Functional architecture of the retromer cargo-recognition complex-Reference-Cited by-同舟云学术

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Functional architecture of the retromer cargo-recognition complex

Published:2007-09-23 Issue:7165 Volume:449 Page:1063-1067
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Hierro Aitor,Rojas Adriana L.,Rojas Raul,Murthy Namita,Effantin Grégory,Kajava Andrey V.,Steven Alasdair C.,Bonifacino Juan S.,Hurley James H.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature06216.pdf

Reference45 articles.

1. Seaman, M. N. Recycle your receptors with retromer. Trends Cell Biol. 15, 68–75 (2005)

2. Bonifacino, J. S. & Rojas, R. Retrograde transport from endosomes to the trans-Golgi network. Nature Rev. Mol. Cell Biol. 7, 568–579 (2006)

3. Seaman, M. N. J., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665–681 (1998)

4. Haft, C. R. et al. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes. Mol. Biol. Cell 11, 4105–4116 (2000)

5. Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R. & Bonifacino, J. S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123–133 (2004)

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1. Stabilization of the retromer complex: Analysis of novel binding sites of bis-1,3-phenyl guanylhydrazone 2a to the VPS29/VPS35 interface;Computational and Structural Biotechnology Journal;2024-12

2. VPS35 or retromer as a potential target for neurodegenerative disorders: barriers to progress;Expert Opinion on Therapeutic Targets;2024-08-02

3. Assembly and fission of tubular carriers mediating protein sorting in endosomes;Nature Reviews Molecular Cell Biology;2024-06-17

4. Retromer‐mediated recruitment of the WASH complex involves discrete interactions between VPS35, VPS29, and FAM21;Protein Science;2024-04-12

5. EhVps35, a retromer component, is involved in the recycling of the EhADH and Gal/GalNac virulent proteins of Entamoeba histolytica;Frontiers in Parasitology;2024-03-26

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