2010
DOI: 10.1016/j.fgb.2010.06.014
|View full text |Cite
|
Sign up to set email alerts
|

Development of resistance against blackleg disease in Brassica oleracea var. botrytis through in silico methods

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
5
0

Year Published

2011
2011
2021
2021

Publication Types

Select...
5
3

Relationship

2
6

Authors

Journals

citations
Cited by 10 publications
(5 citation statements)
references
References 54 publications
(43 reference statements)
0
5
0
Order By: Relevance
“…Simulations involving the search for conformations with the substrates on the surface of Pb ICL were limited to only a region surrounding the binding pocket of the protein, which was defined as involving the same residues of the template provided by [49] . Amino acids within the Pb ICL binding site (ASP24-GLN55 and ILE227-THR236) were 100% identical to the template An ICL.…”
Section: Resultsmentioning
confidence: 99%
“…Simulations involving the search for conformations with the substrates on the surface of Pb ICL were limited to only a region surrounding the binding pocket of the protein, which was defined as involving the same residues of the template provided by [49] . Amino acids within the Pb ICL binding site (ASP24-GLN55 and ILE227-THR236) were 100% identical to the template An ICL.…”
Section: Resultsmentioning
confidence: 99%
“…In Arabidopsis , approximately 10,000 orthologs have been detected in at least one reference species (i.e., in yeast, Drosophila , or humans) (Morsy et al 2008 ). Structure modeling and docking approaches have also been used to develop a peptide which can competitively inhibit the crucial glyoxylate pathway in fungi (Srivastava et al 2010 ).…”
Section: Different Plant-fungus Studiesmentioning
confidence: 99%
“…Protein-protein superposition, brings ligand into the target active site with an orientation similar to the one found in the original ligand-receptor crystal structure [39]. The adenine binding site of curcin was predicted by superposition of curcin with the ricin-adenine complex (PDB id: 2P8N).…”
Section: Active Site Predictionmentioning
confidence: 99%