Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability-Reference-Cited by-同舟云学术

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Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability

Published:2014-12 Issue: Volume:192 Page:123-129
ISSN:0168-1656
Container-title:Journal of Biotechnology
language:en
Short-container-title:Journal of Biotechnology

Author:

Béhar Ghislaine,Pacheco Sabino,Maillasson Mike,Mouratou Barbara,Pecorari Frédéric

Funder

Pasteur Institute

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology,Bioengineering

Reference32 articles.

1. Architecture of nonspecific protein–DNA interactions in the Sso7d-DNA complex;Agback;Nat. Struct. Biol.,1998

2. Identification and removal of immunogenicity in therapeutic proteins;Baker;Curr. Opin. Drug Discov. Dev.,2007

3. Tolerance of the archaeal Sac7d scaffold protein to alternative library designs: characterization of anti-immunoglobulin G Affitins;Béhar;Protein Eng. Des. Sel.,2013

4. High-throughput screening for enhanced protein stability;Bommarius;Curr. Opin. Biotechnol.,2006

5. Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane;Buddelmeijer;J. Bacteriol.,2009

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2. Albumin binding Nanofitins, a new scaffold to extend half-life of biologics – a case study with exenatide peptide;Peptides;2022-06

3. Application of Affitins for Affinity Purification of Proteins;Methods in Molecular Biology;2022

4. Gastrobodies are engineered antibody mimetics resilient to pepsin and hydrochloric acid;Communications Biology;2021-08-11

5. Characterization of Affitin proteolytic digestion in biorelevant media and improvement of their stabilities via protein engineering;Scientific Reports;2020-11-12

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