Jing Hu

ORCID: 0009-0000-3605-2185
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About
Contact & Profiles
Research Areas
  • Supramolecular Self-Assembly in Materials
  • Alzheimer's disease research and treatments
  • Acoustic Wave Resonator Technologies
  • Lipid Membrane Structure and Behavior
  • Proteins in Food Systems
  • Advanced biosensing and bioanalysis techniques
  • Bacterial Genetics and Biotechnology
  • Extracellular vesicles in disease
  • 3D Printing in Biomedical Research
  • Bacteriophages and microbial interactions
  • Biosensors and Analytical Detection
  • Magnetic Properties and Applications
  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Phytoplasmas and Hemiptera pathogens
  • Advanced Biosensing Techniques and Applications
  • Prion Diseases and Protein Misfolding
  • Probiotics and Fermented Foods
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Characterization and Applications of Magnetic Nanoparticles

Lund University
2023-2025

University of Guelph
2014

Shear forces affect self-assembly processes ranging from crystallization to fiber formation. Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides and investigated in detail A <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline" overflow="scroll"> <mml:mrow> <mml:mi mathvariant="bold">β</mml:mi> </mml:mrow> </mml:math> 42, which is associated with Alzheimer’s disease. To gain mechanistic insights into agitation, nonseeded seeded...

10.1073/pnas.2322572121 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2024-06-14

Formation of amyloid-β (Aβ) fibrils is a central pathogenic feature Alzheimer's disease. Cell-secreted extracellular vesicles (EVs) have been suggested as disease modulators, although their exact roles and relations to Aβ pathology remain unclear. We combined kinetics assays biophysical analyses explore how small (<220 nm) EVs from neuronal non-neuronal human cell lines affected the aggregation disease-associated variant Aβ(1-42) into amyloid fibrils. Using thioflavin-T monitored seeding...

10.1021/acschemneuro.3c00655 article EN cc-by ACS Chemical Neuroscience 2024-02-26

The nucleation of amyloid fibrils from monomeric protein, catalyzed by the surface existing fibrils, is an important driver many disorders such as Alzheimer's and Parkinson's diseases. structural basis this secondary process, however, poorly understood. Here, we ask whether sites are found predominantly at rare growth defects: defects in fibril core structure generated during their original assembly. We first demonstrate using specific inhibitor nucleation, Brichos, that on...

10.1101/2025.03.31.646415 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2025-04-01

Amyloid β peptide (Aβ) is the crucial protein component of extracellular plaques in Alzheimer's disease. The also contain gangliosides lipids, which are abundant membranes neuronal cells and cell-derived vesicles exosomes. When present at concentrations above its critical micelle concentration (cmc), can occur as mixed micelles. Here, we study coassembly ganglioside GM1 Aβ peptides Aβ40 42 by means microfluidic diffusional sizing, confocal microscopy, cryogenic transmission electron...

10.1021/acschemneuro.3c00524 article EN cc-by ACS Chemical Neuroscience 2023-12-05
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