J
James W Larrick
Researcher at Peking Union Medical College
Publications - 88
Citations - 3462
James W Larrick is an academic researcher from Peking Union Medical College. The author has contributed to research in topics: Stem cell & Senescence. The author has an hindex of 22, co-authored 87 publications receiving 3202 citations.
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Human CAP18 : a novel antimicrobial lipopolysaccharide-binding protein
TL;DR: The cloning of human CAP18 is reported and the anti-LPS activity of the C-terminal fragment is characterized, suggesting that CAP18(104-140) may have therapeutic utility for conditions associated with elevated concentrations of LPS.
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Cytotoxic mechanism of tumor necrosis factor-alpha.
James W Larrick,Susan Wright +1 more
TL;DR: Many intracellular pathways are set in motion by the binding of tumor necrosis factor to its cell surface receptor, and understanding how TNF initiates these pathways will facilitate the rational design of pharmaceuticals that can attenuate or potentiate the action of this important cytokine.
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Antibody engineering by parsimonious mutagenesis
Robert F. Balint,James W Larrick +1 more
TL;DR: A computer-assisted method for oligodeoxyribonucleotide-directed scanning mutagenesis, called parsimonious mutagenisation (PM), whereby all three complementarity-determining regions (CDR) of a variable region (V-region) gene can be simultaneously and thoroughly searched for improved variants in libraries of manageable size is developed.
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Autoinducer of virulence as a target for vaccine and therapy against Staphylococcus aureus.
Naomi Balaban,Tzipora Goldkorn,Rachael T. Nhan,Luong B. Dang,Steven Scott,Rose M. Ridgley,Avraham Rasooly,Susan Wright,James W Larrick,Reuven Rasooly,James R. Carlson +10 more
TL;DR: Mice vaccinated with RAP or treated with purified or synthetic RIP were protected from S. aureus pathology, suggesting that these two molecules may provide useful approaches for the prevention and treatment of diseases caused by S.Aureus.
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Identification of functional and structural amino-acid residues by parsimonious mutagenesis
TL;DR: Parsimonious mutagenesis was used to increase the affinity of C6.5, a human single-chain Fv that binds the glycoprotein tumor antigen, c-erbB-2, and identified three types of aa: structural aa, functional aa which modulate affinity, and functional a a, which are critical for recognition.