Potent antibody therapeutics by design

By P. Carter. Nature reviews. Immunology, 2006

1,121 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/a045e9fb5561243c50de44936a822104819eb9b3

How researchers see this paper

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In Molecular Biology

1. A. Chan
2. P. Carter
3. Tong Li
4. R. Jefferis
5. K. Imai
6. A. Takaoka
7. Robert J. Pantazes
8. Costas D. Maranas

In Oncology

1. R. Jefferis
2. K. Imai
3. A. Takaoka
4. A. Chan
5. W. Hurley
6. P. Theil
7. David A. Weitz
8. P. Carter

In Radiology, Nuclear Medicine and Imaging

1. A. Chan
2. P. Carter
3. Tong Li
4. R. Jefferis
5. K. Imai
6. A. Takaoka
7. Costas D. Maranas
8. Robert J. Pantazes

Citations in the corpus

• Glycosylation as a strategy to improve antibody-based therapeutics (2009, background): “Additionally, it is estimated that ∼30% of new drugs that are likely to be licensed during the next decade will be based on antibody product”
• Therapeutic antibodies for autoimmunity and inflammation (2010, background): “The quest for better therapeutic antibodies has gained great momentum in recent years, motivated by a convergence of clinical, scientific, technological and commercial factor”
• Design of therapeutic proteins with enhanced stability (2009, background): “Because of their potential in the cure of various diseases, antibodies currently constitute the most rapidly growing class of human therapeutics (1).”
• Ultrahigh-throughput screening in drop-based microfluidics for directed evolution (2010, methodology): “A particularly powerful tool for these technologies is directed evolution (2–4), which is a means of producing proteins and nucleic acids with tailor-made activities, and which has led to new classes of drugs (2), as well as improved enzymes (3) and strains of microorganisms for industrial applicati”
• The CamSol method of rational design of protein mutants with enhanced solubility. (2015, background): “Strategies on this type based on expert analysis of antibody structures have been proposed [11,31–33].”
• Perspectives on Immunoglobulins in Colostrum and Milk (2011, background): “Intact immunoglobulin, F(ab’)2 and other antibody formats are being exploited in development of antibody therapeutics [198].”
• Clinical Pharmacokinetics of Therapeutic Monoclonal Antibodies (2010, background): “In a recent review, the development and enhancement of current and investigational antibodies was discussed.([16]) Antibody fragments, consisting of only an antigen-binding part (Fab fragments) or single-chain variable fragments, have been developed as well, and have shown certain interesting distri”
• Deep mutational scanning of an antibody against epidermal growth factor receptor using mammalian cell display and massively parallel pyrosequencing (2013, background): “In particular, the ability to alter binding of antibodies to their antigens has been shown to have substantial effects on their biological function and has led to the creation of numerous antibody therapeutics.(1,2) Established display-based methods for engineering protein affinity involve generatin”
• OptMAVEn – A New Framework for the de novo Design of Antibody Variable Region Models Targeting Specific Antigen Epitopes (2014, background): “Although widely utilized, the low clinical success rate using mouse antibodies reflects that these foreign proteins can be highly immunogenic in humans, and they typically have weak interactions with human complement and antibody receptors, resulting in inefficient effector functions [3].”
• Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, high-throughput selection and analytical tool. (2013, background): “…generation of target-binding antibodies has become more routine with improvements of in vivo and in vitro discovery technologies (Hoogenboom, 2005; Carter, 2006), there are additional attributes that often preclude antibody leads from becoming successful drugs (Jacobs et al., 2010; Wu et al.,…”
• Comparing antibody and small-molecule therapies for cancer (2006, background): “Because of their inability to pass through the cellular membrane, mAbs can only act on molecules that are expressed on the cell surface or secrete”