Identification of amino acid residues crucial for chemokine receptor dimerization
- 11 January 2004
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Immunology
- Vol. 5 (2), 216-223
- https://doi.org/10.1038/ni1027
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Automatic Methods for Predicting Functionally Important ResiduesJournal of Molecular Biology, 2003
- Multiple Active States and Oligomerization of CCR5 Revealed by Functional Properties of Monoclonal AntibodiesMolecular Biology of the Cell, 2002
- Structural models for dimerization of G-protein coupled receptors: The opioid receptor homodimersPeptide Science, 2002
- T-coffee: a novel method for fast and accurate multiple sequence alignmentJournal of Molecular Biology, 2000
- Cryptic Dimer Interface and Domain Organization of the Extracellular Region of Metabotropic Glutamate Receptor Subtype 1Published by Elsevier BV ,2000
- Identification of the Binding Site for a Novel Class of CCR2b Chemokine Receptor AntagonistsPublished by Elsevier BV ,2000
- The Biology of Chemokines and their ReceptorsAnnual Review of Immunology, 2000
- Mechanism of Transdominant Inhibition of CCR5-mediated HIV-1 Infection by ccr5Δ32Published by Elsevier BV ,1997
- Correlated mutations contain information about protein-protein interactionJournal of Molecular Biology, 1997
- Stimulation of the phosphatidyl-inositol pathway can induce T-cell activationNature, 1990