Quantitative Fluorescence Microscopy

References

• Grynkiewicz GM, Poenie M, Tsien RY: A new generation of Ca2+ indicators with greatly improved fluorescence proper-ties. J Biol Chem 260:3440–3450, 1985
   PubMed Web of Science ®Google Scholar
• Ward WW, Prentice HJ, Roth AF et al: Spectral perturbations of the Aequorea green fluorescent protein. Photochem Photo-bio 35:803–808, 1982
   Web of Science ®Google Scholar
• Llopis J, McCaffery JM, Miyawaki A et al: Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc Nat Acad Sci 5:6803–6808, 1998
   Web of Science ®Google Scholar
• Miyawaki A, Llopis J, Heim R, McCarrery JM et al: Fluores-cent indicators for based on green fluorescent proteins and calmodulin. Nature 388:882–887, 1997
   PubMed Web of Science ®Google Scholar
• Centonze VE, Maryon E, Wokosin D et al: Excitation-contraction coupling in C. elegans muscle cells as monitored by multiphoton excitation FRET imaging of calcium indicator proteins, Abstr 226. 1999 International Worm Meeting 1999
   Google Scholar
• Tsien RY, Pozzan T: Measurement of cytosolic free Ca2+ with quin2. Meth Enzymol 172:230–262,
   PubMed Web of Science ®Google Scholar
• Williams DA, Fay FS: Intracellular calibration of fluorescent calcium indicator Fura-2. Cell Calci 11:75–83, 1990
   PubMed Web of Science ®Google Scholar
• Westerblad H, Allen DG: Intracellular calibration of the cal-cium indicator indo-1 in isolated fibers of Xenopus muscle. Biophys J 71:908–917, 1996
   PubMed Web of Science ®Google Scholar
• Cheng H, Lederer WJ, Cannell MB: Calcium sparks: elemen-tary events underlying excitation-contraction coupling in heart muscle. Science 262:740–744, 1993
   PubMed Web of Science ®Google Scholar
• Svoboda K, Denk W, Kleinfeld D, Tank DW: In vivo den-dritic calcium dynamics in neocortical pyramidal neurons. Na-ture 385:161–165, 1997
   PubMed Web of Science ®Google Scholar
• Baird GS, Zacharias DA, Tsein RY: Circular permutation and receptor insertion within green fluorescent proteins. Proc Natl Acad Sci 96:1241–11246, 1999
   Google Scholar
• Dos Remedios CG, Moens PDJ: Fluorescence resonance en-ergy transfer spectroscopy is a reliable “ruler” for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. j Struct Biol 115:175–185,
   PubMed Web of Science ®Google Scholar
• Herman B: Fluorescence Microscopy. BIOS Scientific Pub-lishers Ltd, Oxford, UK, 1998
   Google Scholar
• Erikson JW, Cerione RA: Resonance energy transfer as a di-rect monitor of GTP-binding protein-effector interactions: ac-tivated a-transducin binding to the cGMP phosphodiesterase in the bovine phototransduction cascade. Biochemistry 30: 7112-7118
   Google Scholar
• Gordon GW, Berry G., Liang XH, Levine B, Herman B: Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74:2702-2713
   Google Scholar
• Damelin M, Silver PA: Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Molec Cell 5:133–140, 2000
   PubMed Web of Science ®Google Scholar
• Youvan DC, Coleman WJ, Silva CM et al: Fluorescence im-aging micro-spectrophotometer (FIMS). Biotechnology 1:1–16, 1997
   Google Scholar
• Mahajan NP, Linder K, Berry G et al: Bc1-2 and Bax inter-actions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nature Biotech 16:547–552, 1998
   PubMed Web of Science ®Google Scholar
• Mahajan NP, Harrison-Shostak DC, Michaux J, Herman B: Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis. Chem Biol 6:401–409, 1999
   PubMed Web of Science ®Google Scholar
• Matayoshi ED, Wang GT, Krafft GA, Erickson J: Novel duorogenic substrates for assaying retroviral proteases by reso-nance energy transfer. Science 247:954–958, 1990
   PubMed Web of Science ®Google Scholar
• Taliani M, Bianchi E, Narjes F et al: A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates. Anal Biochem 240:60–67, 1996
   PubMed Web of Science ®Google Scholar
• Wang GT, Chung CC, Holzman TF, Kraft GA: A continuous fluorescence assay of rennin activity. Anal Biochem 210:351–359, 1993
   PubMed Web of Science ®Google Scholar
• Ju J, Glazer AN, Mathies RA: Energy transfer primers: A new fluorescence labeling paradigm for DNA sequencing and analysis. Nature Med 2:246–249, 1996
   PubMed Web of Science ®Google Scholar
• Gelsthorp AR, Wells RS, Lowe AP et al: High-throughput class I HLA genotyping using fluorescence resonance energy transfer (FRET) probes and sequence-specific primer-polymerase chain reaction (SSP-PCR). Tiss Antigens 54:603–14, 1999
   PubMed Web of Science ®Google Scholar
• Gonzalez JE, Oades K, Leychkis Y et al: Cell-based assays and instrumentation for screening ion-channel targets. Drug Discov Today 4:431–439
   PubMed Web of Science ®Google Scholar
• Szmacinski H, Lakowicz JR, Johnson ML: Fluorescence life-time imaging microscopy: homodyne technique using high-speed gated image intensifier. Meth Enzymol 240:723–748, 1994
   PubMed Web of Science ®Google Scholar
• Lakowicz JR, Szmacinski H, Nowaczyk K et al: Fluorescence lifetime imaging of intracellular calcium in COS cells using Quin-2. Cell Calci 15:7–27, 1994
   PubMed Web of Science ®Google Scholar
• Gerritsen HC, Vroom JM, deGrauw CJ: Combining twophoton excitation with fluorescence lifetime imaging. IEEE Eng Med Biol 18:31–36, 1999
   PubMed Web of Science ®Google Scholar
• Lakowicz JR, Szmacinski H, Nowaczyk K et al: Fluores-cence lifetime imaging. Anal Biochem 202:316–330, 1992
   PubMed Web of Science ®Google Scholar
• Wang XF, Periasamy A, Coleman DM, Herman B: Fluores-cence lifetime imaging microscopy (FLIM): instrumentation and applications. Crit Rev Anal Chem 23:365–395, 1992
   Web of Science ®Google Scholar
• Gadella TWJ, Jovin TM, Clegg RM: Fluorescence lifetime imaging microscopy (FLIM): Spatial resolution of microstruc-tures on the nanosecond time scale. Biophys Chem 48:221–239, 1993
   Web of Science ®Google Scholar
• Sanders R, Draaijer A, Gerritsen HC et al: Quantitative pH imaging in cells using confocal fluorescence lifetime imaging microscopy. Analyt Biochem 227:302–308, 1995
   PubMed Web of Science ®Google Scholar
• Piston DW, Masters BR, Webb. WW: Three-dimensionally resolved NAD(P)H cellular metabolic redox imaging of the in situ cornea with two-photon excitation laser scanning micros-copy. J Microse 178:20–27, 1995
   PubMed Web of Science ®Google Scholar
• French T, So PT, Weaver DJ et al: Two-photon fluorescence lifetime imaging microscopy of macrophage- mediated anti-gen processing. J Micron. 185:339–353, 1997
   Web of Science ®Google Scholar
• Godella TW, Jovin, TM: Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluo-rescence imaging microscopy: A stereochemical model for tyrosine kinase receptor activation. J Cell Bio 129:1543–1548, 1995
   PubMed Web of Science ®Google Scholar