메뉴 건너뛰기




Volumn 175, Issue 2, 2011, Pages 106-112

Investigating a macromolecular complex: The toolkit of methods

Author keywords

Macromolecular complexes; Multidisciplinarity; Protein protein interactions

Indexed keywords

CELL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PHOSPHOPEPTIDE; RAS PROTEIN; RNA POLYMERASE; SMALL INTERFERING RNA;

EID: 79959972140     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.05.014     Document Type: Review
Times cited : (19)

References (69)
  • 2
    • 0032718632 scopus 로고    scopus 로고
    • Genetic approaches to the study of protein-protein interactions
    • Appling D.R. Genetic approaches to the study of protein-protein interactions. Methods 1999, 19:338-349.
    • (1999) Methods , vol.19 , pp. 338-349
    • Appling, D.R.1
  • 3
    • 67649841614 scopus 로고    scopus 로고
    • The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions
    • Arkin M.R., Whitty A. The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions. Curr. Opin. Chem. Biol. 2009, 13:284-290.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 284-290
    • Arkin, M.R.1    Whitty, A.2
  • 4
    • 0030923133 scopus 로고    scopus 로고
    • Isolation of an ap-1 repressor by a novel method for detecting protein-protein interactions
    • Aronheim A., Zandi E., Hennemann H., Elledge S.J., Karin M. Isolation of an ap-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell. Biol. 1997, 17:3094-3102.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3094-3102
    • Aronheim, A.1    Zandi, E.2    Hennemann, H.3    Elledge, S.J.4    Karin, M.5
  • 5
    • 41249097444 scopus 로고    scopus 로고
    • Interaction networks for systems biology
    • Bader S., Kuhner S., Gavin A.C. Interaction networks for systems biology. FEBS Lett. 2008, 582:1220-1224.
    • (2008) FEBS Lett. , vol.582 , pp. 1220-1224
    • Bader, S.1    Kuhner, S.2    Gavin, A.C.3
  • 6
    • 78650057290 scopus 로고    scopus 로고
    • Fluorescence perturbation techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, photoactivation, photoconversion, and FLIP. Cold Spring Harb. Protoc. 2010, pdb top90
    • Bancaud, A., Huet, S., Rabut, G., Ellenberg, J., 2010. Fluorescence perturbation techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, photoactivation, photoconversion, and FLIP. Cold Spring Harb. Protoc. 2010, pdb top90
    • (2010)
    • Bancaud, A.1    Huet, S.2    Rabut, G.3    Ellenberg, J.4
  • 7
    • 72449161758 scopus 로고    scopus 로고
    • Visualizing cellular processes at the molecular level by cryo-electron tomography
    • Ben-Harush K., Maimon T., Patla I., Villa E., Medalia O. Visualizing cellular processes at the molecular level by cryo-electron tomography. J. Cell. Sci. 2010, 123:7-12.
    • (2010) J. Cell. Sci. , vol.123 , pp. 7-12
    • Ben-Harush, K.1    Maimon, T.2    Patla, I.3    Villa, E.4    Medalia, O.5
  • 8
    • 0032497564 scopus 로고    scopus 로고
    • The ras recruitment system, a novel approach to the study of protein-protein interactions
    • Broder Y.C., Katz S., Aronheim A. The ras recruitment system, a novel approach to the study of protein-protein interactions. Curr. Biol. 1998, 8:1121-1124.
    • (1998) Curr. Biol. , vol.8 , pp. 1121-1124
    • Broder, Y.C.1    Katz, S.2    Aronheim, A.3
  • 9
    • 40549097122 scopus 로고    scopus 로고
    • Protein-protein interactions identified by pull-down experiments and mass spectrometry
    • Chapter 17, Unit 17.5
    • Brymora A., Valova V.A., Robinson P.J. Protein-protein interactions identified by pull-down experiments and mass spectrometry. Curr. Protoc. Cell Biol. 2004, Chapter 17, Unit 17.5.
    • (2004) Curr. Protoc. Cell Biol.
    • Brymora, A.1    Valova, V.A.2    Robinson, P.J.3
  • 10
    • 79851499733 scopus 로고    scopus 로고
    • HomoFRET fluorescence anisotropy imaging as a tool to study molecular self-assembly in live cells
    • Chan F.T., Kaminski C.F., Kaminski Schierle G.S. HomoFRET fluorescence anisotropy imaging as a tool to study molecular self-assembly in live cells. Chemphyschem. 2011, 12:500-509.
    • (2011) Chemphyschem. , vol.12 , pp. 500-509
    • Chan, F.T.1    Kaminski, C.F.2    Kaminski Schierle, G.S.3
  • 11
    • 46349091971 scopus 로고    scopus 로고
    • The social network of a cell: recent advances in interactome mapping
    • Charbonnier S., Gallego O., Gavin A.C. The social network of a cell: recent advances in interactome mapping. Biotechnol. Annu. Rev. 2008, 14:1-28.
    • (2008) Biotechnol. Annu. Rev. , vol.14 , pp. 1-28
    • Charbonnier, S.1    Gallego, O.2    Gavin, A.C.3
  • 13
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium
    • Cole J.L., Lary J.W., Moody T., Laue T.M. Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium. Methods Cell Biol. 2008, 84:143-179.
    • (2008) Methods Cell Biol. , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.3    Laue, T.M.4
  • 14
    • 77954834510 scopus 로고    scopus 로고
    • The current state of chromatin immunoprecipitation
    • Collas P. The current state of chromatin immunoprecipitation. Mol. Biotechnol. 2010, 45:87-100.
    • (2010) Mol. Biotechnol. , vol.45 , pp. 87-100
    • Collas, P.1
  • 15
    • 49549092476 scopus 로고    scopus 로고
    • Mapping multiprotein complexes by affinity purification and mass spectrometry
    • Collins M.O., Choudhary J.S. Mapping multiprotein complexes by affinity purification and mass spectrometry. Curr. Opin. Biotechnol. 2008, 19:324-330.
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 324-330
    • Collins, M.O.1    Choudhary, J.S.2
  • 16
    • 59649092360 scopus 로고    scopus 로고
    • Co-immunoprecipitation techniques for assessing RNA-protein interactions in vivo
    • Chapter 15
    • Conrad N.K. Co-immunoprecipitation techniques for assessing RNA-protein interactions in vivo. Methods Enzymol. 2008, 449:317-342. Chapter 15.
    • (2008) Methods Enzymol. , vol.449 , pp. 317-342
    • Conrad, N.K.1
  • 19
    • 0033776891 scopus 로고    scopus 로고
    • Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast
    • Ehrhard K.N., Jacoby J.J., Fu X.Y., Jahn R., Dohlman H.G. Use of G-protein fusions to monitor integral membrane protein-protein interactions in yeast. Nat. Biotechnol. 2000, 18:1075-1079.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1075-1079
    • Ehrhard, K.N.1    Jacoby, J.J.2    Fu, X.Y.3    Jahn, R.4    Dohlman, H.G.5
  • 21
    • 78650894342 scopus 로고    scopus 로고
    • Survey of the year 2009: applications of isothermal titration calorimetry
    • Falconer R.J., Collins B.M. Survey of the year 2009: applications of isothermal titration calorimetry. J. Mol. Recognit. 2011, 24:1-16.
    • (2011) J. Mol. Recognit. , vol.24 , pp. 1-16
    • Falconer, R.J.1    Collins, B.M.2
  • 22
    • 40849126953 scopus 로고    scopus 로고
    • Integrating global gene expression analysis and genetics
    • Farber C.R., Lusis A.J. Integrating global gene expression analysis and genetics. Adv. Genet. 2008, 60:571-601.
    • (2008) Adv. Genet. , vol.60 , pp. 571-601
    • Farber, C.R.1    Lusis, A.J.2
  • 23
    • 77954650144 scopus 로고    scopus 로고
    • Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    • Fischer N., Konevega A.L., Wintermeyer W., Rodnina M.V., Stark H. Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy. Nature 2010, 466:329-333.
    • (2010) Nature , vol.466 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Wintermeyer, W.3    Rodnina, M.V.4    Stark, H.5
  • 24
    • 33846285730 scopus 로고    scopus 로고
    • Solution NMR of large molecules and assemblies
    • Foster M.P., McElroy C.A., Amero C.D. Solution NMR of large molecules and assemblies. Biochemistry 2007, 46:331-340.
    • (2007) Biochemistry , vol.46 , pp. 331-340
    • Foster, M.P.1    McElroy, C.A.2    Amero, C.D.3
  • 25
    • 79959958491 scopus 로고    scopus 로고
    • Biocrystallography: past, present, future
    • Giege R., Sauter C. Biocrystallography: past, present, future. HFSP J. 2010, 4:109-121.
    • (2010) HFSP J. , vol.4 , pp. 109-121
    • Giege, R.1    Sauter, C.2
  • 26
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff N., Harrison S.C. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy. Curr. Opin. Struct. Biol. 2011, 21:265-278.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-278
    • Grigorieff, N.1    Harrison, S.C.2
  • 27
    • 34247492103 scopus 로고    scopus 로고
    • Footprinting: a method for determining the sequence selectivity, affinity and kinetics of DNA-binding ligands
    • Hampshire A.J., Rusling D.A., Broughton-Head V.J., Fox K.R. Footprinting: a method for determining the sequence selectivity, affinity and kinetics of DNA-binding ligands. Methods 2007, 42:128-140.
    • (2007) Methods , vol.42 , pp. 128-140
    • Hampshire, A.J.1    Rusling, D.A.2    Broughton-Head, V.J.3    Fox, K.R.4
  • 28
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: novel variations of an established technique
    • Haustein E., Schwille P. Fluorescence correlation spectroscopy: novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:151-169.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 29
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: super-resolution imaging of cells
    • Huang B., Babcock H., Zhuang X. Breaking the diffraction barrier: super-resolution imaging of cells. Cell 2010, 143:1047-1058.
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 30
    • 36949000237 scopus 로고    scopus 로고
    • Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps
    • Huang H., Jedynak B.M., Bader J.S. Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps. PLoS Comput. Biol. 2007, 3:e214.
    • (2007) PLoS Comput. Biol. , vol.3
    • Huang, H.1    Jedynak, B.M.2    Bader, J.S.3
  • 32
    • 77952538407 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy in diagnostics and imaging
    • Jameson D.M., Ross J.A. Fluorescence polarization/anisotropy in diagnostics and imaging. Chem. Rev. 2010, 110:2685-2708.
    • (2010) Chem. Rev. , vol.110 , pp. 2685-2708
    • Jameson, D.M.1    Ross, J.A.2
  • 33
    • 34250621337 scopus 로고    scopus 로고
    • Chemical genetics: elucidating biological systems with small-molecule compounds
    • Kawasumi M., Nghiem P. Chemical genetics: elucidating biological systems with small-molecule compounds. J. Invest. Dermatol. 2007, 127:1577-1584.
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 1577-1584
    • Kawasumi, M.1    Nghiem, P.2
  • 34
    • 50649096663 scopus 로고    scopus 로고
    • Analyzing protein interaction networks using structural information
    • Kiel C., Beltrao P., Serrano L. Analyzing protein interaction networks using structural information. Annu. Rev. Biochem. 2008, 77:415-441.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 415-441
    • Kiel, C.1    Beltrao, P.2    Serrano, L.3
  • 38
    • 67649208715 scopus 로고    scopus 로고
    • Detection of protein-protein interactions by far-western blotting
    • Machida K., Mayer B.J. Detection of protein-protein interactions by far-western blotting. Methods Mol. Biol. 2009, 536:313-329.
    • (2009) Methods Mol. Biol. , vol.536 , pp. 313-329
    • Machida, K.1    Mayer, B.J.2
  • 39
    • 34548231009 scopus 로고    scopus 로고
    • Co-immunoprecipitations revisited: an update on experimental concepts and their implementation for sensitive interactome investigations of endogenous proteins
    • Markham K., Bai Y., Schmitt-Ulms G. Co-immunoprecipitations revisited: an update on experimental concepts and their implementation for sensitive interactome investigations of endogenous proteins. Anal. Bioanal. Chem. 2007, 389:461-473.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 461-473
    • Markham, K.1    Bai, Y.2    Schmitt-Ulms, G.3
  • 40
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • Mertens H.D., Svergun D.I. Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J. Struct. Biol. 2010, 172:128-141.
    • (2010) J. Struct. Biol. , vol.172 , pp. 128-141
    • Mertens, H.D.1    Svergun, D.I.2
  • 42
    • 3242721602 scopus 로고    scopus 로고
    • Confocal microscopy for intracellular co-localization of proteins
    • Miyashita T. Confocal microscopy for intracellular co-localization of proteins. Methods Mol. Biol. 2004, 261:399-410.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 399-410
    • Miyashita, T.1
  • 43
    • 3242687293 scopus 로고    scopus 로고
    • Using light scattering to determine the stoichiometry of protein complexes
    • Mogridge J. Using light scattering to determine the stoichiometry of protein complexes. Methods Mol. Biol. 2004, 261:113-118.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 113-118
    • Mogridge, J.1
  • 44
    • 77953626646 scopus 로고    scopus 로고
    • Genomic screening with RNAi: results and challenges
    • Mohr S., Bakal C., Perrimon N. Genomic screening with RNAi: results and challenges. Annu. Rev. Biochem. 2010, 79:37-64.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 37-64
    • Mohr, S.1    Bakal, C.2    Perrimon, N.3
  • 46
    • 78650890720 scopus 로고    scopus 로고
    • Synthetic lethality: general principles, utility and detection using genetic screens in human cells
    • Nijman S.M. Synthetic lethality: general principles, utility and detection using genetic screens in human cells. FEBS Lett. 2011, 585:1-6.
    • (2011) FEBS Lett. , vol.585 , pp. 1-6
    • Nijman, S.M.1
  • 47
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren I.M., Thornton J.M. Diversity of protein-protein interactions. EMBO J. 2003, 22:3486-3492.
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 48
    • 77957292751 scopus 로고    scopus 로고
    • Methods for three-dimensional reconstruction of heterogeneous assemblies
    • Orlova E.V., Saibil H.R. Methods for three-dimensional reconstruction of heterogeneous assemblies. Methods Enzymol. 2010, 482:321-341.
    • (2010) Methods Enzymol. , vol.482 , pp. 321-341
    • Orlova, E.V.1    Saibil, H.R.2
  • 49
    • 77957017501 scopus 로고    scopus 로고
    • Phage display: concept, innovations, applications and future
    • Pande J., Szewczyk M.M., Grover A.K. Phage display: concept, innovations, applications and future. Biotechnol. Adv. 2010, 28:849-858.
    • (2010) Biotechnol. Adv. , vol.28 , pp. 849-858
    • Pande, J.1    Szewczyk, M.M.2    Grover, A.K.3
  • 50
    • 62649101310 scopus 로고    scopus 로고
    • Microcalorimetry of proteins and their complexes
    • Privalov P.L. Microcalorimetry of proteins and their complexes. Methods Mol. Biol. 2009, 490:1-39.
    • (2009) Methods Mol. Biol. , vol.490 , pp. 1-39
    • Privalov, P.L.1
  • 51
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber J. The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 2011, 173:530-540.
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 52
    • 73249137770 scopus 로고    scopus 로고
    • Grading the commercial optical biosensor literature-class of 2008: 'the mighty binders'
    • Rich R.L., Myszka D.G. Grading the commercial optical biosensor literature-class of 2008: 'the mighty binders'. J. Mol. Recognit. 2010, 23:1-64.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 1-64
    • Rich, R.L.1    Myszka, D.G.2
  • 54
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • Schiemann O., Prisner T.F. Long-range distance determinations in biomacromolecules by EPR spectroscopy. Q. Rev. Biophys. 2007, 40:1-53.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 55
    • 79551667263 scopus 로고    scopus 로고
    • Single mimivirus particles intercepted and imaged with an X-ray laser
    • Seibert M.M., Ekeberg T., Maia F.R., Svenda M., Andreasson J., et al. Single mimivirus particles intercepted and imaged with an X-ray laser. Nature 2011, 470:78-81.
    • (2011) Nature , vol.470 , pp. 78-81
    • Seibert, M.M.1    Ekeberg, T.2    Maia, F.R.3    Svenda, M.4    Andreasson, J.5
  • 56
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M., Robinson C.V. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 2007, 76:167-193.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 57
    • 53949107378 scopus 로고    scopus 로고
    • Fluorescence complementation: an emerging tool for biological research
    • Shyu Y.J., Hu C.D. Fluorescence complementation: an emerging tool for biological research. Trends Biotechnol. 2008, 26:622-630.
    • (2008) Trends Biotechnol. , vol.26 , pp. 622-630
    • Shyu, Y.J.1    Hu, C.D.2
  • 58
    • 0035800729 scopus 로고    scopus 로고
    • Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis
    • Singh S.K., Rozycki J., Ortega J., Ishikawa T., Lo J., et al. Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J. Biol. Chem. 2001, 276:29420-29429.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29420-29429
    • Singh, S.K.1    Rozycki, J.2    Ortega, J.3    Ishikawa, T.4    Lo, J.5
  • 59
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar I., Korostensky C., Johnsson N., te Heesen S. A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. USA. 1998, 95:5187-5192.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    te Heesen, S.4
  • 60
    • 79951963011 scopus 로고    scopus 로고
    • FRET microscopy in 2010: the legacy of Theodor Forster on the 100th anniversary of his birth
    • Sun Y., Wallrabe H., Seo S.A., Periasamy A. FRET microscopy in 2010: the legacy of Theodor Forster on the 100th anniversary of his birth. Chemphyschem. 2011, 12:462-474.
    • (2011) Chemphyschem. , vol.12 , pp. 462-474
    • Sun, Y.1    Wallrabe, H.2    Seo, S.A.3    Periasamy, A.4
  • 62
    • 79952676403 scopus 로고    scopus 로고
    • Literature curation of protein interactions: measuring agreement across major public databases. Database (Oxford), 2010, baq026
    • Turinsky, A.L., Razick, S., Turner, B., Donaldson, I.M., Wodak, S.J., 2010. Literature curation of protein interactions: measuring agreement across major public databases. Database (Oxford), 2010, baq026.
    • (2010)
    • Turinsky, A.L.1    Razick, S.2    Turner, B.3    Donaldson, I.M.4    Wodak, S.J.5
  • 64
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • Vidal M., Cusick M.E., Barabasi A.L. Interactome networks and human disease. Cell 2011, 144:986-998.
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabasi, A.L.3
  • 65
    • 70449133428 scopus 로고    scopus 로고
    • The transcriptional regulation of protein complexes: a cross-species perspective
    • Webb E.C., Westhead D.R. The transcriptional regulation of protein complexes: a cross-species perspective. Genomics 2009, 94:369-376.
    • (2009) Genomics , vol.94 , pp. 369-376
    • Webb, E.C.1    Westhead, D.R.2
  • 66
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken C.J., Baaske P., Rothbauer U., Braun D., Duhr S. Protein-binding assays in biological liquids using microscale thermophoresis. Nat. Commun. 2010, 1:100.
    • (2010) Nat. Commun. , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 67
    • 55749085411 scopus 로고    scopus 로고
    • Features and applications of blue-native and clear-native electrophoresis
    • Wittig I., Schagger H. Features and applications of blue-native and clear-native electrophoresis. Proteomics 2008, 8:3974-3990.
    • (2008) Proteomics , vol.8 , pp. 3974-3990
    • Wittig, I.1    Schagger, H.2
  • 68
    • 70349156763 scopus 로고    scopus 로고
    • Dissecting protein function and signaling using protein microarrays
    • Wolf-Yadlin A., Sevecka M., MacBeath G. Dissecting protein function and signaling using protein microarrays. Curr. Opin. Chem. Biol. 2009, 13:398-405.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 398-405
    • Wolf-Yadlin, A.1    Sevecka, M.2    MacBeath, G.3
  • 69
    • 67349276056 scopus 로고    scopus 로고
    • A network medicine approach to human disease
    • Zanzoni A., Soler-Lopez M., Aloy P. A network medicine approach to human disease. FEBS Lett. 2009, 583:1759-1765.
    • (2009) FEBS Lett. , vol.583 , pp. 1759-1765
    • Zanzoni, A.1    Soler-Lopez, M.2    Aloy, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.