Ying T.,Protein Interactions Group |
Chen W.,Protein Interactions Group |
Feng Y.,Protein Interactions Group |
Wang Y.,Protein Interactions Group |
And 3 more authors.
Journal of Biological Chemistry | Year: 2013
Background: The CH3 domain of an antibody is a homodimer. Results: Soluble monomeric IgG1 CH3 (mCH3) exhibits pH-dependent binding to FcRn. Conclusion: The mCH3 can be used as a new scaffold for generation of binders with potentially enhanced half-life. Significance: The mCH3 is a promising fusion partner for therapeutic proteins with increased therapeutic efficacy. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
PubMed | Protein Interactions Group
Type: Journal Article | Journal: Oncoimmunology | Year: 2012
The insulin-like growth factor I (IGF-I) receptor (IGF-1R) is overexpressed in most human neoplasms tested so far. Many tumors in young patients produce high levels of the IGF-1R ligands, IGF-I and IGF-II. Given the complexity of the IGF signaling pathway, its complete inhibition may require combination therapies with antibodies targeting both IGF-1R and IGF-II.