Chia‐Heng Hsiung

ORCID: 0000-0003-3542-587X
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About
Contact & Profiles
Research Areas
  • RNA Research and Splicing
  • Advanced Fluorescence Microscopy Techniques
  • RNA modifications and cancer
  • Cellular Mechanics and Interactions
  • Endoplasmic Reticulum Stress and Disease
  • Nuclear Structure and Function
  • Luminescence and Fluorescent Materials
  • HIV/AIDS drug development and treatment
  • Photoreceptor and optogenetics research
  • Advanced biosensing and bioanalysis techniques
  • Mass Spectrometry Techniques and Applications
  • Sirtuins and Resveratrol in Medicine
  • Protein Structure and Dynamics
  • Parvovirus B19 Infection Studies
  • Heat shock proteins research
  • Virus-based gene therapy research
  • Click Chemistry and Applications
  • Biotin and Related Studies
  • HIV Research and Treatment
  • Caveolin-1 and cellular processes
  • Lipid Membrane Structure and Behavior
  • Biochemical and Molecular Research
  • Ubiquitin and proteasome pathways
  • Cancer-related gene regulation
  • Advanced Biosensing Techniques and Applications

Westlake University
2022-2025

Institute of Natural Science
2023-2024

Hangzhou Xixi hospital
2024

Pennsylvania State University
2020-2023

Chinese Academy of Sciences
2023

Dalian Institute of Chemical Physics
2023

Central Michigan University
2014-2022

Aberrantly processed or mutant proteins misfold and assemble into a variety of soluble oligomers insoluble aggregates, process that is associated with an increasing number diseases are not curable manageable. Herein, we present chemical toolbox, AggFluor, allows for live cell imaging differentiation complex aggregated conformations in cells. Based on the chromophore core green fluorescent proteins, AggFluor comprised series molecular rotor fluorophores span wide range viscosity sensitivity....

10.1021/jacs.0c07245 article EN Journal of the American Chemical Society 2020-09-11

Protein aggregation is a biological phenomenon in which aberrantly processed or mutant proteins misfold and assemble into variety of insoluble aggregates. Decades studies have delineated the structure, interaction, activity either their natively folded structures aggregates such as amyloid fibrils. However, intermediate species exist between these two extreme states protein folding landscape. Herein, we collectively term misfolded oligomers, including soluble oligomers preamyloid that are...

10.1021/acs.accounts.1c00648 article EN Accounts of Chemical Research 2022-01-18

Abstract Fluorescence lifetime imaging has been a powerful tool for biomedical research. Recently, fluorescence lifetime‐based multiplexing expanded channels by using probes that harbor the same spectral and distinct excited state lifetime. While it is desirable to control of any given fluorescent probes, rational lifetimes remains challenge. Herein, we chose boron dipyrromethene (BODIPY) as model system provided chemical strategies regulate its derivatives with varying features. We find...

10.1002/anie.202403029 article EN Angewandte Chemie International Edition 2024-04-20

Using a single atom substitution approach, we have developed series of solvatochromic fluorophores that respond solely to polarity. The utility these is demonstrated by quantifying the polarity misfolded and aggregated proteins.

10.1039/d2sc05004h article EN cc-by-nc Chemical Science 2022-01-01

The formation of cellular condensates, akin to membraneless organelles, is typically mediated by liquid-liquid phase separation (LLPS), during which proteins and RNA molecules interact with each other via multivalent interactions. Gaining a comprehensive understanding these interactions holds significance in unraveling the mechanisms underlying condensate pathology related diseases. In an attempt toward this end, fluorescence microscopy often used examine colocalization target proteins/RNAs....

10.1091/mbc.e23-11-0442 article EN Molecular Biology of the Cell 2024-01-17

Abstract Microenvironment is critical to the function of cells and organisms. One example provided by biomolecular condensates, whose microenvironment can be vastly different from surrounding cellular environments engage unique biological functions. How microenvironments condensates affect their structure remains unknown. Here, we show that arrangements partitioning biomolecules are dictated differences between micropolarity each subcompartment. Sufficient difference in results layered...

10.1101/2023.03.30.534881 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-03-30

Cellular viscosity plays an essential role in physiology and pathology. Quantitative measurements of could be acquired from fluorescence lifetime microscopy. However, it remains a challenge to regulate how the excited-state given molecular rotor responds local viscosity. Herein, we chose BODIPY as model probe present chemical strategy rationally control its derivatives report on via lifetime. Through experimental computational analyses, found that modulating π-electron density at...

10.1021/acs.analchem.5c00482 article EN Analytical Chemistry 2025-04-29

Diabetic cardiomyopathy is preceded by mitochondrial alterations, and progresses to heart failure. We studied whether treatment with methylene blue (MB), a compound that was reported serve as an alternate electron carrier within the transport chain (ETC), improves metabolism cardiac function in type 1 diabetes. MB administered at 10 mg/kg/day control diabetic rats. Both echocardiography hemodynamic studies were performed assess function. Mitochondrial comprised measurement of oxidative...

10.1007/s11010-017-2993-1 article EN cc-by Molecular and Cellular Biochemistry 2017-03-16

Abstract RNA-binding proteins (RBPs) containing intrinsically disordered domains undergo liquid-liquid phase separation to form nuclear bodies under stress conditions. This process is also connected the misfolding and aggregation of RBPs, which are associated with a series neurodegenerative diseases. However, it remains elusive how folding states RBPs changes upon formation maturation bodies. Here, we describe SNAP-tag based imaging methods visualize in live cells via time-resolved...

10.1101/2023.04.19.537522 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2023-04-21

The primary pathway of TTP synthesis in the heart requires thymidine salvage by mitochondrial kinase 2 (TK2). However, compartmentalization this and transport nucleotides are not well understood. We investigated metabolism [3H]thymidine or [3H]TMP as precursors [3H]TTP isolated intact broken mitochondria from rat heart. results demonstrated that was readily metabolized enzymes to mitochondria. equivalent addition produced far less than amount observed with precursor. Using zidovudine inhibit...

10.1074/jbc.m114.624213 article EN cc-by Journal of Biological Chemistry 2014-12-12

The prevention of mother-to-child transmission (MTCT) HIV is a crucial component in therapy. Nucleoside reverse transcriptase inhibitors (NRTIs), primarily 3'-azido-3'-thymidine (AZT [zidovudine]), have been used to treat both mothers and neonates. While AZT being replaced with less toxic drugs treating MTCT prevention, it still commonly Problems related mitochondrial toxicity potential mutagenesis associated treatment reported treated cohorts. Yet little known concerning the metabolism on...

10.1128/aac.01180-15 article EN Antimicrobial Agents and Chemotherapy 2015-07-28

RNA-binding proteins (RBPs) containing intrinsically disordered domains undergo liquid-liquid phase separation to form nuclear bodies under stress conditions. This process is also connected the misfolding and aggregation of RBPs, which are associated with a series neurodegenerative diseases. However, it remains elusive how folding states RBPs changes upon formation maturation bodies. Here, we describe SNAP-tag based imaging methods visualize in live cells via time-resolved quantitative...

10.7554/elife.88237.1 preprint EN 2023-06-22

Abstract Fluorescence lifetime imaging has been a powerful tool for biomedical research. Recently, fluorescence lifetime‐based multiplexing expanded channels by using probes that harbor the same spectral and distinct excited state lifetime. While it is desirable to control of any given fluorescent probes, rational lifetimes remains challenge. Herein, we chose boron dipyrromethene (BODIPY) as model system provided chemical strategies regulate its derivatives with varying features. We find...

10.1002/ange.202403029 article EN Angewandte Chemie 2024-04-20

ABSTRACT Fluorescence microscopy has been widely applied in life sciences. While steady-state fluorescence intensity is mostly used, the time-resolved detection mode relying on lifetime remains underexplored. Herein, we present a family of fluorescent proteins (TRFP). Using strategy that regulates without affecting spectra FPs, have developed different TRFPs cover visible spectrum and wide range lifetime. are employed temporal-spectral resolved microscopy, allowing simultaneous imaging 9...

10.1101/2024.12.16.628778 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-20

Deoxyguanosine kinase (dGK) is reported responsible for the phosphorylation of deoxyadenosine (dA) and deoxyguanosine (dG) in mitochondrial purine salvage pathway. Antiviral nucleoside analogs known as reverse transcriptase inhibitors (NRTIs) must be phosphorylated by host enzymes analog to become active. We address possibility that NRTI may competitive dGK. From a group such analogs, we demonstrate entecavir (ETV) competitively inhibited dG dA rat mitochondria. Mitochondria from brain,...

10.1016/j.jbc.2022.101876 article EN cc-by Journal of Biological Chemistry 2022-03-28

Abstract RNA-binding proteins (RBPs) containing intrinsically disordered domains undergo liquid-liquid phase separation to form nuclear bodies under stress conditions. This process is also connected the misfolding and aggregation of RBPs, which are associated with a series neurodegenerative diseases. However, it remains elusive how folding states RBPs changes upon formation maturation bodies. Here, we describe SNAP-tag based imaging methods visualize in live cells via time-resolved...

10.7554/elife.88237 preprint EN 2023-06-22
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