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Volumn 34, Issue 10, 2016, Pages 825-834

Characterizing Protein–Protein Interactions Using Mass Spectrometry: Challenges and Opportunities

Author keywords

crosslinking mass spectrometry; mass spectrometry based proteomics; protein complex stoichiometry; protein protein interactions; ultra sensitive interaction proteomics

Indexed keywords

MASS SPECTROMETRY; MOLECULAR BIOLOGY; PURIFICATION; SPECTROMETRY; STOICHIOMETRY;

EID: 84961226693     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2016.02.014     Document Type: Review
Times cited : (125)

References (86)
  • 1
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • 1 Gavin, A.C., et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440 (2006), 631–636.
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1
  • 2
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • 2 Krogan, N.J., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440 (2006), 637–643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1
  • 3
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: a critical review
    • 3 Bantscheff, M., et al. Quantitative mass spectrometry in proteomics: a critical review. Anal. Bioanal. Chem. 389 (2007), 1017–1031.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 1017-1031
    • Bantscheff, M.1
  • 4
    • 49549121813 scopus 로고    scopus 로고
    • High confidence determination of specific protein–protein interactions using quantitative mass spectrometry
    • 4 Vermeulen, M., et al. High confidence determination of specific protein–protein interactions using quantitative mass spectrometry. Curr. Opin. Biotechnol. 19 (2008), 331–337.
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 331-337
    • Vermeulen, M.1
  • 5
    • 79957575162 scopus 로고    scopus 로고
    • Analysis of the human endogenous coregulator complexome
    • 5 Malovannaya, A., et al. Analysis of the human endogenous coregulator complexome. Cell 145 (2011), 787–799.
    • (2011) Cell , vol.145 , pp. 787-799
    • Malovannaya, A.1
  • 6
    • 84937213168 scopus 로고    scopus 로고
    • The BioPlex network: a systematic exploration of the human interactome
    • 6 Huttlin, E.L., et al. The BioPlex network: a systematic exploration of the human interactome. Cell 162 (2015), 425–440.
    • (2015) Cell , vol.162 , pp. 425-440
    • Huttlin, E.L.1
  • 7
    • 84948067587 scopus 로고    scopus 로고
    • A human interactome in three quantitative dimensions organized by stoichiometries and abundances
    • 7 Hein, M.Y., et al. A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 163 (2015), 712–723.
    • (2015) Cell , vol.163 , pp. 712-723
    • Hein, M.Y.1
  • 8
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • 8 Ho, Y., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 (2002), 180–183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 9
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • 9 Gavin, A.C., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002), 141–147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 10
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • 10 Selbach, M., Mann, M., Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat. Methods 3 (2006), 981–983.
    • (2006) Nat. Methods , vol.3 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 11
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • 11 Sowa, M.E., et al. Defining the human deubiquitinating enzyme interaction landscape. Cell 138 (2009), 389–403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1
  • 12
    • 29244474603 scopus 로고    scopus 로고
    • Fluorescent proteins as proteomic probes
    • 12 Cristea, I.M., et al. Fluorescent proteins as proteomic probes. Mol. Cell. Proteomics 4 (2005), 1933–1941.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1933-1941
    • Cristea, I.M.1
  • 13
    • 77952344256 scopus 로고    scopus 로고
    • Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions
    • 13 Hubner, N.C., et al. Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions. J. Cell Biol. 189 (2010), 739–754.
    • (2010) J. Cell Biol. , vol.189 , pp. 739-754
    • Hubner, N.C.1
  • 14
    • 84875701652 scopus 로고    scopus 로고
    • Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells
    • 14 Stadler, C., et al. Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. Nat. Methods 10 (2013), 315–323.
    • (2013) Nat. Methods , vol.10 , pp. 315-323
    • Stadler, C.1
  • 15
    • 20844434337 scopus 로고    scopus 로고
    • A FlAsH-based FRET approach to determine G protein-coupled receptor activation in living cells
    • 15 Hoffmann, C., et al. A FlAsH-based FRET approach to determine G protein-coupled receptor activation in living cells. Nat. Methods 2 (2005), 171–176.
    • (2005) Nat. Methods , vol.2 , pp. 171-176
    • Hoffmann, C.1
  • 16
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: natural single-domain antibodies
    • 16 Muyldermans, S., Nanobodies: natural single-domain antibodies. Annu. Rev. Biochem. 82 (2013), 775–797.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 17
    • 33750328972 scopus 로고    scopus 로고
    • Targeting and tracing antigens in live cells with fluorescent nanobodies
    • 17 Rothbauer, U., et al. Targeting and tracing antigens in live cells with fluorescent nanobodies. Nat. Methods 3 (2006), 887–889.
    • (2006) Nat. Methods , vol.3 , pp. 887-889
    • Rothbauer, U.1
  • 18
    • 39749193861 scopus 로고    scopus 로고
    • A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
    • 18 Rothbauer, U., et al. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteomics 7 (2008), 282–289.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 282-289
    • Rothbauer, U.1
  • 19
    • 84925883476 scopus 로고    scopus 로고
    • Identifying nuclear protein–protein interactions using GFP affinity purification and SILAC-based quantitative mass spectrometry
    • 19 Baymaz, H.I., et al. Identifying nuclear protein–protein interactions using GFP affinity purification and SILAC-based quantitative mass spectrometry. Methods Mol. Biol. 1188 (2014), 207–226.
    • (2014) Methods Mol. Biol. , vol.1188 , pp. 207-226
    • Baymaz, H.I.1
  • 20
    • 84927174857 scopus 로고    scopus 로고
    • A robust pipeline for rapid production of versatile nanobody repertoires
    • 20 Fridy, P.C., et al. A robust pipeline for rapid production of versatile nanobody repertoires. Nat. Methods 11 (2014), 1253–1260.
    • (2014) Nat. Methods , vol.11 , pp. 1253-1260
    • Fridy, P.C.1
  • 21
    • 84949099771 scopus 로고    scopus 로고
    • A strategy for dissecting the architectures of native macromolecular assemblies
    • 21 Shi, Y., et al. A strategy for dissecting the architectures of native macromolecular assemblies. Nat. Methods 12 (2015), 1135–1138.
    • (2015) Nat. Methods , vol.12 , pp. 1135-1138
    • Shi, Y.1
  • 22
    • 0038611015 scopus 로고    scopus 로고
    • Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice
    • 22 de Boer, E., et al. Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 100 (2003), 7480–7485.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 7480-7485
    • de Boer, E.1
  • 23
    • 33751092246 scopus 로고    scopus 로고
    • A protein interaction network for pluripotency of embryonic stem cells
    • 23 Wang, J., et al. A protein interaction network for pluripotency of embryonic stem cells. Nature 444 (2006), 364–368.
    • (2006) Nature , vol.444 , pp. 364-368
    • Wang, J.1
  • 24
    • 36849072573 scopus 로고    scopus 로고
    • The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA
    • 24 Sharif, J., et al. The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA. Nature 450 (2007), 908–912.
    • (2007) Nature , vol.450 , pp. 908-912
    • Sharif, J.1
  • 25
    • 40749104852 scopus 로고    scopus 로고
    • An extended transcriptional network for pluripotency of embryonic stem cells
    • 25 Kim, J., et al. An extended transcriptional network for pluripotency of embryonic stem cells. Cell 132 (2008), 1049–1061.
    • (2008) Cell , vol.132 , pp. 1049-1061
    • Kim, J.1
  • 26
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • 26 Mito, Y., et al. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 37 (2005), 1090–1097.
    • (2005) Nat. Genet. , vol.37 , pp. 1090-1097
    • Mito, Y.1
  • 27
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
    • 27 Roux, K.J., et al. A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J. Cell Biol. 196 (2012), 801–810.
    • (2012) J. Cell Biol. , vol.196 , pp. 801-810
    • Roux, K.J.1
  • 28
    • 84869458315 scopus 로고    scopus 로고
    • Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy
    • 28 Martell, J.D., et al. Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy. Nat. Biotechnol., 30, 2012, 1143.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1143
    • Martell, J.D.1
  • 29
    • 84874956967 scopus 로고    scopus 로고
    • Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging
    • 29 Rhee, H.W., et al. Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging. Science 339 (2013), 1328–1331.
    • (2013) Science , vol.339 , pp. 1328-1331
    • Rhee, H.W.1
  • 30
    • 84881475940 scopus 로고    scopus 로고
    • The CRAPome: a contaminant repository for affinity purification-mass spectrometry data
    • 30 Mellacheruvu, D., et al. The CRAPome: a contaminant repository for affinity purification-mass spectrometry data. Nat. Methods 10 (2013), 730–736.
    • (2013) Nat. Methods , vol.10 , pp. 730-736
    • Mellacheruvu, D.1
  • 31
    • 31044452870 scopus 로고    scopus 로고
    • Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in multiple small-RNA-mediated pathways
    • 31 Duchaine, T.F., et al. Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in multiple small-RNA-mediated pathways. Cell 124 (2006), 343–354.
    • (2006) Cell , vol.124 , pp. 343-354
    • Duchaine, T.F.1
  • 32
    • 14644444197 scopus 로고    scopus 로고
    • Analyzing protein complexes in Drosophila with tandem affinity purification-mass spectrometry
    • 32 Veraksa, A., et al. Analyzing protein complexes in Drosophila with tandem affinity purification-mass spectrometry. Dev. Dyn. 232 (2005), 827–834.
    • (2005) Dev. Dyn. , vol.232 , pp. 827-834
    • Veraksa, A.1
  • 33
    • 79958007632 scopus 로고    scopus 로고
    • In vivo analysis of proteomes and interactomes using parallel affinity capture (iPAC) coupled to mass spectrometry
    • M110.002386
    • 33 Rees, J.S., et al. In vivo analysis of proteomes and interactomes using parallel affinity capture (iPAC) coupled to mass spectrometry. Mol. Cell. Proteomics, 10, 2011 M110.002386.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Rees, J.S.1
  • 34
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • 34 Angrand, P.O., et al. Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol. Cell. Proteomics 5 (2006), 2211–2227.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1
  • 35
    • 84865677098 scopus 로고    scopus 로고
    • A census of human soluble protein complexes
    • 35 Havugimana, P.C., et al. A census of human soluble protein complexes. Cell 150 (2012), 1068–1081.
    • (2012) Cell , vol.150 , pp. 1068-1081
    • Havugimana, P.C.1
  • 36
    • 84866134921 scopus 로고    scopus 로고
    • A high-throughput approach for measuring temporal changes in the interactome
    • 36 Kristensen, A.R., et al. A high-throughput approach for measuring temporal changes in the interactome. Nat. Methods 9 (2012), 907–909.
    • (2012) Nat. Methods , vol.9 , pp. 907-909
    • Kristensen, A.R.1
  • 37
    • 84942031770 scopus 로고    scopus 로고
    • Panorama of ancient metazoan macromolecular complexes
    • 37 Wan, C., et al. Panorama of ancient metazoan macromolecular complexes. Nature 525 (2015), 339–344.
    • (2015) Nature , vol.525 , pp. 339-344
    • Wan, C.1
  • 38
    • 77956167600 scopus 로고    scopus 로고
    • The protein composition of mitotic chromosomes determined using multiclassifier combinatorial proteomics
    • 38 Ohta, S., et al. The protein composition of mitotic chromosomes determined using multiclassifier combinatorial proteomics. Cell 142 (2010), 810–821.
    • (2010) Cell , vol.142 , pp. 810-821
    • Ohta, S.1
  • 39
    • 84898648341 scopus 로고    scopus 로고
    • Proteomics of a fuzzy organelle: interphase chromatin
    • 39 Kustatscher, G., et al. Proteomics of a fuzzy organelle: interphase chromatin. EMBO J. 33 (2014), 648–664.
    • (2014) EMBO J. , vol.33 , pp. 648-664
    • Kustatscher, G.1
  • 40
    • 84954545040 scopus 로고    scopus 로고
    • A draft map of the mouse pluripotent stem cell spatial proteome
    • 40 Christoforou, A., et al. A draft map of the mouse pluripotent stem cell spatial proteome. Nat. Commun., 7, 2016, 9992.
    • (2016) Nat. Commun. , vol.7 , pp. 9992
    • Christoforou, A.1
  • 41
    • 84907485591 scopus 로고    scopus 로고
    • Tracking cancer drugs in living cells by thermal profiling of the proteome
    • 41 Savitski, M.M., et al. Tracking cancer drugs in living cells by thermal profiling of the proteome. Science, 346, 2014, 1255784.
    • (2014) Science , vol.346 , pp. 1255784
    • Savitski, M.M.1
  • 42
    • 84948953323 scopus 로고    scopus 로고
    • Thermal proteome profiling monitors ligand interactions with cellular membrane proteins
    • 42 Reinhard, F.B., et al. Thermal proteome profiling monitors ligand interactions with cellular membrane proteins. Nat. Methods 12 (2015), 1129–1131.
    • (2015) Nat. Methods , vol.12 , pp. 1129-1131
    • Reinhard, F.B.1
  • 43
    • 84946480594 scopus 로고    scopus 로고
    • Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling
    • 43 Huber, K.V.M., et al. Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling. Nat. Methods 12 (2015), 1055–1057.
    • (2015) Nat. Methods , vol.12 , pp. 1055-1057
    • Huber, K.V.M.1
  • 44
    • 84942513706 scopus 로고    scopus 로고
    • Thermal proteome profiling for unbiased identification of direct and indirect drug targets using multiplexed quantitative mass spectrometry
    • 44 Franken, H., et al. Thermal proteome profiling for unbiased identification of direct and indirect drug targets using multiplexed quantitative mass spectrometry. Nat. Protoc. 10 (2015), 1567–1593.
    • (2015) Nat. Protoc. , vol.10 , pp. 1567-1593
    • Franken, H.1
  • 45
    • 40349092949 scopus 로고    scopus 로고
    • Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics
    • 45 Sardiu, M.E., et al. Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics. Proc. Natl. Acad. Sci. U.S.A. 105 (2008), 1454–1459.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1454-1459
    • Sardiu, M.E.1
  • 46
    • 67049118963 scopus 로고    scopus 로고
    • Evaluation of clustering algorithms for protein complex and protein interaction network assembly
    • 46 Sardiu, M.E., et al. Evaluation of clustering algorithms for protein complex and protein interaction network assembly. J. Proteome Res. 8 (2009), 2944–2952.
    • (2009) J. Proteome Res. , vol.8 , pp. 2944-2952
    • Sardiu, M.E.1
  • 47
    • 84855282772 scopus 로고    scopus 로고
    • Recovering protein–protein and domain–domain interactions from aggregation of IP-MS proteomics of coregulator complexes
    • 47 Mazloom, A.R., et al. Recovering protein–protein and domain–domain interactions from aggregation of IP-MS proteomics of coregulator complexes. PLoS Comput. Biol., 7, 2011, e1002319.
    • (2011) PLoS Comput. Biol. , vol.7 , pp. e1002319
    • Mazloom, A.R.1
  • 48
    • 78650861777 scopus 로고    scopus 로고
    • SAINT: probabilistic scoring of affinity purification-mass spectrometry data
    • 48 Choi, H., et al. SAINT: probabilistic scoring of affinity purification-mass spectrometry data. Nat. Methods 8 (2011), 70–73.
    • (2011) Nat. Methods , vol.8 , pp. 70-73
    • Choi, H.1
  • 49
    • 61449237172 scopus 로고    scopus 로고
    • Quantitative interaction proteomics using mass spectrometry
    • 49 Wepf, A., et al. Quantitative interaction proteomics using mass spectrometry. Nat. Methods 6 (2009), 203–205.
    • (2009) Nat. Methods , vol.6 , pp. 203-205
    • Wepf, A.1
  • 50
    • 84871740411 scopus 로고    scopus 로고
    • Stoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomics
    • 50 Smits, A.H., et al. Stoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomics. Nucleic Acids Res., 41, 2013, e28.
    • (2013) Nucleic Acids Res. , vol.41 , pp. e28
    • Smits, A.H.1
  • 51
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • 51 Schwanhausser, B., et al. Global quantification of mammalian gene expression control. Nature 473 (2011), 337–342.
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhausser, B.1
  • 52
    • 84878199030 scopus 로고    scopus 로고
    • Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes
    • 52 van Nuland, R., et al. Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes. Mol. Cell. Biol. 33 (2013), 2067–2077.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2067-2077
    • van Nuland, R.1
  • 53
    • 65249180173 scopus 로고    scopus 로고
    • An embryonic stem cell chromatin remodeling complex, esBAF, is essential for embryonic stem cell self-renewal and pluripotency
    • 53 Ho, L., et al. An embryonic stem cell chromatin remodeling complex, esBAF, is essential for embryonic stem cell self-renewal and pluripotency. Proc. Natl. Acad. Sci. U.S.A. 106 (2009), 5181–5186.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5181-5186
    • Ho, L.1
  • 54
    • 84876686460 scopus 로고    scopus 로고
    • From neural development to cognition: unexpected roles for chromatin
    • 54 Ronan, J.L., et al. From neural development to cognition: unexpected roles for chromatin. Nat. Rev. Genet. 14 (2013), 347–359.
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 347-359
    • Ronan, J.L.1
  • 55
    • 84888871108 scopus 로고    scopus 로고
    • Mapping differential interactomes by affinity purification coupled with data-independent mass spectrometry acquisition
    • 55 Lambert, J.P., et al. Mapping differential interactomes by affinity purification coupled with data-independent mass spectrometry acquisition. Nat. Methods 10 (2013), 1239–1245.
    • (2013) Nat. Methods , vol.10 , pp. 1239-1245
    • Lambert, J.P.1
  • 56
    • 84929709547 scopus 로고    scopus 로고
    • Quantitative interaction proteomics of neurodegenerative disease proteins
    • 56 Hosp, F., et al. Quantitative interaction proteomics of neurodegenerative disease proteins. Cell Rep. 11 (2015), 1134–1146.
    • (2015) Cell Rep. , vol.11 , pp. 1134-1146
    • Hosp, F.1
  • 57
    • 84892888891 scopus 로고    scopus 로고
    • Cdyl, a new partner of the inactive X chromosome and potential reader of H3K27me3 and H3K9me2
    • 57 Escamilla-Del-Arenal, M., et al. Cdyl, a new partner of the inactive X chromosome and potential reader of H3K27me3 and H3K9me2. Mol. Cell. Biol. 33 (2013), 5005–5020.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 5005-5020
    • Escamilla-Del-Arenal, M.1
  • 58
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics
    • 58 Bennett, E.J., et al. Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 143 (2010), 951–965.
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1
  • 59
    • 77950395166 scopus 로고    scopus 로고
    • Determination of protein stoichiometry within protein complexes using absolute quantification and multiple reaction monitoring
    • 59 Schmidt, C., et al. Determination of protein stoichiometry within protein complexes using absolute quantification and multiple reaction monitoring. Anal. Chem. 82 (2010), 2784–2796.
    • (2010) Anal. Chem. , vol.82 , pp. 2784-2796
    • Schmidt, C.1
  • 60
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • 60 Young, M.M., et al. High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 97 (2000), 5802–5806.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5802-5806
    • Young, M.M.1
  • 61
    • 77955381399 scopus 로고    scopus 로고
    • Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics
    • 61 Leitner, A., et al. Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics. Mol. Cell. Proteomics 9 (2010), 1634–1649.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1634-1649
    • Leitner, A.1
  • 62
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • 62 Rappsilber, J., The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 173 (2011), 530–540.
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 63
    • 84866095385 scopus 로고    scopus 로고
    • Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry
    • 63 Herzog, F., et al. Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337 (2012), 1348–1352.
    • (2012) Science , vol.337 , pp. 1348-1352
    • Herzog, F.1
  • 64
    • 84962576477 scopus 로고    scopus 로고
    • xIP-MS: topological analysis of chromatin-associated protein complexes using single affinity purification
    • 64 Makowski, M.M., et al. xIP-MS: topological analysis of chromatin-associated protein complexes using single affinity purification. Mol. Cell. Proteomics 15 (2016), 854–865.
    • (2016) Mol. Cell. Proteomics , vol.15 , pp. 854-865
    • Makowski, M.M.1
  • 65
    • 84949106630 scopus 로고    scopus 로고
    • Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
    • 65 Liu, F., et al. Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry. Nat. Methods 12 (2015), 1179–1184.
    • (2015) Nat. Methods , vol.12 , pp. 1179-1184
    • Liu, F.1
  • 66
    • 84938917929 scopus 로고    scopus 로고
    • Unveiling contacts within macro-molecular assemblies by solving minimum weight connectivity inference (MWC) problems
    • 66 Agarwal, D., et al. Unveiling contacts within macro-molecular assemblies by solving minimum weight connectivity inference (MWC) problems. Mol. Cell. Proteomics 14 (2015), 2274–2284.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 2274-2284
    • Agarwal, D.1
  • 67
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: a bridge between interactomics and structural biology
    • 67 Heck, A.J., Native mass spectrometry: a bridge between interactomics and structural biology. Nat. Methods 5 (2008), 927–933.
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.1
  • 68
    • 84926488713 scopus 로고    scopus 로고
    • Mass spectrometry of protein complexes: from origins to applications
    • 68 Mehmood, S., et al. Mass spectrometry of protein complexes: from origins to applications. Annu. Rev. Phys. Chem. 66 (2015), 453–474.
    • (2015) Annu. Rev. Phys. Chem. , vol.66 , pp. 453-474
    • Mehmood, S.1
  • 69
    • 84897954111 scopus 로고    scopus 로고
    • A mass spectrometry-based hybrid method for structural modeling of protein complexes
    • 69 Politis, A., et al. A mass spectrometry-based hybrid method for structural modeling of protein complexes. Nat. Methods 11 (2014), 403–406.
    • (2014) Nat. Methods , vol.11 , pp. 403-406
    • Politis, A.1
  • 70
    • 36749045172 scopus 로고    scopus 로고
    • The molecular architecture of the nuclear pore complex
    • 70 Alber, F., et al. The molecular architecture of the nuclear pore complex. Nature 450 (2007), 695–701.
    • (2007) Nature , vol.450 , pp. 695-701
    • Alber, F.1
  • 71
    • 36749088906 scopus 로고    scopus 로고
    • Determining the architectures of macromolecular assemblies
    • 71 Alber, F., et al. Determining the architectures of macromolecular assemblies. Nature 450 (2007), 683–694.
    • (2007) Nature , vol.450 , pp. 683-694
    • Alber, F.1
  • 72
    • 84929687804 scopus 로고    scopus 로고
    • Cryo-EM: a unique tool for the visualization of macromolecular complexity
    • 72 Nogales, E., Scheres, S.H., Cryo-EM: a unique tool for the visualization of macromolecular complexity. Mol. Cell 58 (2015), 677–689.
    • (2015) Mol. Cell , vol.58 , pp. 677-689
    • Nogales, E.1    Scheres, S.H.2
  • 73
    • 84928400353 scopus 로고    scopus 로고
    • Single-particle cryo-EM at crystallographic resolution
    • 73 Cheng, Y., Single-particle cryo-EM at crystallographic resolution. Cell 161 (2015), 450–457.
    • (2015) Cell , vol.161 , pp. 450-457
    • Cheng, Y.1
  • 74
    • 84884225242 scopus 로고    scopus 로고
    • Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1
    • 74 Nguyen, V.Q., et al. Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1. Cell 154 (2013), 1220–1231.
    • (2013) Cell , vol.154 , pp. 1220-1231
    • Nguyen, V.Q.1
  • 75
    • 84884228389 scopus 로고    scopus 로고
    • Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex
    • 75 Tosi, A., et al. Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex. Cell 154 (2013), 1207–1219.
    • (2013) Cell , vol.154 , pp. 1207-1219
    • Tosi, A.1
  • 76
    • 84892797558 scopus 로고    scopus 로고
    • Architecture of the large subunit of the mammalian mitochondrial ribosome
    • 76 Greber, B.J., et al. Architecture of the large subunit of the mammalian mitochondrial ribosome. Nature 505 (2014), 515–519.
    • (2014) Nature , vol.505 , pp. 515-519
    • Greber, B.J.1
  • 77
    • 84911413825 scopus 로고    scopus 로고
    • Characterization of a DNA exit gate in the human cohesin ring
    • 77 Huis in't Veld, P.J., et al. Characterization of a DNA exit gate in the human cohesin ring. Science 346 (2014), 968–972.
    • (2014) Science , vol.346 , pp. 968-972
    • Huis in't Veld, P.J.1
  • 78
    • 84943612692 scopus 로고    scopus 로고
    • A single alpha helix drives extensive remodeling of the proteasome lid and completion of regulatory particle assembly
    • 78 Tomko, R.J. Jr, et al. A single alpha helix drives extensive remodeling of the proteasome lid and completion of regulatory particle assembly. Cell 163 (2015), 432–444.
    • (2015) Cell , vol.163 , pp. 432-444
    • Tomko, R.J.1
  • 79
    • 84937393334 scopus 로고    scopus 로고
    • Evolution of orbitrap mass spectrometry instrumentation
    • 79 Eliuk, S., Makarov, A., Evolution of orbitrap mass spectrometry instrumentation. Annu. Rev. Anal. Chem. 8 (2015), 61–80.
    • (2015) Annu. Rev. Anal. Chem. , vol.8 , pp. 61-80
    • Eliuk, S.1    Makarov, A.2
  • 80
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • 80 Kulak, N.A., et al. Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat. Methods 11 (2014), 319–324.
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1
  • 81
    • 84910061461 scopus 로고    scopus 로고
    • Ultrasensitive proteome analysis using paramagnetic bead technology
    • 81 Hughes, C.S., et al. Ultrasensitive proteome analysis using paramagnetic bead technology. Mol. Syst. Biol., 10, 2014, 757.
    • (2014) Mol. Syst. Biol. , vol.10 , pp. 757
    • Hughes, C.S.1
  • 82
    • 84936792339 scopus 로고    scopus 로고
    • A double-barrel liquid chromatography-tandem mass spectrometry (LC-MS/MS) system to quantify 96 interactomes per day
    • 82 Hosp, F., et al. A double-barrel liquid chromatography-tandem mass spectrometry (LC-MS/MS) system to quantify 96 interactomes per day. Mol. Cell. Proteomics 14 (2015), 2030–2041.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 2030-2041
    • Hosp, F.1
  • 83
    • 84880784583 scopus 로고    scopus 로고
    • A microfluidic device for preparing next generation DNA sequencing libraries and for automating other laboratory protocols that require one or more column chromatography steps
    • 83 Tan, S.J., et al. A microfluidic device for preparing next generation DNA sequencing libraries and for automating other laboratory protocols that require one or more column chromatography steps. PLoS ONE, 8, 2013, e64084.
    • (2013) PLoS ONE , vol.8 , pp. e64084
    • Tan, S.J.1
  • 84
    • 84864619937 scopus 로고    scopus 로고
    • Beyond hairballs: the use of quantitative mass spectrometry data to understand protein–protein interactions
    • 84 Gingras, A.C., Raught, B., Beyond hairballs: the use of quantitative mass spectrometry data to understand protein–protein interactions. FEBS Lett. 586 (2012), 2723–2731.
    • (2012) FEBS Lett. , vol.586 , pp. 2723-2731
    • Gingras, A.C.1    Raught, B.2
  • 85
    • 84897139457 scopus 로고    scopus 로고
    • Every cell is special: genome-wide studies add a new dimension to single-cell biology
    • 85 Junker, J.P., van Oudenaarden, A., Every cell is special: genome-wide studies add a new dimension to single-cell biology. Cell 157 (2014), 8–11.
    • (2014) Cell , vol.157 , pp. 8-11
    • Junker, J.P.1    van Oudenaarden, A.2
  • 86
    • 84859631603 scopus 로고    scopus 로고
    • Trends in ultrasensitive proteomics
    • 86 Altelaar, A.F., Heck, A.J., Trends in ultrasensitive proteomics. Curr. Opin. Chem. Biol. 16 (2012), 206–213.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 206-213
    • Altelaar, A.F.1    Heck, A.J.2


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