Measurement of Intermolecular Distances for the Natural Agonist Peptide Docked at the Cholecystokinin Receptor Expressed in Situ Using Fluorescence Resonance Energy Transfer

2004 ◽  
Vol 65 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Kaleeckal G. Harikumar ◽  
Delia I. Pinon ◽  
William S. Wessels ◽  
Eric S. Dawson ◽  
Terry P. Lybrand ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Agonist Peptide ◽  
Cholecystokinin Receptor ◽  
Fluorescence Resonance ◽  
Intermolecular Distances

In situ manipulation of fluorescence resonance energy transfer between quantum dots and monolayer graphene oxide by laser irradiation

Nanoscale ◽  
2019 ◽  
Vol 11 (3) ◽  
pp. 1236-1244 ◽  
Author(s):  
Wenjun He ◽  
Chengbing Qin ◽  
Zhixing Qiao ◽  
Yani Gong ◽  
Xiaorong Zhang ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Graphene Oxide ◽  
Energy Transfer ◽  
Laser Irradiation ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Monolayer Graphene ◽  
Fluorescence Resonance

Fluorescence resonance energy transfer between CdSeTe/ZnS quantum dots and monolayer graphene oxide is in situ manipulated by laser irradiation.

scholarly journals Imaging specific newly synthesized proteins within cells by fluorescence resonance energy transfer

2017 ◽  
Vol 8 (1) ◽  
pp. 748-754
Author(s):  
Linfeng Sheng ◽  
Lesi Cai ◽  
Jie Liu ◽  
Sichun Zhang ◽  
Jing-Juan Xu ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Resonance ◽  
Endogenous Proteins

A FRET-based strategy is developed to image and track specific newly synthesized endogenous proteinsin situ.

scholarly journals Follice-Stimulating Hormone Receptor Forms Oligomers and Shows Evidence of Carboxyl-Terminal Proteolytic Processing

Endocrinology ◽  
2007 ◽  
Vol 148 (5) ◽  
pp. 1987-1995 ◽  
Author(s):  
Richard M. Thomas ◽  
Cheryl A. Nechamen ◽  
Joseph E. Mazurkiewicz ◽  
Marco Muda ◽  
Stephen Palmer ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Ovarian Follicle ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Extracellular Domain ◽  
Proteolytic Processing ◽  
Full Length ◽  
Fluorescence Resonance

FSH receptor (FSHR), a member of the G protein-coupled receptor superfamily, is present in the plasma membrane of ovarian granulosa cells and testicular Sertoli cells. FSH regulates normal ovarian follicle development and spermatogenesis through FSHR. The extracellular domain of FSHR is a weakly associated homodimer in the recently solved crystal structure of FSH in complex with the extracellular domain of FSHR. However, there is currently no biochemical data that demonstrate that FSHR exists as a dimer or higher-order oligomer in cell membranes. A fluorescence resonance energy transfer assay was used to determine whether full-length native FSHR is an oligomer. FSHR-specific monoclonal antibody or Fab fragments, labeled with two different fluorophores, allowed the study of nontagged receptor in situ. Unoccupied FSHR exhibited strong fluorescence resonance energy transfer profiles in situ. Complementary coimmunoprecipitation experiments of myc- or FLAG-tagged FSHR indicated that FSHR forms oligomers early in receptor biosynthesis. No effect of FSH treatment was observed. Thus, immature forms of FSHR, not yet fully processed, were observed to coimmunoprecipitate. An unexpected observation was made that the C-terminal epitope tags are removed from FSHR before arrival at the cell surface. These results provide the first evidence for oligomers of full-length FSHR in situ and for C-terminal proteolytic processing of FSHR and that both events take place during biosynthesis. This may explain how heterozygous mutations in the FSHR gene that affect receptor trafficking may be ameliorated by oligomer formation.

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