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Cited by 399

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Molecular Identification of a Novel Candidate Sorting Receptor Purified from Human Brain by Receptor-associated Protein Affinity Chromatography

Petersen, Claus M., Nielsen, Morten S., Nykjær, Anders, Jacobsen, Linda, Tommerup, Niels, Rasmussen, Hanne H., RØigaard, Hans, Gliemann, JØrgen, Madsen, Peder, Moestrup, SØren K.·1997·Journal of Biological Chemistry
DOI 10.1074/jbc.272.6.3599
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Crossref · 10.1074/jbc.272.6.3599

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  • Sortilin predominates in intracellular compartments, with only a minor fraction on the cell surface and about 90% in Golgi and vesicles co-localizing with MPR300.

    “Only a minor fraction of the receptors is expressed on the cell surface, whereas ~90% are found in Golgi and vesicles, showing extensive co-localization with MPR300 (Petersen et al., 1997;Morris et al., 1998).”

    From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Petersen et al., 1997

    In “Transient Expression of gp95/Sortilin and Chimeric Receptors” (page unavailable), full-length sortilin localized particularly to the Golgi, with no detectable cell-surface staining. A receptor bearing sortilin’s tail co-localized with the cation-independent mannose-6-phosphate receptor in the Golgi and endosome-like vesicles. The paper does not report that approximately 90% of sortilin is in those compartments, and the co-localization experiment used a chimeric receptor rather than full-length sortilin. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Previous evidence on sortilin and MPR300 co-localization supports full-length sortilin as a functional sorting receptor.

    “This is in good agreement with previous evidence on sortilin and MPR300 co-localization, and in strong support of full-length sortilin as a functional sorting receptor (Petersen et al., 1997;Morris et al., 1998).”

    From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Petersen et al., 1997

    The section headed “Transient Expression of gp95/Sortilin and Chimeric Receptors” (page not provided) reports co-localization with the CI-M6P receptor for a chimera bearing sortilin’s cytoplasmic tail, not for full-length sortilin. The paper describes sortilin as a candidate sorting receptor; it does not establish that the full-length protein functions as one. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • In mouse and human liver, sortilin expression is rather poor.

    “In situ hybridization in adult mouse liver or 10-day-old whole body revealed that the colon, small intestine, retina, olfactory tract, and cerebellum express high levels of PCSK9, APLP2, and sortilin (Fig. 8, left panel), whereas in the mouse (Fig. 8, right panel) and human (56) liver, sortilin expression is rather poor.”

    From Amyloid Precursor-like Protein 2 and Sortilin Do Not Regulate the PCSK9 Convertase-mediated Low Density Lipoprotein Receptor Degradation but Interact with Each Other (2015) · cites this paper as [56]

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Research works printed but not linked: 40

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Metadata

Authors
Petersen, C. M., Nielsen, M. S., Nykjær, A., Jacobsen, L., Tommerup, N., Rasmussen, H. H., RØigaard, H., Gliemann, J., Madsen, P., & Moestrup, S. K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-02
Volume
272
Issue
6
Pages
3599-3605
ISSN
0021-9258
DOI
10.1074/jbc.272.6.3599
Cited by
399
References
2
Language
en
Licence

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