Please use this identifier to cite or link to this item:
http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/14991
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chandrasekar, Balakumaran | |
dc.date.accessioned | 2024-07-29T09:08:14Z | |
dc.date.available | 2024-07-29T09:08:14Z | |
dc.date.issued | 2019-04 | |
dc.identifier.uri | https://www.science.org/doi/full/10.1126/science.aav0748 | |
dc.identifier.uri | http://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/14991 | |
dc.description.abstract | Plants produce receptors that recognize fragments of microbial flagellin, thus monitoring for infection by bacteria. Buscaill et al. studied how a flagellin fragment is made accessible for recognition by host glycosidases, which degrade the glycosylations shielding the peptide that triggers the immune response. The pathogen, in turn, evades detection by altering flagellin glycosylation and inhibiting the host glycosidase. This aspect of plant defense against infection plays out in the apoplast, the extracellular space within plant tissues. | en_US |
dc.language.iso | en | en_US |
dc.publisher | AAAS | en_US |
dc.subject | Biology | en_US |
dc.subject | Glycosidase | en_US |
dc.subject | Glycan Polymorphism | en_US |
dc.subject | Peptides and proteins | en_US |
dc.title | Glycosidase and glycan polymorphism control hydrolytic release of immunogenic flagellin peptides | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Biological Sciences |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.