메뉴 건너뛰기




Volumn 2, Issue 10, 2011, Pages 724-728

Exploiting fluorescence lifetime plasticity in FLIM: Target molecule localization in cells and tissues

Author keywords

opioid receptor; FLIM; G protein coupled receptors; ligand binding; nanocarrier

Indexed keywords

CYSTEINE; G PROTEIN COUPLED RECEPTOR KINASE; MU OPIATE RECEPTOR; NALOXONE; NANOCARRIER;

EID: 80054750807     PISSN: None     EISSN: 19485875     Source Type: Journal    
DOI: 10.1021/ml200092m     Document Type: Article
Times cited : (35)

References (22)
  • 1
    • 34249724978 scopus 로고    scopus 로고
    • Imaging proteins in vivo using fluorescence lifetime microscopy
    • DOI 10.1039/b617204k
    • Festy, F.; Ameer-Beg, S. M.; Ng, T.; Suhling, K. Imaging proteins in vivo using fluorescence lifetime microscopy Mol. Biosyst. 2007, 3 (6) 381-91 (Pubitemid 46838787)
    • (2007) Molecular BioSystems , vol.3 , Issue.6 , pp. 381-391
    • Festy, F.1    Ameer-Beg, S.M.2    Ng, T.3    Suhling, K.4
  • 2
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • DOI 10.1006/meth.2001.1189
    • Kenworthy, A. K. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy Methods 2001, 24 (3) 289-96 (Pubitemid 32846434)
    • (2001) Methods , vol.24 , Issue.3 , pp. 289-296
    • Kenworthy, A.K.1
  • 3
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P. J.; Wouters, F. S.; Reynolds, A. R.; Bastiaens, P. I. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane Science 2000, 290 (5496) 1567-70
    • (2000) Science , vol.290 , Issue.5496 , pp. 1567-70
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 4
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B. N.; Adams, S. R.; Ellisman, M. H.; Tsien, R. Y. The fluorescent toolbox for assessing protein location and function Science 2006, 312 (5771) 217-24
    • (2006) Science , vol.312 , Issue.5771 , pp. 217-24
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 5
    • 0242637558 scopus 로고    scopus 로고
    • Fluorescent ligands, antibodies, and proteins for the study of receptors
    • DOI 10.1016/j.pharmthera.2003.08.001
    • Daly, C. J.; McGrath, J. C. Fluorescent ligands, antibodies, and proteins for the study of receptors Pharmacol. Ther. 2003, 100 (2) 101-18 (Pubitemid 37377908)
    • (2003) Pharmacology and Therapeutics , vol.100 , Issue.2 , pp. 101-118
    • Daly, C.J.1    McGrath, J.C.2
  • 7
    • 25144446146 scopus 로고    scopus 로고
    • Fluorophore-tagged GPCR ligands
    • DOI 10.1016/j.cbpa.2005.08.016, PII S1367593105001134, Mechanisms / Analytical Techniques
    • Middleton, R. J.; Kellam, B. Fluorophore-tagged GPCR ligands Curr. Opin. Chem. Biol. 2005, 9 (5) 517-25 (Pubitemid 41338206)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.5 , pp. 517-525
    • Middleton, R.J.1    Kellam, B.2
  • 8
    • 52249114490 scopus 로고    scopus 로고
    • Fluorophore labeling enables imaging and evaluation of specific CXCR4-ligand interaction at the cell membrane for fluorescence-based screening
    • Nomura, W.; Tanabe, Y.; Tsutsumi, H.; Tanaka, T.; Ohba, K.; Yamamoto, N.; Tamamura, H. Fluorophore labeling enables imaging and evaluation of specific CXCR4-ligand interaction at the cell membrane for fluorescence-based screening Bioconjugate Chem. 2008, 19 (9) 1917-20
    • (2008) Bioconjugate Chem. , vol.19 , Issue.9 , pp. 1917-20
    • Nomura, W.1    Tanabe, Y.2    Tsutsumi, H.3    Tanaka, T.4    Ohba, K.5    Yamamoto, N.6    Tamamura, H.7
  • 10
    • 0037414446 scopus 로고    scopus 로고
    • Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study
    • DOI 10.1016/S0022-2836(03)00326-7
    • Alexiev, U.; Rimke, I.; Pohlmann, T. Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: a time-resolved fluorescence depolarization study J. Mol. Biol. 2003, 328 (3) 705-19 (Pubitemid 36438583)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.3 , pp. 705-719
    • Alexiev, U.1    Rimke, I.2    Pohlmann, T.3
  • 11
    • 60849087699 scopus 로고    scopus 로고
    • Dissection of environmental changes at the cytoplasmic surface of light-activated bacteriorhodopsin and visual rhodopsin: Sequence of spectrally silent steps
    • Kim, T. Y.; Moeller, M.; Winkler, K.; Kirchberg, K.; Alexiev, U. Dissection of environmental changes at the cytoplasmic surface of light-activated bacteriorhodopsin and visual rhodopsin: sequence of spectrally silent steps Photochem. Photobiol. 2009, 85 (2) 570-7
    • (2009) Photochem. Photobiol. , vol.85 , Issue.2 , pp. 570-7
    • Kim, T.Y.1    Moeller, M.2    Winkler, K.3    Kirchberg, K.4    Alexiev, U.5
  • 12
    • 76249091631 scopus 로고    scopus 로고
    • Functional interaction structures of the photochromic retinal protein rhodopsin
    • Kirchberg, K.; Kim, T. Y.; Haase, S.; Alexiev, U. Functional interaction structures of the photochromic retinal protein rhodopsin. Photochem. Photobiol. Sci. 2010, 9, (2), 226-33.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , Issue.2 , pp. 226-33
    • Kirchberg, K.1    Kim, T.Y.2    Haase, S.3    Alexiev, U.4
  • 13
    • 34247191984 scopus 로고    scopus 로고
    • Picosecond multidimensional fluorescence spectroscopy: A tool to measure real-time protein dynamics during function
    • DOI 10.1562/2006-06-21-RA-943
    • Kim, T. Y.; Winkler, K.; Alexiev, U. Picosecond multidimensional fluorescence spectroscopy: a tool to measure real-time protein dynamics during function Photochem. Photobiol. 2007, 83 (2) 378-84 (Pubitemid 46623075)
    • (2007) Photochemistry and Photobiology , vol.83 , Issue.2 , pp. 378-384
    • Kim, T.-Y.1    Winkler, K.2    Alexiev, U.3
  • 14
    • 0029130047 scopus 로고
    • Phosphorylation and agonist-specific intracellular trafficking of an epitope-tagged mu-opioid receptor expressed in HEK 293 cells
    • Arden, J. R.; Segredo, V.; Wang, Z.; Lameh, J.; Sadee, W. Phosphorylation and agonist-specific intracellular trafficking of an epitope-tagged mu-opioid receptor expressed in HEK 293 cells J. Neurochem. 1995, 65 (4) 1636-45
    • (1995) J. Neurochem. , vol.65 , Issue.4 , pp. 1636-45
    • Arden, J.R.1    Segredo, V.2    Wang, Z.3    Lameh, J.4    Sadee, W.5
  • 17
    • 73649133635 scopus 로고    scopus 로고
    • GRIN1 regulates micro-opioid receptor activities by tethering the receptor and G protein in the lipid raft
    • Ge, X.; Qiu, Y.; Loh, H. H.; Law, P. Y. GRIN1 regulates micro-opioid receptor activities by tethering the receptor and G protein in the lipid raft J. Biol. Chem. 2009, 284 (52) 36521-34
    • (2009) J. Biol. Chem. , vol.284 , Issue.52 , pp. 36521-34
    • Ge, X.1    Qiu, Y.2    Loh, H.H.3    Law, P.Y.4
  • 18
    • 77949653204 scopus 로고    scopus 로고
    • Structure-biocompatibility relationship of dendritic polyglycerol derivatives
    • Khandare, J.; Mohr, A.; Calderon, M.; Welker, P.; Licha, K.; Haag, R. Structure-biocompatibility relationship of dendritic polyglycerol derivatives. Biomaterials 2010, 31, (15), 4268-77.
    • (2010) Biomaterials , vol.31 , Issue.15 , pp. 4268-77
    • Khandare, J.1    Mohr, A.2    Calderon, M.3    Welker, P.4    Licha, K.5    Haag, R.6
  • 21
    • 48249085467 scopus 로고    scopus 로고
    • Orientation dependence in fluorescent energy transfer between Cy3 and Cy5 terminally attached to double-stranded nucleic acids
    • Iqbal, A.; Arslan, S.; Okumus, B.; Wilson, T. J.; Giraud, G.; Norman, D. G.; Ha, T.; Lilley, D. M. Orientation dependence in fluorescent energy transfer between Cy3 and Cy5 terminally attached to double-stranded nucleic acids Proc. Natl. Acad. Sci. U.S.A. 2008, 105 (32) 11176-81
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.32 , pp. 11176-81
    • Iqbal, A.1    Arslan, S.2    Okumus, B.3    Wilson, T.J.4    Giraud, G.5    Norman, D.G.6    Ha, T.7    Lilley, D.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.