The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
The ER membrane protein complex is a transmembrane domain insertase
Open accessAbstract
A new way into the ER: Membrane-embedded proteins are highly diverse in topology, physical characteristics, and location. This diversity necessitates multiple pathways for their effective membrane insertion. Guna et al. found that a widely conserved protein complex is responsible for inserting a subset of membrane proteins into the endoplasmic reticulum (ER) membrane (see the Perspective by Fry and Clemons Jr.). This ER membrane protein complex (EMC) inserts transmembrane domains whose topology and hydrophobicity preclude effective recognition by other insertion factors. This finding helps explain why the loss of EMC causes ER stress and altered protein trafficking. Science , this issue p. 470 ; see also p. 390
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Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Miller-Vedam, L. E., Bräuning, B., Popova, K. D., Schirle Oakdale, N. T., Bonnar, J. L., Prabu, J. R., Boydston, E. A., Sevillano, N., Shurtleff, M. J., Stroud, R. M., et al. (2020) · eLife · doi:10.7554/elife.62611 · Cited by 87
Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily.
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Metadata
- Authors
- Guna, A., Volkmar, N., Christianson, J. C., & Hegde, R. S.
- Venue
- Science
- Published
- 2018-01-26
- Volume
- 359
- Issue
- 6374
- Pages
- 470-473
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2774806607
- Cited by
- 300
- References
- 44
- FWCI
- 13.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
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