Confocal FRET Microscopy To Measure Clustering Of Receptor-Ligand Complexes In Endocytic Membranes
ABSTRACT: Our main objective is to address the molecular mechanisms underlying the dynamics of protein distribution within membranes, which is involved in several cellular processes, such as protein sorting, organelle and membrane microdomain biogenesis, protein-protein interactions, receptor function and spatial organization of signal transduction....
Fret Imaging Of Pit-1 Protein Interactions In Living Cells
ABSTRACT: The combined use of fluorescence resonance energy transfer (FRET) microscopy and expression of genetic vectors encoding protein fusions with green fluorescent protein (GFP) and blue fluorescent protein (BFP) provides an exceptionally esnsitive method for detecting the interaction of protein partners in living cells....
Journal Of Biomedical Optics 3(2), 154-160 (April 1998)
Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
Rajesh Babu Sekar
ABSTRACT: The current advances in fluorescence microscopy, coupled with the development of new fluorescent probes, make fluorescence resonance energy transfer (FRET) a powerful technique for studying molecular interactions inside living cells with improved spatial (angstrom) and temporal (nanosecond) resolution, distance range, and sensitivity and a broader range of biological applications....
Fluorescence Resonance Energy Transfer Microscopyl A Mini Review
ABSTRACT: Fluorescence resonance energy transfer (FRET) microscopy is a better method than the x-ray diffraction, nuclear magnetic resonance, or electron microscopy for studying the structure and localization of proteins under physiological conditions....
Journal Of Biomedical Optics 6(3) 28-291 (July 2001)
Visualizing Protein Interactions In Living Cells Using Digitized GFP Imaging And FRET Microscopy
ABSTRACT: Determining when and where specific proteins associate with one another in the living cell is of considerable importance to many biologists. Through the use of conventional fluorescence microscopy, proteins labeled with different fluophores can be localized within fixed or lving cell preparations....
Methods In Cell Biology, Vol. 58
Characterization Of One- And Two-Photon Excitation Fluorescence Resonance Energy Transfer Microscopy
ABSTRACT: Advances in molecular biology provide various methods to define the structure and function of the individual proteins that form the component parts of subcellular structures. The ability to see the dynamic behavior of a specific protein inside the living cell became possible through the application of advanced fluorescence resonance energy transfer (FRET) microscope techniques....
Methods In Press (December, 2002)
Fluorescence Resonance Energy Transfer Microscopy Of Localized Protein Interactions In The Living Cell Nucleus
Richard N. Day
ABSTRACT: Early in the 19th century the art of light microscopy Cells respond to environmental cues by modifying protein com- had advanced sufficiently to allow the identification of plexes in the nucleus to produce a change in the pattern of gene the cell as the vital unit of the living organism. Improveexpression. In this article, we review techniques that allow us to visualize these protein interactions as they occur in living cells....
Methods 25, 4-18 (2001)
Imaging The Localized Protein Interactions Between Pit-1 And The CCAAT/Enhancer Binding Protein Alpha (C/EBP?) In The Living Pituitary Cell Nucleus
ABSTRACT: The homeodomain (HD) protein Pit-1 cooperates with the basic-leucine zipper (b-ZIP) protein CCAAT/enhancer binding protein alpha (C/EBPá) to control pituitary-specific prolactin (PRL) gene transcription. We previously observed that C/EBPá was concentrated in regions of centromeric heterochromatin in pituitary GHFT1-5 cells and that co-expressed Pit-1 re-distributed C/EBPá to the subnuclear sites occupied by Pit-1. Here, we used fluorescence resonance energy transfer (FRET) microscopy to show when C/EBPá was recruited by Pit-1, the average distance separating the fluorophores labeling the proteins was less than 7 nm....
Day Et Al. Revised ME 02-0136