Target intelligence / Profile preview

Protein disulfide-isomerase A4 (PDIA4)

Target
PDIA4
Molecular classification
Enzyme, Protein disulfide isomerase, Chaperone
01

Overview

Protein disulfide-isomerase A4 (PDIA4) is an enzyme that functions as a chaperone in the endoplasmic reticulum (ER). It catalyzes the formation, breakage, and rearrangement of disulfide bonds during protein folding. PDIA4 has been implicated in several disease processes including tumorigenesis, angiogenesis, and therapy resistance in cancers. It also interacts with viral proteins during microbial infection. Inhibitors targeting this enzyme are under investigation for their ability to disrupt aberrant protein folding or stress responses associated with malignancy or infection.

Other names
ERp72Protein disulfide-isomerase family A member 4
02

Mechanism of action

Inhibition of protein folding, disruption of aberrant protein folding or stress responses

03

Biological functions

Protein foldingDisulfide bond formationDisulfide bond isomerizationChaperone activity
04

Disease associations

CancerTumorigenesisAngiogenesisTherapy resistanceMicrobial infection

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