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CCR5 adopts three homodimeric conformations that control cell surface delivery
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Preferential recognition of monomeric CCR5 expressed in cultured cells by the HIV-1 envelope glycoprotein gp120 for the entry of R5 HIV-1
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Propagation of conformational changes during μ-opioid receptor activation
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Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer
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CC CKR5: A RANTES, MIP-1α, MIP-1β Receptor as a Fusion Cofactor for Macrophage-Tropic HIV-1
inferredcites →https://doi.org/10.1128/aac.49.11.4721-4732.2005openalex-snapshot
Maraviroc (UK-427,857), a Potent, Orally Bioavailable, and Selective Small-Molecule Inhibitor of Chemokine Receptor CCR5 with Broad-Spectrum Anti-Human Immunodeficiency Virus Type 1 Activity
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A single-residue change in the HIV-1 V3 loop associated with maraviroc resistance impairs CCR5 binding affinity while increasing replicative capacity
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Dopamine Receptor-Interacting Protein 78 Acts as a Molecular Chaperone for CCR5 Chemokine Receptor Signaling Complex Organization
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Author response: Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain
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Reviewer #2 (Public Review): Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain
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eLife Assessment: Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain
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Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain
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