Chung‐Jung Tsai

ORCID: 0000-0003-1524-9928
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About
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Research Areas
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • RNA and protein synthesis mechanisms
  • Protein Kinase Regulation and GTPase Signaling
  • Bioinformatics and Genomic Networks
  • Cancer Genomics and Diagnostics
  • Computational Drug Discovery Methods
  • PI3K/AKT/mTOR signaling in cancer
  • Receptor Mechanisms and Signaling
  • Genomics and Chromatin Dynamics
  • Melanoma and MAPK Pathways
  • Protein Degradation and Inhibitors
  • Hippo pathway signaling and YAP/TAZ
  • Hemoglobin structure and function
  • Machine Learning in Bioinformatics
  • Ubiquitin and proteasome pathways
  • Bacteriophages and microbial interactions
  • Alzheimer's disease research and treatments
  • Supramolecular Self-Assembly in Materials
  • Monoclonal and Polyclonal Antibodies Research
  • RNA Research and Splicing
  • Lung Cancer Treatments and Mutations
  • Cancer-related Molecular Pathways
  • Endoplasmic Reticulum Stress and Disease
  • Genetics and Neurodevelopmental Disorders

Frederick National Laboratory for Cancer Research
2014-2023

Chung Hwa University of Medical Technology
2009-2023

National Cancer Institute
2014-2023

Harvard University
2020

National Institutes of Health
2017-2020

Yale University
2020

Rockefeller University
2020

Leidos (United States)
2013-2019

Tel Aviv University
1997-2019

Leidos Biomedical Research Inc. (United States)
2015-2019

Data sets of 362 structurally nonredundant protein-protein interfaces and 57 symmetry-related oligomeric have been used to explore whether the hydrophobic effect that guides protein folding is also main driving force for associations. The buried nonpolar surface area has measure effect. Our analysis indicates that, although plays a dominant role in binding, it not as strong observed interior monomers. Comparison interiors monomers with those reveals general, amino acids are more frequent...

10.1002/pro.5560060106 article EN Protein Science 1997-01-01

The question of how allostery works was posed almost 50 years ago. Since then it has been the focus much effort. This is for two reasons: first, intellectual curiosity basic science and desire to understand fundamental phenomena, second, its vast practical importance. Allostery at play in all processes living cell, increasingly drug discovery. Many models have successfully formulated, are able describe even absence a detailed structural mechanism. However, conceptual schemes designed...

10.1371/journal.pcbi.1003394 article EN cc-by PLoS Computational Biology 2014-02-06

Here, we present a diverse, structurally nonredundant data set of two-chain protein-protein interfaces derived from the PDB. Using sequence order-independent structural comparison algorithm and hierarchical clustering, 3799 interface clusters are obtained. These yield 103 with at least five nonhomologous members. We divide into three types. In Type I clusters, global structures chains which also similar. This cluster type is expected because, in general, related proteins associate similar...

10.1110/ps.03484604 article EN Protein Science 2004-03-25

Currently, there are two types of drugs on the market: orthosteric, which bind at active site; and allosteric, elsewhere protein surface, allosterically change conformation binding site. In this perspective we argue that different mechanisms through drug affect activity their potential pitfalls call for considerations in design. The key problem facing orthosteric is side effects can occur by to homologous proteins sharing a similar Hence, should have very high affinity target; would allow...

10.2174/138161212799436377 article EN Current Pharmaceutical Design 2012-02-20
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