The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT)
Open accessAbstract
Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin, but the mechanism of lysosomal reduction is unknown. We describe here a lysosomal thiol reductase optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. The active site, determined by mutagenesis, consists of a pair of cysteine residues separated by two amino acids, similar to other enzymes of the thioredoxin family. The enzyme is a soluble glycoprotein that is synthesized as a precursor. After delivery into the endosomal/lysosomal system by the mannose 6-phosphate receptor, N- and C-terminal prosequences are removed. The enzyme is expressed constitutively in antigen-presenting cells and induced by IFN-γ in other cell types, suggesting a potentially important role in antigen processing.
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Self-citation[21] Thioredoxin and thioredoxin reductase
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Self-citationREGULATION OF MHC CLASS II GENES: Lessons from a Disease
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Cited by
Kamaly, N., Yameen, B., Wu, J., & Farokhzad, O. C. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00346 · Cited by 3,070
Saito, G., Swanson, J. A., & Lee, K.-D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00179-5 · Cited by 1,407
Role of integrated cancer nanomedicine in overcoming drug resistance
Iyer, A. K., Singh, A., Ganta, S., & Amiji, M. M. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.07.012 · Cited by 343
Prevention of oxidant-induced cell death by lysosomotropic iron chelators
Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00106-0 · Cited by 185
Metadata
- Authors
- Arunachalam, B., Phan, U. T., Geuze, H. J., & Cresswell, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-18
- Volume
- 97
- Issue
- 2
- Pages
- 745-750
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2068181993
- Cited by
- 438
- References
- 36
- FWCI
- 4.62
- Type
- journal article
- Language
- en
- Open access
- green
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- Arunachalam, B., Phan, U. T., Geuze, H. J., & Cresswell, P. (2000). Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT). Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.2.745
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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