Associated Papers
Two HIV-1 variants resistant to small molecule CCR5 inhibitors differ in how they use CCR5 for entry.
Berro R et al.
Plos Pathogens, 2009
The second extracellular loop of CCR5 contains the dominant epitopes for highly potent anti-human immunodeficiency virus monoclonal antibodies.
Zhang J et al.
Antimicrobial Agents and Chemotherapy, 2007
Identification of amino acid residues critical for LD78beta, a variant of human macrophage inflammatory protein-1alpha, binding to CCR5 and inhibition of R5 human immunodeficiency virus type 1 replication.
Miyakawa T et al.
The Journal of Biological Chemistry, 2002
Structural comparison of monomeric variants of the chemokine MIP-1beta having differing ability to bind the receptor CCR5.
Kim S et al.
Biochemistry, 2001
Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions.
Laurence JS et al.
Biochemistry, 2001
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding.
Laurence JS et al.
Biochemistry, 2000
Multiple charged and aromatic residues in CCR5 amino-terminal domain are involved in high affinity binding of both chemokines and HIV-1 Env protein.
Blanpain C et al.
The Journal of Biological Chemistry, 1999
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