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Volumn 893, Issue , 2012, Pages 223-240

Post-digestion 18O exchange/labeling for quantitative shotgun proteomics of membrane proteins

Author keywords

Mass spectrometry; Membrane protein quantiation; Quantitative shotgun proteomics

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS;

EID: 84864135949     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-885-6_15     Document Type: Article
Times cited : (2)

References (28)
  • 1
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary C, Mann M (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol 11:427-439
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 2
    • 77954523086 scopus 로고    scopus 로고
    • Options and considerations when selecting a quantitative proteomics strategy
    • Domon B, Aebersold R (2010) Options and considerations when selecting a quantitative proteomics strategy. Nat Biotechnol 28: 710-721
    • (2010) Nat. Biotechnol. , vol.28 , pp. 710-721
    • Domon, B.1    Aebersold, R.2
  • 3
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometrybased proteomics turns quantitative
    • Ong SE, Mann M (2005) Mass spectrometrybased proteomics turns quantitative. Nat Chem Biol 1:252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 4
    • 0020807419 scopus 로고
    • Preparation of stable isotope-incorporated peptide internal standards for field desorption mass spectrometry quantification of peptides in biologic tissue
    • Desiderio DM, Kai M (1983) Preparation of stable isotope-incorporated peptide internal standards for field desorption mass spectrometry quantification of peptides in biologic tissue. Biomed Mass Spectrom 10:471-479
    • (1983) Biomed. Mass. Spectrom. , vol.10 , pp. 471-479
    • Desiderio, D.M.1    Kai, M.2
  • 5
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18 O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao X, Freas A, Ramirez J et al (2001) Proteolytic 18 O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal Chem 73:2836-2842
    • (2001) Anal. Chem. , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3
  • 7
    • 0019575864 scopus 로고
    • Studies on the mechanisms of action of proteolytic enzymes using heavy oxygen exchange
    • Antonov VK, Ginodman LM, Rumsh LD et al (1981) Studies on the mechanisms of action of proteolytic enzymes using heavy oxygen exchange. Eur J Biochem 117:195-200
    • (1981) Eur. J. Biochem. , vol.117 , pp. 195-200
    • Antonov, V.K.1    Ginodman, L.M.2    Rumsh, L.D.3
  • 8
    • 0037578010 scopus 로고    scopus 로고
    • Dissection of proteolytic 18O labeling: Endoproteasecatalyzed 16 O-to-18 O exchange of truncated peptide substrates
    • Yao X, Afonso C, Fenselau C (2003) Dissection of proteolytic 18O labeling: Endoproteasecatalyzed 16 O-to-18 O exchange of truncated peptide substrates. J Proteome Res 2: 147-152
    • (2003) J. Proteome. Res. , vol.2 , pp. 147-152
    • Yao, X.1    Afonso, C.2    Fenselau, C.3
  • 9
    • 20544437625 scopus 로고    scopus 로고
    • Quantitative proteome analysis of human plasma following in vivo lipopolysaccharide administration using 16 O 18 O labeling and the accurate mass and time tag approach
    • Qian WJ, Monroe ME, Liu T et al (2005) Quantitative proteome analysis of human plasma following in vivo lipopolysaccharide administration using 16 O/ 18 O labeling and the accurate mass and time tag approach. Mol Cell Proteomics 4:700-709
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 700-709
    • Qian, W.J.1    Monroe, M.E.2    Liu, T.3
  • 10
    • 4444228797 scopus 로고    scopus 로고
    • Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 16 O/ 18 O isotopic labeling
    • Zang L, Palmer Toy D, Hancock WS et al (2004) Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 16 O/ 18 O isotopic labeling. J Proteome Res 3:604-612
    • (2004) J. Proteome. Res. , vol.3 , pp. 604-612
    • Zang, L.1    Palmer Toy, D.2    Hancock, W.S.3
  • 11
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu CC, Yates JR 3rd (2003) The application of mass spectrometry to membrane proteomics. Nat Biotechnol 21:262-267
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 12
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins-theory and application
    • Speers AE, Wu CC (2007) Proteomics of integral membrane proteins-theory and application. Chem Rev 107:3687-3714
    • (2007) Chem. Rev. , vol.107 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 13
    • 0942276251 scopus 로고    scopus 로고
    • A detergent-and cyanogen bromide-free method for integral membrane proteomics: Application to halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder J, Conrads TP, Yu LR et al (2004) A detergent-and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 4:31-45
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3
  • 14
    • 4444343944 scopus 로고    scopus 로고
    • Analysis of murine natural killer cell microsomal proteins using two-dimensional liquid chromatography coupled to tandem electrospray ionization mass spectrometry
    • Blonder J, Rodriguez-Galan MC, Chan KC et al (2004) Analysis of murine natural killer cell microsomal proteins using two-dimensional liquid chromatography coupled to tandem electrospray ionization mass spectrometry. J Proteome Res 3:862-870
    • (2004) J. Proteome. Res. , vol.3 , pp. 862-870
    • Blonder, J.1    Rodriguez-Galan, M.C.2    Chan, K.C.3
  • 15
    • 4644252123 scopus 로고    scopus 로고
    • A proteomic characterization of the plasma membrane of human epidermis by high-throughput mass spectrometry
    • Blonder J, Terunuma A, Conrads TP et al (2004) A proteomic characterization of the plasma membrane of human epidermis by high-throughput mass spectrometry. J Invest Dermatol 4:691-699
    • (2004) J. Invest. Dermatol. , vol.4 , pp. 691-699
    • Blonder, J.1    Terunuma, A.2    Conrads, T.P.3
  • 16
    • 70349991237 scopus 로고    scopus 로고
    • Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS
    • Ye X, Johann DJ Jr, Hakami RM et al (2009) Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS. J Proteomics 73:112-122
    • (2009) J. Proteomics , vol.73 , pp. 112-122
    • Ye, X.1    Johann, Jr.D.J.2    Hakami, R.M.3
  • 17
    • 20244374564 scopus 로고    scopus 로고
    • Quantitative pro filing of the detergent-resistant membrane proteome of iota-b toxin induced vero cells
    • Blonder J, Hale ML, Chan KC et al (2005) Quantitative pro filing of the detergent-resistant membrane proteome of iota-b toxin induced Vero cells. J Proteome Res 4: 523-531
    • (2005) J. Proteome. Res. , vol.4 , pp. 523-531
    • Blonder, J.1    Hale, M.L.2    Chan, K.C.3
  • 18
    • 32344443165 scopus 로고    scopus 로고
    • Combined chemical and enzymatic stable isotope labeling for quantitative pro filing of detergent-insoluble membrane proteins isolated using triton X-100 and brij-96
    • Blonder J, Yu LR, Radeva G et al (2006) Combined chemical and enzymatic stable isotope labeling for quantitative pro filing of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96. J Proteome Res 5:349-360
    • (2006) J. Proteome. Res. , vol.5 , pp. 349-360
    • Blonder, J.1    Yu, L.R.2    Radeva, G.3
  • 19
    • 33751011581 scopus 로고    scopus 로고
    • Proteomic analysis of plasma membrane from hypoxia-adapted malignant melanoma
    • Stockwin LH, Blonder J, Bumke MA et al (2006) Proteomic analysis of plasma membrane from hypoxia-adapted malignant melanoma. J Proteome Res 5:2996-3007
    • (2006) J. Proteome. Res. , vol.5 , pp. 2996-3007
    • Stockwin, L.H.1    Blonder, J.2    Bumke, M.A.3
  • 20
    • 77954198163 scopus 로고    scopus 로고
    • Optimized method for computing 18 O 16 O ratios of differentially stable-isotope labeled peptides in the context of postdigestion 18 O exchange/labeling
    • Ye X, Luke BT, Johann DJ et al (2010) Optimized method for computing (18)O/(16)O ratios of differentially stable-isotope labeled peptides in the context of postdigestion (18)O exchange/labeling. Anal Chem 82:5878-5886
    • (2010) Anal. Chem. , vol.82 , pp. 5878-5886
    • Ye, X.1    Luke, B.T.2    Johann, D.J.3
  • 21
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed EO (1998) HIV-1 gag proteins: Diverse functions in the virus life cycle. Virology 251:1-15
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 22
    • 77953372726 scopus 로고    scopus 로고
    • Relationships between plasma membrane microdomains and HIV-1 assembly
    • Ono A (2010) Relationships between plasma membrane microdomains and HIV-1 assembly. Biol Cell 102:335-350
    • (2010) Biol. Cell. , vol.102 , pp. 335-350
    • Ono, A.1
  • 23
    • 27644522295 scopus 로고    scopus 로고
    • Association of human immunode ficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: Use of a novel gag multimerization assay
    • Ono A, Waheed AA, Joshi A, Freed EO (2005) Association of human immunode ficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: Use of a novel Gag multimerization assay. J Virol 79:14131-14140
    • (2005) J. Virol. , vol.79 , pp. 14131-14140
    • Ono, A.1    Waheed, A.A.2    Joshi, A.3    Freed, E.O.4
  • 24
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunode ficiency virus type 1 gag promotes its localization to barges, raft-like membrane microdomains
    • Lindwasser OW, Resh MD (2001) Multimerization of human immunode ficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J Virol 75:7913-7924
    • (2001) J. Virol. , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 25
    • 0028207238 scopus 로고
    • An improved procedure for enzymatic digestion of polyvinylidene di fl uoride-bound proteins for internal sequence analysis
    • Fernandez J, Andrews L, Mische SM (1994) An improved procedure for enzymatic digestion of polyvinylidene di fl uoride-bound proteins for internal sequence analysis. Anal Biochem 218:112-117
    • (1994) Anal. Biochem. , vol.218 , pp. 112-117
    • Fernandez, J.1    Andrews, L.2    Mische, S.M.3
  • 26
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409:241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 27
    • 33845309673 scopus 로고    scopus 로고
    • Considerations for proteolytic labeling-optimization of 18 O incorporation and prohibition of back-exchange
    • Storms HF, Van Der Heijden R, Tjaden UR, van Der Greef J (2006) Considerations for proteolytic labeling-optimization of 18 O incorporation and prohibition of back-exchange. Rapid Commun Mass Spectrom 20: 3491-3497
    • (2006) Rapid. Commun. Mass Spectrom , vol.20 , pp. 3491-3497
    • Storms, H.F.1    Van Der Heijden, R.2    Tjaden, U.R.3    Van Der Greef, J.4
  • 28
    • 0034101218 scopus 로고    scopus 로고
    • Solid-state UV laser-induced fl uorescence detection in capillary electrophoresis
    • Chan KC, Muschik GM, Issaq HJ (2000) Solid-state UV laser-induced fl uorescence detection in capillary electrophoresis. Electrophoresis 21:2062-2066
    • (2000) Electrophoresis , vol.21 , pp. 2062-2066
    • Chan, K.C.1    Muschik, G.M.2    Issaq, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.