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Volumn 10, Issue 3, 2011, Pages 1052-1061

Hexapeptide libraries for enhanced protein PTM identification and relative abundance profiling in whole human saliva

Author keywords

breast cancer; dynamic range compression proteomics; N linked glycoproteins; proteominer; saliva

Indexed keywords

GLYCOPEPTIDE; HEXAPEPTIDE; PEPTIDE LIBRARY;

EID: 79952415542     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100857t     Document Type: Article
Times cited : (45)

References (46)
  • 1
    • 63049100764 scopus 로고    scopus 로고
    • The art of observing rare protein species in proteomes with peptide ligand libraries
    • Boschetti, E.; Righetti, P. G. The art of observing rare protein species in proteomes with peptide ligand libraries Proteomics 2009, 9 (6) 1492-510
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1492-510
    • Boschetti, E.1    Righetti, P.G.2
  • 3
    • 33750112796 scopus 로고    scopus 로고
    • Protein Equalizer Technology: The quest for a democratic proteome
    • Righetti, P. G.; Boschetti, E.; Lomas, L.; Citterio, A. Protein Equalizer Technology: the quest for a democratic proteome Proteomics 2006, 6 (14) 3980-92
    • (2006) Proteomics , vol.6 , Issue.14 , pp. 3980-92
    • Righetti, P.G.1    Boschetti, E.2    Lomas, L.3    Citterio, A.4
  • 4
    • 20544478148 scopus 로고    scopus 로고
    • Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands
    • DOI 10.1002/elps.200500147
    • Thulasiraman, V.; Lin, S.; Gheorghiu, L.; Lathrop, J.; Lomas, L.; Hammond, D.; Boschetti, E. Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands Electrophoresis 2005, 26 (18) 3561-71 (Pubitemid 41410379)
    • (2005) Electrophoresis , vol.26 , Issue.18 , pp. 3561-3571
    • Thulasiraman, V.1    Lin, S.2    Gheorghiu, L.3    Lathrop, J.4    Lomas, L.5    Hammond, D.6    Boschetti, E.7
  • 6
    • 71549145619 scopus 로고    scopus 로고
    • A dynamic range compression and three-dimensional peptide fractionation analysis platform expands proteome coverage and the diagnostic potential of whole saliva
    • Bandhakavi, S.; Stone, M. D.; Onsongo, G.; Van Riper, S. K.; Griffin, T. J. A dynamic range compression and three-dimensional peptide fractionation analysis platform expands proteome coverage and the diagnostic potential of whole saliva J. Proteome Res. 2009, 8 (12) 5590-600
    • (2009) J. Proteome Res. , vol.8 , Issue.12 , pp. 5590-600
    • Bandhakavi, S.1    Stone, M.D.2    Onsongo, G.3    Van Riper, S.K.4    Griffin, T.J.5
  • 7
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • Helenius, A.; Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 2004, 73, 1019-49 (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 8
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • DOI 10.1111/j.1432-1033.1993.tb18347.x
    • Lis, H.; Sharon, N. Protein glycosylation. Structural and functional aspects Eur. J. Biochem. 1993, 218 (1) 1-27 (Pubitemid 23350356)
    • (1993) European Journal of Biochemistry , vol.218 , Issue.1 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 9
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • DOI 10.1016/S0076-6879(05)05007-X, PII S007668790505007X, Mass Spectrometry: Modified Proteins and Glycoconjugates
    • Peter-Katalinic, J. Methods in enzymology: O-glycosylation of proteins Methods Enzymol. 2005, 405, 139-71 (Pubitemid 43081959)
    • (2006) Methods in Enzymology , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 10
    • 77949822351 scopus 로고    scopus 로고
    • Combinatorial peptide libraries facilitate development of multiple reaction monitoring assays for low-abundance proteins
    • Drabovich, A. P.; Diamandis, E. P. Combinatorial peptide libraries facilitate development of multiple reaction monitoring assays for low-abundance proteins J. Proteome Res. 2010, 9 (3) 1236-45
    • (2010) J. Proteome Res. , vol.9 , Issue.3 , pp. 1236-45
    • Drabovich, A.P.1    Diamandis, E.P.2
  • 11
    • 72049093356 scopus 로고    scopus 로고
    • Combinatorial hexapeptide ligand libraries (ProteoMiner): An innovative fractionation tool for differential quantitative clinical proteomics
    • Hartwig, S.; Czibere, A.; Kotzka, J.; Passlack, W.; Haas, R.; Eckel, J.; Lehr, S. Combinatorial hexapeptide ligand libraries (ProteoMiner): an innovative fractionation tool for differential quantitative clinical proteomics Arch. Physiol. Biochem. 2009, 115 (3) 155-60
    • (2009) Arch. Physiol. Biochem. , vol.115 , Issue.3 , pp. 155-60
    • Hartwig, S.1    Czibere, A.2    Kotzka, J.3    Passlack, W.4    Haas, R.5    Eckel, J.6    Lehr, S.7
  • 12
    • 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 (3) 170-4
    • (2002) J. Can. Dent. Assoc. , vol.68 , Issue.3 , pp. 170-4
    • Lawrence, H.P.1
  • 13
    • 33645035375 scopus 로고    scopus 로고
    • Salivary diagnostics powered by nanotechnologies, proteomics and genomics
    • Wong, D. T. Salivary diagnostics powered by nanotechnologies, proteomics and genomics J. Am. Dent. Assoc. 2006, 137 (3) 313-21 (Pubitemid 43416224)
    • (2006) Journal of the American Dental Association , vol.137 , Issue.3 , pp. 313-321
    • Wong, D.T.1
  • 15
    • 30744469116 scopus 로고    scopus 로고
    • Salivary agglutinin and lung scavenger receptor cysteine-rich glycoprotein 340 have broad anti-influenza activities and interactions with surfactant protein D that vary according to donor source and sialylation
    • DOI 10.1042/BJ20050695
    • Hartshorn, K. L.; Ligtenberg, A.; White, M. R.; Van Eijk, M.; Hartshorn, M.; Pemberton, L.; Holmskov, U.; Crouch, E. Salivary agglutinin and lung scavenger receptor cysteine-rich glycoprotein 340 have broad anti-influenza activities and interactions with surfactant protein D that vary according to donor source and sialylation Biochem. J. 2006, 393 (Pt 2) 545-53 (Pubitemid 43099094)
    • (2006) Biochemical Journal , vol.393 , Issue.2 , pp. 545-553
    • Hartshorn, K.L.1    Ligtenberg, A.2    White, M.R.3    Van Eijk, M.4    Hartshorn, M.5    Pemberton, L.6    Holmskov, U.7    Crouch, E.8
  • 16
    • 0022376312 scopus 로고
    • Masticatory lubrication. The role of carbohydrate in the lubricating property of a salivary glycoprotein-albumin complex
    • Hatton, M. N.; Loomis, R. E.; Levine, M. J.; Tabak, L. A. Masticatory lubrication. The role of carbohydrate in the lubricating property of a salivary glycoprotein-albumin complex Biochem. J. 1985, 230 (3) 817-20 (Pubitemid 16236343)
    • (1985) Biochemical Journal , vol.230 , Issue.3 , pp. 817-820
    • Hatton, M.N.1    Loomis, R.E.2    Levine, M.J.3    Tabak, L.A.4
  • 17
    • 0023203158 scopus 로고
    • Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva
    • DOI 10.1016/0003-9861(87)90366-3
    • Loomis, R. E.; Prakobphol, A.; Levine, M. J.; Reddy, M. S.; Jones, P. C. Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva Arch. Biochem. Biophys. 1987, 258 (2) 452-64 (Pubitemid 17155019)
    • (1987) Archives of Biochemistry and Biophysics , vol.258 , Issue.2 , pp. 452-464
    • Loomis, R.E.1    Prakobphol, A.2    Levine, M.J.3    Reddy, M.S.4    Jones, P.C.5
  • 18
    • 0017715265 scopus 로고
    • Role of sialic acid in saliva-induced aggregation of Streptococcus sanguis
    • McBride, B. C.; Gisslow, M. T. Role of sialic acid in saliva-induced aggregation of Streptococcus sanguis Infect. Immun. 1977, 18 (1) 35-40 (Pubitemid 8203216)
    • (1977) Infection and Immunity , vol.18 , Issue.1 , pp. 35-40
    • McBride, B.C.1    Gisslow, M.T.2
  • 19
    • 0033602996 scopus 로고    scopus 로고
    • Separate oligosaccharide determinants mediate interactions of the low-molecular-weight salivary mucin with neutrophils and bacteria
    • Prakobphol, A.; Tangemann, K.; Rosen, S. D.; Hoover, C. I.; Leffler, H.; Fisher, S. J. Separate oligosaccharide determinants mediate interactions of the low-molecular-weight salivary mucin with neutrophils and bacteria Biochemistry 1999, 38 (21) 6817-25
    • (1999) Biochemistry , vol.38 , Issue.21 , pp. 6817-25
    • Prakobphol, A.1    Tangemann, K.2    Rosen, S.D.3    Hoover, C.I.4    Leffler, H.5    Fisher, S.J.6
  • 20
    • 33846488076 scopus 로고    scopus 로고
    • Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics
    • DOI 10.1074/mcp.T60006-MCP200
    • Sun, B.; Ranish, J. A.; Utleg, A. G.; White, J. T.; Yan, X.; Lin, B.; Hood, L. Shotgun glycopeptide capture approach coupled with mass spectrometry for comprehensive glycoproteomics Mol. Cell. Proteomics 2007, 6 (1) 141-9 (Pubitemid 46152699)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.1 , pp. 141-149
    • Sun, B.1    Ranish, J.A.2    Utleg, A.G.3    White, J.T.4    Yan, X.5    Lin, B.6    Hood, L.7
  • 21
    • 34547800600 scopus 로고    scopus 로고
    • Isolation of N-linked glycopeptides from plasma
    • DOI 10.1021/ac0623181
    • Zhou, Y.; Aebersold, R.; Zhang, H. Isolation of N-linked glycopeptides from plasma Anal. Chem. 2007, 79 (15) 5826-37 (Pubitemid 47229834)
    • (2007) Analytical Chemistry , vol.79 , Issue.15 , pp. 5826-5837
    • Zhou, Y.1    Aebersold, R.2    Zhang, H.3
  • 22
    • 14144249198 scopus 로고    scopus 로고
    • NF-κB dependent cytokine levels in saliva of patients with oral preneoplastic lesions and oral squamous cell carcinoma
    • DOI 10.1016/j.cdp.2004.10.003
    • Rhodus, N. L.; Ho, V.; Miller, C. S.; Myers, S.; Ondrey, F. NF-kappaB dependent cytokine levels in saliva of patients with oral preneoplastic lesions and oral squamous cell carcinoma Cancer Detect. Prev. 2005, 29 (1) 42-5 (Pubitemid 40283497)
    • (2005) Cancer Detection and Prevention , vol.29 , Issue.1 , pp. 42-45
    • Rhodus, N.L.1    Ho, V.2    Miller, C.S.3    Myers, S.4    Ondrey, F.5
  • 23
    • 0037317228 scopus 로고    scopus 로고
    • Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • DOI 10.1021/ac026117i
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics Anal. Chem. 2003, 75 (3) 663-70 (Pubitemid 36176744)
    • (2003) Analytical Chemistry , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 24
    • 77954366021 scopus 로고    scopus 로고
    • Quantitative analysis of mTRAQ-labeled proteome using full MS scans
    • Kang, U. B.; Yeom, J.; Kim, H.; Lee, C. Quantitative analysis of mTRAQ-labeled proteome using full MS scans J. Proteome Res. 2010, 9 (7) 3750-8
    • (2010) J. Proteome Res. , vol.9 , Issue.7 , pp. 3750-8
    • Kang, U.B.1    Yeom, J.2    Kim, H.3    Lee, C.4
  • 26
    • 0344737959 scopus 로고    scopus 로고
    • Automated Statistical Analysis of Protein Abundance Ratios from Data Generated by Stable-Isotope Dilution and Tandem Mass Spectrometry
    • DOI 10.1021/ac034633i
    • Li, X. J.; Zhang, H.; Ranish, J. A.; Aebersold, R. Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry Anal. Chem. 2003, 75 (23) 6648-57 (Pubitemid 37493927)
    • (2003) Analytical Chemistry , vol.75 , Issue.23 , pp. 6648-6657
    • Li, X.-J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 27
    • 45449086085 scopus 로고    scopus 로고
    • Hsf1 activation inhibits rapamycin resistance and TOR signaling in yeast revealed by combined proteomic and genetic analysis
    • Bandhakavi, S.; Xie, H.; OCallaghan, B.; Sakurai, H.; Kim, D. H.; Griffin, T. J. Hsf1 activation inhibits rapamycin resistance and TOR signaling in yeast revealed by combined proteomic and genetic analysis PLoS One 2008, 3 (2) e1598
    • (2008) PLoS One , vol.3 , Issue.2 , pp. 1598
    • Bandhakavi, S.1    Xie, H.2    Ocallaghan, B.3    Sakurai, H.4    Kim, D.H.5    Griffin, T.J.6
  • 29
    • 74849087123 scopus 로고    scopus 로고
    • Interaction among proteins and peptide libraries in proteome analysis: PH involvement for a larger capture of species
    • Fasoli, E.; Farinazzo, A.; Sun, C. J.; Kravchuk, A. V.; Guerrier, L.; Fortis, F.; Boschetti, E.; Righetti, P. G. Interaction among proteins and peptide libraries in proteome analysis: pH involvement for a larger capture of species J. Proteomics 2010, 73 (4) 733-42
    • (2010) J. Proteomics , vol.73 , Issue.4 , pp. 733-42
    • Fasoli, E.1    Farinazzo, A.2    Sun, C.J.3    Kravchuk, A.V.4    Guerrier, L.5    Fortis, F.6    Boschetti, E.7    Righetti, P.G.8
  • 30
    • 77953575828 scopus 로고    scopus 로고
    • The proteome buccaneers: How to unearth your treasure chest via combinatorial peptide ligand libraries
    • Righetti, P. G.; Boschetti, E.; Kravchuk, A. V.; Fasoli, E. The proteome buccaneers: how to unearth your treasure chest via combinatorial peptide ligand libraries Expert Rev. Proteomics 2010, 7 (3) 373-85
    • (2010) Expert Rev. Proteomics , vol.7 , Issue.3 , pp. 373-85
    • Righetti, P.G.1    Boschetti, E.2    Kravchuk, A.V.3    Fasoli, E.4
  • 31
    • 34250014373 scopus 로고    scopus 로고
    • Solid-phase extraction of N-linked glycopeptides
    • DOI 10.1038/nprot.2007.42, PII NPROT.2007.42
    • Tian, Y.; Zhou, Y.; Elliott, S.; Aebersold, R.; Zhang, H. Solid-phase extraction of N-linked glycopeptides Nat. Protoc. 2007, 2 (2) 334-9 (Pubitemid 47040048)
    • (2007) Nature Protocols , vol.2 , Issue.2 , pp. 334-339
    • Tian, Y.1    Zhou, Y.2    Elliott, S.3    Aebersold, R.4    Zhang, H.5
  • 32
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • DOI 10.1038/nbt827
    • Zhang, H.; Li, X. J.; Martin, D. B.; Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat. Biotechnol. 2003, 21 (6) 660-6 (Pubitemid 36638093)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 33
    • 78649297298 scopus 로고    scopus 로고
    • ProteoMiner() and SELDI-TOF-MS: A robust and highly reproducible combination for biomarker discovery from whole blood serum
    • Frobel, J.; Hartwig, S.; Passlack, W.; Eckel, J.; Haas, R.; Czibere, A.; Lehr, S., ProteoMiner() and SELDI-TOF-MS: A robust and highly reproducible combination for biomarker discovery from whole blood serum. Arch Physiol Biochem. 2010, 116 (4-5), 174 - 80.
    • (2010) Arch Physiol Biochem. , vol.116 , Issue.4-5 , pp. 174-180
    • Frobel, J.1    Hartwig, S.2    Passlack, W.3    Eckel, J.4    Haas, R.5    Czibere, A.6    Lehr, S.7
  • 34
    • 38949159130 scopus 로고    scopus 로고
    • Breast cancer related proteins are present in saliva and are modulated secondary to ductal carcinoma in situ of the breast
    • DOI 10.1080/07357900701783883, PII 789439485
    • Streckfus, C. F.; Mayorga-Wark, O.; Arreola, D.; Edwards, C.; Bigler, L.; Dubinsky, W. P. Breast cancer related proteins are present in saliva and are modulated secondary to ductal carcinoma in situ of the breast Cancer Invest. 2008, 26 (2) 159-67 (Pubitemid 351225470)
    • (2008) Cancer Investigation , vol.26 , Issue.2 , pp. 159-167
    • Streckfus, C.F.1    Mayorga-Wark, O.2    Arreola, D.3    Edwards, C.4    Bigler, L.5    Dubinsky, W.P.6
  • 35
    • 75449116517 scopus 로고    scopus 로고
    • A Comparison of the Proteomic Expression in Pooled Saliva Specimens from Individuals Diagnosed with Ductal Carcinoma of the Breast with and without Lymph Node Involvement
    • Streckfus, C. F.; Storthz, K. A.; Bigler, L.; Dubinsky, W. P. A Comparison of the Proteomic Expression in Pooled Saliva Specimens from Individuals Diagnosed with Ductal Carcinoma of the Breast with and without Lymph Node Involvement J. Oncol. 2009, 2009, 737619
    • (2009) J. Oncol. , vol.2009 , pp. 737619
    • Streckfus, C.F.1    Storthz, K.A.2    Bigler, L.3    Dubinsky, W.P.4
  • 36
    • 61349189010 scopus 로고    scopus 로고
    • CD44 variant isoforms promote metastasis formation by a tumor cell-matrix cross-talk that supports adhesion and apoptosis resistance
    • Klingbeil, P.; Marhaba, R.; Jung, T.; Kirmse, R.; Ludwig, T.; Zoller, M. CD44 variant isoforms promote metastasis formation by a tumor cell-matrix cross-talk that supports adhesion and apoptosis resistance Mol. Cancer Res. 2009, 7 (2) 168-79
    • (2009) Mol. Cancer Res. , vol.7 , Issue.2 , pp. 168-79
    • Klingbeil, P.1    Marhaba, R.2    Jung, T.3    Kirmse, R.4    Ludwig, T.5    Zoller, M.6
  • 38
    • 1542346401 scopus 로고    scopus 로고
    • Mammaglobin: A candidate diagnostic marker for breast cancer
    • DOI 10.1016/j.clinbiochem.2003.11.005, PII S0009912003002236
    • Zehentner, B. K.; Carter, D. Mammaglobin: a candidate diagnostic marker for breast cancer Clin. Biochem. 2004, 37 (4) 249-57 (Pubitemid 38314877)
    • (2004) Clinical Biochemistry , vol.37 , Issue.4 , pp. 249-257
    • Zehentner, B.K.1    Carter, D.2
  • 39
    • 19344371357 scopus 로고    scopus 로고
    • Human tissue kallikrein gene family: Applications in cancer
    • DOI 10.1016/j.canlet.2004.09.024, PII S030438350400730X
    • Obiezu, C. V.; Diamandis, E. P. Human tissue kallikrein gene family: applications in cancer Cancer Lett. 2005, 224 (1) 1-22 (Pubitemid 40720363)
    • (2005) Cancer Letters , vol.224 , Issue.1 , pp. 1-22
    • Obiezu, C.V.1    Diamandis, E.P.2
  • 41
    • 16844384058 scopus 로고    scopus 로고
    • Emerging role of RAB GTPases in cancer and human disease
    • DOI 10.1158/0008-5472.CAN-05-0573
    • Cheng, K. W.; Lahad, J. P.; Gray, J. W.; Mills, G. B. Emerging role of RAB GTPases in cancer and human disease Cancer Res. 2005, 65 (7) 2516-9 (Pubitemid 40490043)
    • (2005) Cancer Research , vol.65 , Issue.7 , pp. 2516-2519
    • Cheng, K.W.1    Lahad, J.P.2    Gray, J.W.3    Mills, G.B.4
  • 43
    • 77956614939 scopus 로고    scopus 로고
    • Selectins promote tumor metastasis
    • Laubli, H.; Borsig, L. Selectins promote tumor metastasis Semin. Cancer Biol. 2010, 20 (3) 169-77
    • (2010) Semin. Cancer Biol. , vol.20 , Issue.3 , pp. 169-77
    • Laubli, H.1    Borsig, L.2
  • 44
    • 2042498844 scopus 로고    scopus 로고
    • RT-PCR for Mammaglobin Genes, MGB1 and MGB2, Identifies Breast Cancer Micrometastases in Sentinel Lymph Nodes
    • DOI 10.1309/MMAC-TXT5-5L8Q-TKC1
    • Ouellette, R. J.; Richard, D.; Maicas, E. RT-PCR for mammaglobin genes, MGB1 and MGB2, identifies breast cancer micrometastases in sentinel lymph nodes Am. J. Clin. Pathol. 2004, 121 (5) 637-43 (Pubitemid 38533995)
    • (2004) American Journal of Clinical Pathology , vol.121 , Issue.5 , pp. 637-643
    • Ouellette, R.J.1    Richard, D.2    Maicas, E.3
  • 45
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • DOI 10.1021/pr050492k
    • Ramachandran, P.; Boontheung, P.; Xie, Y.; Sondej, M.; Wong, D. T.; Loo, J. A. Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry J. Proteome Res. 2006, 5 (6) 1493-503 (Pubitemid 43865819)
    • (2006) Journal of Proteome Research , vol.5 , Issue.6 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4    Wong, D.T.5    Loo, J.A.6
  • 46
    • 62549163033 scopus 로고    scopus 로고
    • Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry
    • Ramachandran, P. B., P; Pang, E; Yan, W; Wong, D. T.; Loo, J. A. Comparison of N-linked glycoproteins in human whole saliva, parotid, submandibular, and sublingual glandular secretions identified using hydrazide chemistry and mass spectrometry Clin. Proteomics 2008, 4, 80-104
    • (2008) Clin. Proteomics , vol.4 , pp. 80-104
    • Ramachandran, P.B..P.1    Pang, E.2    Yan, W.3    Wong, D.T.4    Loo, J.A.5


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