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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Lysosomal Hydrolases01:22

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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Phosphorylation01:02

Phosphorylation

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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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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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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. 
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Updated: Jan 10, 2026

A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations
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A Novel Strategy Combining Array-CGH, Whole-exome Sequencing and In Utero Electroporation in Rodents to Identify Causative Genes for Brain Malformations

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Structure, function, and pathology of PHF23.

Linlin Liu1,2, Rui Zhang1, Rui Liu2

  • 1Department of Neurosurgery, West China Hospital, Sichuan University, Chengdu, China.

Frontiers in Cell and Developmental Biology
|November 21, 2025
PubMed
Summary
This summary is machine-generated.

Plant Homeodomain Finger Protein 23 (PHF23) is vital for gene regulation and linked to diseases like cancer. This review explores PHF23

Keywords:
PHD domainPHF23cancerdegenerative diseaseepigenetic regulation

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Plant Homeodomain Finger Protein 23 (PHF23) is a key protein in the PHD finger family.
  • PHF23 is implicated in critical cellular functions including gene expression regulation, autophagy, and tumorigenesis.
  • Dysregulation of PHF23 is associated with significant diseases such as malignancies, osteoarthritis, and tuberculosis.

Purpose of the Study:

  • To systematically review and synthesize existing literature on PHF23.
  • To provide a comprehensive overview of PHF23 structure, function, and its association with various diseases.
  • To highlight PHF23 as a potential therapeutic and diagnostic target for related diseases.

Main Methods:

  • Literature review of scientific publications on PHF23.
  • Analysis of studies detailing PHF23's role in biological processes.
  • Examination of research linking PHF23 to disease pathogenesis.

Main Results:

  • PHF23 plays a fundamental role in regulating gene expression.
  • PHF23 is involved in cellular processes like autophagy and has implications in tumorigenesis.
  • PHF23 is demonstrably linked to the progression of malignancies, osteoarthritis, and tuberculosis.

Conclusions:

  • PHF23 is a critical protein with diverse biological functions.
  • PHF23's involvement in multiple diseases underscores its clinical relevance.
  • Targeting PHF23 offers potential for novel therapeutic and diagnostic strategies, aiming to improve patient outcomes.