http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51593
Mapping phosphoproteins in Neisseria meningitidis serogroup A. (Articolo in rivista)
- Type
- Label
- Mapping phosphoproteins in Neisseria meningitidis serogroup A. (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/pmic.201000406 (literal)
- Alternative label
Bernardini G, Laschi M, Serchi T, Arena S, D'Ambrosio C, Braconi D, Scaloni A, Santucci A. (2011)
Mapping phosphoproteins in Neisseria meningitidis serogroup A.
in Proteomics (Weinh., Print); Wiley-VCH Verlag Gmbh, Weinheim (Germania)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Bernardini G, Laschi M, Serchi T, Arena S, D'Ambrosio C, Braconi D, Scaloni A, Santucci A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://onlinelibrary.wiley.com/doi/10.1002/pmic.201000406/abstract (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
- Proteomics. 2011 Feb 2. doi: 10.1002/pmic.201000406. [Epub ahead of print]
Proteomics. 2011 Apr;11(7):1351-8. doi: 10.1002/pmic.201000406. Epub 2011 Feb 17. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
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- Dipartimento di Biologia Molecolare, Universita`degli Studi di Siena, via Fiorentina, Siena, Italy
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, via Argine, Naples, Italy (literal)
- Titolo
- Mapping phosphoproteins in Neisseria meningitidis serogroup A. (literal)
- Abstract
- To investigate the phosphorylation capability of serogroup A Neisseria meningitidis (MenA) and to implement our knowledge in meningococcal biology and in bacterial post-translational modifications, cell extracts were separated by 2-DE and 51 novel phosphoproteins were revealed by the use of the highly specific Ser/Thr/Tyr-phosphorylated proteins staining by Pro-Q Diamond and identified by MALDI-ToF/MS. Our results indicate that phosphorylation in MenA is comparable to that of other bacterial species. A first functional characterization of the identified modified proteins was also given, in order to understand their role in meningococcal physiopathology. (literal)
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