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Sökning: WFRF:(Nicolae A)

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  • Chiulan, I., et al. (författare)
  • Comprehensive characterization of silica-modified silicon rubbers
  • 2020
  • Ingår i: Journal of The Mechanical Behavior of Biomedical Materials. - : Elsevier Ltd. - 1751-6161 .- 1878-0180. ; 101
  • Tidskriftsartikel (refereegranskat)abstract
    • In this study a commercially liquid silicone rubber was filled with fumed silica particles in different concentrations and evaluated for medical applications. The thermal, morphological and mechanical properties of silicone/silica composite samples were studied before and after aging, flexural tests and immersion in saline environment. Understanding the effect of silica content, aging conditions and thickness (from 0.6 to 2 mm) of the samples on the behavior of these materials in different environments is crucial for applications as implantable devices. Before inducing any mechanical stress, tensile strength was found to increase for samples containing 3 or 5 wt% of fumed silica, depending on the thickness. A similar trend was observed after 106 flexes for tensile strength, storage modulus and hardness at room temperature, which increased with the concentration of fumed silica. Moreover, tensile strength decreased with increasing the thickness of the samples from 0.6 to 2 mm. The thermal degradation was found to start at higher temperature in the case of the composites as compared with neat silicone, however, the glass transition and melting temperatures were only slightly modified by the presence of the silica particles, regardless the mechanical aging. The MTT assay using L929 fibroblasts mouse cells showed a good short-time cytocompatibility for both silicone elastomer and the composite with 3 wt% fumed silica. Similarly, the measurement of the cytokine secretion revealed no inflammatory response.
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  • Sandholm, Niina, et al. (författare)
  • New susceptibility loci associated with kidney disease in type 1 diabetes
  • 2012
  • Ingår i: PLOS Genetics. - San Francisco, USA : Public Library of Science, PLOS. - 1553-7390 .- 1553-7404. ; 8:9, s. e1002921-
  • Tidskriftsartikel (refereegranskat)abstract
    • Diabetic kidney disease, or diabetic nephropathy (DN), is a major complication of diabetes and the leading cause of end-stage renal disease (ESRD) that requires dialysis treatment or kidney transplantation. In addition to the decrease in the quality of life, DN accounts for a large proportion of the excess mortality associated with type 1 diabetes (T1D). Whereas the degree of glycemia plays a pivotal role in DN, a subset of individuals with poorly controlled T1D do not develop DN. Furthermore, strong familial aggregation supports genetic susceptibility to DN. However, the genes and the molecular mechanisms behind the disease remain poorly understood, and current therapeutic strategies rarely result in reversal of DN. In the GEnetics of Nephropathy: an International Effort (GENIE) consortium, we have undertaken a meta-analysis of genomewide association studies (GWAS) of T1D DN comprising similar to 2.4 million single nucleotide polymorphisms (SNPs) imputed in 6,691 individuals. After additional genotyping of 41 top ranked SNPs representing 24 independent signals in 5,873 individuals, combined meta-analysis revealed association of two SNPs with ESRD: rs7583877 in the AFF3 gene (P = 1.2 x 10(-8)) and an intergenic SNP on chromosome 15q26 between the genes RGMA and MCTP2, rs12437854 (P = 2.0 x 10(-9)). Functional data suggest that AFF3 influences renal tubule fibrosis via the transforming growth factor-beta (TGF-beta 1) pathway. The strongest association with DN as a primary phenotype was seen for an intronic SNP in the ERBB4 gene (rs7588550, P = 2.1 x 10(-7)), a gene with type 2 diabetes DN differential expression and in the same intron as a variant with cis-eQTL expression of ERBB4. All these detected associations represent new signals in the pathogenesis of DN.
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9.
  • Bengtsson, T, et al. (författare)
  • Loss of alpha 10 beta 1 integrin expression leads to moderate dysfunction of growth plate chondrocytes
  • 2005
  • Ingår i: Journal of Cell Science. - : The Company of Biologists. - 0021-9533 .- 1477-9137. ; 118:5, s. 929-936
  • Tidskriftsartikel (refereegranskat)abstract
    • Integrin alpha 10 beta 1 is a collagen-binding integrin expressed on chondrocytes. In order to unravel the role of the alpha 10 integrin during development, we generated mice carrying a constitutive deletion of the alpha 10 integrin gene. The mutant mice had a normal lifespan and were fertile but developed a growth retardation of the long bones. Analysis of the skeleton revealed defects in the growth plate after birth characterized by a disturbed columnar arrangement of chondrocytes, abnormal chondrocyte shape and reduced chondrocyte proliferation. Electron microscopy of growth plates from newborn mice revealed an increased number of apoptotic chondrocytes and reduced density of the collagen fibrillar network compared to these structures in control mice. These results demonstrate that integrin alpha 10 beta 1 plays a specific role in growth plate morphogenesis and function.
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  • Cournia, Zoe, et al. (författare)
  • Membrane Protein Structure, Function, and Dynamics : a Perspective from Experiments and Theory
  • 2015
  • Ingår i: Journal of Membrane Biology. - : Springer. - 0022-2631 .- 1432-1424. ; 248:4, s. 611-640
  • Tidskriftsartikel (refereegranskat)abstract
    • Membrane proteins mediate processes that are fundamental for the flourishing of biological cells. Membrane-embedded transporters move ions and larger solutes across membranes; receptors mediate communication between the cell and its environment and membrane-embedded enzymes catalyze chemical reactions. Understanding these mechanisms of action requires knowledge of how the proteins couple to their fluid, hydrated lipid membrane environment. We present here current studies in computational and experimental membrane protein biophysics, and show how they address outstanding challenges in understanding the complex environmental effects on the structure, function, and dynamics of membrane proteins.
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