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Volumn 12, Issue 6, 2017, Pages 1110-1135

Using hyperLOPIT to perform high-resolution mapping of the spatial proteome

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CELL COMPONENT; CELL FRACTIONATION; CELL ORGANELLE; CLINICAL PROTOCOL; CONTROLLED STUDY; DENSITY GRADIENT CENTRIFUGATION; HUMAN; HUMAN CELL; HYPER LOCALIZATION OF ORGANELLE PROTEINS BY ISOTOPE TAGGING; IMAGE PROCESSING; IMAGE QUALITY; INTERMETHOD COMPARISON; MACHINE LEARNING; MASS SPECTROMETRY; MOLECULAR IMAGING; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEOMICS; QUANTITATIVE ANALYSIS; CHEMISTRY; EUKARYOTIC CELL; PROCEDURES; SPATIAL ANALYSIS;

EID: 85019675158     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2017.026     Document Type: Article
Times cited : (100)

References (63)
  • 1
    • 84888384111 scopus 로고    scopus 로고
    • Unexpected gain of function for the scaffolding protein plectin due to mislocalization in pancreatic cancer
    • Shin, S.J. et al. Unexpected gain of function for the scaffolding protein plectin due to mislocalization in pancreatic cancer. Proc. Natl. Acad. Sci. 110, 19414-19419 (2013).
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. 19414-19419
    • Shin, S.J.1
  • 2
    • 84899041155 scopus 로고    scopus 로고
    • The many functions of mRNA localization during normal development and disease: From pillar to post
    • Cody, N.A.L., Iampietro, C. & Lécuyer, E. The many functions of mRNA localization during normal development and disease: from pillar to post. Wiley Interdiscip. Rev.: Dev. Biol. 2, 781-796 (2013).
    • (2013) Wiley Interdiscip. Rev.: Dev. Biol. , vol.2 , pp. 781-796
    • Cody, N.A.L.1    Iampietro, C.2    Lécuyer, E.3
  • 3
    • 80052592689 scopus 로고    scopus 로고
    • Mendelian disorders of membrane trafficking
    • De Matteis, M.A. & Luini, A. Mendelian disorders of membrane trafficking. N. Engl. J. Med. 365, 927-938 (2011).
    • (2011) N. Engl. J. Med. , vol.365 , pp. 927-938
    • De Matteis, M.A.1    Luini, A.2
  • 4
    • 33846163431 scopus 로고    scopus 로고
    • When intracellular logistics fails - Genetic defects in membrane trafficking
    • Olkkonen, V.M. & Ikonen, E. When intracellular logistics fails - genetic defects in membrane trafficking. J. Cell Sci. 119, 5031 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 5031
    • Olkkonen, V.M.1    Ikonen, E.2
  • 5
    • 34248650933 scopus 로고    scopus 로고
    • Quantitative proteomic approach to study subcellular localization of membrane proteins
    • Sadowski, P.G. et al. Quantitative proteomic approach to study subcellular localization of membrane proteins. Nat. Protoc. 1, 1778-1789 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1778-1789
    • Sadowski, P.G.1
  • 6
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric labeling multiplexed quantitative proteomics
    • Ting, L., Rad, R., Gygi, S.G. & Haas, W. MS3 eliminates ratio distortion in isobaric labeling multiplexed quantitative proteomics. Nat. Methods 8, 937-940 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.G.3    Haas, W.4
  • 7
    • 80155150331 scopus 로고    scopus 로고
    • Taming the isobaric tagging elephant in the room in quantitative proteomics
    • Christoforou, A. & Lilley, K.S. Taming the isobaric tagging elephant in the room in quantitative proteomics. Nat. Methods 8, 911-913 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 911-913
    • Christoforou, A.1    Lilley, K.S.2
  • 8
    • 85050276537 scopus 로고    scopus 로고
    • A Bioconductor workflow for processing and analysing spatial proteomics data
    • Breckels, L.M., Mulvey, C.M., Lilley , K.S. & Gatto, L. A Bioconductor workflow for processing and analysing spatial proteomics data. F1000 Res. 5, 2926 (2016).
    • (2016) F1000 Res. , vol.5 , pp. 2926
    • Breckels, L.M.1    Mulvey, C.M.2    Lilley, K.S.3    Gatto, L.4
  • 9
    • 84893355890 scopus 로고    scopus 로고
    • The effect of organelle discovery upon sub-cellular protein localisation
    • Breckels, L.M. et al. The effect of organelle discovery upon sub-cellular protein localisation. J. Proteomics 88, 129-140 (2013).
    • (2013) J. Proteomics , vol.88 , pp. 129-140
    • Breckels, L.M.1
  • 10
    • 84975853447 scopus 로고    scopus 로고
    • Learning from heterogeneous data sources: An application in spatial proteomics
    • Breckels, L.M. et al. Learning from heterogeneous data sources: an application in spatial proteomics. PLoS Comput. Biol. 12, e1004920 (2016).
    • (2016) PLoS Comput. Biol. , vol.12 , pp. e1004920
    • Breckels, L.M.1
  • 11
    • 84899504030 scopus 로고    scopus 로고
    • Mass-spectrometry-based spatial proteomics data analysis using pRoloc and pRolocdata
    • Gatto, L., Breckels, L.M., Wieczorek, S., Burger, T. & Lilley, K.S. Mass-spectrometry-based spatial proteomics data analysis using pRoloc and pRolocdata. Bioinformatics 30, 1322-1324 (2014).
    • (2014) Bioinformatics , vol.30 , pp. 1322-1324
    • Gatto, L.1    Breckels, L.M.2    Wieczorek, S.3    Burger, T.4    Lilley, K.S.5
  • 13
    • 84905215664 scopus 로고    scopus 로고
    • A foundation for reliable spatial proteomics data analysis
    • Gatto, L. et al. A foundation for reliable spatial proteomics data analysis. Mol. Cell. Proteomics 13, 1937-1952 (2014).
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1937-1952
    • Gatto, L.1
  • 14
    • 84954545040 scopus 로고    scopus 로고
    • A draft map of the mouse pluripotent stem cell spatial proteome
    • Christoforou, A. et al. A draft map of the mouse pluripotent stem cell spatial proteome. Nat. Commun. 7, 8992 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 8992
    • Christoforou, A.1
  • 16
    • 28744458859 scopus 로고    scopus 로고
    • Bioconductor: Open software development for computational biology and bioinformatics
    • Gentleman, R. et al. Bioconductor: open software development for computational biology and bioinformatics. Genome Biol. 5, R80 (2004).
    • (2004) Genome Biol. , vol.5 , pp. R80
    • Gentleman, R.1
  • 17
    • 84961289551 scopus 로고    scopus 로고
    • Orchestrating high-throughput genomic analysis with bioconductor
    • Huber, W. et al. Orchestrating high-throughput genomic analysis with bioconductor. Nat. Methods 12, 115-121 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 115-121
    • Huber, W.1
  • 18
    • 84856104821 scopus 로고    scopus 로고
    • MSnbase-an R/bioconductor package for isobaric tagged mass spectrometry data visualization, processing and quantitation
    • Gatto, L. & Lilley, K.S. MSnbase-an R/bioconductor package for isobaric tagged mass spectrometry data visualization, processing and quantitation. Bioinformatics 28, 288-289 (2012).
    • (2012) Bioinformatics , vol.28 , pp. 288-289
    • Gatto, L.1    Lilley, K.S.2
  • 19
    • 0026635749 scopus 로고
    • A new mouse embryonic stem cell line with good germ line contribution and gene targeting frequency
    • Magin, T.M., McWhir, J. & Melton, D.W. A new mouse embryonic stem cell line with good germ line contribution and gene targeting frequency. Nucleic Acids Res. 20, 3795-3796 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3795-3796
    • Magin, T.M.1    McWhir, J.2    Melton, D.W.3
  • 20
    • 33646236590 scopus 로고    scopus 로고
    • Mapping the Arabidopsis organelle proteome
    • Dunkley, T.P.J. et al. Mapping the Arabidopsis organelle proteome. Proc. Natl. Acad. Sci. USA 103, 6518-6523 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6518-6523
    • Dunkley, T.P.J.1
  • 21
    • 84893841383 scopus 로고    scopus 로고
    • Identification of trans-Golgi network proteins in Arabidopsis thaliana root tissue
    • Groen, A.J. et al. Identification of trans-Golgi network proteins in Arabidopsis thaliana root tissue. J. Proteome Res. 13, 763-776 (2013).
    • (2013) J. Proteome Res. , vol.13 , pp. 763-776
    • Groen, A.J.1
  • 23
    • 67049146295 scopus 로고    scopus 로고
    • Mapping organelle proteins and protein complexes in Drosophila melanogaster
    • Tan, D.J.L. et al. Mapping organelle proteins and protein complexes in Drosophila melanogaster. J. Proteome Res. 8, 2667-2678 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 2667-2678
    • Tan, D.J.L.1
  • 24
    • 84979673478 scopus 로고    scopus 로고
    • Global quantitative and dynamic mapping of protein subcellular localization
    • Itzhak, D.N., Tyanova, S., Cox, J. & Borner, G.H.H. Global, quantitative and dynamic mapping of protein subcellular localization. eLife 5, e16950 (2016).
    • (2016) ELife , vol.5 , pp. e16950
    • Itzhak, D.N.1    Tyanova, S.2    Cox, J.3    Borner, G.H.H.4
  • 25
    • 84984640047 scopus 로고    scopus 로고
    • MetaMass, a tool for meta-analysis of subcellular proteomics data
    • Lund-Johansen, F. et al. MetaMass, a tool for meta-analysis of subcellular proteomics data. Nat. Methods 13, 837-840 (2016).
    • (2016) Nat. Methods , vol.13 , pp. 837-840
    • Lund-Johansen, F.1
  • 26
    • 77952850720 scopus 로고    scopus 로고
    • Free-flow electrophoresis in the proteomic era: A technique in flux
    • Islinger, M., Eckerskorn, C. & Völkl, A. Free-flow electrophoresis in the proteomic era: a technique in flux. Electrophoresis 31, 1754-1763 (2010).
    • (2010) Electrophoresis , vol.31 , pp. 1754-1763
    • Islinger, M.1    Eckerskorn, C.2    Völkl, A.3
  • 27
    • 84860573550 scopus 로고    scopus 로고
    • Isolation and proteomic characterization of the Arabidopsis Golgi defines functional and novel components involved in plant cell wall biosynthesis
    • Parsons, H.T. et al. Isolation and proteomic characterization of the Arabidopsis Golgi defines functional and novel components involved in plant cell wall biosynthesis. Plant Physiol. 159, 12-26 (2012).
    • (2012) Plant Physiol. , vol.159 , pp. 12-26
    • Parsons, H.T.1
  • 28
    • 84960374877 scopus 로고    scopus 로고
    • Free-flow electrophoresis of plasma membrane vesicles enriched by two-phase partitioning enhances the quality of the proteome from Arabidopsis seedlings
    • de Michele, R. et al. Free-flow electrophoresis of plasma membrane vesicles enriched by two-phase partitioning enhances the quality of the proteome from Arabidopsis seedlings. J. Proteome Res. 15, 900-913 (2016).
    • (2016) J. Proteome Res. , vol.15 , pp. 900-913
    • De Michele, R.1
  • 29
    • 84983735488 scopus 로고    scopus 로고
    • Proteomic analysis of unbounded cellular compartments: Synaptic clefts
    • Loh, K.H. et al. Proteomic analysis of unbounded cellular compartments: synaptic clefts. Cell 166, 1295-1307.e21 (2016).
    • (2016) Cell , vol.166 , pp. 1295-1295e21
    • Loh, K.H.1
  • 30
    • 84907772320 scopus 로고    scopus 로고
    • Proteomic mapping of the human mitochondrial intermembrane space in live cells via ratiometric APEX tagging
    • Hung, V. et al. Proteomic mapping of the human mitochondrial intermembrane space in live cells via ratiometric APEX tagging. Mol. Cell 55, 332-341 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 332-341
    • Hung, V.1
  • 31
    • 58149263147 scopus 로고    scopus 로고
    • The phagosomal proteome in interferon-γ-activated macrophages
    • Trost, M. et al. The phagosomal proteome in interferon-γ-activated macrophages. Immunity 30, 143-154 (2009).
    • (2009) Immunity , vol.30 , pp. 143-154
    • Trost, M.1
  • 32
    • 80055066891 scopus 로고    scopus 로고
    • A novel strategy for the comprehensive analysis of the biomolecular composition of isolated plasma membranes
    • Thimiri Govinda Raj, D.B. et al. A novel strategy for the comprehensive analysis of the biomolecular composition of isolated plasma membranes. Mol. Syst. Biol. 7, 541-541 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 541
    • Thimiri Govinda Raj, D.B.1
  • 33
    • 84936805568 scopus 로고    scopus 로고
    • Identification of regulatory and cargo proteins of endosomal and secretory pathways in Arabidopsis thaliana by proteomic dissection
    • Heard, W., Sklenáč, J., Tomé, D.F.A., Robatzek, S. & Jones, A.M.E. Identification of regulatory and cargo proteins of endosomal and secretory pathways in Arabidopsis thaliana by proteomic dissection. Mol. Cell. Proteomics 14, 1796-1813 (2015).
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1796-1813
    • Heard, W.1    Sklenáč, J.2    Tomé, D.F.A.3    Robatzek, S.4    Jones, A.M.E.5
  • 34
    • 84928746968 scopus 로고    scopus 로고
    • A mass spectrometric-derived cell surface protein atlas
    • Bausch-Fluck, D. et al. A mass spectrometric-derived cell surface protein atlas. PLoS One 10, e0121314 (2015).
    • (2015) PLoS One , vol.10 , pp. e0121314
    • Bausch-Fluck, D.1
  • 35
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Chap. 3: Unit 3.22
    • Théry, C., Amigorena, S., Raposo, G. & Clayton, A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr. Protoc. Cell Biol. Chap. 3: Unit 3.22 (2006).
    • (2006) Curr. Protoc. Cell Biol.
    • Théry, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 36
    • 84990834226 scopus 로고    scopus 로고
    • Integrative analysis of subcellular quantitative proteomics studies reveals functional cytoskeleton membrane-lipid raft interactions in cancer
    • Shah, A.D. et al. Integrative analysis of subcellular quantitative proteomics studies reveals functional cytoskeleton membrane-lipid raft interactions in cancer. J. Proteome Res. 15, 3451-3462 (2016).
    • (2016) J. Proteome Res. , vol.15 , pp. 3451-3462
    • Shah, A.D.1
  • 37
    • 84957860866 scopus 로고    scopus 로고
    • The extracellular matrix: Tools and insights for the "omics" era
    • Naba, A. et al. The extracellular matrix: tools and insights for the "omics" era. Matrix Biol. 49, 10-24 (2016).
    • (2016) Matrix Biol. , vol.49 , pp. 10-24
    • Naba, A.1
  • 38
    • 0035019156 scopus 로고    scopus 로고
    • Loss of HCF-1-chromatin association precedes temperature-induced growth arrest of tsBN67 cells
    • Wysocka, J., Reilly, P.T. & Herr, W. Loss of HCF-1-chromatin association precedes temperature-induced growth arrest of tsBN67 cells. Mol. Cell. Biol. 21, 3820-3829 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3820-3829
    • Wysocka, J.1    Reilly, P.T.2    Herr, W.3
  • 39
    • 84875701652 scopus 로고    scopus 로고
    • Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells
    • Stadler, C. et al. Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. Nat. Methods 10, 315-323 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 315-323
    • Stadler, C.1
  • 40
    • 46349103594 scopus 로고    scopus 로고
    • A mitochondrial protein compendium elucidates complex i disease biology
    • Pagliarini, D.J. et al. A mitochondrial protein compendium elucidates complex I disease biology. Cell 134, 112-123 (2008).
    • (2008) Cell , vol.134 , pp. 112-123
    • Pagliarini, D.J.1
  • 41
    • 84874956967 scopus 로고    scopus 로고
    • Proteomic mapping of mitochondria in living cells via spatially-restricted enzymatic tagging
    • Rhee, H.-W. et al. Proteomic mapping of mitochondria in living cells via spatially-restricted enzymatic tagging. Science 339, 1328-1331 (2013).
    • (2013) Science , vol.339 , pp. 1328-1331
    • Rhee, H.-W.1
  • 42
    • 0015099032 scopus 로고
    • Tissue fractionation
    • de Duve, C. Tissue fractionation. J. Cell Biol. 50, 20D-55D (1971).
    • (1971) J. Cell Biol. , vol.50 , pp. 20D-55D
    • De Duve, C.1
  • 43
    • 33646473345 scopus 로고    scopus 로고
    • A mammalian organelle map by protein correlation profiling
    • Foster, L.J. et al. A mammalian organelle map by protein correlation profiling. Cell 125, 187-199 (2006).
    • (2006) Cell , vol.125 , pp. 187-199
    • Foster, L.J.1
  • 44
    • 85013157796 scopus 로고    scopus 로고
    • Accounting for protein subcellular localization: A compartmental map of the rat liver proteome
    • Jadot, M. et al. Accounting for protein subcellular localization: a compartmental map of the rat liver proteome. Mol. Cell. Proteomics 16, 194-212 (2016).
    • (2016) Mol. Cell. Proteomics , vol.16 , pp. 194-212
    • Jadot, M.1
  • 45
    • 84994577484 scopus 로고    scopus 로고
    • A portrait of the human organelle proteome in space and time during cytomegalovirus infection
    • e366
    • Jean Beltran, P.M., Mathias, R.A. & Cristea, I.M. A portrait of the human organelle proteome in space and time during cytomegalovirus infection. Cell Syst. 3, 361-373.e366 (2016).
    • (2016) Cell Syst. , vol.3 , pp. 361-373
    • Jean Beltran, P.M.1    Mathias, R.A.2    Cristea, I.M.3
  • 46
    • 79955009072 scopus 로고    scopus 로고
    • Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods
    • Jakobsen, L. et al. Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods. EMBO J. 30, 1520-1535 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1520-1535
    • Jakobsen, L.1
  • 48
    • 84989159501 scopus 로고    scopus 로고
    • Identification of cargo for adaptor protein (AP) complexes 3 and 4 by sucrose gradient profiling
    • Pertl-Obermeyer, H. et al. Identification of cargo for adaptor protein (AP) complexes 3 and 4 by sucrose gradient profiling. Mol. Cell. Proteomics 15, 2877-2889 (2016).
    • (2016) Mol. Cell. Proteomics , vol.15 , pp. 2877-2889
    • Pertl-Obermeyer, H.1
  • 50
    • 84963706086 scopus 로고    scopus 로고
    • Accounting for the multiple natures of missing values in label-free quantitative proteomics data sets to compare imputation strategies
    • Lazar, C., Gatto, L., Ferro, M., Bruley, C. & Burger, T. Accounting for the multiple natures of missing values in label-free quantitative proteomics data sets to compare imputation strategies. J. Proteome Res. 15, 1116-1125 (2016).
    • (2016) J. Proteome Res. , vol.15 , pp. 1116-1125
    • Lazar, C.1    Gatto, L.2    Ferro, M.3    Bruley, C.4    Burger, T.5
  • 51
    • 84929657508 scopus 로고    scopus 로고
    • Review, evaluation, and discussion of the challenges of missing value imputation for mass spectrometry-based label-free global proteomics
    • Webb-Robertson, B.J. et al. Review, evaluation, and discussion of the challenges of missing value imputation for mass spectrometry-based label-free global proteomics. J. Proteome Res. 14, 1993-2001 (2015).
    • (2015) J. Proteome Res. , vol.14 , pp. 1993-2001
    • Webb-Robertson, B.J.1
  • 52
    • 84943153270 scopus 로고    scopus 로고
    • Generation of multiple reporter ions from a single isobaric reagent increases multiplexing capacity for quantitative proteomics
    • Braun, C.R. et al. Generation of multiple reporter ions from a single isobaric reagent increases multiplexing capacity for quantitative proteomics. Anal. Chem. 87, 9855-9863 (2015).
    • (2015) Anal. Chem. , vol.87 , pp. 9855-9863
    • Braun, C.R.1
  • 53
    • 84907789935 scopus 로고    scopus 로고
    • Label free protein quantification for plant Golgi protein localisation and abundance
    • Nikolovski, N., Shliaha, P.V., Gatto, L., Dupree, P. & Lilley, K.S. Label free protein quantification for plant Golgi protein localisation and abundance. Plant Physiol. 66, 1033-1043 (2014).
    • (2014) Plant Physiol. , vol.66 , pp. 1033-1043
    • Nikolovski, N.1    Shliaha, P.V.2    Gatto, L.3    Dupree, P.4    Lilley, K.S.5
  • 54
    • 84934877492 scopus 로고    scopus 로고
    • Beyond the Western front: Targeted proteomics and organelle abundance profiling
    • Parsons, H.T. & Heazlewood, J.L. Beyond the Western front: targeted proteomics and organelle abundance profiling. Front. Plant Sci. 6, 301 (2015).
    • (2015) Front. Plant Sci. , vol.6 , pp. 301
    • Parsons, H.T.1    Heazlewood, J.L.2
  • 55
    • 78649680828 scopus 로고    scopus 로고
    • Improved sub-cellular resolution via simultaneous analysis of organelle proteomics data across varied experimental conditions
    • Trotter, M.W.B., Sadowski, P.G., Dunkley, T.P.J., Groen, A.J. & Lilley, K.S. Improved sub-cellular resolution via simultaneous analysis of organelle proteomics data across varied experimental conditions. Proteomics 10, 4213-4219 (2010).
    • (2010) Proteomics , vol.10 , pp. 4213-4219
    • Trotter, M.W.B.1    Sadowski, P.G.2    Dunkley, T.P.J.3    Groen, A.J.4    Lilley, K.S.5
  • 56
    • 84904325891 scopus 로고    scopus 로고
    • MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes
    • McAlister, G.C. et al. MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal. Chem. 86, 7150-7158 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 7150-7158
    • McAlister, G.C.1
  • 57
    • 84976274986 scopus 로고    scopus 로고
    • The Perseus computational platform for comprehensive analysis of (prote)omics data
    • Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731-740 (2016).
    • (2016) Nat. Methods , vol.13 , pp. 731-740
    • Tyanova, S.1
  • 58
    • 84905252677 scopus 로고    scopus 로고
    • Deciphering thylakoid sub-compartments using a mass spectrometry-based approach
    • Tomizioli, M. et al. Deciphering thylakoid sub-compartments using a mass spectrometry-based approach. Mol. Cell. Proteom. 13, 2147-2167 (2014).
    • (2014) Mol. Cell. Proteom. , vol.13 , pp. 2147-2167
    • Tomizioli, M.1
  • 59
    • 68049139696 scopus 로고    scopus 로고
    • Regulated fluctuations in Nanog expression mediate cell fate decisions in embryonic stem cells
    • Kalmar, T. et al. Regulated fluctuations in Nanog expression mediate cell fate decisions in embryonic stem cells. PLoS Biol. 7, e1000149 (2009).
    • (2009) PLoS Biol. , vol.7 , pp. e1000149
    • Kalmar, T.1
  • 60
    • 84897561498 scopus 로고    scopus 로고
    • A protocol for the subcellular fractionation of Saccharomyces cerevisiae using nitrogen cavitation and density gradient centrifugation
    • Wang, Y., Lilley, K.S. & Oliver, S.G. A protocol for the subcellular fractionation of Saccharomyces cerevisiae using nitrogen cavitation and density gradient centrifugation. Yeast 31, 127-135 (2014).
    • (2014) Yeast , vol.31 , pp. 127-135
    • Wang, Y.1    Lilley, K.S.2    Oliver, S.G.3
  • 61
    • 0032775896 scopus 로고    scopus 로고
    • Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles
    • Baldwin, D.N. & Linial, M.L. Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles. J. Virol. 73, 6387-6393 (1999).
    • (1999) J. Virol. , vol.73 , pp. 6387-6393
    • Baldwin, D.N.1    Linial, M.L.2
  • 62
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: A hub for protein information
    • The UniProt Consortium
    • The UniProt Consortium. UniProt: a hub for protein information. Nucleic Acids Res. 43, D204-D212 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. D204-D212
  • 63
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • The Gene Ontology Consortium et al
    • The Gene Ontology Consortium et al. Gene Ontology: tool for the unification of biology. Nat. Genet. 25, 25-29 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 25-29


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.