메뉴 건너뛰기




Volumn 49, Issue 5, 2010, Pages 793-803

An improved bimolecular fluorescence complementation assay with a high signal-to-noise ratio

Author keywords

BiFC; Fluorescent protein; Protein protein interaction; S N ratio; Venus; Visualization

Indexed keywords

SELF ASSEMBLED MONOLAYER;

EID: 78349235354     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/000113519     Document Type: Article
Times cited : (154)

References (32)
  • 1
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R. and R.Y. Tsien. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6:178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 2
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., D.W. Piston, and C.H. Johnson. 1999. A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. USA 96:151-156.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 3
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Applications to the green fluorescent protein
    • Ghosh, I., A.D. Hamilton, and L. Regan. 2000. Antiparallel leucine zipper-directed protein reassembly: applications to the green fluorescent protein. J. Am. Chem. Soc. 122:5658-5659.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 4
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C.-D., Y. Chinenov, and T.K. Kerppola. 2002. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9:789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.-D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 5
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu, Y.J., H. Liu, X. Deng, and C.-D. Hu. 2006. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. BioTechniques 40:61-66.
    • (2006) BioTechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.-D.4
  • 6
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., K. Ibata, E.S. Park, M. Kubota, K. Mikoshiba, and A. Miyawaki. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 7
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C.-D. and T.K. Kerppola. 2003. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 21:539-545.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.-D.1    Kerppola, T.K.2
  • 8
    • 33746435428 scopus 로고    scopus 로고
    • An improved mRFP1 adds red to bimolecular fluorescence complementation
    • Jach, G., M. Pesch, K. Richter, S. Frings, and J.F. Uhrig. 2006. An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat. Methods 3:597-600.
    • (2006) Nat. Methods , vol.3 , pp. 597-600
    • Jach, G.1    Pesch, M.2    Richter, K.3    Frings, S.4    Uhrig, J.F.5
  • 9
    • 38049115791 scopus 로고    scopus 로고
    • Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells
    • Fan, J.-Y., Z.-Q. Cui, H.-P. Wei, Z.-P. Zhang, Y.-F. Zhou, Y.-P. Wang, and X.-E. Zhang. 2008. Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells. Biochem. Biophys. Res. Commun. 367:47-53.
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 47-53
    • Fan, J.-Y.1    Cui, Z.-Q.2    Wei, H.-P.3    Zhang, Z.-P.4    Zhou, Y.-F.5    Wang, Y.-P.6    Zhang, X.-E.7
  • 10
    • 64249110099 scopus 로고    scopus 로고
    • Simultaneous visualization of two protein complexes in a single plant cell using multicolor fluorescence complementation analysis
    • Kodama, Y. and M. Wada. 2009. Simultaneous visualization of two protein complexes in a single plant cell using multicolor fluorescence complementation analysis. Plant Mol. Biol. 70:211-217.
    • (2009) Plant Mol. Biol. , vol.70 , pp. 211-217
    • Kodama, Y.1    Wada, M.2
  • 11
    • 68049137311 scopus 로고    scopus 로고
    • A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions
    • Chu, J., Z. Zhang, Y. Zheng, J. Yang, L. Qin, J. Lu, Z.L. Huang, S. Zeng, and Q. Luo. 2009. A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions. Biosens. Bioelectron. 25:234-239.
    • (2009) Biosens. Bioelectron. , vol.25 , pp. 234-239
    • Chu, J.1    Zhang, Z.2    Zheng, Y.3    Yang, J.4    Qin, L.5    Lu, J.6    Huang, Z.L.7    Zeng, S.8    Luo, Q.9
  • 12
    • 78049348351 scopus 로고    scopus 로고
    • Development of bimolecular fluorescence complementation using dronpa for visualization of protein-protein interactions in cells
    • Lee, Y.R., J.H. Park, S.H. Hahm, L.W. Kang, J.H. Chung, K.H. Nam, K.Y. Hwang, I.C. Kwon, and Y.S. Han. 2010. Development of bimolecular fluorescence complementation using dronpa for visualization of protein-protein interactions in cells. Mol. Imaging Biol. 12:468-478.
    • (2010) Mol. Imaging Biol. , vol.12 , pp. 468-478
    • Lee, Y.R.1    Park, J.H.2    Hahm, S.H.3    Kang, L.W.4    Chung, J.H.5    Nam, K.H.6    Hwang, K.Y.7    Kwon, I.C.8    Han, Y.S.9
  • 13
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular f luorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola, T.K. 2008. Bimolecular f luorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu. Rev. Biophys. 37:465-487.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 14
    • 53949107378 scopus 로고    scopus 로고
    • Fluorescence complementation: An emerging tool for biological research
    • Shyu, Y.J. and C.-D. Hu. 2008. Fluorescence complementation: an emerging tool for biological research. Trends Biotechnol. 26:622-630.
    • (2008) Trends Biotechnol. , vol.26 , pp. 622-630
    • Shyu, Y.J.1    Hu, C.-D.2
  • 15
    • 38349191944 scopus 로고    scopus 로고
    • Visualization of AP-1 NF-kappaB ternary complexes in living cells by using a BiFC-based FRET
    • Shyu, Y.J., C.D. Suarez, and C.-D. Hu. 2008. Visualization of AP-1 NF-kappaB ternary complexes in living cells by using a BiFC-based FRET. Proc. Natl. Acad. Sci. USA 105:151-156.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 151-156
    • Shyu, Y.J.1    Suarez, C.D.2    Hu, C.-D.3
  • 16
    • 54349105689 scopus 로고    scopus 로고
    • Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta
    • Waadt, R., L.K. Schmidt, M. Lohse, K. Hashimoto, R. Bock, and J. Kudla. 2008. Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta. Plant J. 56:505-516.
    • (2008) Plant J. , vol.56 , pp. 505-516
    • Waadt, R.1    Schmidt, L.K.2    Lohse, M.3    Hashimoto, K.4    Bock, R.5    Kudla, J.6
  • 17
    • 38348998668 scopus 로고    scopus 로고
    • Nuclear accumulation of Smad complexes occurs only after the midblastula transition in Xenopus
    • Saka, Y., A.I. Hagemann, O. Piepenburg, and J.C. Smith. 2007. Nuclear accumulation of Smad complexes occurs only after the midblastula transition in Xenopus. Development 134:4209-4218.
    • (2007) Development , vol.134 , pp. 4209-4218
    • Saka, Y.1    Hagemann, A.I.2    Piepenburg, O.3    Smith, J.C.4
  • 18
    • 0029170835 scopus 로고
    • PCR-ligation-PCR (PLP) mutagenesis: A protocol for creating gene fusions and mutations
    • Ali, S.A. and A. Steinkasserer. 1995. PCR-ligation-PCR (PLP) mutagenesis: a protocol for creating gene fusions and mutations. BioTechniques 18:746-750.
    • (1995) BioTechniques , vol.18 , pp. 746-750
    • Ali, S.A.1    Steinkasserer, A.2
  • 19
    • 0024590007 scopus 로고
    • Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains
    • Gentz, R., F.J. Rauscher 3rd, C. Abate, and T. Curran. 1989. Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains. Science 243:1695-1699.
    • (1989) Science , vol.243 , pp. 1695-1699
    • Gentz, R.1    Rauscher III, F.J.2    Abate, C.3    Curran, T.4
  • 20
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo, M.A., G.H. Springer, B. Granada, and D.W. Piston. 2004. An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22:445-449.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 21
    • 0037184962 scopus 로고    scopus 로고
    • Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity
    • Rekas, A., J.R. Alattia, T. Nagai, A. Miyawaki, and M. Ikura. 2002. Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity. J. Biol. Chem. 277:50573-50578.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50573-50578
    • Rekas, A.1    Alattia, J.R.2    Nagai, T.3    Miyawaki, A.4    Ikura, M.5
  • 22
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C.N., B.A. Shirley, M. McNutt, and K. Gajiwala. 1996. Forces contributing to the conformational stability of proteins. FASEB J. 10:75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 24
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and R.F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 25
    • 70350738339 scopus 로고    scopus 로고
    • Bimolecular f luorescence complementation analysis of inducible protein interactions: Effects of factors affecting protein folding on fluorescent protein fragment association
    • Robida, A.M. and T.K. Kerppola. 2009. Bimolecular f luorescence complementation analysis of inducible protein interactions: effects of factors affecting protein folding on fluorescent protein fragment association. J. Mol. Biol. 394:391-409.
    • (2009) J. Mol. Biol. , vol.394 , pp. 391-409
    • Robida, A.M.1    Kerppola, T.K.2
  • 26
    • 48049095013 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans
    • Hiatt, S.M., Y.J. Shyu, H.M. Duren, and C.-D. Hu. 2008. Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans. Methods 45:185-191.
    • (2008) Methods , vol.45 , pp. 185-191
    • Hiatt, S.M.1    Shyu, Y.J.2    Duren, H.M.3    Hu, C.-D.4
  • 27
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive proteinprotein interaction assay based on Gaussia luciferase
    • Remy, I. and S.W. Michnick. 2006. A highly sensitive proteinprotein interaction assay based on Gaussia luciferase. Nat. Methods 3:977-979.
    • (2006) Nat. Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 28
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: Scope and mechanism
    • Magliery, T.J., C.G.M. Wilson, W. Pan, D. Mishler, and L. Regan. 2005. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127:146-157.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.M.2    Pan, W.3    Mishler, D.4    Regan, L.5
  • 29
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous, S., T.C. Terwilliger, and G.S. Waldo. 2005. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat. Biotechnol. 23:102-107.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 32
    • 78349284118 scopus 로고    scopus 로고
    • LEC-BiFC: A new method for rapid assay of protein interaction
    • May 14. [Epub ahead of print]
    • Lin, J., N. Wang, Y. Li, Z. Liu, S. Tian, L. Zhao, Y. Zheng, S. Liu, et al. 2010. LEC-BiFC: a new method for rapid assay of protein interaction. Biotech. Histochem. May 14. [Epub ahead of print].
    • (2010) Biotech. Histochem
    • Lin, J.1    Wang, N.2    Li, Y.3    Liu, Z.4    Tian, S.5    Zhao, L.6    Zheng, Y.7    Liu, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.