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Plant defence peptides
Citation
García Olmedo, Francisco and Molina Fernández, Antonio and Alamillo, Josefa M. and Rodriguez Palenzuela, Pablo (1998). Plant defence peptides. "Peptide Science", v. 47 (n. 6); pp. 479-491. ISSN 1097-0282. https://doi.org/10.1002/(SICI)1097-0282(1998)47:6<479::AID-BIP6>3.0.CO;2-K.
Description
| Title: | Plant defence peptides |
|---|---|
| Author/s: |
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| Item Type: | Article |
| Título de Revista/Publicación: | Peptide Science |
| Date: | May 1998 |
| ISSN: | 1097-0282 |
| Volume: | 47 |
| Subjects: | |
| Freetext Keywords: | antimicrobial peptides; plant defense peptides; thionin; defensin; lipid transfer protein; hevein- and knottin-like peptides; MBPI; IbAMP; snakin; disulfide bridge; pathogen |
| Faculty: | E.T.S.I. Agrónomos (UPM) [antigua denominación] |
| Department: | Biotecnologia [hasta 2014] |
| Creative Commons Licenses: | Recognition - No derivative works - Non commercial |
Abstract
Eight families of antimicrobial peptides, ranging in size from 2 to 9 kD, have been identified in plants. These are thionins, defcnsins, so-called lipid iransfer proteins, hevein- and knottin-Iike peptides, MBPJ, lb AMP, and the recently reported snakins. All of them have compact structures that are stabilized by 2-6 disulfide bridges. They are part of both permanent and inducible defense barriers. Transgenic overe.xpression of the corresponding genes leads to enhanced tolerance to pathogens, and peptide-sensitive pathogen mutants have reduced virulence.
More information
| Item ID: | 6015 |
|---|---|
| DC Identifier: | https://oa.upm.es/6015/ |
| OAI Identifier: | oai:oa.upm.es:6015 |
| DOI: | 10.1002/(SICI)1097-0282(1998)47:6<479::AID-BIP6>3.0.CO;2-K |
| Official URL: | http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0282(1998)47:6%3C479::AID-BIP6%3E3.0.CO;2-K/abstract;jsessionid=B7AE8505748D09B51B8DF0951BB1FECA.d02t04 |
| Deposited by: | Memoria Investigacion |
| Deposited on: | 15 Feb 2011 12:33 |
| Last Modified: | 20 Apr 2016 14:40 |
