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Volumn 84, Issue 10, 2012, Pages 4383-4395

Defining intact protein primary structures from saliva: A step toward the human proteome project

Author keywords

[No Author keywords available]

Indexed keywords

ASSIGNMENT OF; COVALENT MODIFICATIONS; DATA SETS; ELECTRON-CAPTURE; HIGH RESOLUTION; HUMAN PROTEOME; INTACT PROTEINS; ION CYCLOTRON RESONANCE; ISOFORMS; ITERATIVE PROCESSING; LOW RESOLUTION; MASS ACCURACY; POST-TRANSLATIONAL MODIFICATIONS; PRIMARY STRUCTURES; PROTEIN SEQUENCES; QUADRUPOLES; SALIVARY PROTEINS; STRUCTURAL DIVERSITY; TIME-OF-FLIGHT INSTRUMENTS; TOPDOWN;

EID: 84861151967     PISSN: 00032700     EISSN: None     Source Type: Journal    
DOI: 10.1021/ac203337s     Document Type: Article
Times cited : (20)

References (62)
  • 1
    • 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 (2) 197-212
    • (2002) Crit. Rev. Oral Biol. Med. , vol.13 , Issue.2 , pp. 197-212
    • Kaufman, E.1    Lamster, I.B.2
  • 2
    • 0036215665 scopus 로고    scopus 로고
    • Saliva as a diagnostic fluid
    • Streckfus, C. F.; Bigler, L. R. Saliva as a diagnostic fluid Oral Dis. 2002, 8 (2) 69-76
    • (2002) Oral Dis. , vol.8 , Issue.2 , pp. 69-76
    • Streckfus, C.F.1    Bigler, L.R.2
  • 3
    • 14344257981 scopus 로고    scopus 로고
    • Toward defining the human parotid gland salivary proteome and peptidome: Identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry
    • Hardt, M.; Thomas, L. R.; Dixon, S. E.; Newport, G.; Agabian, N.; Prakobphol, A.; Hall, S. C.; Witkowska, H. E.; Fisher, S. J. Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry Biochemistry 2005, 44 (8) 2885-2899
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2885-2899
    • Hardt, M.1    Thomas, L.R.2    Dixon, S.E.3    Newport, G.4    Agabian, N.5    Prakobphol, A.6    Hall, S.C.7    Witkowska, H.E.8    Fisher, S.J.9
  • 4
    • 33644634632 scopus 로고    scopus 로고
    • Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis
    • Walz, A.; Stuhler, K.; Wattenberg, A.; Hawranke, E.; Meyer, H. E.; Schmalz, G.; Bluggel, M.; Ruhl, S. Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis Proteomics 2006, 6 (5) 1631-1639
    • (2006) Proteomics , vol.6 , Issue.5 , pp. 1631-1639
    • Walz, A.1    Stuhler, K.2    Wattenberg, A.3    Hawranke, E.4    Meyer, H.E.5    Schmalz, G.6    Bluggel, M.7    Ruhl, S.8
  • 6
    • 23044504427 scopus 로고    scopus 로고
    • Assessing the effects of diurnal variation on the composition of human parotid saliva: Quantitative analysis of native peptides using iTRAQ reagents
    • Hardt, M.; Witkowska, H. E.; Webb, S.; Thomas, L. R.; Dixon, S. E.; Hall, S. C.; Fisher, S. J. Assessing the effects of diurnal variation on the composition of human parotid saliva: quantitative analysis of native peptides using iTRAQ reagents Anal. Chem. 2005, 77 (15) 4947-4954
    • (2005) Anal. Chem. , vol.77 , Issue.15 , pp. 4947-4954
    • Hardt, M.1    Witkowska, H.E.2    Webb, S.3    Thomas, L.R.4    Dixon, S.E.5    Hall, S.C.6    Fisher, S.J.7
  • 8
    • 51349165234 scopus 로고    scopus 로고
    • Carbachol-induced in vitro secretion of certain human submandibular proteins investigated by mass-spectrometry
    • Cabras, T.; Castagnola, M.; Inzitari, R.; Ekstrom, J.; Isola, M.; Riva, A.; Messana, I. Carbachol-induced in vitro secretion of certain human submandibular proteins investigated by mass-spectrometry Arch. Oral Biol. 2008, 53 (11) 1077-1083
    • (2008) Arch. Oral Biol. , vol.53 , Issue.11 , pp. 1077-1083
    • Cabras, T.1    Castagnola, M.2    Inzitari, R.3    Ekstrom, J.4    Isola, M.5    Riva, A.6    Messana, I.7
  • 17
    • 11144228025 scopus 로고    scopus 로고
    • The coupling of RP-HPLC and ESI-MS in the study of small peptides and proteins secreted in vitro by human salivary glands that are soluble in acidic solution
    • Messana, I.; Loffredo, F.; Inzitari, R.; Cabras, T.; Giardina, B.; Onnis, G.; Piludu, M.; Castagnola, M. The coupling of RP-HPLC and ESI-MS in the study of small peptides and proteins secreted in vitro by human salivary glands that are soluble in acidic solution Eur. J. Morphol. 2003, 41 (2) 103-106
    • (2003) Eur. J. Morphol. , vol.41 , Issue.2 , pp. 103-106
    • Messana, I.1    Loffredo, F.2    Inzitari, R.3    Cabras, T.4    Giardina, B.5    Onnis, G.6    Piludu, M.7    Castagnola, M.8
  • 20
    • 50649088005 scopus 로고    scopus 로고
    • Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases
    • Helmerhorst, E. J.; Sun, X.; Salih, E.; Oppenheim, F. G. Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases J. Biol. Chem. 2008, 283 (29) 19957-19966
    • (2008) J. Biol. Chem. , vol.283 , Issue.29 , pp. 19957-19966
    • Helmerhorst, E.J.1    Sun, X.2    Salih, E.3    Oppenheim, F.G.4
  • 24
    • 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 (11) 1948-1963
    • (2008) J. Sep. Sci. , vol.31 , Issue.11 , pp. 1948-1963
    • Messana, I.1    Inzitari, R.2    Fanali, C.3    Cabras, T.4    Castagnola, M.5
  • 25
    • 40449087487 scopus 로고    scopus 로고
    • Analysis of peptides by separation and mass spectrometric methods
    • Messana, I.; Kasicka, V. Analysis of peptides by separation and mass spectrometric methods J. Sep. Sci. 2008, 31 (3) 425-426
    • (2008) J. Sep. Sci. , vol.31 , Issue.3 , pp. 425-426
    • Messana, I.1    Kasicka, V.2
  • 26
    • 1542267837 scopus 로고    scopus 로고
    • Targeted analysis and discovery of posttranslational modifications in proteins from methanogenic archaea by top-down MS
    • Forbes, A. J.; Patrie, S. M.; Taylor, G. K.; Kim, Y. B.; Jiang, L.; Kelleher, N. L. Targeted analysis and discovery of posttranslational modifications in proteins from methanogenic archaea by top-down MS Proc. Natl. Acad. Sci. U. S. A. 2004, 101 (9) 2678-2683
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.9 , pp. 2678-2683
    • Forbes, A.J.1    Patrie, S.M.2    Taylor, G.K.3    Kim, Y.B.4    Jiang, L.5    Kelleher, N.L.6
  • 27
    • 33646903914 scopus 로고    scopus 로고
    • ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and fingerprinting complex protein mixtures
    • Savitski, M. M.; Nielsen, M. L.; Zubarev, R. A. ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and fingerprinting complex protein mixtures Mol. Cell. Proteomics 2006, 5 (5) 935-948
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.5 , pp. 935-948
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 28
    • 24944544077 scopus 로고    scopus 로고
    • Precise and parallel characterization of coding polymorphisms, alternative splicing, and modifications in human proteins by mass spectrometry
    • Roth, M. J.; Forbes, A. J.; Boyne, M. T., 2nd; Kim, Y. B.; Robinson, D. E.; Kelleher, N. L. Precise and parallel characterization of coding polymorphisms, alternative splicing, and modifications in human proteins by mass spectrometry Mol. Cell. Proteomics 2005, 4 (7) 1002-1008
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.7 , pp. 1002-1008
    • Roth, M.J.1    Forbes, A.J.2    Boyne II, M.T.3    Kim, Y.B.4    Robinson, D.E.5    Kelleher, N.L.6
  • 29
    • 27844511528 scopus 로고    scopus 로고
    • New and automated MSn approaches for top-down identification of modified proteins
    • Zabrouskov, V.; Senko, M. W.; Du, Y.; Leduc, R. D.; Kelleher, N. L. New and automated MSn approaches for top-down identification of modified proteins J. Am. Soc. Mass Spectrom. 2005, 16 (12) 2027-2038
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , Issue.12 , pp. 2027-2038
    • Zabrouskov, V.1    Senko, M.W.2    Du, Y.3    Leduc, R.D.4    Kelleher, N.L.5
  • 31
  • 32
    • 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.; Bassilian, S.; Yan, W.; Wolinsky, L.; Loo, J. A.; Wong, D. T.; Faull, K. F. 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 (2-3) 190-197
    • (2007) Int. J. Mass Spectrom. , vol.268 , Issue.2-3 , pp. 190-197
    • Whitelegge, J.P.1    Zabrouskov, V.2    Halgand, F.3    Souda, P.4    Bassilian, S.5    Yan, W.6    Wolinsky, L.7    Loo, J.A.8    Wong, D.T.9    Faull, K.F.10
  • 33
  • 35
    • 0345866745 scopus 로고    scopus 로고
    • Prediction of posttranslational modifications using intact-protein mass spectrometric data
    • Holmes, M. R.; Giddings, M. C. Prediction of posttranslational modifications using intact-protein mass spectrometric data Anal. Chem. 2004, 76 (2) 276-282
    • (2004) Anal. Chem. , vol.76 , Issue.2 , pp. 276-282
    • Holmes, M.R.1    Giddings, M.C.2
  • 36
    • 0031279479 scopus 로고    scopus 로고
    • A novel system of human submandibular/sublingual saliva collection
    • Wolff, A.; Begleiter, A.; Moskona, D. A novel system of human submandibular/sublingual saliva collection J. Dent. Res. 1997, 76 (11) 1782-1786
    • (1997) J. Dent. Res. , vol.76 , Issue.11 , pp. 1782-1786
    • Wolff, A.1    Begleiter, A.2    Moskona, D.3
  • 37
    • 0012252011 scopus 로고    scopus 로고
    • Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: Cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus
    • Whitelegge, J. P.; Zhang, H.; Aguilera, R.; Taylor, R. M.; Cramer, W. A. Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus Mol. Cell. Proteomics 2002, 1 (10) 816-827
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.10 , pp. 816-827
    • Whitelegge, J.P.1    Zhang, H.2    Aguilera, R.3    Taylor, R.M.4    Cramer, W.A.5
  • 38
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge, J. P.; Gundersen, C. B.; Faull, K. F. Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins Protein Sci. 1998, 7 (6) 1423-1430
    • (1998) Protein Sci. , vol.7 , Issue.6 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 39
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P.; Fohlman, J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides Biomed. Mass Spectrom. 1984, 11 (11) 601
    • (1984) Biomed. Mass Spectrom. , vol.11 , Issue.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 40
    • 3242887156 scopus 로고    scopus 로고
    • ProSight PTM: An integrated environment for protein identification and characterization by top-down mass spectrometry
    • WEB SERVER ISSUE
    • LeDuc, R. D.; Taylor, G. K.; Kim, Y. B.; Januszyk, T. E.; Bynum, L. H.; Sola, J. V.; Garavelli, J. S.; Kelleher, N. L. ProSight PTM: an integrated environment for protein identification and characterization by top-down mass spectrometry Nucleic Acids Res. 2004, 32 (Web Server issue) W340-5
    • (2004) Nucleic Acids Res. , vol.32 , pp. 340-345
    • Leduc, R.D.1    Taylor, G.K.2    Kim, Y.B.3    Januszyk, T.E.4    Bynum, L.H.5    Sola, J.V.6    Garavelli, J.S.7    Kelleher, N.L.8
  • 41
    • 58149116970 scopus 로고    scopus 로고
    • Evaluation of gas-phase rearrangement and competing fragmentation reactions on protein phosphorylation site assignment using collision induced dissociation-MS/MS and MS3
    • Palumbo, A. M.; Reid, G. E. Evaluation of gas-phase rearrangement and competing fragmentation reactions on protein phosphorylation site assignment using collision induced dissociation-MS/MS and MS3 Anal. Chem. 2008, 80 (24) 9735-9747
    • (2008) Anal. Chem. , vol.80 , Issue.24 , pp. 9735-9747
    • Palumbo, A.M.1    Reid, G.E.2
  • 42
    • 39749196893 scopus 로고    scopus 로고
    • Mechanistic insights into the multistage gas-phase fragmentation behavior of phosphoserine- and phosphothreonine-containing peptides
    • Palumbo, A. M.; Tepe, J. J.; Reid, G. E. Mechanistic insights into the multistage gas-phase fragmentation behavior of phosphoserine- and phosphothreonine-containing peptides J. Proteome Res. 2008, 7 (2) 771-779
    • (2008) J. Proteome Res. , vol.7 , Issue.2 , pp. 771-779
    • Palumbo, A.M.1    Tepe, J.J.2    Reid, G.E.3
  • 44
    • 0032190208 scopus 로고    scopus 로고
    • Encoding of human basic and glycosylated proline-rich proteins by the PRB gene complex and proteolytic processing of their precursor proteins
    • Stubbs, M.; Chan, J.; Kwan, A.; So, J.; Barchynsky, U.; Rassouli-Rahsti, M.; Robinson, R.; Bennick, A. Encoding of human basic and glycosylated proline-rich proteins by the PRB gene complex and proteolytic processing of their precursor proteins Arch. Oral Biol. 1998, 43 (10) 753-770
    • (1998) Arch. Oral Biol. , vol.43 , Issue.10 , pp. 753-770
    • Stubbs, M.1    Chan, J.2    Kwan, A.3    So, J.4    Barchynsky, U.5    Rassouli-Rahsti, M.6    Robinson, R.7    Bennick, A.8
  • 46
    • 0038610834 scopus 로고    scopus 로고
    • Reactions of polypeptide ions with electrons in the gas phase
    • Zubarev, R. A. Reactions of polypeptide ions with electrons in the gas phase Mass Spectrom. Rev. 2003, 22 (1) 57-77
    • (2003) Mass Spectrom. Rev. , vol.22 , Issue.1 , pp. 57-77
    • Zubarev, R.A.1
  • 47
    • 26844524261 scopus 로고    scopus 로고
    • Data-dependent electron capture dissociation FT-ICR mass spectrometry for proteomic analyses
    • Cooper, H. J.; Akbarzadeh, S.; Heath, J. K.; Zeller, M. Data-dependent electron capture dissociation FT-ICR mass spectrometry for proteomic analyses J. Proteome Res. 2005, 4 (5) 1538-1544
    • (2005) J. Proteome Res. , vol.4 , Issue.5 , pp. 1538-1544
    • Cooper, H.J.1    Akbarzadeh, S.2    Heath, J.K.3    Zeller, M.4
  • 49
    • 33645125878 scopus 로고    scopus 로고
    • Observation of pronounced b*,y cleavages in the electron capture dissociation mass spectrometry of polyamidoamine (PAMAM) dendrimer ions with amide functionalities
    • Lee, S.; Han, S. Y.; Lee, T. G.; Chung, G.; Lee, D.; Oh, H. B. Observation of pronounced b*,y cleavages in the electron capture dissociation mass spectrometry of polyamidoamine (PAMAM) dendrimer ions with amide functionalities J. Am. Soc. Mass Spectrom. 2006, 17 (4) 536-543
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , Issue.4 , pp. 536-543
    • Lee, S.1    Han, S.Y.2    Lee, T.G.3    Chung, G.4    Lee, D.5    Oh, H.B.6
  • 50
    • 1642272372 scopus 로고    scopus 로고
    • Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry
    • Pesavento, J. J.; Kim, Y. B.; Taylor, G. K.; Kelleher, N. L. Shotgun annotation of histone modifications: a new approach for streamlined characterization of proteins by top down mass spectrometry J. Am. Chem. Soc. 2004, 126 (11) 3386-3387
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.11 , pp. 3386-3387
    • Pesavento, J.J.1    Kim, Y.B.2    Taylor, G.K.3    Kelleher, N.L.4
  • 53
    • 68949163674 scopus 로고    scopus 로고
    • Metabolite signal identification in accurate mass metabolomics data with MZedDB, an interactive m/z annotation tool utilising predicted ionisation behaviour 'rules'
    • Draper, J.; Enot, D. P.; Parker, D.; Beckmann, M.; Snowdon, S.; Lin, W.; Zubair, H. Metabolite signal identification in accurate mass metabolomics data with MZedDB, an interactive m/z annotation tool utilising predicted ionisation behaviour 'rules' BMC Bioinf. 2009, 10, 227
    • (2009) BMC Bioinf. , vol.10 , pp. 227
    • Draper, J.1    Enot, D.P.2    Parker, D.3    Beckmann, M.4    Snowdon, S.5    Lin, W.6    Zubair, H.7
  • 54
    • 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 (2) 162-169
    • (2001) J. Prosthet. Dent. , vol.85 , Issue.2 , pp. 162-169
    • Humphrey, S.P.1    Williamson, R.T.2
  • 55
    • 0026496892 scopus 로고
    • Engineering dehydrated amino acid residues in the antimicrobial peptide nisin
    • Kuipers, O. P.; Rollema, H. S.; Yap, W. M.; Boot, H. J.; Siezen, R. J.; de Vos, W. M. Engineering dehydrated amino acid residues in the antimicrobial peptide nisin J. Biol. Chem. 1992, 267 (34) 24340-24346
    • (1992) J. Biol. Chem. , vol.267 , Issue.34 , pp. 24340-24346
    • Kuipers, O.P.1    Rollema, H.S.2    Yap, W.M.3    Boot, H.J.4    Siezen, R.J.5    De Vos, W.M.6
  • 56
    • 0033560968 scopus 로고    scopus 로고
    • Post-translational modification of nisin. The involvement of NisB in the dehydration process
    • Karakas Sen, A.; Narbad, A.; Horn, N.; Dodd, H. M.; Parr, A. J.; Colquhoun, I.; Gasson, M. J. Post-translational modification of nisin. The involvement of NisB in the dehydration process Eur. J. Biochem. 1999, 261 (2) 524-532
    • (1999) Eur. J. Biochem. , vol.261 , Issue.2 , pp. 524-532
    • Karakas Sen, A.1    Narbad, A.2    Horn, N.3    Dodd, H.M.4    Parr, A.J.5    Colquhoun, I.6    Gasson, M.J.7
  • 57
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I.; Breukink, E.; van Kraaij, C.; Kuipers, O. P.; Bierbaum, G.; de Kruijff, B.; Sahl, H. G. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity J. Biol. Chem. 2001, 276 (3) 1772-1779
    • (2001) J. Biol. Chem. , vol.276 , Issue.3 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    Van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    De Kruijff, B.6    Sahl, H.G.7
  • 58
    • 0342602049 scopus 로고    scopus 로고
    • Identification of essential amino acids in phenylalanine ammonia-lyase by site-directed mutagenesis
    • Langer, B.; Rother, D.; Retey, J. Identification of essential amino acids in phenylalanine ammonia-lyase by site-directed mutagenesis Biochemistry 1997, 36 (36) 10867-10871
    • (1997) Biochemistry , vol.36 , Issue.36 , pp. 10867-10871
    • Langer, B.1    Rother, D.2    Retey, J.3
  • 59
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C.; Paul, M.; Xie, L.; van der Donk, W. A. Biosynthesis and mode of action of lantibiotics Chem. Rev. 2005, 105 (2) 633-684
    • (2005) Chem. Rev. , vol.105 , Issue.2 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 60
    • 80052092565 scopus 로고    scopus 로고
    • Nine post-translational modifications during the biosynthesis of cinnamycin
    • Okesli, A.; Cooper, L. E.; Fogle, E. J.; van der Donk, W. A. Nine post-translational modifications during the biosynthesis of cinnamycin J. Am. Chem. Soc. 2011, 133 (34) 13753-13760
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.34 , pp. 13753-13760
    • Okesli, A.1    Cooper, L.E.2    Fogle, E.J.3    Van Der Donk, W.A.4


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