Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1. 1Vpu Directs the Degradation of the Human Immunodeficiency Virus Restriction Factor BST-2/Tetherin via a βTrCP-Dependent Mechanism2009 · 345 citations
2. 2Cooperative Binding of the Class I Major Histocompatibility Complex Cytoplasmic Domain and Human Immunodeficiency Virus Type 1 Nef to the Endosomal AP-1 Complex via Its μ Subunit2007 · 80 citations
3. 3The Medium Subunits of Adaptor Complexes Recognize Distinct but Overlapping Sets of Tyrosine-based Sorting Signals1998 · 258 citations
4. 4Tetherin/BST-2 Antagonism by Nef Depends on a Direct Physical Interaction between Nef and Tetherin, and on Clathrin-mediated Endocytosis2013 · 61 citations
5. 5The AP-2 Adaptor β2 Appendage Scaffolds Alternate Cargo Endocytosis2008 · 53 citations