메뉴 건너뛰기




Volumn 14, Issue 10, 2014, Pages 1211-1222

Quantitative analysis of human salivary gland-derived intact proteome using top-down mass spectrometry

Author keywords

AMT; FT ICR; FTMS; Saliva; Technology; Top down

Indexed keywords

BETA 2 MICROGLOBULIN; CYSTATIN; HISTATIN; PROLACTIN; PROLACTIN INDUCIBLE PROTEIN; PROTEOME; PRP2 PROTEIN; PRP3 PROTEIN; SALIVA PROTEIN; SM3A PROTEIN; SM3B PROTEIN; STATHERIN; UNCLASSIFIED DRUG; ISOPROTEIN; GLYCOSYLATED PROTEIN;

EID: 84899839171     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300378     Document Type: Article
Times cited : (47)

References (44)
  • 1
    • 0027754063 scopus 로고
    • The application of saliva, sweat and tear fluid for diagnostic purposes
    • Haeckel, R., Hanecke, P., The application of saliva, sweat and tear fluid for diagnostic purposes. Ann. Biol. Clin. 1993, 51, 903-910.
    • (1993) Ann. Biol. Clin. , vol.51 , pp. 903-910
    • Haeckel, R.1    Hanecke, P.2
  • 2
    • 0035257183 scopus 로고    scopus 로고
    • A review of saliva: normal composition, flow, and function
    • Humphrey, S. P., Williamson, R. T., A review of saliva: normal composition, flow, and function. J. Prosthet. Dent. 2001, 85, 162-169.
    • (2001) J. Prosthet. Dent. , vol.85 , pp. 162-169
    • Humphrey, S.P.1    Williamson, R.T.2
  • 4
    • 48949117187 scopus 로고    scopus 로고
    • Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us
    • Messana, I., Inzitari, R., Fanali, C., Cabras, T., Castagnola, M., Facts and artifacts in proteomics of body fluids. What proteomics of saliva is telling us? J. Sep. Sci. 2008, 31, 1948-1963.
    • (2008) J. Sep. Sci. , vol.31 , pp. 1948-1963
    • Messana, I.1    Inzitari, R.2    Fanali, C.3    Cabras, T.4    Castagnola, M.5
  • 7
    • 84874625369 scopus 로고    scopus 로고
    • Proteoform: a single term describing protein complexity
    • Smith, L. M., Kelleher, N. L., Proteoform: a single term describing protein complexity. Nat. Methods 2013, 10, 186-187.
    • (2013) Nat. Methods , vol.10 , pp. 186-187
    • Smith, L.M.1    Kelleher, N.L.2
  • 8
    • 33748550994 scopus 로고    scopus 로고
    • A novel saliva test for caries risk assessment
    • 292-294.
    • Denny, P. C., Denny, P. A., Takashima, J., Si, Y. et al., A novel saliva test for caries risk assessment. J. Calif. Dent. Assoc. 2006, 34, 287-290, 292-294.
    • (2006) J. Calif. Dent. Assoc. , vol.34 , pp. 287-290
    • Denny, P.C.1    Denny, P.A.2    Takashima, J.3    Si, Y.4
  • 10
    • 0036071261 scopus 로고    scopus 로고
    • The diagnostic applications of saliva-a review
    • Kaufman, E., Lamster, I. B., The diagnostic applications of saliva-a review. Crit. Rev. Oral. Biol. Med. 2002, 13, 197-212.
    • (2002) Crit. Rev. Oral. Biol. Med. , vol.13 , pp. 197-212
    • Kaufman, E.1    Lamster, I.B.2
  • 11
    • 0036512301 scopus 로고    scopus 로고
    • Salivary markers of systemic disease: noninvasive diagnosis of disease and monitoring of general health
    • Lawrence, H. P., Salivary markers of systemic disease: noninvasive diagnosis of disease and monitoring of general health. J. Can. Dent. Assoc. 2002, 68, 170-174.
    • (2002) J. Can. Dent. Assoc. , vol.68 , pp. 170-174
    • Lawrence, H.P.1
  • 12
    • 0032578688 scopus 로고    scopus 로고
    • p53 antibodies in the saliva of patients with squamous cell carcinoma of the oral cavity
    • Tavassoli, M., Brunel, N., Maher, R., Johnson, N. W., Soussi, T., p53 antibodies in the saliva of patients with squamous cell carcinoma of the oral cavity. Int. J. Cancer 1998, 78, 390-391.
    • (1998) Int. J. Cancer , vol.78 , pp. 390-391
    • Tavassoli, M.1    Brunel, N.2    Maher, R.3    Johnson, N.W.4    Soussi, T.5
  • 13
    • 0034096263 scopus 로고    scopus 로고
    • The presence of soluble c-erbB-2 in saliva and serum among women with breast carcinoma: a preliminary study
    • Streckfus, C., Bigler, L., Dellinger, T., Dai, X. et al., The presence of soluble c-erbB-2 in saliva and serum among women with breast carcinoma: a preliminary study. Clin. Cancer Res. 2000, 6, 2363-2370.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2363-2370
    • Streckfus, C.1    Bigler, L.2    Dellinger, T.3    Dai, X.4
  • 14
    • 0034004679 scopus 로고    scopus 로고
    • A preliminary study of CA15-3, c-erbB-2, epidermal growth factor receptor, cathepsin-D, and p53 in saliva among women with breast carcinoma
    • Streckfus, C., Bigler, L., Tucci, M., Thigpen, J. T., A preliminary study of CA15-3, c-erbB-2, epidermal growth factor receptor, cathepsin-D, and p53 in saliva among women with breast carcinoma. Cancer Invest. 2000, 18, 101-109.
    • (2000) Cancer Invest. , vol.18 , pp. 101-109
    • Streckfus, C.1    Bigler, L.2    Tucci, M.3    Thigpen, J.T.4
  • 15
    • 12344295469 scopus 로고    scopus 로고
    • Serum, salivary and tissue proteomics for discovery of biomarkers for head and neck cancers
    • Drake, R. R., Cazare, L. H., Semmes, O. J., Wadsworth, J. T., Serum, salivary and tissue proteomics for discovery of biomarkers for head and neck cancers. Expert Rev. Mol. Diagn. 2005, 5, 93-100.
    • (2005) Expert Rev. Mol. Diagn. , vol.5 , pp. 93-100
    • Drake, R.R.1    Cazare, L.H.2    Semmes, O.J.3    Wadsworth, J.T.4
  • 16
    • 84861151967 scopus 로고    scopus 로고
    • Defining intact protein primary structures from saliva: a step toward the human proteome project
    • Halgand, F., Zabrouskov, V., Bassilian, S., Souda, P. et al., Defining intact protein primary structures from saliva: a step toward the human proteome project. Anal. Chem. 2012, 84, 4383-4395.
    • (2012) Anal. Chem. , vol.84 , pp. 4383-4395
    • Halgand, F.1    Zabrouskov, V.2    Bassilian, S.3    Souda, P.4
  • 17
    • 77951206392 scopus 로고    scopus 로고
    • Micro-heterogeneity of human saliva Peptide P-C characterized by high-resolution top-down Fourier-transform mass spectrometry
    • Halgand, F., Zabrouskov, V., Bassilian, S., Souda, P. et al., Micro-heterogeneity of human saliva Peptide P-C characterized by high-resolution top-down Fourier-transform mass spectrometry. J. Am. Soc. Mass. Spectrom. 2010, 21, 868-877.
    • (2010) J. Am. Soc. Mass. Spectrom. , vol.21 , pp. 868-877
    • Halgand, F.1    Zabrouskov, V.2    Bassilian, S.3    Souda, P.4
  • 18
    • 77952876623 scopus 로고    scopus 로고
    • Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry
    • Ryan, C. M., Souda, P., Halgand, F., Wong, D. T. et al., Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry. J. Am. Soc. Mass. Spectrom. 2010, 21, 908-917.
    • (2010) J. Am. Soc. Mass. Spectrom. , vol.21 , pp. 908-917
    • Ryan, C.M.1    Souda, P.2    Halgand, F.3    Wong, D.T.4
  • 19
    • 35748956431 scopus 로고    scopus 로고
    • Protein-sequence polymorphisms and post-translational modifications in proteins from human saliva using top-down fourier-transform ion cyclotron resonance mass spectrometry
    • Whitelegge, J. P., Zabrouskov, V., Halgand, F., Souda, P. et al., Protein-sequence polymorphisms and post-translational modifications in proteins from human saliva using top-down fourier-transform ion cyclotron resonance mass spectrometry. Int. J. Mass Spectrom. 2007, 268, 190-197.
    • (2007) Int. J. Mass Spectrom. , vol.268 , pp. 190-197
    • Whitelegge, J.P.1    Zabrouskov, V.2    Halgand, F.3    Souda, P.4
  • 20
    • 33645033710 scopus 로고    scopus 로고
    • Salivary diagnostics: the future is now
    • Malamud, D., Salivary diagnostics: the future is now. J. Am. Dent. Assoc. 2006, 137, 284-286.
    • (2006) J. Am. Dent. Assoc. , vol.137 , pp. 284-286
    • Malamud, D.1
  • 21
    • 0032134726 scopus 로고    scopus 로고
    • Toward molecularly based diagnostics for the oral cavity
    • Slavkin, H. C., Toward molecularly based diagnostics for the oral cavity. J. Am. Dent. Assoc. 1998, 129, 1138-1143.
    • (1998) J. Am. Dent. Assoc. , vol.129 , pp. 1138-1143
    • Slavkin, H.C.1
  • 22
    • 0035747461 scopus 로고    scopus 로고
    • A revolution in biomedical assessment: the development of salivary diagnostics
    • Tabak, L. A., A revolution in biomedical assessment: the development of salivary diagnostics. J. Dent. Educ. 2001, 65, 1335-1339.
    • (2001) J. Dent. Educ. , vol.65 , pp. 1335-1339
    • Tabak, L.A.1
  • 23
    • 17844368916 scopus 로고    scopus 로고
    • Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry
    • Hu, S., Xie, Y., Ramachandran, P., Ogorzalek Loo, R. R. et al., Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry. Proteomics 2005, 5, 1714-1728.
    • (2005) Proteomics , vol.5 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3    Ogorzalek Loo, R.R.4
  • 24
    • 61349129152 scopus 로고    scopus 로고
    • Hypo-phosphorylation of salivary peptidome as a clue to the molecular pathogenesis of autism spectrum disorders
    • Castagnola, M., Messana, I., Inzitari, R., Fanali, C. et al., Hypo-phosphorylation of salivary peptidome as a clue to the molecular pathogenesis of autism spectrum disorders. J. Proteome. Res. 2008, 7, 5327-5332.
    • (2008) J. Proteome. Res. , vol.7 , pp. 5327-5332
    • Castagnola, M.1    Messana, I.2    Inzitari, R.3    Fanali, C.4
  • 25
    • 84880077164 scopus 로고    scopus 로고
    • Significant modifications of the salivary proteome potentially associated with complications of down syndrome revealed by top-down proteomics
    • Cabras, T., Pisano, E., Montaldo, C., Giuca, M. R. et al., Significant modifications of the salivary proteome potentially associated with complications of down syndrome revealed by top-down proteomics. Mol. Cell. Proteomics. 2013, 12, 1844-1852.
    • (2013) Mol. Cell. Proteomics. , vol.12 , pp. 1844-1852
    • Cabras, T.1    Pisano, E.2    Montaldo, C.3    Giuca, M.R.4
  • 26
    • 77958013445 scopus 로고    scopus 로고
    • Alterations of the salivary secretory peptidome profile in children affected by type 1 diabetes
    • Cabras, T., Pisano, E., Mastinu, A., Denotti, G. et al., Alterations of the salivary secretory peptidome profile in children affected by type 1 diabetes. Mol. Cell. Proteomics 2010, 9, 2099-2108.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2099-2108
    • Cabras, T.1    Pisano, E.2    Mastinu, A.3    Denotti, G.4
  • 27
    • 43849108752 scopus 로고    scopus 로고
    • Trafficking and postsecretory events responsible for the formation of secreted human salivary peptides: a proteomics approach
    • Messana, I., Cabras, T., Pisano, E., Sanna, M. T. et al., Trafficking and postsecretory events responsible for the formation of secreted human salivary peptides: a proteomics approach. Mol. Cell. Proteomics 2008, 7, 911-926.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 911-926
    • Messana, I.1    Cabras, T.2    Pisano, E.3    Sanna, M.T.4
  • 28
    • 6344280371 scopus 로고    scopus 로고
    • Proteomic analyses using an accurate mass and time tag strategy
    • 626-633.
    • Pasa-Tolic, L., Masselon, C., Barry, R. C., Shen, Y., Smith, R. D., Proteomic analyses using an accurate mass and time tag strategy. Biotechniques 2004, 37, 621, 626-633.
    • (2004) Biotechniques , vol.37 , pp. 621
    • Pasa-Tolic, L.1    Masselon, C.2    Barry, R.C.3    Shen, Y.4    Smith, R.D.5
  • 29
    • 79952116936 scopus 로고    scopus 로고
    • An integrated top-down and bottom-up strategy for characterization of protein isoforms and modifications
    • Wu, S., Tolic, N., Tian, Z., Robinson, E. W., Pasa-Tolic, L., An integrated top-down and bottom-up strategy for characterization of protein isoforms and modifications. Methods Mol. Biol. 2011, 694, 291-304.
    • (2011) Methods Mol. Biol. , vol.694 , pp. 291-304
    • Wu, S.1    Tolic, N.2    Tian, Z.3    Robinson, E.W.4    Pasa-Tolic, L.5
  • 30
    • 65249157969 scopus 로고    scopus 로고
    • An integrated top-down and bottom-up strategy for broadly characterizing protein isoforms and modifications
    • Wu, S., Lourette, N. M., Tolic, N., Zhao, R. et al., An integrated top-down and bottom-up strategy for broadly characterizing protein isoforms and modifications. J. Proteome. Res. 2009, 8, 1347-1357.
    • (2009) J. Proteome. Res. , vol.8 , pp. 1347-1357
    • Wu, S.1    Lourette, N.M.2    Tolic, N.3    Zhao, R.4
  • 31
    • 66349135588 scopus 로고    scopus 로고
    • Integrated workflow for characterizing intact phosphoproteins from complex mixtures
    • Wu, S., Yang, F., Zhao, R., Tolic, N. et al., Integrated workflow for characterizing intact phosphoproteins from complex mixtures. Anal. Chem. 2009, 81, 4210-4219.
    • (2009) Anal. Chem. , vol.81 , pp. 4210-4219
    • Wu, S.1    Yang, F.2    Zhao, R.3    Tolic, N.4
  • 33
    • 41449112363 scopus 로고    scopus 로고
    • Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags
    • Shen, Y., Tolic, N., Hixson, K. K., Purvine, S. O., et al., Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags. Anal. Chem. 2008, 80, 1871-1882.
    • (2008) Anal. Chem. , vol.80 , pp. 1871-1882
    • Shen, Y.1    Tolic, N.2    Hixson, K.K.3    Purvine, S.O.4
  • 35
    • 43349084842 scopus 로고    scopus 로고
    • Using ProSight PTM and related tools for targeted protein identification and characterization with high mass accuracy tandem MS data
    • Chapter 13, Unit 13.6.
    • Leduc, R. D., Kelleher, N. L., Using ProSight PTM and related tools for targeted protein identification and characterization with high mass accuracy tandem MS data. Curr. Protoc. Bioinformatics 2007, Chapter 13, Unit 13.6.
    • (2007) Curr. Protoc. Bioinformatics
    • Leduc, R.D.1    Kelleher, N.L.2
  • 36
    • 34547595546 scopus 로고    scopus 로고
    • ProSight PTM 2.0: improved protein identification and characterization for top down mass spectrometry
    • Zamdborg, L., LeDuc, R. D., Glowacz, K. J., Kim, Y. B., et al., ProSight PTM 2.0: improved protein identification and characterization for top down mass spectrometry. Nucleic Acids Res. 2007, 35(Web Server issue), W701-W706.
    • (2007) Nucleic Acids Res. , vol.35 , Issue.Web Server issue
    • Zamdborg, L.1    LeDuc, R.D.2    Glowacz, K.J.3    Kim, Y.B.4
  • 37
    • 3242887156 scopus 로고    scopus 로고
    • ProSight PTM: an integrated environment for protein identification and characterization by top-down mass spectrometry
    • LeDuc, R. D., Taylor, G. K., Kim, Y. B., Januszyk, T. E. et al., ProSight PTM: an integrated environment for protein identification and characterization by top-down mass spectrometry. Nucleic Acids Res. 2004, 32(Web Server issue), W340-W345.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.Web Server issue
    • LeDuc, R.D.1    Taylor, G.K.2    Kim, Y.B.3    Januszyk, T.E.4
  • 38
    • 77955441004 scopus 로고    scopus 로고
    • Identification of disulfide bonds in protein proteolytic degradation products using de novo-protein unique sequence tags approach
    • Shen, Y., Tolic, N., Purvine, S. O., Smith, R. D., Identification of disulfide bonds in protein proteolytic degradation products using de novo-protein unique sequence tags approach. J. Proteome Res. 2010, 9, 4053-4060.
    • (2010) J. Proteome Res. , vol.9 , pp. 4053-4060
    • Shen, Y.1    Tolic, N.2    Purvine, S.O.3    Smith, R.D.4
  • 39
    • 84862833002 scopus 로고    scopus 로고
    • Preclinical validation of salivary biomarkers for primary Sjogren's syndrome
    • Hu, S., Gao, K., Pollard, R., Arellano-Garcia, M. et al., Preclinical validation of salivary biomarkers for primary Sjogren's syndrome. Arthritis Care Res. (Hoboken) 2010, 62, 1633-1638.
    • (2010) Arthritis Care Res. (Hoboken) , vol.62 , pp. 1633-1638
    • Hu, S.1    Gao, K.2    Pollard, R.3    Arellano-Garcia, M.4
  • 41
    • 78649396351 scopus 로고    scopus 로고
    • Finding new posttranslational modifications in salivary proline-rich proteins
    • Vitorino, R., Alves, R., Barros, A., Caseiro, A. et al., Finding new posttranslational modifications in salivary proline-rich proteins. Proteomics 2010, 10, 3732-3742.
    • (2010) Proteomics , vol.10 , pp. 3732-3742
    • Vitorino, R.1    Alves, R.2    Barros, A.3    Caseiro, A.4
  • 42
    • 1642267482 scopus 로고    scopus 로고
    • Histatins: antimicrobial peptides with therapeutic potential
    • Kavanagh, K., Dowd, S., Histatins: antimicrobial peptides with therapeutic potential. J. Pharm. Pharmacol. 2004, 56, 285-289.
    • (2004) J. Pharm. Pharmacol. , vol.56 , pp. 285-289
    • Kavanagh, K.1    Dowd, S.2
  • 44
    • 0017348985 scopus 로고
    • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva
    • Schlesinger, D. H., Hay, D. I., Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva. J. Biol. Chem. 1977, 252, 1689-1695.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.