HT
Hai M. Ta
Baylor College of Medicine, Rice University, Sungkyunkwan University - Natural Sciences Campus, University of California, San Francisco
Research areas: Biochemistry, Genetics and Molecular Biology · Structural Biology · Enzyme Structure and Function · Computational Drug Discovery Methods · Protein Structure and Dynamics
0000-0002-7298-6177
Employment
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Baylor College of Medicine Staff Scientist2021 - Present
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Rice University Postdoctoral Researcher2017 - 2021
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University of California San Francisco Postdoctoral Researcher2013 - 2016
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Yale University Postdoc2011 - 2013
Education
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Sungkyunkwan University - Natural Sciences Campus Ph.D2004 - 2010
Projects & Funding
Projects & funding information is unavailable.
Publications (14)
- Identification of potent inhibitors of JUN N-terminal kinases for treatment of endometriosis and associated pain Save
- Fyn–Saracatinib Complex Structure Reveals an Active State-like Conformation Save
- Reversible male contraception by targeted inhibition of serine/threonine kinase 33 Save
- Stereospecific NANOG PEST Stabilization by Pin1 Save
- Discovery of potent BET bromodomain 1 stereoselective inhibitors using DNA-encoded chemical library selections. Save
- Characterization of an A3G-VifHIV-1-CRL5-CBFβ Structure Using a Cross-linking Mass Spectrometry Pipeline for Integrative Modeling of Host-Pathogen Complexes. Save
- Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA. Save
- Targeting Mannitol Metabolism as an Alternative Antimicrobial Strategy Based on the Structure-Function Study of Mannitol-1-Phosphate Dehydrogenase in Staphylococcus aureus. Save
- Conformational Dynamics of the HIV-Vif Protein Complex. Save
- Fab-based inhibitors reveal ubiquitin independent functions for HIV Vif neutralization of APOBEC3 restriction factors. Save
- Design of a RANK-Mimetic Peptide Inhibitor of Osteoclastogenesis with Enhanced RANKL-Binding Affinity. Save
- Structure-based elucidation of the regulatory mechanism for aminopeptidase activity. Save
- Structure-based development of a receptor activator of nuclear factor-kappaB ligand (RANKL) inhibitor peptide and molecular basis for osteopetrosis. Save
- Crystal structure of Streptococcus pneumoniae Sp1610, a putative tRNA methyltransferase, in complex with S-adenosyl-L-methionine. Save