Genomes and Genes
Affiliation: University of Trieste
- Transglutaminase-catalyzed preparation of human elastin-like polypeptide-based three-dimensional matrices for cell encapsulationAntonella Bandiera
Dipartimento di Scienze della Vita, Universita degli Studi di Trieste, Via Giorgieri, 1, 34127 Trieste, Italy
Enzyme Microb Technol 49:347-52. 2011..An advantage of the here-presented method is the use of mild conditions that preserve cell viability. This can be a powerful tool for many applications that require direct embedding of cells in the matrix...
- Assembly and optimization of expression of synthetic genes derived from the human elastin repeated motifAntonella Bandiera
Department of Life Science, Universita degli Studi di Trieste, Trieste, Italy
Prep Biochem Biotechnol 40:198-212. 2010..Electron micrographs of expressing bacteria under optimized conditions showed the accumulation of the recombinant product in the induced cells...
- Comparison of thermal behavior of two recombinantly expressed human elastin-like polypeptides for cell culture applicationsAntonella Bandiera
Department of Life Sciences, University of Trieste, Via L Giorgieri, 1, 34127 Trieste, Italy
Biomacromolecules 11:3256-65. 2010..The cells were found to retain their neural differentiation potential. The data presented in our work support the usefulness of these versatile biopolymers for a variety of applications related to biotechnology and biomedicine...
- Spontaneous patterning obtained by evaporation of Human Elastin-like Polypeptide solutionsAntonella Bandiera
Department of Life Sciences, University of Trieste, Italy
Conf Proc IEEE Eng Med Biol Soc 2010:819-22. 2010..Thus, HELPs represent a very promising class of macromolecule for future applications in surface engineering...
- Expression and characterization of human-elastin-repeat-based temperature-responsive protein polymers for biotechnological purposesAntonella Bandiera
Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Universita degli Studi di Trieste, Via Giorgieri 1, 34127 Trieste, Italy
Biotechnol Appl Biochem 42:247-56. 2005..The rapid one-step in-frame cloning of any biologically active sequence can be achieved directly in the expression vector, allowing further improvement of the potential of the resulting product...
- In-vitro dual binding activity of a evolutionarily related subgroup of hnRNP proteinsAntonella Bandiera
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, 34127 Trieste, Italy
Mol Cell Biochem 268:121-7. 2005..This binding activity appears to be related to a subgroup of the 2xRBD+Glycine rich hnRNP, suggesting functionally distinct properties of these proteins, in agreement with their evolutionary relationship...
- Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequencesAkintunde A Akindahunsi
Department of Biochemistry, Biophysics and Macromolecular Chemistry, and Centre of Excellence of Biocrystallography, University of Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy
Comput Biol Chem 29:13-23. 2005..Some clues to the evolution of introns in these genes have come from the analysis of their distribution in homologous genes of other eukaryotes, namely Ciona, Drosophila, Caenorhabditis, Saccharomyces and Arabidopsis...
- Cytosine-block telomeric type DNA-binding activity of hnRNP proteins from human cell linesAntonella Bandiera
Department of Biochemistry, Biophysics, and Macromolecular Chemistry, University of Trieste, Via L. Giorgieri 1, 34127, Trieste, Italy
Arch Biochem Biophys 409:305-14. 2003..In the light of the current knowledge about these proteins, their possible involvement in telomere functioning is discussed...
- Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptidesMaura Mattiuzzo
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
Mol Microbiol 66:151-63. 2007....