The DOI matches its Crossref record; 326 of the 326 references it cites were found in a registry or an index.
Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway
Open accessAbstract
The secretory pathway is responsible for the synthesis, folding, and delivery of a diverse array of cellular proteins. Secretory protein synthesis begins in the endoplasmic reticulum (ER), which is charged with the tasks of correctly integrating nascent proteins and ensuring correct post-translational modification and folding. Once ready for forward traffic, proteins are captured into ER-derived transport vesicles that form through the action of the COPII coat. COPII-coated vesicles are delivered to the early Golgi via distinct tethering and fusion machineries. Escaped ER residents and other cycling transport machinery components are returned to the ER via COPI-coated vesicles, which undergo similar tethering and fusion reactions. Ultimately, organelle structure, function, and cell homeostasis are maintained by modulating protein and lipid flux through the early secretory pathway. In the last decade, structural and mechanistic studies have added greatly to the strong foundation of yeast genetics on which this field was built. Here we discuss the key players that mediate secretory protein biogenesis and trafficking, highlighting recent advances that have deepened our understanding of the complexity of this conserved and essential process.
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Cites
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Cited by
Amm, I., Sommer, T., & Wolf, D. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493
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Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport
Watanabe, S., Kise, Y., Yonezawa, K., Inoue, M., Shimizu, N., Nureki, O., & Inaba, K. (2024) · Nature Communications · doi:10.1038/s41467-024-46747-1 · Cited by 12
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Metadata
- Authors
- Barlowe, C. K., & Miller, E. A.
- Venue
- Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-02-01
- Volume
- 193
- Issue
- 2
- Pages
- 383-410
- ISSN
- 0016-6731 (ISSN-L)
- 1943-2631
- OpenAlex
- W2008801986
- Cited by
- 330
- References
- 326
- FWCI
- 9.96
- Type
- journal article
- Language
- en
- Open access
- bronze
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