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Related Concept Videos

Phosphorylation01:02

Phosphorylation

53.7K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Amyloid Fibrils03:03

Amyloid Fibrils

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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Kendall's Tau Test01:16

Kendall's Tau Test

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Kendall's tau test, also known as the Kendall rank coefficient test, is a nonparametric method for assessing association between two variables. This test is particularly useful for identifying significant correlations when the distributions of the sample and population are unknown. Developed in 1938 by the British statistician Sir Maurice George Kendall, the tau coefficient (denoted as τ) serves as a rank correlation coefficient, with values ranging from -1 to +1.
A τ value of +1 indicates...
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Chemotherapy-Induced Nausea and Vomiting: Dopamine Receptor Antagonists01:29

Chemotherapy-Induced Nausea and Vomiting: Dopamine Receptor Antagonists

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Dopamine receptor antagonists, also known as antipsychotic agents, are critical in managing chemotherapy-induced vomiting. These antiemetic agents block dopamine receptors in the chemoreceptor trigger zone (CTZ), inhibiting signal transmission to the vomiting center. Antipsychotic agents encompass phenothiazines (PTZ), butyrophenones, benzamides, and thienobenzodiazepines (Zyprexa), which are utilized for their antiemetic and sedative properties.
Phenothiazines, such as prochlorperazine...
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Updated: Jan 21, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Dopamine-Induced Tau Modification Prevents Pathological Phosphorylation and Generates a Distinct Fibril Polymorph.

Zhengtao Liu1,2, Xiang Li3,4, Qianwen Wang5

  • 1Interdisciplinary Research Center on Biology and Chemistry, State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China.

Journal of the American Chemical Society
|January 20, 2026
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Summary
This summary is machine-generated.

Dopamine modification of tau protein prevents its pathological aggregation and phosphorylation, offering a protective mechanism against tauopathies like Alzheimer's disease.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Tau aggregation is central to tauopathies, including Alzheimer's disease.
  • Dopamine modification of tau has been identified as protective, but its mechanisms are unclear.

Purpose of the Study:

  • To elucidate the structural and functional consequences of dopamine modification on tau protein.
  • To investigate how dopamination affects tau phosphorylation, fibrillization, and structure.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy
  • In vitro fibrillization assays
  • Cellular seeding assays
  • Cryo-electron microscopy (cryo-EM)

Main Results:

  • Dopamine modification at Cys322 suppressed pathogenic tau phosphorylation.
  • Dopaminated tau showed reduced in vitro fibrillization and cellular seeding activity.
  • Cryo-EM revealed a unique tau fibril polymorph with a minimal core structure.

Conclusions:

  • Dopamine modification protects against tau pathology by altering tau structure and reducing aggregation.
  • Atomic-level insights into post-translational modifications of tau are crucial for understanding tauopathies.