메뉴 건너뛰기




Volumn 18, Issue 6, 2009, Pages 1221-1229

Green fluorescence induced by EF-hand assembly in a split GFP system

Author keywords

Calcium dependence; EF hand; Fragment complementation; Protein reconstitution; Protein stability; Split GFP

Indexed keywords

GREEN FLUORESCENT PROTEIN; LEUCINE ZIPPER PROTEIN;

EID: 66349114038     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.131     Document Type: Article
Times cited : (14)

References (27)
  • 1
    • 34249657467 scopus 로고    scopus 로고
    • Stable Intermediate States and High Energy Barriers in the Unfolding of GFP
    • DOI 10.1016/j.jmb.2007.04.039, PII S0022283607005165
    • Huang JR, Craggs TD, Christodoulou J, Jackson SE (2007) Stable intermediate states and high energy barriers in the unfolding of GFP. J Mol Biol 370: 356-371. (Pubitemid 46829211)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.2 , pp. 356-371
    • Huang, J.-R.1    Craggs, T.D.2    Christodoulou, J.3    Jackson, S.E.4
  • 2
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormö M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ (1996) Crystal structure of the Aequorea victoria green fluorescent protein. Science 273: 1392-1395. (Pubitemid 26296528)
    • (1996) Science , vol.273 , Issue.5280 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 3
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • DOI 10.1146/annurev.biochem.67.1.509
    • Tsien RY (1998) The green fluorescent protein. Ann Rev Biochem 67: 509-544. (Pubitemid 28411137)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 5
    • 0032788447 scopus 로고    scopus 로고
    • Circularly permuted variants of the green fluorescent protein
    • DOI 10.1016/S0014-5793(99)01044-3, PII S0014579399010443
    • Topell S, Hennecke J, Glockshuber R (1999) Circularly permuted variants of the green fluorescent protein. FEBS Lett 457: 283-289. (Pubitemid 29401943)
    • (1999) FEBS Letters , vol.457 , Issue.2 , pp. 283-289
    • Topell, S.1    Hennecke, J.2    Glockshuber, R.3
  • 6
    • 35648930538 scopus 로고    scopus 로고
    • Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency
    • DOI 10.1110/ps.072985007
    • Carey J, Lindman S, Bauer M, Linse S (2007) Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency. Protein Sci 16: 2317-2333. (Pubitemid 350036739)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2317-2333
    • Carey, J.1    Lindman, S.2    Bauer, M.3    Linse, S.4
  • 7
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein [12]
    • DOI 10.1021/ja994421w
    • Ghosh I, Hamilton AD, Regan L (2000) Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J Am Chem Soc 122: 5658-5659. (Pubitemid 30431094)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.23 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 8
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson CG, Magliery TJ, Regan L (2004) Detecting protein-protein interactions with GFP-fragment reassembly. Nat Methods 1: 255-262.
    • (2004) Nat Methods , vol.1 , pp. 255-262
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 10
    • 0032518204 scopus 로고    scopus 로고
    • Green fluorescent protein as a scaffold for intracellular presentation of peptides
    • DOI 10.1093/nar/26.2.623
    • Abedi MR, Caponigro G, Kamb A (1998) Green fluorescent protein as a scaffold for intracellular presentation of peptides. Nucl Acids Res 26: 623-630. (Pubitemid 28295298)
    • (1998) Nucleic Acids Research , vol.26 , Issue.2 , pp. 623-630
    • Abedi, M.R.1    Caponigro, G.2    Kamb, A.3
  • 11
    • 43949104399 scopus 로고    scopus 로고
    • Engineering a split-GFP reassembly screen to examine RING-domain interactions between BARD1 and BRCA1 mutants observed in cancer patients
    • Sarkar M, Magliery TJ (2008) Engineering a split-GFP reassembly screen to examine RING-domain interactions between BARD1 and BRCA1 mutants observed in cancer patients. Mol Biosyst 4: 599-605.
    • (2008) Mol Biosyst , vol.4 , pp. 599-605
    • Sarkar, M.1    Magliery, T.J.2
  • 12
    • 45249092170 scopus 로고    scopus 로고
    • Development and implementation of split- GFP-based bimolecular fluorescence complementation (BiFC) assays in yeast
    • Barnard E, McFerran NV, Trudgett A, Nelson J, Timson DJ (2008) Development and implementation of split- GFP-based bimolecular fluorescence complementation (BiFC) assays in yeast. Biochem Soc Trans 36: 479-482.
    • (2008) Biochem Soc Trans , vol.36 , pp. 479-482
    • Barnard, E.1    McFerran, N.V.2    Trudgett, A.3    Nelson, J.4    Timson, D.J.5
  • 13
    • 41649087742 scopus 로고    scopus 로고
    • Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method
    • Barnard E, McFerran NV, Trudgett A, Nelson J, Timson DJ (2008) Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method. Fungal Genet Biol 45: 597-604.
    • (2008) Fungal Genet Biol , vol.45 , pp. 597-604
    • Barnard, E.1    McFerran, N.V.2    Trudgett, A.3    Nelson, J.4    Timson, D.J.5
  • 14
    • 37249039990 scopus 로고    scopus 로고
    • The analysis of protein-protein interactions in plants by bimolecular fluorescence complementation
    • DOI 10.1104/pp.107.107284
    • Ohad N, Shichrur K, Yalovsky S (2007) The analysis of protein-protein interactions in plants by bimolecular fluorescence complementation. Plant Physiol 145: 1090-1099. (Pubitemid 350276728)
    • (2007) Plant Physiology , vol.145 , Issue.4 , pp. 1090-1099
    • Ohad, N.1    Shichrur, K.2    Yalovsky, S.3
  • 16
    • 26444492138 scopus 로고    scopus 로고
    • Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis
    • DOI 10.1007/s10969-005-5247-5
    • Cabantous S, Pédelacq JD, Mark BL, Naranjo C, Terwilliger TC, Waldo GS (2005) Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from Mycobacterium tuberculosis. J Struct Funct Genomics 6: 113-119. (Pubitemid 41428118)
    • (2005) Journal of Structural and Functional Genomics , vol.6 , Issue.2-3 , pp. 113-119
    • Cabantous, S.1    Pedelacq, J.-D.2    Mark, B.L.3    Naranjo, C.4    Terwilliger, T.C.5    Waldo, G.S.6
  • 17
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • DOI 10.1038/nbt1044
    • Cabantous S, Terwilliger TC, Waldo GS (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol 23: 102-107. (Pubitemid 41724632)
    • (2005) Nature Biotechnology , vol.23 , Issue.1 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 18
    • 33749005086 scopus 로고    scopus 로고
    • In vivo and in vitro protein solubility assays using split GFP
    • Cabantous S, Waldo GS (2006) In vivo and in vitro protein solubility assays using split GFP. Nat Methods 3: 845-854.
    • (2006) Nat Methods , vol.3 , pp. 845-854
    • Cabantous, S.1    Waldo, G.S.2
  • 19
    • 36448995426 scopus 로고    scopus 로고
    • Split GFP complementation assay: A novel approach to quantitatively measure aggregation of tau in situ: Effects of GSK3beta activation and caspase 3 cleavage
    • DOI 10.1111/j.1471-4159.2007.04941.x
    • Chun WJ, Waldo GS, Johnson GVW (2007) Split GFP complementation assay: a novel approach to quantitatively measure aggregation of tau in situ: effects of GSK3 beta activation and caspase 3 cleavage. J Neurochem 103: 2529-2539. (Pubitemid 350173576)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.6 , pp. 2529-2539
    • Chun, W.1    Waldo, G.S.2    Johnson, G.V.W.3
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 21
    • 0026612261 scopus 로고
    • Dissection of calbindin-D(9k) into 2 Ca2+-binding subdomains by a combination of mutagenesis and chemical cleavage
    • Finn BE, Kordel J, Thulin E, Sellers P, Forsen S (1992) Dissection of calbindin-D(9k) into 2 Ca2+-binding subdomains by a combination of mutagenesis and chemical cleavage. FEBS Lett 298: 211-214.
    • (1992) FEBS Lett , vol.298 , pp. 211-214
    • Finn, B.E.1    Kordel, J.2    Thulin, E.3    Sellers, P.4    Forsen, S.5
  • 22
    • 0035814792 scopus 로고    scopus 로고
    • Fragment complementation studies of protein stabilization by hydrophobic core residues
    • DOI 10.1021/bi0014812
    • BerggA°rd T, Julenius K, Ogard A, Drakenberg T, Linse S (2001) Fragment complementation studies of protein stabilization by hydrophobic core residues. Biochemistry 40: 1257-1264. (Pubitemid 32142886)
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1257-1264
    • Berggard, T.1    Julenius, K.2    Ogard, A.3    Drakenberg, T.4    Linse, S.5
  • 23
    • 0035055932 scopus 로고    scopus 로고
    • An extended hydrophobic core induces EF-hand swapping
    • DOI 10.1110/ps.47501
    • HA°kansson M, Fast J, Svensson A, Linse S (2001) An extended hydrophobic core induces EF-hand swapping. Protein Sci 10: 927-933. (Pubitemid 32367483)
    • (2001) Protein Science , vol.10 , Issue.5 , pp. 927-933
    • Hakansson, M.1    Svensson, A.2    Fast, J.3    Linse, S.4
  • 24
    • 21244433239 scopus 로고    scopus 로고
    • Electrostatic contributions to the kinetics and thermodynamics of protein assembly
    • DOI 10.1529/biophysj.104.049189
    • Dell'Orco D, Xue WF, Thulin E, Linse S (2005) Electrostatic contributions to the kinetics and thermodynamics of protein assembly. Biophys J 88: 1991-2002. (Pubitemid 40976209)
    • (2005) Biophysical Journal , vol.88 , Issue.3 , pp. 1991-2002
    • Dell'Orco, D.1    Xue, W.-F.2    Thulin, E.3    Linse, S.4
  • 26
    • 0036365845 scopus 로고    scopus 로고
    • Calcium binding to proteins studied via competition with chromophoric chelators
    • Linse S (2002) Calcium binding to proteins studied via competition with chromophoric chelators. Methods Mol Biol 173: 15-24.
    • (2002) Methods Mol Biol , vol.173 , pp. 15-24
    • Linse, S.1
  • 27
    • 33646091307 scopus 로고    scopus 로고
    • Intra- versus intermolecular interactions in monellin: Contribution of surface charges to protein assembly
    • Xue WF, Szczepankiewicz O, Bauer MC, Thulin E, Linse S (2006) Intra- versus intermolecular interactions in monellin: contribution of surface charges to protein assembly. J Mol Biol 358: 1244-1255.
    • (2006) J Mol Biol , vol.358 , pp. 1244-1255
    • Xue, W.F.1    Szczepankiewicz, O.2    Bauer, M.C.3    Thulin, E.4    Linse, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.