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Volumn 15, Issue 5, 2016, Pages 1725-1731

Spectral library searching to identify cross-linked peptides

Author keywords

protein cross linking; spectral library; XL MS

Indexed keywords

PEPTIDE;

EID: 84969141892     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.6b00014     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 84930190486 scopus 로고    scopus 로고
    • Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry
    • Navare, A. T. et al. Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry Structure 2015, 23, 762-773 10.1016/j.str.2015.01.022
    • (2015) Structure , vol.23 , pp. 762-773
    • Navare, A.T.1
  • 2
    • 41449110185 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from large sequence databases
    • Rinner, O. et al. Identification of cross-linked peptides from large sequence databases Nat. Methods 2008, 5, 315-318 10.1038/nmeth.1192
    • (2008) Nat. Methods , vol.5 , pp. 315-318
    • Rinner, O.1
  • 3
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz, A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes J. Mass Spectrom. 2003, 38, 1225-1237 10.1002/jms.559
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 4
    • 84947933635 scopus 로고    scopus 로고
    • Host-Microbe Protein Interactions during Bacterial Infection
    • Schweppe, D. K. et al. Host-Microbe Protein Interactions during Bacterial Infection Chem. Biol. 2015, 22, 1521-1530 10.1016/j.chembiol.2015.09.015
    • (2015) Chem. Biol. , vol.22 , pp. 1521-1530
    • Schweppe, D.K.1
  • 5
    • 84866117936 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from complex samples
    • Yang, B. et al. Identification of cross-linked peptides from complex samples Nat. Methods 2012, 9, 904-906 10.1038/nmeth.2099
    • (2012) Nat. Methods , vol.9 , pp. 904-906
    • Yang, B.1
  • 6
    • 33947366516 scopus 로고    scopus 로고
    • Development and validation of a spectral library searching method for peptide identification from MS/MS
    • Lam, H. et al. Development and validation of a spectral library searching method for peptide identification from MS/MS Proteomics 2007, 7, 655-667 10.1002/pmic.200600625
    • (2007) Proteomics , vol.7 , pp. 655-667
    • Lam, H.1
  • 8
    • 84875913034 scopus 로고    scopus 로고
    • In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy
    • Weisbrod, C. R. et al. In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy J. Proteome Res. 2013, 12, 1569-1579 10.1021/pr3011638
    • (2013) J. Proteome Res. , vol.12 , pp. 1569-1579
    • Weisbrod, C.R.1
  • 9
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K.; McCormack, A. L.; Yates, J. R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 1994, 5, 976-989 10.1016/1044-0305(94)80016-2
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 10
    • 84945473599 scopus 로고    scopus 로고
    • A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies
    • Depke, M. et al. A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies Proteomics 2015, 15, 3648 10.1002/pmic.201500091
    • (2015) Proteomics , vol.15 , pp. 3648
    • Depke, M.1
  • 11
    • 84888064552 scopus 로고    scopus 로고
    • Refining similarity scoring to enable decoy-free validation in spectral library searching
    • Shao, W.; Zhu, K.; Lam, H. Refining similarity scoring to enable decoy-free validation in spectral library searching Proteomics 2013, 13, 3273-3283 10.1002/pmic.201300232
    • (2013) Proteomics , vol.13 , pp. 3273-3283
    • Shao, W.1    Zhu, K.2    Lam, H.3
  • 12
    • 84877155985 scopus 로고    scopus 로고
    • Spectrum-based method to generate good decoy libraries for spectral library searching in peptide identifications
    • Cheng, C. Y.; Tsai, C. F.; Chen, Y. J.; Sung, T. Y.; Hsu, W. L. Spectrum-based method to generate good decoy libraries for spectral library searching in peptide identifications J. Proteome Res. 2013, 12, 2305-2310 10.1021/pr301039b
    • (2013) J. Proteome Res. , vol.12 , pp. 2305-2310
    • Cheng, C.Y.1    Tsai, C.F.2    Chen, Y.J.3    Sung, T.Y.4    Hsu, W.L.5
  • 13
    • 76149142168 scopus 로고    scopus 로고
    • Repeatability and reproducibility in proteomic identifications by liquid chromatography-tandem mass spectrometry
    • Tabb, D. L. et al. Repeatability and reproducibility in proteomic identifications by liquid chromatography-tandem mass spectrometry J. Proteome Res. 2010, 9, 761-776 10.1021/pr9006365
    • (2010) J. Proteome Res. , vol.9 , pp. 761-776
    • Tabb, D.L.1
  • 14
    • 84910595462 scopus 로고    scopus 로고
    • Structural characterization by cross-linking reveals the detailed architecture of a coatomer-related heptameric module from the nuclear pore complex
    • Shi, Y. et al. Structural characterization by cross-linking reveals the detailed architecture of a coatomer-related heptameric module from the nuclear pore complex Mol. Cell. Proteomics 2014, 13, 2927-2943 10.1074/mcp.M114.041673
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2927-2943
    • Shi, Y.1
  • 15
    • 84930177614 scopus 로고    scopus 로고
    • Rapid, optimized interactomic screening
    • Hakhverdyan, Z. et al. Rapid, optimized interactomic screening Nat. Methods 2015, 12, 553-560 10.1038/nmeth.3395
    • (2015) Nat. Methods , vol.12 , pp. 553-560
    • Hakhverdyan, Z.1
  • 16
    • 84910622339 scopus 로고    scopus 로고
    • A pipeline for determining protein-protein interactions and proximities in the cellular milieu
    • Subbotin, R. I.; Chait, B. T. A pipeline for determining protein-protein interactions and proximities in the cellular milieu Mol. Cell. Proteomics 2014, 13, 2824-2835 10.1074/mcp.M114.041095
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2824-2835
    • Subbotin, R.I.1    Chait, B.T.2
  • 17
    • 84855867436 scopus 로고    scopus 로고
    • Analysis of stable and transient protein-protein interactions
    • Byrum, S.; Smart, S. K.; Larson, S.; Tackett, A. J. Analysis of stable and transient protein-protein interactions Methods Mol. Biol. 2012, 833, 143-152 10.1007/978-1-61779-477-3-10
    • (2012) Methods Mol. Biol. , vol.833 , pp. 143-152
    • Byrum, S.1    Smart, S.K.2    Larson, S.3    Tackett, A.J.4
  • 18
    • 84938516297 scopus 로고    scopus 로고
    • Quantitative interactome analysis reveals a chemoresistant edgotype
    • Chavez, J. D. Quantitative interactome analysis reveals a chemoresistant edgotype Nat. Commun. 2015, 6, 7928 10.1038/ncomms8928
    • (2015) Nat. Commun. , vol.6 , pp. 7928
    • Chavez, J.D.1
  • 19
    • 84921469305 scopus 로고    scopus 로고
    • A new in vivo cross-linking mass spectrometry platform to define protein-protein interactions in living cells
    • Kaake, R. M. et al. A new in vivo cross-linking mass spectrometry platform to define protein-protein interactions in living cells Mol. Cell. Proteomics 2014, 13, 3533-3543 10.1074/mcp.M114.042630
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3533-3543
    • Kaake, R.M.1
  • 20
    • 84949106630 scopus 로고    scopus 로고
    • Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
    • Liu, F.; Rijkers, D. T.; Post, H.; Heck, A. J. Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry Nat. Methods 2015, 12, 1179 10.1038/nmeth.3603
    • (2015) Nat. Methods , vol.12 , pp. 1179
    • Liu, F.1    Rijkers, D.T.2    Post, H.3    Heck, A.J.4
  • 21
    • 84923073621 scopus 로고    scopus 로고
    • Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules
    • Trowitzsch, S. et al. Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules Nat. Commun. 2015, 6, 6011 10.1038/ncomms7011
    • (2015) Nat. Commun. , vol.6 , pp. 6011
    • Trowitzsch, S.1
  • 22
    • 80051918561 scopus 로고    scopus 로고
    • PGAT: A multistrain analysis resource for microbial genomes
    • Brittnacher, M. J. et al. PGAT: a multistrain analysis resource for microbial genomes Bioinformatics 2011, 27, 2429-2430 10.1093/bioinformatics/btr418
    • (2011) Bioinformatics , vol.27 , pp. 2429-2430
    • Brittnacher, M.J.1
  • 23
    • 84955273184 scopus 로고    scopus 로고
    • Parallel Spectral Acquisition with an Ion Cyclotron Resonance Cell Array
    • Park, S. G.; Anderson, G. A.; Navare, A. T.; Bruce, J. E. Parallel Spectral Acquisition with an Ion Cyclotron Resonance Cell Array Anal. Chem. 2016, 88, 1162-1168 10.1021/acs.analchem.5b02987
    • (2016) Anal. Chem. , vol.88 , pp. 1162-1168
    • Park, S.G.1    Anderson, G.A.2    Navare, A.T.3    Bruce, J.E.4
  • 24
    • 84938516297 scopus 로고    scopus 로고
    • Quantitative interactome analysis reveals a chemoresistant edgotype
    • Chavez, J. D. et al. Quantitative interactome analysis reveals a chemoresistant edgotype Nat. Commun. 2015, 6, 7928 10.1038/ncomms8928
    • (2015) Nat. Commun. , vol.6 , pp. 7928
    • Chavez, J.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.