Kent, Stephen B.H., 1945-....
Stephen Kent American chemist
Kent, Stephen B. H.
VIAF ID: 31166357246406641446 (Personal)
Permalink: http://viaf.org/viaf/31166357246406641446
Preferred Forms
- 100 1 _ ‡a Kent, Stephen B. H.
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- 100 1 _ ‡a Kent, Stephen B. H. ‡d 1945-
- 100 1 _ ‡a Kent, Stephen B.H., ‡d 1945-....
- 100 0 _ ‡a Stephen Kent ‡c American chemist
4xx's: Alternate Name Forms (20)
Works
Title | Sources |
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Anti-Influenza Hyperimmune Immunoglobulin Enhances Fc-Functional Antibody Immunity During Human Influenza Infection | |
Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule | |
Fc functional antibody responses to adjuvanted versus unadjuvanted seasonal influenza vaccination in community-dwelling older adults | |
Immune profiling of influenza-specific B cell and T cell responses in macaques using flow cytometry-based assays | |
Immunogenic profile of SARS-CoV-2 spike in individuals recovered from COVID-19 | |
Inducible Bronchus-Associated Lymphoid Tissues (iBALT) Serve as Sites of B Cell Selection and Maturation Following Influenza Infection in Mice | |
Inventing synthetic methods to discover how enzymes work | |
Low pH Exposure During Immunoglobulin G Purification Methods Results in Aggregates That Avidly Bind Fcγ Receptors: Implications for Measuring Fc Dependent Antibody Functions | |
Modular total chemical synthesis of a human immunodeficiency virus type 1 protease | |
A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA. | |
Peptide sequences by mass spectrometry | |
Sequencing B cell receptors from ferrets (Mustela putorius furo) | |
A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface | |
Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A | |
X-ray Structure of Native Scorpion Toxin BmBKTx1 by Racemic Protein Crystallography Using Direct Methods | |
X-ray Structure of Snow Flea Antifreeze Protein Determined by Racemic Crystallization of Synthetic Protein Enantiomers |