Kyou‐Hoon Han

ORCID: 0000-0001-8829-6157
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About
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Research Areas
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Nicotinic Acetylcholine Receptors Study
  • Receptor Mechanisms and Signaling
  • Cancer-related Molecular Pathways
  • RNA and protein synthesis mechanisms
  • Chemical Synthesis and Analysis
  • Ion channel regulation and function
  • Ubiquitin and proteasome pathways
  • Parkinson's Disease Mechanisms and Treatments
  • Biochemical and Structural Characterization
  • Insect and Pesticide Research
  • RNA modifications and cancer
  • Alzheimer's disease research and treatments
  • Antimicrobial Peptides and Activities
  • Carbohydrate Chemistry and Synthesis
  • Analytical Chemistry and Chromatography
  • Cancer Research and Treatments
  • Toxin Mechanisms and Immunotoxins
  • Glycosylation and Glycoproteins Research
  • Heat shock proteins research
  • Epigenetics and DNA Methylation
  • Advanced NMR Techniques and Applications
  • Cholinesterase and Neurodegenerative Diseases
  • Neurotransmitter Receptor Influence on Behavior

Korea Research Institute of Bioscience and Biotechnology
2011-2021

Korea University of Science and Technology
2011-2019

University of Science and Technology
2013-2016

Daejeon University
2013

Yuhan University
2013

Interuniversity Consortium for Magnetic Resonance
2012

University of Florence
2012

University of Utah
1997

Case Western Reserve University
1997

National Heart Lung and Blood Institute
1988-1993

DNA transcription is initiated by a small regulatory region of transactivators known as the transactivation domain. In contrast to rapid progress made on functional aspect this promiscuous domain, its structural feature still poorly characterized. Here, our multidimensional NMR study reveals that an unbound full-length p53 although similar recently discovered group loosely folded proteins in it does not have tertiary structure, nevertheless populated amphipathic helix and two nascent turns....

10.1074/jbc.m003107200 article EN cc-by Journal of Biological Chemistry 2000-09-01

Mdm2 is a cellular antagonist of p53 that keeps balanced level p53. The two proteins are linked by negative regulatory feedback loop and physically bind to each other via putative helix formed residues 18-26 transactivation domain (TAD) its binding pocket located within the N-terminal 100-residue mdm2 (Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. Pavletich, N. (1996) Science 274, 948-953). In previous report we demonstrated TAD in mdm2-freee state mostly...

10.1074/jbc.m508578200 article EN cc-by Journal of Biological Chemistry 2005-09-14

Abstract When analyzing the Free Induction Decay (FID) signal produced by nuclear magnetic resonance (NMR) spectroscopy, Fourier transforms (FT) are used to decompose time-domain signals arising from interactions. This transformation enables extraction of frequency-domain information, allowing for recognition patterns within generated NMR spectra. Most modern processing software applies FT generate final Researchers process FID using various techniques, such as phase correction, windowing,...

10.1186/s40543-025-00474-4 article EN cc-by Journal of Analytical Science & Technology 2025-02-03

The p53−MDM2 interaction regulates p53-mediated cellular responses to DNA damage, and MDM2 is overexpressed in 7% of all cancers. Structure-based computational design was applied this system libraries centered on a scaffold that projects side chain functionalities with distance angular relationships equivalent those seen the interacting motif p53. A library 173 such compounds synthesized using solution phase parallel chemistry. vitro competitive ability block p53 peptide binding determined...

10.1021/cc050142v article EN Journal of Combinatorial Chemistry 2006-03-15

Abstract The preS1 surface antigen of hepatitis B virus (HBV) is known to play an important role in the initial attachment HBV hepatocytes. We have characterized structural features full‐length using heteronuclear NMR methods and discovered that this 119‐residue protein inherently unstructured without a unique tertiary structure under nondenaturing condition. Yet, combination various parameters shows contains “pre‐structured” domains broadly covering its functional domains. most prominent...

10.1110/ps.072983507 article EN Protein Science 2007-09-01

The molluskan acetylcholine-binding protein (AChBP) is a homolog of the extracellular binding domain pentameric ligand-gated ion channel family. AChBP most closely resembles α-subunit nicotinic acetylcholine receptors and in particular homomeric α7 receptor. We report isolation characterization an α-conotoxin that has highest known affinity for Lymnaea also potently blocks nAChR subtype when expressed Xenopus oocytes. Remarkably, peptide high α3β2 indicating OmIA combination with may serve...

10.1074/jbc.m602969200 article EN cc-by Journal of Biological Chemistry 2006-06-28

Abstract Background A candidate oncogene GIG47, previously known as a neudesin with neurotrophic activity, was identified by applying the differential expression analysis method. Methods As first step to understand molecular role of we analyzed profile GIG47 in multiple human cancers including breast cancer and characterized its function related carcinogenesis. Based on this oncogenic then embarked determining high-resolution structure GIG47. We have applied multidimensional heteronuclear...

10.1186/1471-2407-12-274 article EN cc-by BMC Cancer 2012-07-02

Researchers are discovering an ever-increasing number of proteins that perform key cellular tasks without having the fixed, three-dimensional structure once thought mandatory for a protein to do its job.

10.1063/pt.3.1689 article EN Physics Today 2012-08-01

Intrinsically disordered proteins (IDPs) lack a stable tertiary structure, but their short binding regions termed Pre-Structured Motifs (PreSMo) can form transient secondary structure elements in solution. Although are crucial many biological processes and designing strategies to modulate function is highly important, both experimental computational tools describe conformational ensembles the initial steps of folding sparse. Here we report that discrete molecular dynamics (DMD) simulations...

10.1371/journal.pone.0095795 article EN cc-by PLoS ONE 2014-04-24

Disordered plant chaperones play key roles in helping plants survive harsh conditions, and they are indispensable for seeds to remain viable. Aside from well-known thoroughly characterized globular chaperone proteins, there a number of intrinsically disordered proteins (IDPs) that can also serve as highly effective protecting agents the cells. One largest groups is group dehydrins, expressed at high levels under different abiotic stress such drought, temperature, or osmotic stress. Dehydrins...

10.3390/ijms22126190 article EN International Journal of Molecular Sciences 2021-06-08

Recent experiments claiming that Naf-BBL protein follows a global downhill folding raised an important controversy as to the mechanism of fast-folding proteins. Under scenario, not only do proteins undergo gradual folding, but events along continuous pathway also could be mapped out from equilibrium denaturation experiment. Based on exact calculation using free energy landscape, relaxation eigenmodes master equation, and Monte Carlo simulation extended Muñoz–Eaton model incorporates...

10.1073/pnas.0708480105 article EN Proceedings of the National Academy of Sciences 2008-02-13

Human papillomavirus (HPV) is the major cause of cervical cancer, a deadly threat to millions females. The early oncogene product (E7) high-risk HPV16 primary agent associated with HPV-related cancers. In order understand how E7 contributes transforming activity, we investigated structural features flexible N-terminal region (46 residues) by carrying out N-15 heteronuclear NMR experiments and replica exchange molecular dynamics simulations. Several parameters as well simulation ensemble...

10.5483/bmbrep.2016.49.8.021 article EN cc-by-nc BMB Reports 2016-08-31

(1) Background: Processivity is common among enzymes and mechanochemical motors that synthesize, degrade, modify or move along polymeric substrates, such as DNA, RNA, polysaccharides proteins. Processive can make multiple rounds of modification without releasing the substrate/partner, making their operation extremely effective economical. The molecular mechanism processivity rather well understood in cases when enzyme structurally confines substrate, DNA replication factor PCNA, also ATP...

10.3390/ijms20092119 article EN International Journal of Molecular Sciences 2019-04-29
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