Conserved aromatic residues as determinants in the folding and assembly of immunoglobulin variable domains

Author:

Campion Stephen R.ORCID

Publisher

Elsevier BV

Subject

Molecular Biology,Immunology

Reference37 articles.

1. Interchain disulphide bond formation in the assembly of immunoglobulin G: heavy-chain dimer as intermediate;Askonas;Biochem. J.,1968

2. The regulation of immunoglobulin synthesis and assembly;Baumal;Ann. N.Y. Acad. Sci.,1971

3. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP;Blond-Elguindi;Cell,1993

4. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers;Blond-Elguindi;J. Biol. Chem.,1993

5. Cysteine-associated distribution of aromatic residues in disulfide-stabilized extracellular protein families;Campion;Adv. Biol. Chem.,2013

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1. Towards a structural and functional analysis of the immunoglobulin-fold proteome;Advances in Protein Chemistry and Structural Biology;2024

2. Local and global anatomy of antibody-protein antigen recognition;Journal of Molecular Recognition;2017-12-08

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