Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Sophie B. Sun"'
Publikováno v:
Journal of the American Chemical Society. 140(5)
The monoclonal antibody 48G7 differs from its germline precursor by ten somatic mutations, a number of which appear to be functionally silent. We analyzed the effects of individual somatic mutations and combinations thereof on both antibody binding a
Publikováno v:
ChemBioChem. 15:1721-1729
To date, over 100 noncanonical amino acids (ncAAs) have been genetically encoded in living cells in order to expand the functional repertoire of the canonical 20 amino acids. More recently, this technology has been expanded to the field of protein th
Autor:
Vaughn V. Smider, Erik D. Wold, Mingchao Kang, Sei-hyun Choi, Jennifer L. Furman, Peter G. Schultz, Chan Hyuk Kim, Sophie B. Sun, Yu Cao
Publikováno v:
Journal of the American Chemical Society
Selective covalent bond formation at a protein-protein interface potentially can be achieved by genetically introducing into a protein an appropriately "tuned" electrophilic unnatural amino acid that reacts with a native nucleophilic residue in its c
Publikováno v:
Journal of the American Chemical Society. 135:9980-9983
The monoclonal antibody 48G7 differs from its germline precursor by 10 somatic mutations, a number of which appear to be functionally silent. We analyzed the effects of individual somatic mutations and combinations thereof on both antibody binding af
Autor:
Lorenzo de Lichtervelde, Sophie B. Sun, Vaughn V. Smider, Yong Zhang, Danling Wang, Feng Wang, Peter G. Schultz
Publikováno v:
Angewandte Chemie International Edition. 52:8295-8298
Most mammalian antibodies have complementarity determining region (CDR) loops of 8–16 residues, while some human antibodies have longer, protruding CDR loops that play a role in virus neutralization.[1] The bovine antibody repertoire features a sub
Autor:
Yong Zhang, Danling Wang, Lorenzo de Lichtervelde, Sophie B. Sun, Vaughn V. Smider, Peter G. Schultz, Feng Wang
Publikováno v:
Angewandte Chemie. 125:8453-8456
Publikováno v:
Biochemistry. 52:1828-1837
To site-specifically incorporate an unnatural amino acid (UAA) into target proteins in Escherichia coli, we use a suppressor plasmid that provides an engineered suppressor tRNA and an aminoacyl-tRNA synthetase (aaRS) specific for the UAA of interest.
Autor:
Travis S. Young, Sophie B. Sun, Holly Pugh, Hwayoung Yun, Timothy M. Wright, Stephanie A. Kazane, Chan Hyuk Kim, Ji Young Kim, James N. Kochenderfer, Peter G. Schultz, Bryan R. Fonslow, Jennifer S. Y. Ma, Min Soo Kim, Sei-hyun Choi, Oded Singer, David T. Rodgers, Yu Cao
Publikováno v:
Proceedings of the National Academy of Sciences. 113
The adoptive transfer of autologous T cells engineered to express a chimeric antigen receptor (CAR) has emerged as a promising cancer therapy. Despite impressive clinical efficacy, the general application of current CAR-T--cell therapy is limited by