http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17407
Immunodetection of partially glycosylated isoforms of alpha-dystroglycan by a new monoclonal antibody against its beta-dystroglycan-binding epitope (Articolo in rivista)
- Type
- Label
- Immunodetection of partially glycosylated isoforms of alpha-dystroglycan by a new monoclonal antibody against its beta-dystroglycan-binding epitope (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Alternative label
Pavoni E., Sciandra F., Barca S., Giardina B., Petrucci T.C., Brancaccio A. (2005)
Immunodetection of partially glycosylated isoforms of alpha-dystroglycan by a new monoclonal antibody against its beta-dystroglycan-binding epitope
in FEBS letters (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Pavoni E., Sciandra F., Barca S., Giardina B., Petrucci T.C., Brancaccio A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- PubMe (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Pavoni E.: Istituto di Biochimica UCSC
Barca S.; Petrucci, T.C.: ISS
Sciandra, F., Giardina, B., Brancaccio, A.: ICRM, CNR (literal)
- Titolo
- Immunodetection of partially glycosylated isoforms of alpha-dystroglycan by a new monoclonal antibody against its beta-dystroglycan-binding epitope (literal)
- Abstract
- The alpha/beta dystroglycan (DG) complex links the extracellular matrix to the actin cytoskeleton. The extensive glycosylation of alpha-DG is believed to be crucial for the interaction with its extracellular matrix-binding partners. We characterized a monoclonal antibody, directed against the beta-DG-binding epitope (approximate to positions 550-565), which recognizes preferentially hypoglycosylated alpha-DG. In Western blot, the antibody was able to detect a number of partially glycosylated alpha-DG isoforms from rat brain and chicken skeletal muscle tissue samples. In addition, we demonstrated its inhibitory effect on the interaction between alpha- and beta-DG in vitro and preliminary immunostaining experiments suggest that such hypoglycosylated alpha-DG isoforms could play a role within cells. (literal)
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- Autore CNR
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