The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Improved mammalian retromer cryo-EM structures reveal a new assembly interface
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This interaction is unique to Retriever, as Retromer uses distinct surfaces to interact with adaptors, such as SNX3 and SNX27, or directly with cargoes, such as DMT1.
“This interaction is unique to Retriever, as Retromer uses distinct surfaces to interact with adaptors, such as SNX3 and SNX27, or directly with cargoes, such as DMT126,29,34”
From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [34]
The paper’s introductory text (labeled Abstract in our copy; no page number available) says retromer binds SNX3 and SNX27 and has been implicated in direct cargo recognition. It does not identify DMT1 as a directly bound cargo or establish that retromer uses distinct surfaces for those interactions. Nor does it establish that the interaction described by the citing paper is unique to Retriever. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe precise mechanisms of cargo selection by Retriever have remained elusive.
“Unlike the well-studied Retromer25,26,34, the precise mechanisms of cargo selection by Retriever have remained elusive37.”
From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [34]
The paper’s introductory discussion (page unavailable) mentions Retriever only to identify VPS26C as a subunit of that complex. A search for Retriever and cargo-selection mechanisms found no passage in our copy saying whether those mechanisms remain elusive; the paper’s cargo-recognition discussion concerns Retromer instead. (LLM, conf=0.76)
Experimental — accuracy not yet measured
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Percentages, sums and reported differences re-computed from the paper’s own numbers.
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Citations
Cites
Retromer: A Master Conductor of Endosome Sorting
Burd, C., & Cullen, P. J. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016774 · Cited by 435
Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3610 · Cited by 346
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Cited by
Sorted by citations
Structural basis for Retriever-SNX17 assembly and endosomal sorting
Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23
Metadata
- Authors
- Kendall, A. K., Chandra, M., Xie, B., Wan, W., & Jackson, L. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2022-11
- Volume
- 298
- Issue
- 11
- Pages
- 102523
- ISSN
- 0021-9258
- PMC
- PMC9636581
- Cited by
- 18
- References
- 2
- Language
- en
- Licence
- Funders
- NIH (U24 GM129539, R35GM119525, DP2GM146321)
- Vanderbilt University
- Simons Foundation (SF349247, R35GM119525, DP2GM146321)
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