top

  Info

  • Utilizzare la checkbox di selezione a fianco di ciascun documento per attivare le funzionalità di stampa, invio email, download nei formati disponibili del (i) record.

  Info

  • Utilizzare questo link per rimuovere la selezione effettuata.
Science and technology against microbial pathogens [[electronic resource] ] : research, development and evaluation : proceedings of the International Conference on Antimicrobial Research (ICAR2010), Valladolid, Spain, 3-5 November 2010 / / editor, A. Mendez-Vilas
Science and technology against microbial pathogens [[electronic resource] ] : research, development and evaluation : proceedings of the International Conference on Antimicrobial Research (ICAR2010), Valladolid, Spain, 3-5 November 2010 / / editor, A. Mendez-Vilas
Pubbl/distr/stampa Singapore, : World Scientific, c2011
Descrizione fisica 1 online resource (447 p.)
Disciplina 579.3165
616.9/041
Altri autori (Persone) Méndez-VilasA
Soggetto topico Drug resistance in microorganisms
Pathogenic bacteria
Soggetto genere / forma Electronic books.
ISBN 1-283-43385-0
9786613433855
981-4354-86-4
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Introduction; Contents; Antimicrobial Peptides; A new class of Scots pine antimicrobial proteins, which act by binding b-glucan Sanjeewani Sooriyaarachchi, Adrian Suárez Covarrubias, Wimal Ubhayasekera, Frederick O. Asiegbu and Sherry L. Mowbray; 1. Introduction; 2. Material and methods; 2.1 Cloning, expression and purification of Sp-AMP3; 2.2 Binding studies; 2.3 Antifungal activity; 2.4 Scanning electron microscopic studies; 2.5 Homology modeling; 3. Results and discussion; 4. Conclusions; References
Antimicrobial aza- -peptides: Structure-activity relationship? B. Legrand, M. Laurencin, C. Zatylny-Gaudin, J. Henry, A. Bondon and M. Baudy Floc'h1. Introduction; 2. Results and Discussion; 3. Conclusion; References; Differential antimicrobial activities of Human Beta-Defensins against Methicillin Resistant (MRSA) and Methicillin sensitive (MSSA) Staphylococcus aureus N. D. S. Herathge, J. T. George and D. A. Rowley; Introduction; Materials and Methods; Results; Discussion; References
Isolation of antimicrobial peptides from New Zealand spinach Tetragonia tetragonioides T. Neubauerová, M. Macková, T. Macek, M. Šanda, M. Králová, I. Doležílková and P. N. Holmsgaard1. General remarks; 2. Materials and methods; 2.1 Extraction of peptides and proteins from spinach leaves; 2.2 Purification of crude extract; 2.3 Reverse-phase chromatography purification (RP-HPLC); 2.4 Microorganisms and antimicrobial assay; 2.5 Antimicrobial activity; 3. Results; 3.1 Isolation of antimicrobial peptides from spinach; 3.2 Antimicrobial assay; 3.3 Characterization by MS; 4. Discussion; References
Lysostaphin: molecular changes that preserve staphylolytic activity S. Becker, J. Foster-Frey, A. Powell, H. Mohammadi, D. E. Kerr and D. M. Donovan1. Introduction; 2. Results and Discussion; 2.1 Effect of N- vs. C-terminal 6 x His tag on mLyso lytic activity; 2.2 Activity changes resulting from N125Q and N232Q mLyso mutations; 2.3 N-terminal deletions of mLyso between residue 1 and 31; Conclusions; References; Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph T. Neubauerová, M. Macková, T. Macek, M. Šanda and Z. Voburka; 1. General remarks
2. Materials and methods2.1 Isolation of larval haemolymph; 2.2 Purification of antimicrobial peptides; 2.3 Ion-exchange and reversed-phase liquid chromatography (Ionex-FPLC, RP-HPLC); 2.4 Microorganisms and antimicrobial assay; 2.5 Tricine gel electrophoresis and electroblotting; 2.6 Mass spectrometry analysis; 3. Results and discussion; References; Structural and functional diversity of natural antimicrobial oligopeptides Aexander A. Zamyatnin; 1. Introduction; 2. Structure; 3. Functions; 4. Potential applications; References
The role of Gram-negative envelope LPS on the bactericidal properties of proteins and peptides: the case of eosinophil cationic protein D. Pulido, M. Torrent, M. V. Nogués and E. Boix
Record Nr. UNINA-9910457789803321
Singapore, : World Scientific, c2011
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Science and technology against microbial pathogens [[electronic resource] ] : research, development and evaluation : proceedings of the International Conference on Antimicrobial Research (ICAR2010), Valladolid, Spain, 3-5 November 2010 / / editor, A. Mendez-Vilas
Science and technology against microbial pathogens [[electronic resource] ] : research, development and evaluation : proceedings of the International Conference on Antimicrobial Research (ICAR2010), Valladolid, Spain, 3-5 November 2010 / / editor, A. Mendez-Vilas
Pubbl/distr/stampa Singapore, : World Scientific, c2011
Descrizione fisica 1 online resource (447 p.)
Disciplina 579.3165
616.9/041
Altri autori (Persone) Méndez-VilasA
Soggetto topico Drug resistance in microorganisms
Pathogenic bacteria
ISBN 1-283-43385-0
9786613433855
981-4354-86-4
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Introduction; Contents; Antimicrobial Peptides; A new class of Scots pine antimicrobial proteins, which act by binding b-glucan Sanjeewani Sooriyaarachchi, Adrian Suárez Covarrubias, Wimal Ubhayasekera, Frederick O. Asiegbu and Sherry L. Mowbray; 1. Introduction; 2. Material and methods; 2.1 Cloning, expression and purification of Sp-AMP3; 2.2 Binding studies; 2.3 Antifungal activity; 2.4 Scanning electron microscopic studies; 2.5 Homology modeling; 3. Results and discussion; 4. Conclusions; References
Antimicrobial aza- -peptides: Structure-activity relationship? B. Legrand, M. Laurencin, C. Zatylny-Gaudin, J. Henry, A. Bondon and M. Baudy Floc'h1. Introduction; 2. Results and Discussion; 3. Conclusion; References; Differential antimicrobial activities of Human Beta-Defensins against Methicillin Resistant (MRSA) and Methicillin sensitive (MSSA) Staphylococcus aureus N. D. S. Herathge, J. T. George and D. A. Rowley; Introduction; Materials and Methods; Results; Discussion; References
Isolation of antimicrobial peptides from New Zealand spinach Tetragonia tetragonioides T. Neubauerová, M. Macková, T. Macek, M. Šanda, M. Králová, I. Doležílková and P. N. Holmsgaard1. General remarks; 2. Materials and methods; 2.1 Extraction of peptides and proteins from spinach leaves; 2.2 Purification of crude extract; 2.3 Reverse-phase chromatography purification (RP-HPLC); 2.4 Microorganisms and antimicrobial assay; 2.5 Antimicrobial activity; 3. Results; 3.1 Isolation of antimicrobial peptides from spinach; 3.2 Antimicrobial assay; 3.3 Characterization by MS; 4. Discussion; References
Lysostaphin: molecular changes that preserve staphylolytic activity S. Becker, J. Foster-Frey, A. Powell, H. Mohammadi, D. E. Kerr and D. M. Donovan1. Introduction; 2. Results and Discussion; 2.1 Effect of N- vs. C-terminal 6 x His tag on mLyso lytic activity; 2.2 Activity changes resulting from N125Q and N232Q mLyso mutations; 2.3 N-terminal deletions of mLyso between residue 1 and 31; Conclusions; References; Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph T. Neubauerová, M. Macková, T. Macek, M. Šanda and Z. Voburka; 1. General remarks
2. Materials and methods2.1 Isolation of larval haemolymph; 2.2 Purification of antimicrobial peptides; 2.3 Ion-exchange and reversed-phase liquid chromatography (Ionex-FPLC, RP-HPLC); 2.4 Microorganisms and antimicrobial assay; 2.5 Tricine gel electrophoresis and electroblotting; 2.6 Mass spectrometry analysis; 3. Results and discussion; References; Structural and functional diversity of natural antimicrobial oligopeptides Aexander A. Zamyatnin; 1. Introduction; 2. Structure; 3. Functions; 4. Potential applications; References
The role of Gram-negative envelope LPS on the bactericidal properties of proteins and peptides: the case of eosinophil cationic protein D. Pulido, M. Torrent, M. V. Nogués and E. Boix
Record Nr. UNINA-9910778959603321
Singapore, : World Scientific, c2011
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui