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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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Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl...
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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.
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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Related Experiment Video

Updated: May 2, 2026

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods
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HEV-ORF3 Encoding Phosphoprotein Interacts With Hepsin.

Chunyan Wang1, Liang Guo1, Dayi Yu2

  • 1Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China.

Hepatitis Monthly
|March 6, 2014
PubMed
Summary
This summary is machine-generated.

Hepatitis E virus ORF3 protein interacts with hepsin, a tumor inhibitor. This study identified hepsin as a key interacting protein, advancing understanding of HEV ORF3's function.

Keywords:
HepsinImmunoprecipitationORF3 protein, Hepatitis E virusTwo-Hybrid System Techniques

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Area of Science:

  • Virology
  • Molecular Biology
  • Hepatology

Background:

  • Hepatitis E virus (HEV) causes significant acute hepatitis globally.
  • The HEV Open Reading Frame 3 (ORF3) protein's function remains unclear.
  • ORF3 protein is a phosphorylated protein associated with the cytoskeleton.

Purpose of the Study:

  • To elucidate the function of the HEV ORF3 protein (pORF3).
  • To identify proteins that interact with pORF3.
  • To validate interactions using co-immunoprecipitation (Co-IP).

Main Methods:

  • Screening of a human hepatocytes cDNA library using the Cyto-Trap two-hybrid system.
  • Verification of protein interactions via co-immunoprecipitation (Co-IP).

Main Results:

  • Eight potential pORF3 interacting proteins were identified using the two-hybrid system.
  • Hepsin, a known tumor inhibitor, was confirmed to interact with pORF3 via Co-IP.

Conclusions:

  • Hepsin specifically interacts with the Hepatitis E virus ORF3 protein.
  • This interaction provides insights into the biological role of pORF3.