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Akademický článek

Pretreatment of Endothelial Progenitor Cells with Osteopontin Enhances Cell Therapy for Peripheral Vascular Disease

Autor: E. E. Vaughan, A. Liew, K. Mashayekhi, P. Dockery, J. McDermott, B. Kealy, A. Flynn, A. Duffy, C. Coleman, A. O'regan, F. P. Barry, T. O'brien

Publikováno v: Cell Transplantation, Vol 21 (2012)

Tissue necrosis resulting from critical limb ischemia (CLI) leads to amputation in a significant number of patients. Autologous cell therapy using angiogenic cells such as endothelial progenitor cells (EPCs) holds promise as a treatment for CLI but a

Externí odkaz: https://doaj.org/article/912e7b3019a64146a28fa3367bddc34e

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Gelatin-based resorbable sponge as a carrier matrix for human mesenchymal stem cells in cartilage regeneration therapy

Autor: M S, Ponticiello, R M, Schinagl, S, Kadiyala, F P, Barry

Publikováno v: Journal of biomedical materials research. 52(2)

Adult mesenchymal stem cells (MSCs), found in the bone marrow, have the potential to differentiate into multiple connective tissue types, including cartilage. In this study, we examined the potential of a porous gelatin sponge, Gelfoam, for use as a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1514b8b4f7f543f0666f9ad461dae6fe
https://pubmed.ncbi.nlm.nih.gov/10951362

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Post-translational modifications in cartilage oligomeric matrix protein. Characterization of the N-linked oligosaccharides by matrix-assisted laser desorption ionization time-of-flight mass spectrometry

Autor: J, Zaia, R E, Boynton, A, McIntosh, D R, Marshak, H, Olsson, D, Heinegârd, F P, Barry

Publikováno v: The Journal of biological chemistry. 272(22)

Analysis of the carboxymethylated subunit of human cartilage oligomeric matrix protein (COMP) by matrix-assisted laser desorption time-of-flight mass spectrometry indicated a protonated molecular mass of 86949 +/- 149 Da, compared with 83547.0 Da cal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::378c8a91faa0da15a7c1d8fff218e6c3
https://pubmed.ncbi.nlm.nih.gov/9162039

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Cleavage by trypsin and by the proteinase from Armillaria mellea at ɛ-N-formyl-lysine residues

Autor: Shawn Doonan, C A Ross, F P Barry

Publikováno v: Biochemical Journal. 193:737-742

Kinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for tryp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f933d9a02e74d6400911444b5ec1ccf
https://doi.org/10.1042/bj1930737

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