Antibody modeling assessment II. Structures and models

By A. Teplyakov, Jinquan Luo, G. Obmolova, T. Malia, R. Sweet, R. Stanfield, S. Kodangattil, J. C. Almagro, Gary Gilliland. 2014

58 citations recorded by the source corpus.

Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Jianzhu Ma
2. Jian Peng
3. Jinbo Xu
4. Ian A. Wilson
5. Bonnie Berger
6. A. Teplyakov
7. Gary Gilliland
8. Shitong Luo

In Radiology, Nuclear Medicine and Imaging

1. Nicholas C. Wu
2. Bonnie Berger
3. A. Teplyakov
4. Gary Gilliland
5. Dennis R. Goulet
6. M. Chiu

Citations in the corpus

• High-resolution de novo structure prediction from primary sequence (2022, background): “Antibody complementarity-determining regions (CDRs) are the most diverse and variable parts of the molecules ( 38 , 39 ).”
• A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV (2020, methodology): “replacement using PHASER with homology models for Fab CR3022 generated from 72 PDB ID: 4KMT (40) and for SARS-CoV-2 RBD generated from a structure of SARS73”
• Antibody Structure and Function: The Basis for Engineering Therapeutics (2019, background): “The results showed an approximately normal distribution of errors with a half width at half maximum of about 2◦, which is within the error observed in the crystal structures of antibodies [54].”