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Volumn 14, Issue 13-14, 2014, Pages 1698-1709

Characterization of lacrimal proline-rich protein 4 (PRR4) in human tear proteome

Author keywords

Biomedicine; Gel electrophoresis; MS; Proline rich protein 4; PTMs; Tear fluid

Indexed keywords

PROLINE RICH PROTEIN; PROLINE RICH PROTEIN 4; PROTEOME; PYROGLUTAMIC ACID; UNCLASSIFIED DRUG; ISOPROTEIN; LACRIMAL PROLINE RICH 4 PROTEIN, HUMAN; PROTEIN;

EID: 84903955214     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300039     Document Type: Article
Times cited : (28)

References (73)
  • 1
    • 0029131474 scopus 로고
    • A major human lacrimal gland mRNA encodes a new proline-rich protein family member
    • Dickinson, D. P., Thiesse, M., A major human lacrimal gland mRNA encodes a new proline-rich protein family member. Invest. Ophthalmol. Vis. Sci. 1995, 36, 2020-2031.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 2020-2031
    • Dickinson, D.P.1    Thiesse, M.2
  • 2
    • 20444460241 scopus 로고    scopus 로고
    • The lacrimal gland transcriptome is an unusually rich source of rare and poorly characterized gene transcripts
    • Ozyildirim, A. M., Wistow, G. J., Gao, J., Wang, J. et al., The lacrimal gland transcriptome is an unusually rich source of rare and poorly characterized gene transcripts. Invest. Ophthalmol. Vis. Sci. 2005, 46, 1572-1580.
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 1572-1580
    • Ozyildirim, A.M.1    Wistow, G.J.2    Gao, J.3    Wang, J.4
  • 3
    • 77955216637 scopus 로고    scopus 로고
    • Proline-rich salivary proteins have extended conformations
    • Boze, H., Marlin, T., Durand, D., Perez, J. et al., Proline-rich salivary proteins have extended conformations. Biophys J. 2010, 99, 656-665.
    • (2010) Biophys J. , vol.99 , pp. 656-665
    • Boze, H.1    Marlin, T.2    Durand, D.3    Perez, J.4
  • 4
    • 0026699260 scopus 로고
    • Influence of saliva on aggregation and adherence of Streptococcus gordonii HG 222
    • Ligtenberg, A. J., Walgreen-Weterings, E., Veerman, E. C., de Soet, J. J. et al., Influence of saliva on aggregation and adherence of Streptococcus gordonii HG 222. Infect. Immun. 1992, 60, 3878-3884.
    • (1992) Infect. Immun. , vol.60 , pp. 3878-3884
    • Ligtenberg, A.J.1    Walgreen-Weterings, E.2    Veerman, E.C.3    de Soet, J.J.4
  • 5
    • 0024672611 scopus 로고
    • Bacterial adhesion to oral tissues: a model for infectious diseases
    • Gibbons, R. J., Bacterial adhesion to oral tissues: a model for infectious diseases. J. Dent. Res. 1989, 68, 750-760.
    • (1989) J. Dent. Res. , vol.68 , pp. 750-760
    • Gibbons, R.J.1
  • 6
    • 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, 817-820.
    • (1985) Biochem J. , vol.230 , pp. 817-820
    • Hatton, M.N.1    Loomis, R.E.2    Levine, M.J.3    Tabak, L.A.4
  • 7
    • 16244363069 scopus 로고    scopus 로고
    • SELDI-TOF-MS ProteinChip array profiling of tears from patients with dry eye
    • Grus, F. H., Podust, V. N., Bruns, K., Lackner, K. et al., SELDI-TOF-MS ProteinChip array profiling of tears from patients with dry eye. Invest. Ophthalmol. Vis. Sci. 2005, 46, 863-876.
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 863-876
    • Grus, F.H.1    Podust, V.N.2    Bruns, K.3    Lackner, K.4
  • 8
    • 84875666688 scopus 로고    scopus 로고
    • Alterations in the tear proteome of dry eye patients-a matter of the clinical phenotype
    • Boehm, N., Funke, S., Wiegand, M., Wehrwein, N. et al., Alterations in the tear proteome of dry eye patients-a matter of the clinical phenotype. Invest. Ophthalmol. Vis. Sci. 2013, 54, 2385-2392.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 2385-2392
    • Boehm, N.1    Funke, S.2    Wiegand, M.3    Wehrwein, N.4
  • 9
    • 77958194106 scopus 로고    scopus 로고
    • Two dimensional electrophoretic analysis of human tears: collection method in dry eye syndrome
    • Saijyothi, A. V., Angayarkanni, N., Syama, C., Utpal, T. et al., Two dimensional electrophoretic analysis of human tears: collection method in dry eye syndrome. Electrophoresis 2010, 31, 3420-3427.
    • (2010) Electrophoresis , vol.31 , pp. 3420-3427
    • Saijyothi, A.V.1    Angayarkanni, N.2    Syama, C.3    Utpal, T.4
  • 10
    • 84871262504 scopus 로고    scopus 로고
    • Lacrimal proline rich 4 (LPRR4) protein in the tear fluid is a potential biomarker of dry eye syndrome
    • Aluru, S. V., Agarwal, S., Srinivasan, B., Iyer, G. K. et al., Lacrimal proline rich 4 (LPRR4) protein in the tear fluid is a potential biomarker of dry eye syndrome. PloS One 2012, 7, e51979.
    • (2012) PloS One , vol.7
    • Aluru, S.V.1    Agarwal, S.2    Srinivasan, B.3    Iyer, G.K.4
  • 11
    • 77449142484 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomic analyses in contact lens-related dry eye
    • Nichols, J. J., Green-Church, K. B., Mass spectrometry-based proteomic analyses in contact lens-related dry eye. Cornea 2009, 28, 1109-1117.
    • (2009) Cornea , vol.28 , pp. 1109-1117
    • Nichols, J.J.1    Green-Church, K.B.2
  • 12
    • 84866989207 scopus 로고    scopus 로고
    • Proteomics of tear fluid in thyroid-associated orbitopathy
    • Matheis, N., Okrojek, R., Grus, F. H., Kahaly, G. J., Proteomics of tear fluid in thyroid-associated orbitopathy. Thyroid 2012, 22, 1039-1045.
    • (2012) Thyroid , vol.22 , pp. 1039-1045
    • Matheis, N.1    Okrojek, R.2    Grus, F.H.3    Kahaly, G.J.4
  • 13
    • 84858751820 scopus 로고    scopus 로고
    • Quantitative analysis of proteins in the tear fluid of patients with diabetic retinopathy
    • Csosz, E., Boross, P., Csutak, A., Berta, A. et al., Quantitative analysis of proteins in the tear fluid of patients with diabetic retinopathy. J. Proteomics 2012, 75, 2196-2204.
    • (2012) J. Proteomics , vol.75 , pp. 2196-2204
    • Csosz, E.1    Boross, P.2    Csutak, A.3    Berta, A.4
  • 14
    • 80052635233 scopus 로고    scopus 로고
    • Changes in tear protein profile in keratoconus disease
    • Acera, A., Vecino, E., Rodriguez-Agirretxe, I., Aloria, K. et al., Changes in tear protein profile in keratoconus disease. Eye 2011, 25, 1225-1233.
    • (2011) Eye , vol.25 , pp. 1225-1233
    • Acera, A.1    Vecino, E.2    Rodriguez-Agirretxe, I.3    Aloria, K.4
  • 15
    • 59149094098 scopus 로고    scopus 로고
    • Differential gene expression in human conducting airway surface epithelia and submucosal glands
    • Fischer, A. J., Goss, K. L., Scheetz, T. E., Wohlford-Lenane, C. L. et al., Differential gene expression in human conducting airway surface epithelia and submucosal glands. Am. J. Respir. Cell Mol. Biol. 2009, 40, 189-199.
    • (2009) Am. J. Respir. Cell Mol. Biol. , vol.40 , pp. 189-199
    • Fischer, A.J.1    Goss, K.L.2    Scheetz, T.E.3    Wohlford-Lenane, C.L.4
  • 16
    • 0030307256 scopus 로고    scopus 로고
    • Temporal and compositional characteristics of salivary protein adsorption to hydroxyapatite
    • Lamkin, M. S., Arancillo, A. A., Oppenheim, F. G., Temporal and compositional characteristics of salivary protein adsorption to hydroxyapatite. J. Dent. Res. 1996, 75, 803-808.
    • (1996) J. Dent. Res. , vol.75 , pp. 803-808
    • Lamkin, M.S.1    Arancillo, A.A.2    Oppenheim, F.G.3
  • 17
    • 38049018400 scopus 로고    scopus 로고
    • Protein expression in sputum of smokers and chronic obstructive pulmonary disease patients: a pilot study by CapLC-ESI-Q-TOF
    • Casado, B., Iadarola, P., Pannell, L. K., Luisetti, M. et al., Protein expression in sputum of smokers and chronic obstructive pulmonary disease patients: a pilot study by CapLC-ESI-Q-TOF. J. Proteome Res. 2007, 6, 4615-4623.
    • (2007) J. Proteome Res. , vol.6 , pp. 4615-4623
    • Casado, B.1    Iadarola, P.2    Pannell, L.K.3    Luisetti, M.4
  • 18
    • 77956907697 scopus 로고    scopus 로고
    • Identification of some human genes oppositely regulated during esophageal squamous cell carcinoma formation and human embryonic esophagus development
    • Zinovyeva, M. V., Monastyrskaya, G. S., Kopantzev, E. P., Vinogradova, T. V. et al., Identification of some human genes oppositely regulated during esophageal squamous cell carcinoma formation and human embryonic esophagus development. Dis. Esophagus. 2010, 23, 260-270.
    • (2010) Dis. Esophagus. , vol.23 , pp. 260-270
    • Zinovyeva, M.V.1    Monastyrskaya, G.S.2    Kopantzev, E.P.3    Vinogradova, T.V.4
  • 19
    • 84867400675 scopus 로고    scopus 로고
    • Tear analysis in ocular surface diseases
    • Zhou, L., Beuerman, R. W., Tear analysis in ocular surface diseases. Prog. Retin. Eye Res. 2012, 31, 527-550.
    • (2012) Prog. Retin. Eye Res. , vol.31 , pp. 527-550
    • Zhou, L.1    Beuerman, R.W.2
  • 20
    • 84861675757 scopus 로고    scopus 로고
    • Longitudinal analysis of taurine induced effects on the tear proteome of contact lens wearers and dry eye patients using a RP-RP-Capillary-HPLC-MALDI TOF/TOF MS approach
    • Funke, S., Azimi, D., Wolters, D., Grus, F. H. et al., Longitudinal analysis of taurine induced effects on the tear proteome of contact lens wearers and dry eye patients using a RP-RP-Capillary-HPLC-MALDI TOF/TOF MS approach. J. Proteomics 2012, 75, 3177-3190.
    • (2012) J. Proteomics , vol.75 , pp. 3177-3190
    • Funke, S.1    Azimi, D.2    Wolters, D.3    Grus, F.H.4
  • 21
    • 78149486003 scopus 로고    scopus 로고
    • Proteomic analysis of the tear film in patients with keratoconus
    • Lema, I., Brea, D., Rodriguez-Gonzalez, R., Diez-Feijoo, E. et al., Proteomic analysis of the tear film in patients with keratoconus. Mol. Vis. 2010, 16, 2055-2061.
    • (2010) Mol. Vis. , vol.16 , pp. 2055-2061
    • Lema, I.1    Brea, D.2    Rodriguez-Gonzalez, R.3    Diez-Feijoo, E.4
  • 22
    • 61849105281 scopus 로고    scopus 로고
    • Elevation of human alpha-defensins and S100 calcium-binding proteins A8 and A9 in tear fluid of patients with pterygium
    • Zhou, L., Beuerman, R. W., Ang, L. P., Chan, C. M. et al., Elevation of human alpha-defensins and S100 calcium-binding proteins A8 and A9 in tear fluid of patients with pterygium. Invest. Ophthalmol. Vis. Sci. 2009, 50, 2077-2086.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 2077-2086
    • Zhou, L.1    Beuerman, R.W.2    Ang, L.P.3    Chan, C.M.4
  • 23
    • 70449392553 scopus 로고    scopus 로고
    • Identification of tear fluid biomarkers in dry eye syndrome using iTRAQ quantitative proteomics
    • Zhou, L., Beuerman, R. W., Chan, C. M., Zhao, S. Z. et al., Identification of tear fluid biomarkers in dry eye syndrome using iTRAQ quantitative proteomics. J. Proteome Res. 2009, 8, 4889-4905.
    • (2009) J. Proteome Res. , vol.8 , pp. 4889-4905
    • Zhou, L.1    Beuerman, R.W.2    Chan, C.M.3    Zhao, S.Z.4
  • 24
    • 41749098309 scopus 로고    scopus 로고
    • Comparative analysis of the tear protein profile in mycotic keratitis patients
    • Ananthi, S., Chitra, T., Bini, R., Prajna, N. V. et al., Comparative analysis of the tear protein profile in mycotic keratitis patients. Mol. Vis. 2008, 14, 500-507.
    • (2008) Mol. Vis. , vol.14 , pp. 500-507
    • Ananthi, S.1    Chitra, T.2    Bini, R.3    Prajna, N.V.4
  • 25
    • 20844436744 scopus 로고    scopus 로고
    • Comparative analysis of the tear protein expression in blepharitis patients using two-dimensional electrophoresis
    • Koo, B. S., Lee, D. Y., Ha, H. S., Kim, J. C. et al., Comparative analysis of the tear protein expression in blepharitis patients using two-dimensional electrophoresis. J. Proteome Res. 2005, 4, 719-724.
    • (2005) J. Proteome Res. , vol.4 , pp. 719-724
    • Koo, B.S.1    Lee, D.Y.2    Ha, H.S.3    Kim, J.C.4
  • 26
    • 38349155717 scopus 로고    scopus 로고
    • Two-dimensional analysis of tear protein patterns of diabetic patients
    • Herber, S., Grus, F. H., Sabuncuo, P., Augustin, A. J., Two-dimensional analysis of tear protein patterns of diabetic patients. Electrophoresis 2001, 22, 1838-1844.
    • (2001) Electrophoresis , vol.22 , pp. 1838-1844
    • Herber, S.1    Grus, F.H.2    Sabuncuo, P.3    Augustin, A.J.4
  • 27
    • 84862701990 scopus 로고    scopus 로고
    • In-depth analysis of the human tear proteome
    • Zhou, L., Zhao, S. Z., Koh, S. K., Chen, L. et al., In-depth analysis of the human tear proteome. J. Proteomics 2012, 75, 3877-3885.
    • (2012) J. Proteomics , vol.75 , pp. 3877-3885
    • Zhou, L.1    Zhao, S.Z.2    Koh, S.K.3    Chen, L.4
  • 28
    • 40749152244 scopus 로고    scopus 로고
    • Investigation of the human tear film proteome using multiple proteomic approaches
    • Green-Church, K. B., Nichols, K. K., Kleinholz, N. M., Zhang, L. et al., Investigation of the human tear film proteome using multiple proteomic approaches. Mol. Vis. 2008, 14, 456-470.
    • (2008) Mol. Vis. , vol.14 , pp. 456-470
    • Green-Church, K.B.1    Nichols, K.K.2    Kleinholz, N.M.3    Zhang, L.4
  • 29
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • de Souza, G. A., Godoy, L. M., Mann, M., Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol. 2006, 7, R72.
    • (2006) Genome Biol. , vol.7
    • de Souza, G.A.1    Godoy, L.M.2    Mann, M.3
  • 30
    • 33748618456 scopus 로고    scopus 로고
    • Characterisation of human tear proteins using high-resolution mass spectrometry
    • Zhou, L., Beuerman, R. W., Foo, Y., Liu, S. et al., Characterisation of human tear proteins using high-resolution mass spectrometry. Ann. Acad. Med. Singapore 2006, 35, 400-407.
    • (2006) Ann. Acad. Med. Singapore , vol.35 , pp. 400-407
    • Zhou, L.1    Beuerman, R.W.2    Foo, Y.3    Liu, S.4
  • 31
    • 29144471957 scopus 로고    scopus 로고
    • Characterization of human tear proteome using multiple proteomic analysis techniques
    • Li, N., Wang, N., Zheng, J., Liu, X. M. et al., Characterization of human tear proteome using multiple proteomic analysis techniques. J. Proteome Res. 2005, 4, 2052-2061.
    • (2005) J. Proteome Res. , vol.4 , pp. 2052-2061
    • Li, N.1    Wang, N.2    Zheng, J.3    Liu, X.M.4
  • 32
    • 10644242580 scopus 로고    scopus 로고
    • Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid
    • Fung, K. Y., Morris, C., Sathe, S., Sack, R. et al., Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid. Proteomics 2004, 4, 3953-3959.
    • (2004) Proteomics , vol.4 , pp. 3953-3959
    • Fung, K.Y.1    Morris, C.2    Sathe, S.3    Sack, R.4
  • 33
    • 0026555830 scopus 로고
    • Diurnal tear cycle: evidence for a nocturnal inflammatory constitutive tear fluid
    • Sack, R. A., Tan, K. O., Tan, A., Diurnal tear cycle: evidence for a nocturnal inflammatory constitutive tear fluid. Invest. Ophthalmol. Vis. Sci. 1992, 33, 626-640.
    • (1992) Invest. Ophthalmol. Vis. Sci. , vol.33 , pp. 626-640
    • Sack, R.A.1    Tan, K.O.2    Tan, A.3
  • 34
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V. et al., In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nature protocols 2006, 1, 2856-2860.
    • (2006) Nature protocols , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4
  • 35
    • 84867416765 scopus 로고    scopus 로고
    • Serum and antibodies of glaucoma patients lead to changes in the proteome, especially cell regulatory proteins, in retinal cells
    • Bell, K., Funke, S., Pfeiffer, N., Grus, F. H., Serum and antibodies of glaucoma patients lead to changes in the proteome, especially cell regulatory proteins, in retinal cells. PloS one 2012, 7, e46910.
    • (2012) PloS one , vol.7
    • Bell, K.1    Funke, S.2    Pfeiffer, N.3    Grus, F.H.4
  • 36
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen, J. V., de Godoy, L. M., Li, G., Macek, B. et al., Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol. Cell Proteomics 2005, 4, 2010-2021.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4
  • 37
    • 0141989734 scopus 로고    scopus 로고
    • PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry
    • Ma, B., Zhang, K., Hendrie, C., Liang, C. et al., PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2003, 17, 2337-2342.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2337-2342
    • Ma, B.1    Zhang, K.2    Hendrie, C.3    Liang, C.4
  • 38
    • 79960010160 scopus 로고    scopus 로고
    • PeaksPTM: mass spectrometry-based identification of peptides with unspecified modifications
    • Han, X., He, L., Xin, L., Shan, B. et al., PeaksPTM: mass spectrometry-based identification of peptides with unspecified modifications. J. Proteome Res. 2011, 10, 2930-2936.
    • (2011) J. Proteome Res. , vol.10 , pp. 2930-2936
    • Han, X.1    He, L.2    Xin, L.3    Shan, B.4
  • 39
    • 0023284808 scopus 로고
    • Structural and genetic aspects of proline-rich proteins
    • Bennick, A., Structural and genetic aspects of proline-rich proteins. J. Dent. Res. 1987, 66, 457-461.
    • (1987) J. Dent. Res. , vol.66 , pp. 457-461
    • Bennick, A.1
  • 40
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange, V., Picotti, P., Domon, B., Aebersold, R., Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 2008, 4, 222.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 42
    • 84857881072 scopus 로고    scopus 로고
    • Automated workflow for large-scale selected reaction monitoring experiments
    • Malmstrom, L., Malmstrom, J., Selevsek, N., Rosenberger, G. et al., Automated workflow for large-scale selected reaction monitoring experiments. J. Proteome Res. 2012, 11, 1644-1653.
    • (2012) J. Proteome Res. , vol.11 , pp. 1644-1653
    • Malmstrom, L.1    Malmstrom, J.2    Selevsek, N.3    Rosenberger, G.4
  • 43
    • 84862778495 scopus 로고    scopus 로고
    • Large-scale isotype-specific quantification of Serum amyloid A 1/2 by multiple reaction monitoring in crude sera
    • Sung, H. J., Jeon, S. A., Ahn, J. M., Seul, K. J. et al., Large-scale isotype-specific quantification of Serum amyloid A 1/2 by multiple reaction monitoring in crude sera. J. Proteomics 2012, 75, 2170-2180.
    • (2012) J. Proteomics , vol.75 , pp. 2170-2180
    • Sung, H.J.1    Jeon, S.A.2    Ahn, J.M.3    Seul, K.J.4
  • 44
    • 84863229203 scopus 로고    scopus 로고
    • Identification and quantification of osteopontin splice variants in the plasma of lung cancer patients using immunoaffinity capture and targeted mass spectrometry
    • Wu, J., Pungaliya, P., Kraynov, E., Bates, B., Identification and quantification of osteopontin splice variants in the plasma of lung cancer patients using immunoaffinity capture and targeted mass spectrometry. Biomarkers 2012, 17, 125-133.
    • (2012) Biomarkers , vol.17 , pp. 125-133
    • Wu, J.1    Pungaliya, P.2    Kraynov, E.3    Bates, B.4
  • 45
    • 84874372391 scopus 로고    scopus 로고
    • Quantification of individual proteins in silicone hydrogel contact lens deposits
    • Omali, N. B., Zhao, Z., Zhu, H., Tilia, D. et al., Quantification of individual proteins in silicone hydrogel contact lens deposits. Mol. Vis. 2013, 19, 390-399.
    • (2013) Mol. Vis. , vol.19 , pp. 390-399
    • Omali, N.B.1    Zhao, Z.2    Zhu, H.3    Tilia, D.4
  • 46
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: new insights from global analyses
    • Blencowe, B. J., Alternative splicing: new insights from global analyses. Cell 2006, 126, 37-47.
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 47
    • 18344364099 scopus 로고    scopus 로고
    • Understanding alternative splicing: towards a cellular code
    • Matlin, A. J., Clark, F., Smith, C. W., Understanding alternative splicing: towards a cellular code. Nat. Rev. Mol. Cell Biol. 2005, 6, 386-398.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 386-398
    • Matlin, A.J.1    Clark, F.2    Smith, C.W.3
  • 48
    • 84867800367 scopus 로고    scopus 로고
    • Analysis of protein isoforms: can we do it better
    • Stastna, M., Van Eyk, J. E., Analysis of protein isoforms: can we do it better? Proteomics 2012, 12, 2937-2948.
    • (2012) Proteomics , vol.12 , pp. 2937-2948
    • Stastna, M.1    Van Eyk, J.E.2
  • 49
    • 82255195536 scopus 로고    scopus 로고
    • Alternative spliced variants as biomarkers of colorectal cancer
    • Yi, Q., Tang, L., Alternative spliced variants as biomarkers of colorectal cancer. Curr. Drug Metab. 2011, 12, 966-974.
    • (2011) Curr. Drug Metab. , vol.12 , pp. 966-974
    • Yi, Q.1    Tang, L.2
  • 50
    • 84862682219 scopus 로고    scopus 로고
    • VEGF spliced variants: possible role of anti-angiogenesis therapy
    • Hilmi, C., Guyot, M., Pages, G., VEGF spliced variants: possible role of anti-angiogenesis therapy. J. Nucleic Acids. 2012, 162692.
    • (2012) J. Nucleic Acids. , pp. 162692
    • Hilmi, C.1    Guyot, M.2    Pages, G.3
  • 51
    • 80355141485 scopus 로고    scopus 로고
    • Potential molecular targeting of splice variants for cancer treatment
    • Blair, C. A., Zi, X., Potential molecular targeting of splice variants for cancer treatment. Indian J. Exp. Biol. 2011, 49, 836-839.
    • (2011) Indian J. Exp. Biol. , vol.49 , pp. 836-839
    • Blair, C.A.1    Zi, X.2
  • 52
    • 77949318365 scopus 로고    scopus 로고
    • Minor modifications of the C-terminal helix reschedule the favored chemical reactions catalyzed by theta class glutathione transferase T1-1
    • Shokeer, A., Mannervik, B., Minor modifications of the C-terminal helix reschedule the favored chemical reactions catalyzed by theta class glutathione transferase T1-1. J. Biol. Chem. 2010, 285, 5639-5645.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5639-5645
    • Shokeer, A.1    Mannervik, B.2
  • 53
    • 77952826226 scopus 로고    scopus 로고
    • Post-translation modification of proteins in tears
    • You, J., Fitzgerald, A., Cozzi, P. J., Zhao, Z. et al., Post-translation modification of proteins in tears. Electrophoresis 2010, 31, 1853-1861.
    • (2010) Electrophoresis , vol.31 , pp. 1853-1861
    • You, J.1    Fitzgerald, A.2    Cozzi, P.J.3    Zhao, Z.4
  • 54
    • 79956352940 scopus 로고    scopus 로고
    • Comparative proteomics of human male and female tears by two-dimensional electrophoresis
    • Ananthi, S., Santhosh, R. S., Nila, M. V., Prajna, N. V. et al., Comparative proteomics of human male and female tears by two-dimensional electrophoresis. Exp. Eye Res. 2011, 92, 454-463.
    • (2011) Exp. Eye Res. , vol.92 , pp. 454-463
    • Ananthi, S.1    Santhosh, R.S.2    Nila, M.V.3    Prajna, N.V.4
  • 56
    • 0031461210 scopus 로고    scopus 로고
    • Establishment of the human reflex tear two-dimensional polyacrylamide gel electrophoresis reference map: new proteins of potential diagnostic value
    • Molloy, M. P., Bolis, S., Herbert, B. R., Ou, K. et al., Establishment of the human reflex tear two-dimensional polyacrylamide gel electrophoresis reference map: new proteins of potential diagnostic value. Electrophoresis 1997, 18, 2811-2815.
    • (1997) Electrophoresis , vol.18 , pp. 2811-2815
    • Molloy, M.P.1    Bolis, S.2    Herbert, B.R.3    Ou, K.4
  • 57
    • 44449117052 scopus 로고    scopus 로고
    • Identification and validation of eukaryotic aspartate and glutamate methylation in proteins
    • Sprung, R., Chen, Y., Zhang, K., Cheng, D. et al., Identification and validation of eukaryotic aspartate and glutamate methylation in proteins. J. Proteome Res. 2008, 7, 1001-1006.
    • (2008) J. Proteome Res. , vol.7 , pp. 1001-1006
    • Sprung, R.1    Chen, Y.2    Zhang, K.3    Cheng, D.4
  • 58
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R., Berlett, B. S., Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 1998, 30, 225-243.
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 59
    • 52049093858 scopus 로고    scopus 로고
    • Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins
    • Bregere, C., Rebrin, I., Sohal, R. S., Detection and characterization of in vivo nitration and oxidation of tryptophan residues in proteins. Methods enzymol. 2008, 441, 339-349.
    • (2008) Methods enzymol. , vol.441 , pp. 339-349
    • Bregere, C.1    Rebrin, I.2    Sohal, R.S.3
  • 60
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamoto, K., Chance, M. R., Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annu. Rev. Biophys. Biomol. Struct. 2006, 35, 251-276.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 61
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez, B., Radi, R., Peroxynitrite reactivity with amino acids and proteins. Amino acids 2003, 25, 295-311.
    • (2003) Amino acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 62
    • 0035473032 scopus 로고    scopus 로고
    • Photo-oxidation of proteins and its role in cataractogenesis
    • Davies, M. J., Truscott, R. J., Photo-oxidation of proteins and its role in cataractogenesis. J. Photochem. Photobiol. B. 2001, 63, 114-125.
    • (2001) J. Photochem. Photobiol. B. , vol.63 , pp. 114-125
    • Davies, M.J.1    Truscott, R.J.2
  • 63
    • 84875361063 scopus 로고    scopus 로고
    • Peptidomic analysis of human reflex tear fluid
    • Hayakawa, E., Landuyt, B., Baggerman, G., Cuyvers, R. et al., Peptidomic analysis of human reflex tear fluid. Peptides 2013, 42, 63-69.
    • (2013) Peptides , vol.42 , pp. 63-69
    • Hayakawa, E.1    Landuyt, B.2    Baggerman, G.3    Cuyvers, R.4
  • 64
    • 0016273305 scopus 로고
    • Amino acid sequence of the amino-terminal region of calf skin collagen
    • Fietzek, P. P., Breitkreutz, D., Kuhn, K., Amino acid sequence of the amino-terminal region of calf skin collagen. Biochim. Biophys. Acta. 1974, 365, 305-310.
    • (1974) Biochim. Biophys. Acta. , vol.365 , pp. 305-310
    • Fietzek, P.P.1    Breitkreutz, D.2    Kuhn, K.3
  • 65
    • 84864826447 scopus 로고    scopus 로고
    • Pyroglutamic acid: throwing light on a lightly studied metabolite
    • Kumar, A., Bachhawat, A. K., Pyroglutamic acid: throwing light on a lightly studied metabolite. Curr. Sci. 2012, 102, 288-297.
    • (2012) Curr. Sci. , vol.102 , pp. 288-297
    • Kumar, A.1    Bachhawat, A.K.2
  • 66
    • 0034635440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs
    • Hinke, S. A., Pospisilik, J. A., Demuth, H. U., Mannhart, S. et al., Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs. J. Biol. Chem. 2000, 275, 3827-3834.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3827-3834
    • Hinke, S.A.1    Pospisilik, J.A.2    Demuth, H.U.3    Mannhart, S.4
  • 67
    • 0032497366 scopus 로고    scopus 로고
    • Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV
    • Van Coillie, E., Proost, P., Van Aelst, I., Struyf, S. et al., Functional comparison of two human monocyte chemotactic protein-2 isoforms, role of the amino-terminal pyroglutamic acid and processing by CD26/dipeptidyl peptidase IV. Biochemistry 1998, 37, 12672-12680.
    • (1998) Biochemistry , vol.37 , pp. 12672-12680
    • Van Coillie, E.1    Proost, P.2    Van Aelst, I.3    Struyf, S.4
  • 68
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • Hwang, C. S., Shemorry, A., Varshavsky, A., N-terminal acetylation of cellular proteins creates specific degradation signals. Science 2010, 327, 973-977.
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 69
    • 79958027934 scopus 로고    scopus 로고
    • N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    • Forte, G. M., Pool, M. R., Stirling, C. J., N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol. 2011, 9, e1001073.
    • (2011) PLoS Biol. , vol.9
    • Forte, G.M.1    Pool, M.R.2    Stirling, C.J.3
  • 70
    • 77956901465 scopus 로고    scopus 로고
    • The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast
    • Coulton, A. T., East, D. A., Galinska-Rakoczy, A., Lehman, W. et al., The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. J. Cell Sci. 2010, 123, 3235-3243.
    • (2010) J. Cell Sci. , vol.123 , pp. 3235-3243
    • Coulton, A.T.1    East, D.A.2    Galinska-Rakoczy, A.3    Lehman, W.4
  • 71
    • 79958039807 scopus 로고    scopus 로고
    • Towards a functional understanding of protein N-terminal acetylation
    • Arnesen, T., Towards a functional understanding of protein N-terminal acetylation. PLoS Biol. 2011, 9, e1001074.
    • (2011) PLoS Biol. , vol.9
    • Arnesen, T.1
  • 72
    • 84859825973 scopus 로고    scopus 로고
    • N-terminal acetylation and other functions of Nalpha-acetyltransferases
    • Hollebeke, J., Van Damme, P., Gevaert, K., N-terminal acetylation and other functions of Nalpha-acetyltransferases. Biol. Chem. 2012, 393, 291-298.
    • (2012) Biol. Chem. , vol.393 , pp. 291-298
    • Hollebeke, J.1    Van Damme, P.2    Gevaert, K.3
  • 73
    • 84874625369 scopus 로고    scopus 로고
    • Consortium for Top Down, P., Proteoform: a single term describing protein complexity
    • Smith, L. M., Kelleher, N. L., Consortium for Top Down, P., 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


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