The diversity of H3 loops determines the antigen-binding tendencies of antibody CDR loops

Prediction of site-specific interactions in antibody-antigen complexes: the proABC method and server

(2013) Pier Paolo Olimpieri et al.   BIOINFORMATICS

SAbDab: the structural antibody database

(2013) James Dunbar et al.   NUCLEIC ACIDS RESEARCH

The indistinguishability of epitopes from protein surface is explained by the distinct binding preferences of each of the six antigen-binding loops

(2013) Vered Kunik et al.   PROTEIN ENGINEERING DESIGN & SELECTION

A Systematic Comparison of Free and Bound Antibodies Reveals Binding-Related Conformational Changes

(2012) I. Sela-Culang et al.   JOURNAL OF IMMUNOLOGY

Paratome: an online tool for systematic identification of antigen-binding regions in antibodies based on sequence or structure

(2012) Vered Kunik et al.   NUCLEIC ACIDS RESEARCH

Structural Consensus among Antibodies Defines the Antigen Binding Site

(2012) Vered Kunik et al.   PLoS Computational Biology

Analyzing and visualizing residue networks of protein structures

(2011) Nadezhda T. Doncheva et al.   TRENDS IN BIOCHEMICAL SCIENCES

A New Clustering of Antibody CDR Loop Conformations

(2010) Benjamin North et al.   JOURNAL OF MOLECULAR BIOLOGY

Structural classification of CDR-H3 revisited: A lesson in antibody modeling

(2008) Daisuke Kuroda et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS