메뉴 건너뛰기




Volumn 1788, Issue 10, 2009, Pages 2124-2131

Tag-probe labeling methods for live-cell imaging of membrane proteins

Author keywords

Coiled coil; Fluorescence imaging; Membrane protein; Tag probe labeling

Indexed keywords

MEMBRANE PROTEIN; METAL CHELATE;

EID: 70349482161     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.07.017     Document Type: Review
Times cited : (54)

References (62)
  • 1
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee A.G. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666 (2004) 62-87
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 2
    • 56249140425 scopus 로고    scopus 로고
    • Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL
    • Powl A.M., East J.M., and Lee A.G. Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL. Biochemistry 47 (2008) 12175-12184
    • (2008) Biochemistry , vol.47 , pp. 12175-12184
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 3
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers
    • Cristian L., Lear J.D., and DeGrado W.F. Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14772-14777
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    DeGrado, W.F.3
  • 4
    • 0035899991 scopus 로고    scopus 로고
    • Self-association of model transmembrane α-helices is modulated by lipid structure
    • Mall S., Broadbridge R., Sharma R.P., East J.M., and Lee A.G. Self-association of model transmembrane α-helices is modulated by lipid structure. Biochemistry 40 (2001) 12379-12386
    • (2001) Biochemistry , vol.40 , pp. 12379-12386
    • Mall, S.1    Broadbridge, R.2    Sharma, R.P.3    East, J.M.4    Lee, A.G.5
  • 5
    • 33644849067 scopus 로고    scopus 로고
    • Measurement of thermodynamic parameters for hydrophobic mismatch 2: intermembrane transfer of a transmembrane helix
    • Yano Y., Ogura M., and Matsuzaki K. Measurement of thermodynamic parameters for hydrophobic mismatch 2: intermembrane transfer of a transmembrane helix. Biochemistry 45 (2006) 3379-3385
    • (2006) Biochemistry , vol.45 , pp. 3379-3385
    • Yano, Y.1    Ogura, M.2    Matsuzaki, K.3
  • 6
    • 1642570286 scopus 로고    scopus 로고
    • Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol
    • Mitra K., Ubarretxena-Belandia I., Taguchi T., Warren G., and Engelman D.M. Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 4083-4088
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4083-4088
    • Mitra, K.1    Ubarretxena-Belandia, I.2    Taguchi, T.3    Warren, G.4    Engelman, D.M.5
  • 9
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans B.N., Adams S.R., Ellisman M.H., and Tsien R.Y. The fluorescent toolbox for assessing protein location and function. Science 312 (2006) 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 10
    • 27944475132 scopus 로고    scopus 로고
    • Fluorescent proteins as a toolkit for in vivo imaging
    • Chudakov D.M., Lukyanov S., and Lukyanov K.A. Fluorescent proteins as a toolkit for in vivo imaging. Trends Biotechnol. 23 (2005) 605-613
    • (2005) Trends Biotechnol. , vol.23 , pp. 605-613
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 12
    • 0038730827 scopus 로고    scopus 로고
    • Overexpression and mislocalization of a tail-anchored GFP redefines the identity of peroxisomal ER
    • Lisenbee C.S., Karnik S.K., and Trelease R.N. Overexpression and mislocalization of a tail-anchored GFP redefines the identity of peroxisomal ER. Traffic 4 (2003) 491-501
    • (2003) Traffic , vol.4 , pp. 491-501
    • Lisenbee, C.S.1    Karnik, S.K.2    Trelease, R.N.3
  • 13
    • 13844276672 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with small molecules in live cells
    • Chen I., and Ting A.Y. Site-specific labeling of proteins with small molecules in live cells. Curr. Opin. Biotechnol. 16 (2005) 35-40
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 35-40
    • Chen, I.1    Ting, A.Y.2
  • 14
    • 49049095153 scopus 로고    scopus 로고
    • Selective labeling of proteins with chemical probes in living cells
    • Lin M.Z., and Wang L. Selective labeling of proteins with chemical probes in living cells. Physiology (Bethesda) 23 (2008) 131-141
    • (2008) Physiology (Bethesda) , vol.23 , pp. 131-141
    • Lin, M.Z.1    Wang, L.2
  • 15
    • 33746431492 scopus 로고    scopus 로고
    • Chemical labeling strategies for cell biology
    • Marks K.M., and Nolan G.P. Chemical labeling strategies for cell biology. Nat. Methods 3 (2006) 591-596
    • (2006) Nat. Methods , vol.3 , pp. 591-596
    • Marks, K.M.1    Nolan, G.P.2
  • 16
    • 13444261101 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins in living cells
    • Miller L.W., and Cornish V.W. Selective chemical labeling of proteins in living cells. Curr. Opin. Chem. Biol. 9 (2005) 56-61
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 56-61
    • Miller, L.W.1    Cornish, V.W.2
  • 17
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez M., and Ting A.Y. Fluorescent probes for super-resolution imaging in living cells. Nat. Rev. Mol. Cell Biol. 9 (2008) 929-943
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 18
    • 40849089438 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins with small fluorescent molecules based on metal-chelation methodology
    • Soh N. Selective chemical labeling of proteins with small fluorescent molecules based on metal-chelation methodology. Sensors 8 (2008) 1004-1024
    • (2008) Sensors , vol.8 , pp. 1004-1024
    • Soh, N.1
  • 20
    • 18744406025 scopus 로고    scopus 로고
    • In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag
    • Miller L.W., Cai Y., Sheetz M.P., and Cornish V.W. In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag. Nat. Methods 2 (2005) 255-257
    • (2005) Nat. Methods , vol.2 , pp. 255-257
    • Miller, L.W.1    Cai, Y.2    Sheetz, M.P.3    Cornish, V.W.4
  • 21
    • 3042793777 scopus 로고    scopus 로고
    • A general approach for chemical labeling and rapid, spatially controlled protein inactivation
    • Marks K.M., Braun P.D., and Nolan G.P. A general approach for chemical labeling and rapid, spatially controlled protein inactivation. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9982-9987
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9982-9987
    • Marks, K.M.1    Braun, P.D.2    Nolan, G.P.3
  • 22
  • 23
    • 27744503306 scopus 로고    scopus 로고
    • Peptide tags for labeling membrane proteins in live cells with multiple fluorophores
    • McCann C.M., Bareyre F.M., Lichtman J.W., and Sanes J.R. Peptide tags for labeling membrane proteins in live cells with multiple fluorophores. Biotechniques 38 (2005) 945-952
    • (2005) Biotechniques , vol.38 , pp. 945-952
    • McCann, C.M.1    Bareyre, F.M.2    Lichtman, J.W.3    Sanes, J.R.4
  • 24
    • 10344223003 scopus 로고    scopus 로고
    • Imaging of receptor trafficking by using α-bungarotoxin-binding-site-tagged receptors
    • Sekine-Aizawa Y., and Huganir R.L. Imaging of receptor trafficking by using α-bungarotoxin-binding-site-tagged receptors. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 17114-17119
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17114-17119
    • Sekine-Aizawa, Y.1    Huganir, R.L.2
  • 26
    • 50949086302 scopus 로고    scopus 로고
    • HaloTag protein-mediated specific labeling of living cells with quantum dots
    • So M.K., Yao H., and Rao J. HaloTag protein-mediated specific labeling of living cells with quantum dots. Biochem. Biophys. Res. Commun. 374 (2008) 419-423
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 419-423
    • So, M.K.1    Yao, H.2    Rao, J.3
  • 27
    • 58849120569 scopus 로고    scopus 로고
    • In vivo labeling method using a genetic construct for nanoscale resolution microscopy
    • Schroder J., Benink H., Dyba M., and Los G.V. In vivo labeling method using a genetic construct for nanoscale resolution microscopy. Biophys. J. 96 (2009) L1-3
    • (2009) Biophys. J. , vol.96
    • Schroder, J.1    Benink, H.2    Dyba, M.3    Los, G.V.4
  • 28
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A., Gendreizig S., Gronemeyer T., Pick H., Vogel H., and Johnsson K. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21 (2003) 86-89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 31
    • 0037020082 scopus 로고    scopus 로고
    • Designing heterodimeric two-stranded α-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity
    • Litowski J.R., and Hodges R.S. Designing heterodimeric two-stranded α-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity. J. Biol. Chem. 277 (2002) 37272-37279
    • (2002) J. Biol. Chem. , vol.277 , pp. 37272-37279
    • Litowski, J.R.1    Hodges, R.S.2
  • 33
    • 3042826388 scopus 로고    scopus 로고
    • In vivo targeting of organic calcium sensors via genetically selected peptides
    • Marks K.M., Rosinov M., and Nolan G.P. In vivo targeting of organic calcium sensors via genetically selected peptides. Chem. Biol. 11 (2004) 347-356
    • (2004) Chem. Biol. , vol.11 , pp. 347-356
    • Marks, K.M.1    Rosinov, M.2    Nolan, G.P.3
  • 34
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., and Tsien R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281 (1998) 269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 35
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin B.R., Giepmans B.N., Adams S.R., and Tsien R.Y. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23 (2005) 1308-1314
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.2    Adams, S.R.3    Tsien, R.Y.4
  • 36
    • 67949104893 scopus 로고    scopus 로고
    • Hairpin structure of a biarsenical-tetracysteine motif determined by NMR spectroscopy
    • Madani F., Lind J., Damberg P., Adams S.R., Tsien R.Y., and Graslund A.O. Hairpin structure of a biarsenical-tetracysteine motif determined by NMR spectroscopy. J. Am. Chem. Soc. 131 (2009) 4613-4615
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4613-4615
    • Madani, F.1    Lind, J.2    Damberg, P.3    Adams, S.R.4    Tsien, R.Y.5    Graslund, A.O.6
  • 37
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., Adams S.R., Jones J., and Tsien R.Y. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol. 327 (2000) 565-578
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 38
    • 51649104138 scopus 로고    scopus 로고
    • 2 for fluorescent labeling of tetracysteine-tagged proteins
    • 2 for fluorescent labeling of tetracysteine-tagged proteins. Nat. Protoc. 3 (2008) 1527-1534
    • (2008) Nat. Protoc. , vol.3 , pp. 1527-1534
    • Adams, S.R.1    Tsien, R.Y.2
  • 41
    • 33747613117 scopus 로고    scopus 로고
    • Oligo-Asp tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins
    • Ojida A., Honda K., Shinmi D., Kiyonaka S., Mori Y., and Hamachi I. Oligo-Asp tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins. J. Am. Chem. Soc. 128 (2006) 10452-10459
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10452-10459
    • Ojida, A.1    Honda, K.2    Shinmi, D.3    Kiyonaka, S.4    Mori, Y.5    Hamachi, I.6
  • 42
    • 37549061836 scopus 로고    scopus 로고
    • Non-enzymatic covalent protein labeling using a reactive tag
    • Nonaka H., Tsukiji S., Ojida A., and Hamachi I. Non-enzymatic covalent protein labeling using a reactive tag. J. Am. Chem. Soc. 129 (2007) 15777-15779
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15777-15779
    • Nonaka, H.1    Tsukiji, S.2    Ojida, A.3    Hamachi, I.4
  • 43
    • 1842582037 scopus 로고    scopus 로고
    • Reversible site-selective labeling of membrane proteins in live cells
    • Guignet E.G., Hovius R., and Vogel H. Reversible site-selective labeling of membrane proteins in live cells. Nat. Biotechnol. 22 (2004) 440-444
    • (2004) Nat. Biotechnol. , vol.22 , pp. 440-444
    • Guignet, E.G.1    Hovius, R.2    Vogel, H.3
  • 44
    • 33644516580 scopus 로고    scopus 로고
    • Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation
    • Lata S., Gavutis M., Tampe R., and Piehler J. Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation. J. Am. Chem. Soc. 128 (2006) 2365-2372
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2365-2372
    • Lata, S.1    Gavutis, M.2    Tampe, R.3    Piehler, J.4
  • 46
    • 31544453367 scopus 로고    scopus 로고
    • Selective labeling of extracellular proteins containing polyhistidine sequences by a fluorescein-nitrilotriacetic acid conjugate
    • Goldsmith C.R., Jaworski J., Sheng M., and Lippard S.J. Selective labeling of extracellular proteins containing polyhistidine sequences by a fluorescein-nitrilotriacetic acid conjugate. J. Am. Chem. Soc. 128 (2006) 418-419
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 418-419
    • Goldsmith, C.R.1    Jaworski, J.2    Sheng, M.3    Lippard, S.J.4
  • 47
    • 38949195955 scopus 로고    scopus 로고
    • Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic, and chromium
    • Salnikow K., and Zhitkovich A. Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic, and chromium. Chem. Res. Toxicol. 21 (2008) 28-44
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 28-44
    • Salnikow, K.1    Zhitkovich, A.2
  • 48
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • George N., Pick H., Vogel H., Johnsson N., and Johnsson K. Specific labeling of cell surface proteins with chemically diverse compounds. J. Am. Chem. Soc. 126 (2004) 8896-8897
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8896-8897
    • George, N.1    Pick, H.2    Vogel, H.3    Johnsson, N.4    Johnsson, K.5
  • 49
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • Yin J., Liu F., Li X., and Walsh C.T. Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc. 126 (2004) 7754-7755
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.3    Walsh, C.T.4
  • 50
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer B.H., Segura J.M., Martinez K.L., Hovius R., George N., Johnsson K., and Vogel H. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2138-2143
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.M.2    Martinez, K.L.3    Hovius, R.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 51
    • 33749243938 scopus 로고    scopus 로고
    • Visualizing odorant receptor trafficking in living cells down to the single-molecule level
    • Jacquier V., Prummer M., Segura J.M., Pick H., and Vogel H. Visualizing odorant receptor trafficking in living cells down to the single-molecule level. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 14325-14330
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14325-14330
    • Jacquier, V.1    Prummer, M.2    Segura, J.M.3    Pick, H.4    Vogel, H.5
  • 52
    • 34347368946 scopus 로고    scopus 로고
    • Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases
    • Zhou Z., Cironi P., Lin A.J., Xu Y., Hrvatin S., Golan D.E., Silver P.A., Walsh C.T., and Yin J. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. ACS Chem. Biol. 2 (2007) 337-346
    • (2007) ACS Chem. Biol. , vol.2 , pp. 337-346
    • Zhou, Z.1    Cironi, P.2    Lin, A.J.3    Xu, Y.4    Hrvatin, S.5    Golan, D.E.6    Silver, P.A.7    Walsh, C.T.8    Yin, J.9
  • 53
    • 18744401100 scopus 로고    scopus 로고
    • Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
    • Chen I., Howarth M., Lin W., and Ting A.Y. Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods 2 (2005) 99-104
    • (2005) Nat. Methods , vol.2 , pp. 99-104
    • Chen, I.1    Howarth, M.2    Lin, W.3    Ting, A.Y.4
  • 56
    • 43149123357 scopus 로고    scopus 로고
    • Site-specific protein modification on living cells catalyzed by sortase
    • Tanaka T., Yamamoto T., Tsukiji S., and Nagamune T. Site-specific protein modification on living cells catalyzed by sortase. Chembiochem 9 (2008) 802-807
    • (2008) Chembiochem , vol.9 , pp. 802-807
    • Tanaka, T.1    Yamamoto, T.2    Tsukiji, S.3    Nagamune, T.4
  • 57
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells
    • Lin C.W., and Ting A.Y. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J. Am. Chem. Soc. 128 (2006) 4542-4543
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4542-4543
    • Lin, C.W.1    Ting, A.Y.2
  • 58
    • 62849090710 scopus 로고    scopus 로고
    • Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid
    • Halo T.L., Appelbaum J., Hobert E.M., Balkin D.M., and Schepartz A. Selective recognition of protein tetraserine motifs with a cell-permeable, pro-fluorescent bis-boronic acid. J. Am. Chem. Soc. 131 (2009) 438-439
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 438-439
    • Halo, T.L.1    Appelbaum, J.2    Hobert, E.M.3    Balkin, D.M.4    Schepartz, A.5
  • 59
    • 33744941073 scopus 로고    scopus 로고
    • Lanthanide-binding tags as luminescent probes for studying protein interactions
    • Sculimbrene B.R., and Imperiali B. Lanthanide-binding tags as luminescent probes for studying protein interactions. J. Am. Chem. Soc. 128 (2006) 7346-7352
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7346-7352
    • Sculimbrene, B.R.1    Imperiali, B.2
  • 60
    • 36048946776 scopus 로고    scopus 로고
    • In vivo measurement of intramolecular distances using genetically encoded reporters
    • Sandtner W., Bezanilla F., and Correa A.M. In vivo measurement of intramolecular distances using genetically encoded reporters. Biophys. J. 93 (2007) L45-47
    • (2007) Biophys. J. , vol.93
    • Sandtner, W.1    Bezanilla, F.2    Correa, A.M.3
  • 62
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: an enabling technology for the biophysical analysis of proteins
    • Muralidharan V., and Muir T.W. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat. Methods 3 (2006) 429-438
    • (2006) Nat. Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.