ECM-coated flat surfaces, cells are presented with an unlimited expanse of adhesive ligand and can spread and migrate freely. Conversely, the availability of ligand in vivo is generally restricte
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Hatami-Marbini, Hamed, and Ebitimi Etebu. "Influence of Ionic Concentration on Swelling Behavior and Shear Properties of the Bovine Cornea." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80896.

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The mechanical properties and structure of connective tissues such as the cornea and the cartilage are derived from the functions and properties of their extracellular matrix, a polyelectrolyte gel composed of collagenous fibers embedded in an aqueous matrix. The collagen fibers in the extracellular matrix of the corneal stroma are arranged in regular lattice structures, which is necessary for corneal transparency and transmitting the incident light to the back of the eye. This regular pseudo hexagonal arrangement is attributed to the interaction of collagen fibers with the proteoglycans as th
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Kishore, Vipuil, Mousa Younesi, Stefi Panit, and Ozan Akkus. "Electrochemical Compaction of the Collagen: Effects on Matrix Mechanics and MSC Response." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14361.

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The molecules of the extracellular matrix in connective tissues are densely packed. Biofabrication methods to attain such molecular packing density are limited and electrochemical processing (EP) of monomeric collagen solutions is one of few means to attain molecular packing. During EP, the pH gradient between electrodes drives the electrophoretic mobility of collagen molecules toward the isoelectric point where molecules are compacted. Our earlier work used linear electrodes to fabricate highly aligned crosslinked collagen fibers for tendon tissue engineering [1–4]. Prior work compared electr
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Reports on the topic "Matrice de collagène"

1

Trier, Steven. Investigation of Rho Signaling Pathways in 3-D Collagen Matrices with Multidimensional Microscopy and Visualization Techniques. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada493648.

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