The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
Open accessAbstract
The wheres and whys of protein translation: Localized protein synthesis is important for a broad range of biological activities, from specifying the animal body plan to coordinating entry into the secretory pathway. Few tools are available that can investigate translation at specific subcellular sites. Jan et al. present a flexible ribosome profiling–based methodology to enable precise characterization of localized protein synthesis (see the Perspective by Shao and Hegde). Proximity-specific ribosome profiling provides a high-precision tool for looking at the mechanism of localized protein targeting and synthesis in living cells. The approach yielded a high-resolution systems-level view of cotranslational translocation at the endoplasmic reticulum. Williams et al. applied the technique to look at localized mRNA translation at the mitochondrial outer membrane. Science , this issue 10.1126/science.1257521 , p. 701 ; see also p. 748
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Cites
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Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
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Self-citationAn ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
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Self-citationA translational profiling approach for the molecular characterization of CNS cell types
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High-Resolution View of the Yeast Meiotic Program Revealed by Ribosome Profiling
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Spatially resolved, highly multiplexed RNA profiling in single cells
Chen, K. H., Boettiger, A. N., Moffitt, J. R., Wang, S., & Zhuang, X. (2015) · Science · doi:10.1126/science.aaa6090 · Cited by 2,969
The endoplasmic reticulum: structure, function and response to cellular signaling
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The mammalian ribo-interactome reveals ribosome functional diversity and heterogeneity
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Metadata
- Authors
- Jan, C. H., Williams, C. C., & Weissman, J. S.
- Venue
- Science
- Published
- 2014-11-07
- Volume
- 346
- Issue
- 6210
- Pages
- 1257521-1257521
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2133469761
- Cited by
- 430
- References
- 6
- FWCI
- 11.56
- Type
- journal article
- Language
- en
- Open access
- green
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