ISIS: interaction sites identified from sequence | Zendy

Yanay Ofran | Zendy; Burkhard Rost | Zendy

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ISIS: interaction sites identified from sequence

Author(s) -

Yanay Ofran,

Burkhard Rost

Publication year - 2007

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btl303

Subject(s) - sequence (biology) , computer science , interface (matter) , computational biology , identification (biology) , protein structure , protein–protein interaction , protein sequencing , sequence alignment , artificial intelligence , data mining , peptide sequence , biology , genetics , biochemistry , botany , bubble , maximum bubble pressure method , parallel computing , gene

Large-scale experiments reveal pairs of interacting proteins but leave the residues involved in the interactions unknown. These interface residues are essential for understanding the mechanism of interaction and are often desired drug targets. Reliable identification of residues that reside in protein-protein interface typically requires analysis of protein structure. Therefore, for the vast majority of proteins, for which there is no high-resolution structure, there is no effective way of identifying interface residues.

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