Добірка наукової літератури з теми "Collagen mutants"
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Статті в журналах з теми "Collagen mutants"
McKinnon, Thomas A. J., Agata Anna Nowak, Alina Hua, Carolyn Millar, and Michael Laffan. "Flow Analysis of Von Willebrand Factor Collagen Binding Mutants." Blood 118, no. 21 (November 18, 2011): 2213. http://dx.doi.org/10.1182/blood.v118.21.2213.2213.
Повний текст джерелаShida, Yasuaki, Christine Brown, Jeff Mewburn, Kate Sponagle, Ozge Danisment, Barbara Vidal, Carol A. Heagadorn, and David Lillicrap. "Comprehensive In Vitro and In Vivo Characterization of Loss and Gain-of-Function Von Willebrand Factor Collagen Binding Variants Using a Mouse Model System,." Blood 118, no. 21 (November 18, 2011): 3266. http://dx.doi.org/10.1182/blood.v118.21.3266.3266.
Повний текст джерелаShitomi, Yasuyuki, Ida B. Thøgersen, Noriko Ito, Birgit Leitinger, Jan J. Enghild, and Yoshifumi Itoh. "ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)." Molecular Biology of the Cell 26, no. 4 (February 15, 2015): 659–73. http://dx.doi.org/10.1091/mbc.e14-10-1463.
Повний текст джерелаPetersen, F. C., S. Assev, H. C. van der Mei, H. J. Busscher, and A. A. Scheie. "Functional Variation of the Antigen I/II Surface Protein in Streptococcus mutans and Streptococcus intermedius." Infection and Immunity 70, no. 1 (January 2002): 249–56. http://dx.doi.org/10.1128/iai.70.1.249-256.2002.
Повний текст джерелаGuimarães-Souza, Nadia Karina, Liliya Marsovna Yamaleyeva, Baisong Lu, Ana Claudia Mallet de Souza Ramos, Colin Edward Bishop, and Karl Erik Andersson. "Superoxide overproduction and kidney fibrosis: a new animal model." Einstein (São Paulo) 13, no. 1 (March 2015): 79–88. http://dx.doi.org/10.1590/s1679-45082015ao3179.
Повний текст джерелаvan der Plas, R., Lucio Gomes, J. Marquart, Tom Vink, Joost C. Meijers, Philip de Groot, Jan Sixma, and Eric Huizinga. "Binding of von Willebrand Factor to Collagen Type III: Role of Specific Amino Acids in the Collagen Binding Domain of vWF and Effects of Neighboring Domains." Thrombosis and Haemostasis 84, no. 12 (2000): 1005–11. http://dx.doi.org/10.1055/s-0037-1614163.
Повний текст джерелаMarx, Isabelle, Olivier D. Christophe, Peter J. Lenting, Alain Rupin, Marie-Odile Vallez, Tony J. Verbeuren, and Cécile V. Denis. "Altered thrombus formation in von Willebrand factor–deficient mice expressing von Willebrand factor variants with defective binding to collagen or GPIIbIIIa." Blood 112, no. 3 (August 1, 2008): 603–9. http://dx.doi.org/10.1182/blood-2008-02-142943.
Повний текст джерелаCruz, Miguel A., and Liza D. Morales. "Mutations in the von Willebrand Factor A1 Domain That Increase the Affinity for Collagen Have Different Effects on the Binding to Glycoprotein Ib." Blood 104, no. 11 (November 16, 2004): 3661. http://dx.doi.org/10.1182/blood.v104.11.3661.3661.
Повний текст джерелаMintz, Keith P. "Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen." Microbiology 150, no. 8 (August 1, 2004): 2677–88. http://dx.doi.org/10.1099/mic.0.27110-0.
Повний текст джерелаLankhof, Hanneke, Conchi Damas, Marion Schiphorst, Martin IJsseldijk, Madelon Bracke, Miha Furlan, Philip de Groot, Tom Vink, and Jan Sixma. "Recombinant vWF Type 2A Mutants R834Q and R834W Show a Defect in Mediating Platelet Adhesion to Collagen, Independent of Enhanced Sensitivity to a Plasma Protease." Thrombosis and Haemostasis 81, no. 06 (1999): 976–83. http://dx.doi.org/10.1055/s-0037-1614609.
Повний текст джерелаДисертації з теми "Collagen mutants"
陳卓榮 and Cheuk-wing Wilson Chan. "Molecular basis for increased bone formation in a mouse expressing mutant collagen X." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2003. http://hub.hku.hk/bib/B31227132.
Повний текст джерелаPfeiffer, Brent J. "Role of Proa(2)I collagen chains and collagen crosslinking in thoracic aortic biochemical integrity during aging using the OIM mouse model." Diss., Columbia, Mo. : University of Missouri-Columbia, 2006. http://hdl.handle.net/10355/4397.
Повний текст джерелаTitle from title screen of research.pdf file (viewed on December 22, 2006). The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Vita. "May 2006" Includes bibliographical references.
Brodeur, Amanda C. "Glomerular deposition of homotrimeric type I collagen in the COL1A2 deficient mouse." Diss., Columbia, Mo. : University of Missouri-Columbia, 2006. http://hdl.handle.net/10355/4479.
Повний текст джерелаTitle from title screen of research.pdf file (viewed on December 22, 2006). The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. "May 2006" Vita. Includes bibliographical references.
Ioannides, Marios. "Detection, Cloning, and Analysis of a U32 Collagenase in Streptococcus mutans GS-5." [Tampa, Fla.] : University of South Florida, 2004. http://purl.fcla.edu/fcla/etd/SFE0000612.
Повний текст джерелаAndrade, Caroline Gomes de. "Avaliação do potencial cariogênico de biofilmes contendo Candida albicans em relação à dentina radicular : estudo in vitro." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2017. http://hdl.handle.net/10183/179883.
Повний текст джерелаAfter root exposure on the oral cavity, caused by gingival recession, a shift in the site microflora occurs. Deposits of microorganisms turn in to a biofilm in the root surface, which if exposed frequently to fermentable carbohydrates may lead to a pH drop on the biofilm matrix, selecting acid tolerant microorganisms causing solubilization of the mineralized tissues and the activation of dentin organic matrix degrading system. Candida albicans presence in root caries has been debated on the literature, some studies suggest that the cariogenicity of the biofilm increases on the fungus presence, although some others have said that the fungus would lead to a biofilm pH neutralization by releasing some metabolites and lactic acid consumption, the acid released on the biofilm matrix as a product of the carbohydrates metabolization. Therefore, the aim of this present study was to evaluate the cariogenic potential of biofilms containing C. albicans in relation to root dentin. Dentin root slabs were obtained from root of bovine teeth and its surface microhardness was accessed. An in vitro trial was performed, by randomizing the slabs in 3 groups: Group 1 – mono-species S. mutans biofilm (SM), Group 2 – monospecies C. albicans biofilm (CA) and Group 3 - dual-species S. mutans and C. albicans biofilm (MIX). The biofilms were grown at the dentin slab surface in 24, 48 and 72. The pH of the culture medium was checked every 24 hours. Biofilms were collected from the surface of six dentin slabs after each time as described above and the CFU/mL counts were determined. Additionally, after each time of biofilm growth, the surface microhardness of the samples was measured again to calculate the surface hardness loss percentage (%SHL) and, also, two samples of each group/time were sent to histological stain by PicroSirius Red to determine the percentage of structured collagen on the organic demineralized dentin. Each trial was performed three times and the data was analysed by Two-Way ANOVA, followed by Bonferroni test, with a significance level of 5%. As related to the results, irrespective from the microbial composition of the biofilm, a higher %SHL was observed in biofilms growth in 48 and 72 hours when compared to the biofilms growth in 24 hours. Regarding the microbial composition of the biofilm, it was observed that the %SHL at the SM biofilm was statistically higher than in the presence of the MIX biofilm, which was also higher than the one found at the CA biofilm. The results also show that the pH values of the culture medium in MIX biofilms were statistically higher than those found in the presence of SM biofilms at 48 and 72 hours (p<0,05). Related to the organic analysis of the dentin, the results suggest that there is a higher tendency to structured collagen maintenance in CA biofilms when compared to the SM and MIX biofilms. Our results suggest that, although C. albicans has a cariogenic potential related to root dentin, the biofilm containing C.albicans associated to S. mutans seems to present a lower cariogenic potential when compared to biofilms growth without this fungus.
Siriani, Luciana Kfouri. "Influência do gene cnm de Streptococcus mutans na formação de biofilme e na interação do microrganismo às células endoteliais." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/42/42132/tde-19042013-110450/.
Повний текст джерелаStreptococcus mutans is considered a primary etiological agent of dental caries and an important etiological agent of infectious endocarditis. It can be classified into four serotypes (c, e, f and k), which serotype c is the most commonly prevalent in the population. The recent breakthrough that the cnm gene, which encodes a collagen binding protein found in some S. mutans strains, has set off new studies on this species, such as biofilm formation and bacteria-cell interactions. Aims: (1) biofilm formation on collagen-treated surfaces and the expression of biofilm formation key genes spaP and brpA; (2) adhesion (30 min and 2h), invasion (5h) and persistence (24h) in endothelial cells and (3) dentin demineralization. Experiments on collagen-dependent biofilm formation, and adhesion, invasion and persistence in HCAEC cells (primary Human Coronary Artery Endothelial Cells) were performed using S. mutans strains UA159 (serotype c), B14 (serotype e), OM50E (serotype e), LM7 (serotype e), OMZ175 (serotype f), NCTC 11060 (serotype f) and the clinical isolates of this study 7.1 (serotype c), C2A4 (serotype e) and 61 (serotype k). Mutants cnm were constructed in all strains presenting the gene, except for C2A4. Strains OMZ175 and 61 and their respective mutants were also employed to evaluate both the expression of spaP and brpA genes by PCR Real Time and the dentin demineralization through Optical Coherence Tomography (OCT). One hundred forty four clinical isolates of S. mutans were collected from 47 patients. Our data have shown that the cnm gene is significant for both biofilm formation on collagen-treated surfaces and invasion of endothelial cells, but it has no influence in cell adhesion. In addition, most of the cnm positive strains were able to persist up to 24h intracellularly. Likewise, the model of experimental caries was not able to demonstrate the importance of cnm in dentin demineralization. Thus, gene cnm is required for S. mutans on collagen-dependent biofilm formation and invasion of endothelial cells, but it was not required for adhesion to HCAEC.
Carson, Valerie. "Cloning and analysis of putative collegenases of the U32 family in Stretococcus mutans and Stretococcus agalactiae (Group B Stretococcus)." [Tampa, Fla] : University of South Florida, 2006. http://purl.fcla.edu/usf/dc/et/SFE0001721.
Повний текст джерелаSandhu, Anjali. "Deciphering the genetic regulators of cuticle barrier function and longevity in Caenorhabditis elegans." Thesis, 2020. https://etd.iisc.ac.in/handle/2005/4807.
Повний текст джерелаIISc and Welcome DBT
Harrington, Dean J., and R. R. B. Russell. "Identification and characterisation of two extracellular proteases of Streptococcus mutans." 1994. http://hdl.handle.net/10454/11595.
Повний текст джерелаStreptococcus mutans was shown to produce two extracellular proteases capable of degrading both gelatin and collagen-like substrates. These enzymes have molecular masses of 52 and 50 kDa when analysed by SDS-PAGE. Both enzymes were inhibited by EDTA, but not by a range of other inhibitors with different specificities, indicating that they are metalloproteases. The activity of EDTA-inactivated enzymes could be restored by the addition of manganese and zinc. The identical inhibition and restoration profiles of the two enzymes suggest that one of the proteases may be a degradation product of the other.
Rebella, Gregory S. "Skeletal muscle collagen alterations induced by recombinant human growth hormone (rhGH) in the mutant dwarf rat." 1996. http://catalog.hathitrust.org/api/volumes/oclc/36400373.html.
Повний текст джерелаTypescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 56-61).
Частини книг з теми "Collagen mutants"
Abe, Yasuhiro, Tetsuya Nomura, Yasuo Yoshioka, Haruhiko Kamada, Shin-ichi Tsunoda, and Yasuo Tsutsumi. "Anti-inflammatory Effects of a Novel TNFR1-Selective Antagonistic TNF Mutant on Established Murine Collagen-Induced Arthritis." In Advances in Experimental Medicine and Biology, 493–500. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6612-4_51.
Повний текст джерелаТези доповідей конференцій з теми "Collagen mutants"
Webb, Watt W. "Multiphoton Microscopy MPM: Imaging Spectra and Dynamics of Molecular Function Deep in Living Tissues." In In Vivo optical Imaging at the NIH. Washington, D.C.: Optica Publishing Group, 1999. http://dx.doi.org/10.1364/ivoi.1999.msi3.
Повний текст джерелаDelgado-Goni, Teresa, Slawomir Wantuch, Teresa Casals-Galobart, Udai Banerji, Nina Tunariu, Simon P. Robinson, Martin O. Leach, and Mounia Beloueche-Babari. "Abstract 4108: Longitudinal diffusion-weighted MRI assessment of NRAS mutant melanoma response to dual RAF-MEK inhibition reveals differences associated with collagen deposition." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4108.
Повний текст джерелаЗвіти організацій з теми "Collagen mutants"
Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7697123.bard.
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