메뉴 건너뛰기




Volumn 13, Issue 10, 2002, Pages 415-421

Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA 3 ADRENERGIC RECEPTOR; BETA ARRESTIN; CHEMOKINE RECEPTOR; CHOLECYSTOKININ A RECEPTOR; COMPLEMENTARY DNA; DELTA OPIATE RECEPTOR; DOPAMINE 2 RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; GONADORELIN RECEPTOR; GREEN FLUORESCENT PROTEIN; GROWTH FACTOR RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HORMONE RECEPTOR; HYBRID PROTEIN; INSULIN RECEPTOR; LUCIFERASE; LUCIFERIN; MATING HORMONE ALPHA FACTOR; NEUROKININ; NEUROKININ 2 RECEPTOR; PROTIRELIN RECEPTOR; RECEPTOR SUBTYPE; SEROTONIN 3 RECEPTOR; SOMATOSTATIN RECEPTOR; STROMAL CELL DERIVED FACTOR 1; TACHYKININ RECEPTOR; THYROTROPIN RECEPTOR;

EID: 0038170289     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(02)00669-0     Document Type: Review
Times cited : (94)

References (55)
  • 1
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewanderung und fluoreszenz
    • Förster, T. (1948) Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. 2, 54-75
    • (1948) Ann. Phys. , vol.2 , pp. 54-75
    • Förster, T.1
  • 2
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P.R. (2000) The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7, 730-734
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 3
    • 0033918209 scopus 로고    scopus 로고
    • Fluorescent probes: Looking backward and looking forward
    • Latif, R. and Graves, P. (2000) Fluorescent probes: looking backward and looking forward. Thyroid 10, 407-412
    • (2000) Thyroid , vol.10 , pp. 407-412
    • Latif, R.1    Graves, P.2
  • 4
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel, P. and Brand, A.H. (2002) Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins. Nat. Cell Biol. 4, E15-20
    • (2002) Nat. Cell Biol. , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 5
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy, A.K. (2001) Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24, 289-296
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 6
    • 0035341596 scopus 로고    scopus 로고
    • Imaging biochemistry inside cells
    • Wouters, F.S. et al. (2001) Imaging biochemistry inside cells. Trends Cell Biol. 11, 203-211
    • (2001) Trends Cell Biol. , vol.11 , pp. 203-211
    • Wouters, F.S.1
  • 7
    • 0034423297 scopus 로고    scopus 로고
    • Observing proteins in their natural habitat: The living cell
    • Bastiaens, P.I. and Pepperkok, R. (2000) Observing proteins in their natural habitat: the living cell. Trends Biochem. Sci. 25, 631-637
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 631-637
    • Bastiaens, P.I.1    Pepperkok, R.2
  • 8
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P.I. and Squire, A. (1999) Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-52
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 9
    • 0033082623 scopus 로고    scopus 로고
    • Photobleaching GFP reveals protein dynamics inside live cells
    • White, J. and Stelzer, E. (1999) Photobleaching GFP reveals protein dynamics inside live cells. Trends Cell Biol. 9, 61-65
    • (1999) Trends Cell Biol. , vol.9 , pp. 61-65
    • White, J.1    Stelzer, E.2
  • 10
    • 0035374872 scopus 로고    scopus 로고
    • Studying protein dynamics in living cells
    • Lippincott-Schwartz, J. et al. (2001) Studying protein dynamics in living cells. Nat. Rev. Mol. Cell Biol. 2, 444-456
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 444-456
    • Lippincott-Schwartz, J.1
  • 11
    • 0035122528 scopus 로고    scopus 로고
    • Imaging FRET between spectrally similar GFP molecules in single cells
    • Harpur, A.G. et al. (2001) Imaging FRET between spectrally similar GFP molecules in single cells. Nat. Biotechnol. 19, 167-169
    • (2001) Nat. Biotechnol. , vol.19 , pp. 167-169
    • Harpur, A.G.1
  • 12
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y. et al. (1999) A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. U. S. A. 96, 151-156
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 151-156
    • Xu, Y.1
  • 13
    • 0035424506 scopus 로고    scopus 로고
    • Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin
    • Waud, J.P. et al. (2001) Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin. Biochem. J. 357, 687-697
    • (2001) Biochem. J. , vol.357 , pp. 687-697
    • Waud, J.P.1
  • 14
    • 0035430589 scopus 로고    scopus 로고
    • Epidermal growth factor receptor, c-erbB2 and c-erbB3 receptor interaction, and related cell cycle kinetics of SK-BR-3 and BT474 breast carcinoma cells
    • Brockhoff, G. et al. (2001) Epidermal growth factor receptor, c-erbB2 and c-erbB3 receptor interaction, and related cell cycle kinetics of SK-BR-3 and BT474 breast carcinoma cells. Cytometry 44, 338-348
    • (2001) Cytometry , vol.44 , pp. 338-348
    • Brockhoff, G.1
  • 15
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P.J. et al. (2000) Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290, 1567-1570
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1
  • 16
    • 0032101894 scopus 로고    scopus 로고
    • EGF-induced redistribution of erbB2 on breast tumor cells: Flow and image cytometric energy transfer measurements
    • Nagy, P. et al. (1998) EGF-induced redistribution of erbB2 on breast tumor cells: flow and image cytometric energy transfer measurements. Cytometry 32, 120-131
    • (1998) Cytometry , vol.32 , pp. 120-131
    • Nagy, P.1
  • 17
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, T.W., Jr and Jovin, T.M. (1995) Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 129, 1543-1558
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella T.W., Jr.1    Jovin, T.M.2
  • 18
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G-protein-coupled receptor ontogeny and function
    • Angers, S. et al. (2002) Dimerization: an emerging concept for G-protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42, 409-435
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1
  • 19
    • 0034937698 scopus 로고    scopus 로고
    • G protein coupled receptor dimerization: Implications in modulating receptor function
    • Gomes, I. et al. (2001) G protein coupled receptor dimerization: implications in modulating receptor function. J. Mol. Med. 79, 226-242
    • (2001) J. Mol. Med. , vol.79 , pp. 226-242
    • Gomes, I.1
  • 20
    • 0035910464 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptor microaggregation. Rate monitored by fluorescent resonance energy transfer
    • Cornea, A. et al. (2001) Gonadotropin-releasing hormone receptor microaggregation. Rate monitored by fluorescent resonance energy transfer. J. Biol. Chem. 276, 2153-2158
    • (2001) J. Biol. Chem. , vol.276 , pp. 2153-2158
    • Cornea, A.1
  • 21
    • 0035002343 scopus 로고    scopus 로고
    • Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors
    • Horvat, R.D. et al. (2001) Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors. Mol. Endocrinol. 15, 695-703
    • (2001) Mol. Endocrinol. , vol.15 , pp. 695-703
    • Horvat, R.D.1
  • 22
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger, K.M. et al. (2001) Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276, 12736-12743
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1
  • 23
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • McVey, M. et al. (2001) Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human δ-opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy. J. Biol. Chem. 276, 14092-14099
    • (2001) J. Biol. Chem. , vol.276 , pp. 14092-14099
    • McVey, M.1
  • 24
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson, S.S. (2001) Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 53, 1-24
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 25
    • 0036473397 scopus 로고    scopus 로고
    • The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell, L.M. and Lefkowitz, R.J. (2002) The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals. J. Cell Sci. 115, 455-465
    • (2002) J. Cell Sci. , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 26
    • 0035860777 scopus 로고    scopus 로고
    • Characterization of sequence determinants within the carboxyl-terminal domain of chemokine receptor CCR5 that regulate signaling and receptor internalization
    • Kraft, K. et al. (2001) Characterization of sequence determinants within the carboxyl-terminal domain of chemokine receptor CCR5 that regulate signaling and receptor internalization. J. Biol. Chem. 276, 34408-34418
    • (2001) J. Biol. Chem. , vol.276 , pp. 34408-34418
    • Kraft, K.1
  • 27
    • 0033568672 scopus 로고    scopus 로고
    • Characterization of RANTES- and aminooxypentane-RANTES-triggered desensitization signals reveals differences in recruitment of the G protein-coupled receptor complex
    • Vila-Coro, A.J. et al. (1999) Characterization of RANTES- and aminooxypentane-RANTES-triggered desensitization signals reveals differences in recruitment of the G protein-coupled receptor complex. J. Immunol. 163, 3037-3044
    • (1999) J. Immunol. , vol.163 , pp. 3037-3044
    • Vila-Coro, A.J.1
  • 28
    • 0034724192 scopus 로고    scopus 로고
    • Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S. et al. (2000) Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. U. S. A. 97, 3684-3689
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3684-3689
    • Angers, S.1
  • 29
    • 0031757743 scopus 로고    scopus 로고
    • Agonist-induced endocytosis and recycling of the gonadotropin-releasing hormone receptor: Effect of β-arrestin on internalization kinetics
    • Vrecl, M. et al. (1998) Agonist-induced endocytosis and recycling of the gonadotropin-releasing hormone receptor: effect of β-arrestin on internalization kinetics. Mol. Endocrinol. 12, 1818-1829
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1818-1829
    • Vrecl, M.1
  • 30
    • 0034463035 scopus 로고    scopus 로고
    • The rat gonadotropin-releasing hormone receptor internalizes via a β-arrestin-independent, but dynamin-dependent, pathway: Addition of a carboxyl-terminal tail confers β-arrestin dependency
    • Heding, A. et al. (2000) The rat gonadotropin-releasing hormone receptor internalizes via a β-arrestin-independent, but dynamin-dependent, pathway: addition of a carboxyl-terminal tail confers β-arrestin dependency. Endocrinology 141, 299-306
    • (2000) Endocrinology , vol.141 , pp. 299-306
    • Heding, A.1
  • 31
    • 0035900018 scopus 로고    scopus 로고
    • Mapping the antagonist binding site of the serotonin type 3 receptor by fluorescence resonance energy transfer
    • Vallotton, P. et al. (2001) Mapping the antagonist binding site of the serotonin type 3 receptor by fluorescence resonance energy transfer. Biochemistry 40, 12237-12242
    • (2001) Biochemistry , vol.40 , pp. 12237-12242
    • Vallotton, P.1
  • 32
    • 0029838186 scopus 로고    scopus 로고
    • Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites
    • Turcatti, G. et al. (1996) Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites. J. Biol. Chem. 271, 19991-19998
    • (1996) J. Biol. Chem. , vol.271 , pp. 19991-19998
    • Turcatti, G.1
  • 33
    • 0032851857 scopus 로고    scopus 로고
    • A homogenous 384-well high throughput screen for novel tumor necrosis factor receptor: Ligand interactions using time resolved energy transfer
    • Moore, K.J. et al. (1999) A homogenous 384-well high throughput screen for novel tumor necrosis factor receptor: ligand interactions using time resolved energy transfer. J. Biomol. Screen. 4, 205-214
    • (1999) J. Biomol. Screen. , vol.4 , pp. 205-214
    • Moore, K.J.1
  • 34
    • 0034083428 scopus 로고    scopus 로고
    • Recent advances in technology for measuring and manipulating cell signals
    • Zacharias, D.A. et al. (2000) Recent advances in technology for measuring and manipulating cell signals. Curr. Opin. Neurobiol. 10, 416-421
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 416-421
    • Zacharias, D.A.1
  • 35
    • 0035253388 scopus 로고    scopus 로고
    • Demonstration of a homogeneous noncompetitive immunoassay based on bioluminescence resonance energy transfer
    • Arai, R. et al. (2001) Demonstration of a homogeneous noncompetitive immunoassay based on bioluminescence resonance energy transfer. Anal. Biochem. 289, 77-81
    • (2001) Anal. Biochem. , vol.289 , pp. 77-81
    • Arai, R.1
  • 36
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and hetero-oligomeric interactions between G protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer
    • Ramsay, D. et al. (2002) Homo- and hetero-oligomeric interactions between G protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer. Biochem. J. 365, 429-440
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1
  • 37
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B.A. et al. (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1
  • 38
    • 0032104550 scopus 로고    scopus 로고
    • Isolation of putative plant transcriptional coactivators using a modified two-hybrid system incorporating a GFP reporter gene
    • Cormack, R.S. et al. (1998) Isolation of putative plant transcriptional coactivators using a modified two-hybrid system incorporating a GFP reporter gene. Plant J. 14, 685-692
    • (1998) Plant J. , vol.14 , pp. 685-692
    • Cormack, R.S.1
  • 39
    • 0034624876 scopus 로고    scopus 로고
    • A green fluorescent protein-reporter mammalian two-hybrid system with extrachromosomal maintenance of a prey expression plasmid: Application to interaction screening
    • Shioda, T. et al. (2000) A green fluorescent protein-reporter mammalian two-hybrid system with extrachromosomal maintenance of a prey expression plasmid: application to interaction screening. Proc. Natl. Acad. Sci. U. S. A. 97, 5220-5224
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5220-5224
    • Shioda, T.1
  • 40
    • 0035866184 scopus 로고    scopus 로고
    • A novel approach for the identification of protein-protein interaction with integral membrane proteins
    • Hubsman, M. et al. (2001) A novel approach for the identification of protein-protein interaction with integral membrane proteins. Nucleic Acids Res. 29, E18
    • (2001) Nucleic Acids Res. , vol.29
    • Hubsman, M.1
  • 41
    • 0035223482 scopus 로고    scopus 로고
    • Membrane recruitment systems for analysis of protein-protein interactions
    • Aronheim, A. (2001) Membrane recruitment systems for analysis of protein-protein interactions. Methods Mol. Biol. 177, 319-328
    • (2001) Methods Mol. Biol. , vol.177 , pp. 319-328
    • Aronheim, A.1
  • 42
    • 0035489334 scopus 로고    scopus 로고
    • Proteomics: An holistic analysis of nature's proteins
    • Hebestreit, H.F. et al. (2001) Proteomics: an holistic analysis of nature's proteins. Curr. Opin. Pharmacol. 1, 513-520
    • (2001) Curr. Opin. Pharmacol. , vol.1 , pp. 513-520
    • Hebestreit, H.F.1
  • 43
    • 0032784646 scopus 로고    scopus 로고
    • Proteomics: Quantitative and physical mapping of cellular proteins
    • Blackstock, W.P. and Weir, M.P. (1999) Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol. 17, 121-127
    • (1999) Trends Biotechnol. , vol.17 , pp. 121-127
    • Blackstock, W.P.1    Weir, M.P.2
  • 44
    • 0035279936 scopus 로고    scopus 로고
    • Towards an understanding of complex protein networks
    • Tucker, C.L. et al. (2001) Towards an understanding of complex protein networks. Trends Cell Biol. 11, 102-106
    • (2001) Trends Cell Biol. , vol.11 , pp. 102-106
    • Tucker, C.L.1
  • 45
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • Cheng, Z.J. and Miller, L.J. (2001) Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276, 48040-48047
    • (2001) J. Biol. Chem. , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 46
    • 0035913955 scopus 로고    scopus 로고
    • Agonist-independent and -dependent oligomerization of dopamine D(2) receptors by fusion to fluorescent proteins
    • Wurch, T. et al. (2001) Agonist-independent and -dependent oligomerization of dopamine D(2) receptors by fusion to fluorescent proteins. FEBS Lett. 507, 109-113
    • (2001) FEBS Lett. , vol.507 , pp. 109-113
    • Wurch, T.1
  • 47
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton, M.C. and Blumer, K.J. (2000) G-protein-coupled receptors function as oligomers in vivo. Curr. Biol. 10, 341-344
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 48
    • 0035976910 scopus 로고    scopus 로고
    • Oligomerization of the human thyrotropin receptor: Fluorescent protein-tagged hTSHR reveals post-translational complexes
    • Latif, R. et al. (2001) Oligomerization of the human thyrotropin receptor: fluorescent protein-tagged hTSHR reveals post-translational complexes. J. Biol. Chem. 276, 45217-45224
    • (2001) J. Biol. Chem. , vol.276 , pp. 45217-45224
    • Latif, R.1
  • 49
    • 0034801960 scopus 로고    scopus 로고
    • Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer
    • Boute, N. et al. (2001) Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer. Mol. Pharmacol. 60, 640-645
    • (2001) Mol. Pharmacol. , vol.60 , pp. 640-645
    • Boute, N.1
  • 50
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville, M. et al. (2000) Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science 288, 154-157
    • (2000) Science , vol.288 , pp. 154-157
    • Rocheville, M.1
  • 51
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo-and heterodimers
    • Rocheville, M. et al. (2000) Subtypes of the somatostatin receptor assemble as functional homo-and heterodimers. J. Biol. Chem. 275, 7862-7869
    • (2000) J. Biol. Chem. , vol.275 , pp. 7862-7869
    • Rocheville, M.1
  • 52
    • 0035315845 scopus 로고    scopus 로고
    • A CD14-independent LPS receptor cluster
    • Triantafilou, K. et al. (2001) A CD14-independent LPS receptor cluster. Nat. Immunol. 2, 338-345
    • (2001) Nat. Immunol. , vol.2 , pp. 338-345
    • Triantafilou, K.1
  • 53
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin, A. et al. (2000) Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 10, 1395-1398
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1
  • 54
    • 0033621359 scopus 로고    scopus 로고
    • Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors
    • Vollmer, J.Y. et al. (1999) Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors. J. Biol. Chem. 274, 37915-37922
    • (1999) J. Biol. Chem. , vol.274 , pp. 37915-37922
    • Vollmer, J.Y.1
  • 55
    • 17444445451 scopus 로고    scopus 로고
    • Optimal inhibition of X4 HIV isolates by the CXC chemokine stromal cell-derived factor 1α requires interaction with cell surface heparan sulfate proteoglycans
    • Valenzuela-Fernandez, A. et al. (2001) Optimal inhibition of X4 HIV isolates by the CXC chemokine stromal cell-derived factor 1α requires interaction with cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276, 26550-26558
    • (2001) J. Biol. Chem. , vol.276 , pp. 26550-26558
    • Valenzuela-Fernandez, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.