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- W2894370306 endingPage "322" @default.
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- W2894370306 abstract "Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family. As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions. Interestingly, TXNDC5 is frequently found overexpressed in specimens of many human diseases including various types of cancer. In this review, we summarized the biochemical function of TXNDC5 in mammalian cells and the recent progress on the understanding of its role and molecular mechanisms in cancer development. Findings of TXNDC5 in the activation of intracellular signaling pathways, stimulation of cell growth & proliferation, facilitation of cell survival and modulation of extracellular matrix to affect cancer cell invasion and metastasis are reviewed. These published studies suggest that strategies of targeting TXNDC5 can be developed as potentially valuable methods for the treatment of certain types of cancer in patients." @default.
- W2894370306 created "2018-10-05" @default.
- W2894370306 creator A5009138695 @default.
- W2894370306 creator A5009933548 @default.
- W2894370306 creator A5060820237 @default.
- W2894370306 creator A5072207454 @default.
- W2894370306 date "2018-12-01" @default.
- W2894370306 modified "2023-10-15" @default.
- W2894370306 title "A critical role of the thioredoxin domain containing protein 5 (TXNDC5) in redox homeostasis and cancer development" @default.
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- W2894370306 doi "https://doi.org/10.1016/j.gendis.2018.09.003" @default.
- W2894370306 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6303481" @default.
- W2894370306 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30591932" @default.
- W2894370306 hasPublicationYear "2018" @default.
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