Bioluminescence Resonance Energy Transfer Reveals Ligand-induced Conformational Changes in CXCR4 Homo- and Heterodimers-Reference-Cited by-同舟云学术

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Bioluminescence Resonance Energy Transfer Reveals Ligand-induced Conformational Changes in CXCR4 Homo- and Heterodimers

Published:2005-03 Issue:11 Volume:280 Page:9895-9903
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Percherancier Yann,Berchiche Yamina A.,Slight Isabelle,Volkmer-Engert Rudolf,Tamamura Hirokazu,Fujii Nobutaka,Bouvier Michel,Heveker Nikolaus

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference60 articles.

1. Roles of G‐protein‐coupled receptor dimerization

2. Monitoring Receptor Oligomerization Using Time-resolved Fluorescence Resonance Energy Transfer and Bioluminescence Resonance Energy Transfer

3. Constitutive Agonist-independent CCR5 Oligomerization and Antibody-mediated Clustering Occurring at Physiological Levels of Receptors

4. Ligand-independent Dimerization of CXCR4, a Principal HIV-1 Coreceptor

5. Oxytocin and Vasopressin V1a and V2 Receptors Form Constitutive Homo- and Heterodimers during Biosynthesis

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