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Volumn 153, Issue , 2017, Pages 30-43

Quantitative body fluid proteomics in medicine — A focus on minimal invasiveness

Author keywords

AMP; Biomarker; Body fluid; Quantitative proteomics; Targeted proteomics

Indexed keywords

BIOLOGICAL MARKER; SALIVA PROTEIN;

EID: 84994759702     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2016.08.009     Document Type: Review
Times cited : (71)

References (215)
  • 1
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions
    • Picotti, P., Aebersold, R., Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat. Methods 9 (2012), 555–566, 10.1038/nmeth.2015.
    • (2012) Nat. Methods , vol.9 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 2
    • 80052024910 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: a tutorial
    • Rabilloud, T., Lelong, C., Two-dimensional gel electrophoresis in proteomics: a tutorial. J. Proteomics 74 (2011), 1829–1841, 10.1016/j.jprot.2011.05.040.
    • (2011) J. Proteomics , vol.74 , pp. 1829-1841
    • Rabilloud, T.1    Lelong, C.2
  • 3
    • 33745787972 scopus 로고    scopus 로고
    • Multiplexed and microparticle-based analyses: quantitative tools for the large-scale analysis of biological systems
    • Nolan, J.P., Mandy, F., Multiplexed and microparticle-based analyses: quantitative tools for the large-scale analysis of biological systems. Cytometry. Part A: The Journal of the International Society for Analytical Cytology 69 (2006), 318–325, 10.1002/cyto.a.20266.
    • (2006) Cytometry. Part A: The Journal of the International Society for Analytical Cytology , vol.69 , pp. 318-325
    • Nolan, J.P.1    Mandy, F.2
  • 4
    • 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., 4, 2008, 222, 10.1038/msb.2008.61.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 5
    • 17444383852 scopus 로고    scopus 로고
    • Depletion of high-abundant proteins in body fluids prior to liquid chromatography fourier transform ion cyclotron resonance mass spectrometry., J. Proteome Res. 4 410–6. doi:.
    • M. Ramström, C. Hagman, J.K. Mitchell, P.J. Derrick, P. Håkansson, J. Bergquist, Depletion of high-abundant proteins in body fluids prior to liquid chromatography fourier transform ion cyclotron resonance mass spectrometry., J. Proteome Res. 4 410–6. doi: http://dx.doi.org/10.1021/pr049812a.
    • Ramström, M.1    Hagman, C.2    Mitchell, J.K.3    Derrick, P.J.4    Håkansson, P.5    Bergquist, J.6
  • 6
    • 84969375479 scopus 로고    scopus 로고
    • Enrichment and identification of glycoproteins in human saliva using lectin magnetic bead arrays
    • Caragata, M., Shah, A.K., Schulz, B.L., Hill, M.M., Punyadeera, C., Enrichment and identification of glycoproteins in human saliva using lectin magnetic bead arrays. Anal. Biochem. 497 (2016), 76–82, 10.1016/j.ab.2015.11.024.
    • (2016) Anal. Biochem. , vol.497 , pp. 76-82
    • Caragata, M.1    Shah, A.K.2    Schulz, B.L.3    Hill, M.M.4    Punyadeera, C.5
  • 7
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate
    • Grønborg, M., Kristiansen, T.Z., Stensballe, A., Andersen, J.S., Ohara, O., Mann, M., et al. A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate. Molecular & Cellular Proteomics: MCP. 1 (2002), 517–527.
    • (2002) Molecular & Cellular Proteomics: MCP. , vol.1 , pp. 517-527
    • Grønborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, O.5    Mann, M.6
  • 8
    • 85058721573 scopus 로고    scopus 로고
    • Peptide immunoaffinity enrichment coupled with mass spectrometry for peptide and protein quantification
    • Whiteaker, J.R., Paulovich, A.G., Peptide immunoaffinity enrichment coupled with mass spectrometry for peptide and protein quantification. Clin. Lab. Med. 31 (2011), 385–396, 10.1016/j.cll.2011.07.004.
    • (2011) Clin. Lab. Med. , vol.31 , pp. 385-396
    • Whiteaker, J.R.1    Paulovich, A.G.2
  • 9
    • 8844233567 scopus 로고    scopus 로고
    • Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • Anderson, N.L., Anderson, N.G., Haines, L.R., Hardie, D.B., Olafson, R.W., Pearson, T.W., Mass spectrometric quantitation of peptides and proteins using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA). J. Proteome Res. 3 (2004), 235–244.
    • (2004) J. Proteome Res. , vol.3 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 10
    • 0042972779 scopus 로고    scopus 로고
    • Biochemical diagnosis of Alzheimer disease by measuring the cerebrospinal fluid ratio of phosphorylated tau protein to beta-amyloid peptide
    • Maddalena, A., Papassotiropoulos, A., Müller-Tillmanns, B., Jung, H.H., Hegi, T., Nitsch, R.M., et al. Biochemical diagnosis of Alzheimer disease by measuring the cerebrospinal fluid ratio of phosphorylated tau protein to beta-amyloid peptide. Arch. Neurol. 60 (2003), 1202–1206, 10.1001/archneur.60.9.1202.
    • (2003) Arch. Neurol. , vol.60 , pp. 1202-1206
    • Maddalena, A.1    Papassotiropoulos, A.2    Müller-Tillmanns, B.3    Jung, H.H.4    Hegi, T.5    Nitsch, R.M.6
  • 11
    • 33646198145 scopus 로고    scopus 로고
    • Tau therapeutic strategies for the treatment of Alzheimer's disease
    • Churcher, I., Tau therapeutic strategies for the treatment of Alzheimer's disease. Curr. Top. Med. Chem. 6 (2006), 579–595.
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 579-595
    • Churcher, I.1
  • 12
    • 0037040525 scopus 로고    scopus 로고
    • Elevated levels of phosphorylated neurofilament proteins in cerebrospinal fluid of Alzheimer disease patients
    • Hu, Y.-Y., He, S.-S., Wang, X.-C., Duan, Q.-H., Khatoon, S., Iqbal, K., et al. Elevated levels of phosphorylated neurofilament proteins in cerebrospinal fluid of Alzheimer disease patients. Neurosci. Lett. 320 (2002), 156–160.
    • (2002) Neurosci. Lett. , vol.320 , pp. 156-160
    • Hu, Y.-Y.1    He, S.-S.2    Wang, X.-C.3    Duan, Q.-H.4    Khatoon, S.5    Iqbal, K.6
  • 13
    • 0035100888 scopus 로고    scopus 로고
    • Biomarkers and surrogate endpoints: preferred definitions and conceptual framework
    • Group, B.D.W., Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Clin. Pharmacol. Ther. 69 (2001), 89–95, 10.1067/mcp.2001.113989.
    • (2001) Clin. Pharmacol. Ther. , vol.69 , pp. 89-95
    • Group, B.D.W.1
  • 14
    • 78649694616 scopus 로고    scopus 로고
    • Reconstructing the pipeline by introducing multiplexed multiple reaction monitoring mass spectrometry for cancer biomarker verification: an NCI-CPTC initiative perspective
    • Rodriguez, H., Rivers, R., Kinsinger, C., Mesri, M., Hiltke, T., Rahbar, A., et al. Reconstructing the pipeline by introducing multiplexed multiple reaction monitoring mass spectrometry for cancer biomarker verification: an NCI-CPTC initiative perspective. Proteomics Clin. Appl. 4 (2010), 904–914, 10.1002/prca.201000057.
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 904-914
    • Rodriguez, H.1    Rivers, R.2    Kinsinger, C.3    Mesri, M.4    Hiltke, T.5    Rahbar, A.6
  • 15
    • 28544446695 scopus 로고    scopus 로고
    • Biomarkers in cancer staging, prognosis and treatment selection
    • Ludwig, J.A., Weinstein, J.N., Biomarkers in cancer staging, prognosis and treatment selection. Nat. Rev. Cancer 5 (2005), 845–856, 10.1038/nrc1739.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 845-856
    • Ludwig, J.A.1    Weinstein, J.N.2
  • 16
    • 75749130354 scopus 로고    scopus 로고
    • The clinical plasma proteome: a survey of clinical assays for proteins in plasma and serum
    • Anderson, N.L., The clinical plasma proteome: a survey of clinical assays for proteins in plasma and serum. Clin. Chem. 56 (2010), 177–185, 10.1373/clinchem.2009.126706.
    • (2010) Clin. Chem. , vol.56 , pp. 177-185
    • Anderson, N.L.1
  • 17
    • 53849144620 scopus 로고    scopus 로고
    • Strategies for discovering novel cancer biomarkers through utilization of emerging technologies
    • Kulasingam, V., Diamandis, E.P., Strategies for discovering novel cancer biomarkers through utilization of emerging technologies. Nat. Clin. Pract. Oncol. 5 (2008), 588–599, 10.1038/ncponc1187.
    • (2008) Nat. Clin. Pract. Oncol. , vol.5 , pp. 588-599
    • Kulasingam, V.1    Diamandis, E.P.2
  • 18
    • 84891774053 scopus 로고    scopus 로고
    • Translation of proteomic biomarkers into FDA approved cancer diagnostics: issues and challenges
    • Füzéry, A.K., Levin, J., Chan, M.M., Chan, D.W., Translation of proteomic biomarkers into FDA approved cancer diagnostics: issues and challenges. Clinical Proteomics, 10, 2013, 13, 10.1186/1559-0275-10-13.
    • (2013) Clinical Proteomics , vol.10 , pp. 13
    • Füzéry, A.K.1    Levin, J.2    Chan, M.M.3    Chan, D.W.4
  • 20
    • 4143067096 scopus 로고    scopus 로고
    • Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer
    • Zhang, Z., Bast, R.C., Yu, Y., Li, J., Sokoll, L.J., Rai, A.J., et al. Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer. Cancer Res. 64 (2004), 5882–5890, 10.1158/0008-5472.CAN-04-0746.
    • (2004) Cancer Res. , vol.64 , pp. 5882-5890
    • Zhang, Z.1    Bast, R.C.2    Yu, Y.3    Li, J.4    Sokoll, L.J.5    Rai, A.J.6
  • 22
    • 66749171697 scopus 로고    scopus 로고
    • Statistical design of quantitative mass spectrometry-based proteomic experiments
    • Oberg, A.L., Vitek, O., Statistical design of quantitative mass spectrometry-based proteomic experiments. J. Proteome Res. 8 (2009), 2144–2156, 10.1021/pr8010099.
    • (2009) J. Proteome Res. , vol.8 , pp. 2144-2156
    • Oberg, A.L.1    Vitek, O.2
  • 23
    • 0029130738 scopus 로고
    • Multivariate receiver-operating characteristic curve analysis: prostate cancer screening as an example
    • Shultz, E.K., Multivariate receiver-operating characteristic curve analysis: prostate cancer screening as an example. Clin. Chem. 41 (1995), 1248–1255.
    • (1995) Clin. Chem. , vol.41 , pp. 1248-1255
    • Shultz, E.K.1
  • 24
    • 77749301726 scopus 로고    scopus 로고
    • Serum retinol-binding protein 4 levels in patients with diabetic retinopathy., J. Int. Med. Res. 38.
    • Z.-Z. Li, X.-Z. Lu, J.-B. Liu, L. Chen, Serum retinol-binding protein 4 levels in patients with diabetic retinopathy., J. Int. Med. Res. 38. 95–9.
    • Li, Z.-Z.1    Lu, X.-Z.2    Liu, J.-B.3    Chen, L.4
  • 25
    • 84858751820 scopus 로고    scopus 로고
    • Quantitative analysis of proteins in the tear fluid of patients with diabetic retinopathy
    • Csősz, É., Boross, P., Csutak, A., Berta, A., Tóth, F., Póliska, S., et al. Quantitative analysis of proteins in the tear fluid of patients with diabetic retinopathy. J. Proteomics 75 (2012), 2196–2204, 10.1016/j.jprot.2012.01.019.
    • (2012) J. Proteomics , vol.75 , pp. 2196-2204
    • Csősz, É.1    Boross, P.2    Csutak, A.3    Berta, A.4    Tóth, F.5    Póliska, S.6
  • 27
    • 0025279885 scopus 로고
    • Protein levels in nonstimulated and stimulated tears of normal human subjects
    • Fullard, R.J., Snyder, C., Protein levels in nonstimulated and stimulated tears of normal human subjects. Invest. Ophthalmol. Vis. Sci. 31 (1990), 1119–1126.
    • (1990) Invest. Ophthalmol. Vis. Sci. , vol.31 , pp. 1119-1126
    • Fullard, R.J.1    Snyder, C.2
  • 28
    • 0348217933 scopus 로고    scopus 로고
    • Tears in health and disease
    • Tiffany, J.M., Tears in health and disease. Eye (Lond.) 17 (2003), 923–926, 10.1038/sj.eye.6700566.
    • (2003) Eye (Lond.) , vol.17 , pp. 923-926
    • Tiffany, J.M.1
  • 30
    • 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.F., Mann, M., Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol., 7, 2006, R72, 10.1186/gb-2006-7-8-R72.
    • (2006) Genome Biol. , vol.7 , pp. R72
    • de Souza, G.A.1    Godoy, L.M.F.2    Mann, M.3
  • 31
    • 84862701990 scopus 로고    scopus 로고
    • In-depth analysis of the human tear proteome
    • Zhou, L., Zhao, S.Z., Koh, S.K., Chen, L., Vaz, C., Tanavde, V., et al. In-depth analysis of the human tear proteome. J. Proteomics 75 (2012), 3877–3885, 10.1016/j.jprot.2012.04.053.
    • (2012) J. Proteomics , vol.75 , pp. 3877-3885
    • Zhou, L.1    Zhao, S.Z.2    Koh, S.K.3    Chen, L.4    Vaz, C.5    Tanavde, V.6
  • 32
    • 29144471957 scopus 로고    scopus 로고
    • Characterization of human tear proteome using multiple proteomic analysis techniques
    • Li, N., Wang, N., Zheng, J., Liu, X.M., Lever, O.W., Erickson, P.M., et al. Characterization of human tear proteome using multiple proteomic analysis techniques. J. Proteome Res. 4 (2005), 2052–2061, 10.1021/pr0501970.
    • (2005) J. Proteome Res. , vol.4 , pp. 2052-2061
    • Li, N.1    Wang, N.2    Zheng, J.3    Liu, X.M.4    Lever, O.W.5    Erickson, P.M.6
  • 34
    • 0032384424 scopus 로고    scopus 로고
    • The lacrimal gland and its veil of tears
    • Walcott, B., The lacrimal gland and its veil of tears. News Physiol. Sci. 13 (1998), 97–103.
    • (1998) News Physiol. Sci. , vol.13 , pp. 97-103
    • Walcott, B.1
  • 35
    • 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. 31 (2012), 527–550, 10.1016/j.preteyeres.2012.06.002.
    • (2012) Prog. Retin. Eye Res. , vol.31 , pp. 527-550
    • Zhou, L.1    Beuerman, R.W.2
  • 36
    • 84888128535 scopus 로고    scopus 로고
    • Tears as a source of biomarkers for ocular and systemic diseases
    • von Thun und Hohenstein-Blaul, N., Funke, S., Grus, F.H., Tears as a source of biomarkers for ocular and systemic diseases. Exp. Eye Res. 117 (2013), 126–137, 10.1016/j.exer.2013.07.015.
    • (2013) Exp. Eye Res. , vol.117 , pp. 126-137
    • von Thun und Hohenstein-Blaul, N.1    Funke, S.2    Grus, F.H.3
  • 37
    • 84924652855 scopus 로고    scopus 로고
    • Cytokine changes in tears and relationship to contact lens discomfort
    • Willcox, M.D.P., Zhao, Z., Naduvilath, T., Lazon de la Jara, P., Cytokine changes in tears and relationship to contact lens discomfort. Mol. Vis. 21 (2015), 293–305.
    • (2015) Mol. Vis. , vol.21 , pp. 293-305
    • Willcox, M.D.P.1    Zhao, Z.2    Naduvilath, T.3    Lazon de la Jara, P.4
  • 38
    • 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., Li, X.R., Yang, H., et al. Identification of tear fluid biomarkers in dry eye syndrome using iTRAQ quantitative proteomics. J. Proteome Res. 8 (2009), 4889–4905, 10.1021/pr900686s.
    • (2009) J. Proteome Res. , vol.8 , pp. 4889-4905
    • Zhou, L.1    Beuerman, R.W.2    Chan, C.M.3    Zhao, S.Z.4    Li, X.R.5    Yang, H.6
  • 40
    • 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., Rajappa, S.M., Tatu, U., et al. Lacrimal proline rich 4 (LPRR4) protein in the tear fluid is a potential biomarker of dry eye syndrome. PLoS One, 7, 2012, e51979, 10.1371/journal.pone.0051979.
    • (2012) PLoS One , vol.7
    • Aluru, S.V.1    Agarwal, S.2    Srinivasan, B.3    Iyer, G.K.4    Rajappa, S.M.5    Tatu, U.6
  • 42
    • 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., Kim, C.-W., Comparative analysis of the tear protein expression in blepharitis patients using two-dimensional electrophoresis. J. Proteome Res. 4 (2005), 719–724, 10.1021/pr0498133.
    • (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    Kim, C.-W.5
  • 43
    • 65249090285 scopus 로고    scopus 로고
    • Quantitative analysis of N-linked glycoproteins in tear fluid of climatic droplet keratopathy by glycopeptide capture and iTRAQ
    • Lei, Z., Beuerman, R.W., Chew, A.P., Koh, S.K., Cafaro, T.A., Urrets-Zavalia, E.A., et al. Quantitative analysis of N-linked glycoproteins in tear fluid of climatic droplet keratopathy by glycopeptide capture and iTRAQ. J. Proteome Res. 8 (2009), 1992–2003, 10.1021/pr800962q.
    • (2009) J. Proteome Res. , vol.8 , pp. 1992-2003
    • Lei, Z.1    Beuerman, R.W.2    Chew, A.P.3    Koh, S.K.4    Cafaro, T.A.5    Urrets-Zavalia, E.A.6
  • 45
    • 84887154754 scopus 로고    scopus 로고
    • Preliminary identification of differentially expressed tear proteins in keratoconus
    • Balasubramanian, S.A., Wasinger, V.C., Pye, D.C., Willcox, M.D.P., Preliminary identification of differentially expressed tear proteins in keratoconus. Mol. Vis. 19 (2013), 2124–2134.
    • (2013) Mol. Vis. , vol.19 , pp. 2124-2134
    • Balasubramanian, S.A.1    Wasinger, V.C.2    Pye, D.C.3    Willcox, M.D.P.4
  • 46
    • 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., Lalitha, P., Dharmalingam, K., Comparative analysis of the tear protein profile in mycotic keratitis patients. Mol. Vis. 14 (2008), 500–507.
    • (2008) Mol. Vis. , vol.14 , pp. 500-507
    • Ananthi, S.1    Chitra, T.2    Bini, R.3    Prajna, N.V.4    Lalitha, P.5    Dharmalingam, K.6
  • 47
    • 84893145907 scopus 로고    scopus 로고
    • Identification of human tear fluid biomarkers in vernal keratoconjunctivitis using iTRAQ quantitative proteomics
    • Leonardi, A., Palmigiano, A., Mazzola, E.A., Messina, A., Milazzo, E.M.S., Bortolotti, M., et al. Identification of human tear fluid biomarkers in vernal keratoconjunctivitis using iTRAQ quantitative proteomics. Allergy 69 (2014), 254–260, 10.1111/all.12331.
    • (2014) Allergy , vol.69 , pp. 254-260
    • Leonardi, A.1    Palmigiano, A.2    Mazzola, E.A.3    Messina, A.4    Milazzo, E.M.S.5    Bortolotti, M.6
  • 49
    • 84976863903 scopus 로고    scopus 로고
    • Changes in the chemical barrier composition of tears in Alzheimer's disease reveal potential tear diagnostic biomarkers
    • Kalló, G., Emri, M., Varga, Z., Ujhelyi, B., Tőzsér, J., Csutak, A., et al. Changes in the chemical barrier composition of tears in Alzheimer's disease reveal potential tear diagnostic biomarkers. PLoS One, 1–14, 2016, 10.1371/journal.pone.0158000.
    • (2016) PLoS One , vol.1-14
    • Kalló, G.1    Emri, M.2    Varga, Z.3    Ujhelyi, B.4    Tőzsér, J.5    Csutak, A.6
  • 50
    • 20844435927 scopus 로고    scopus 로고
    • Diagnostic potential of tear proteomic patterns in Sjögren's syndrome
    • Tomosugi, N., Kitagawa, K., Takahashi, N., Sugai, S., Ishikawa, I., Diagnostic potential of tear proteomic patterns in Sjögren's syndrome. J. Proteome Res. 4 (2005), 820–825, 10.1021/pr0497576.
    • (2005) J. Proteome Res. , vol.4 , pp. 820-825
    • Tomosugi, N.1    Kitagawa, K.2    Takahashi, N.3    Sugai, S.4    Ishikawa, I.5
  • 51
    • 65749105565 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionisation time-of-flight mass spectrometry to detect breast cancer markers in tears and serum
    • doi:6/2/75 [pii]
    • Lebrecht, A., Boehm, D., Schmidt, M., Koelbl, H., Grus, F.H., Surface-enhanced laser desorption/ionisation time-of-flight mass spectrometry to detect breast cancer markers in tears and serum. Cancer Genomics Proteomics 6 (2009), 75–84 doi:6/2/75 [pii].
    • (2009) Cancer Genomics Proteomics , vol.6 , pp. 75-84
    • Lebrecht, A.1    Boehm, D.2    Schmidt, M.3    Koelbl, H.4    Grus, F.H.5
  • 52
    • 67649506543 scopus 로고    scopus 로고
    • Diagnosis of breast cancer by tear proteomic pattern., Cancer Genomics Proteomics. 6
    • A. Lebrecht, D. Boehm, M. Schmidt, H. Koelbl, R.L. Schwirz, F.H. Grus, Diagnosis of breast cancer by tear proteomic pattern., Cancer Genomics Proteomics. 6 177–82.
    • Lebrecht, A.1    Boehm, D.2    Schmidt, M.3    Koelbl, H.4    Schwirz, R.L.5    Grus, F.H.6
  • 53
    • 52049099693 scopus 로고    scopus 로고
    • Antibody protein array analysis of the tear film cytokines
    • Li, S., Sack, R., Vijmasi, T., Sathe, S., Beaton, A., Quigley, D., et al. Antibody protein array analysis of the tear film cytokines. Optom. Vis. Sci. 85 (2008), 653–660, 10.1097/OPX.0b013e3181824e20.
    • (2008) Optom. Vis. Sci. , vol.85 , pp. 653-660
    • Li, S.1    Sack, R.2    Vijmasi, T.3    Sathe, S.4    Beaton, A.5    Quigley, D.6
  • 54
    • 84893496246 scopus 로고    scopus 로고
    • Tear cytokine profile as a noninvasive biomarker of inflammation for ocular surface diseases: standard operating procedures
    • Wei, Y., Gadaria-Rathod, N., Epstein, S., Asbell, P., Tear cytokine profile as a noninvasive biomarker of inflammation for ocular surface diseases: standard operating procedures. Invest. Ophthalmol. Vis. Sci. 54 (2013), 8327–8336, 10.1167/iovs.13-12132.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 8327-8336
    • Wei, Y.1    Gadaria-Rathod, N.2    Epstein, S.3    Asbell, P.4
  • 55
    • 84945130563 scopus 로고    scopus 로고
    • Human tear analysis with miniaturized multiplex cytokine assay on “ wall-less ” 96-well plate
    • Le Guezennec, X., Quah, J., Tong, L., Kim, N., Human tear analysis with miniaturized multiplex cytokine assay on “ wall-less ” 96-well plate. Mol. Vis. 21 (2015), 1151–1161.
    • (2015) Mol. Vis. , vol.21 , pp. 1151-1161
    • Le Guezennec, X.1    Quah, J.2    Tong, L.3    Kim, N.4
  • 56
    • 84862833065 scopus 로고    scopus 로고
    • Proteomic profiling of inflammatory signaling molecules in the tears of patients on chronic glaucoma medication
    • Wong, T.T., Zhou, L., Li, J., Tong, L., Zhao, S.Z., Li, X.R., et al. Proteomic profiling of inflammatory signaling molecules in the tears of patients on chronic glaucoma medication. Invest. Ophthalmol. Vis. Sci. 52 (2011), 7385–7391, 10.1167/iovs.10-6532.
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 7385-7391
    • Wong, T.T.1    Zhou, L.2    Li, J.3    Tong, L.4    Zhao, S.Z.5    Li, X.R.6
  • 57
    • 68949204935 scopus 로고    scopus 로고
    • Tearful relations: oxidative stress, inflammation and eye diseases
    • Wakamatsu, T.H., Dogru, M., Tsubota, K., Tearful relations: oxidative stress, inflammation and eye diseases. Arq. Bras. Oftalmol. 71 (2008), 72–79, 10.1590/S0004-27492008000700015.
    • (2008) Arq. Bras. Oftalmol. , vol.71 , pp. 72-79
    • Wakamatsu, T.H.1    Dogru, M.2    Tsubota, K.3
  • 58
    • 84884364823 scopus 로고    scopus 로고
    • Tear levels of tumor necrosis factor-alpha in patients with Parkinson's disease
    • Çomoğlu, S.S., Güven, H., Acar, M., Öztürk, G., Koçer, B., Tear levels of tumor necrosis factor-alpha in patients with Parkinson's disease. Neurosci. Lett. 553 (2013), 63–67, 10.1016/j.neulet.2013.08.019.
    • (2013) Neurosci. Lett. , vol.553 , pp. 63-67
    • Çomoğlu, S.S.1    Güven, H.2    Acar, M.3    Öztürk, G.4    Koçer, B.5
  • 59
    • 0034929220 scopus 로고    scopus 로고
    • Silver stained isoelectrophoresis of tears and cerebrospinal fluid in multiple sclerosis
    • Devos, D., Forzy, G., de Seze, J., Caillez, S., Louchart, P., Gallois, P., et al. Silver stained isoelectrophoresis of tears and cerebrospinal fluid in multiple sclerosis. J. Neurol. 248 (2001), 672–675, 10.1007/PL00007833.
    • (2001) J. Neurol. , vol.248 , pp. 672-675
    • Devos, D.1    Forzy, G.2    de Seze, J.3    Caillez, S.4    Louchart, P.5    Gallois, P.6
  • 60
    • 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. 85 (2001), 162–169, 10.1067/mpr.2001.113778.
    • (2001) J. Prosthet. Dent. , vol.85 , pp. 162-169
    • Humphrey, S.P.1    Williamson, R.T.2
  • 62
    • 84881142917 scopus 로고    scopus 로고
    • Saliva proteome research: current status and future outlook
    • Schulz, B.L., Cooper-White, J., Punyadeera, C.K., Saliva proteome research: current status and future outlook. Crit. Rev. Biotechnol. 33 (2013), 246–259, 10.3109/07388551.2012.687361.
    • (2013) Crit. Rev. Biotechnol. , vol.33 , pp. 246-259
    • Schulz, B.L.1    Cooper-White, J.2    Punyadeera, C.K.3
  • 63
    • 0001631469 scopus 로고    scopus 로고
    • Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Acta Crystallogr. Sect. D: Biol. Crystallogr. 52 (1996) 435–46. doi:.
    • N. Ramasubbu, V. Paloth, Y. Luo, G.D. Brayer, M.J. Levine, Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Acta Crystallogr. Sect. D: Biol. Crystallogr. 52 (1996) 435–46. doi: http://dx.doi.org/10.1107/S0907444995014119.
    • Ramasubbu, N.1    Paloth, V.2    Luo, Y.3    Brayer, G.D.4    Levine, M.J.5
  • 64
    • 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., Li, Y., Loo, J.A., et al. Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry. Proteomics 5 (2005), 1714–1728, 10.1002/pmic.200401037.
    • (2005) Proteomics , vol.5 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3    Ogorzalek Loo, R.R.4    Li, Y.5    Loo, J.A.6
  • 65
    • 51349132896 scopus 로고    scopus 로고
    • The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions
    • Denny, P., Hagen, F.K., Hardt, M., Liao, L., Yan, W., Arellanno, M., et al. The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions. J. Proteome Res. 7 (2008), 1994–2006, 10.1021/pr700764j.
    • (2008) J. Proteome Res. , vol.7 , pp. 1994-2006
    • Denny, P.1    Hagen, F.K.2    Hardt, M.3    Liao, L.4    Yan, W.5    Arellanno, M.6
  • 66
    • 33744981406 scopus 로고    scopus 로고
    • Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS
    • Guo, T., Rudnick, P.A., Wang, W., Lee, C.S., Devoe, D.L., Balgley, B.M., Characterization of the human salivary proteome by capillary isoelectric focusing/nanoreversed-phase liquid chromatography coupled with ESI-tandem MS. J. Proteome Res. 5 (2006), 1469–1478, 10.1021/pr060065m.
    • (2006) J. Proteome Res. , vol.5 , pp. 1469-1478
    • Guo, T.1    Rudnick, P.A.2    Wang, W.3    Lee, C.S.4    Devoe, D.L.5    Balgley, B.M.6
  • 68
    • 84875509593 scopus 로고    scopus 로고
    • Salivary protein concentration, flow rate, buffer capacity and pH estimation: a comparative study among young and elderly subjects, both normal and with gingivitis and periodontitis
    • Shaila, M., Pai, G.P., Shetty, P., Salivary protein concentration, flow rate, buffer capacity and pH estimation: a comparative study among young and elderly subjects, both normal and with gingivitis and periodontitis. Journal of Indian Society of Periodontology 17 (2013), 42–46, 10.4103/0972-124X.107473.
    • (2013) Journal of Indian Society of Periodontology , vol.17 , pp. 42-46
    • Shaila, M.1    Pai, G.P.2    Shetty, P.3
  • 69
    • 0027355946 scopus 로고
    • Protein, albumin and cystatin concentrations in saliva of healthy subjects and of patients with gingivitis or periodontitis
    • Henskens, Y.M., van der Velden, U., Veerman, E.C., Amerongen, A.V.N., Protein, albumin and cystatin concentrations in saliva of healthy subjects and of patients with gingivitis or periodontitis. J. Periodontal Res. 28 (1993), 43–48.
    • (1993) J. Periodontal Res. , vol.28 , pp. 43-48
    • Henskens, Y.M.1    van der Velden, U.2    Veerman, E.C.3    Amerongen, A.V.N.4
  • 70
    • 84945443308 scopus 로고    scopus 로고
    • Comparative two-dimensional polyacrylamide gel electrophoresis of the salivary proteome of children with autism spectrum disorder
    • Ngounou Wetie, A.G., Wormwood, K.L., Charette, L., Ryan, J.P., Woods, A.G., Darie, C.C., Comparative two-dimensional polyacrylamide gel electrophoresis of the salivary proteome of children with autism spectrum disorder. J. Cell. Mol. Med. 19 (2015), 2664–2678, 10.1111/jcmm.12658.
    • (2015) J. Cell. Mol. Med. , vol.19 , pp. 2664-2678
    • Ngounou Wetie, A.G.1    Wormwood, K.L.2    Charette, L.3    Ryan, J.P.4    Woods, A.G.5    Darie, C.C.6
  • 71
    • 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
    • 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. 26 (2008), 159–167, 10.1080/07357900701783883.
    • (2008) Cancer Invest. , vol.26 , pp. 159-167
    • Streckfus, C.F.1    Mayorga-Wark, O.2    Arreola, D.3    Edwards, C.4    Bigler, L.5    Dubinsky, W.P.6
  • 72
    • 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. Journal of Oncology, 2009, 2009, 737619, 10.1155/2009/737619.
    • (2009) Journal of Oncology , vol.2009 , pp. 737619
    • Streckfus, C.F.1    Storthz, K.A.2    Bigler, L.3    Dubinsky, W.P.4
  • 73
    • 77956217081 scopus 로고    scopus 로고
    • Quantitative proteomics reveals myosin and actin as promising saliva biomarkers for distinguishing pre-malignant and malignant oral lesions
    • de Jong, E.P., Xie, H., Onsongo, G., Stone, M.D., Chen, X.-B., Kooren, J.A., et al. Quantitative proteomics reveals myosin and actin as promising saliva biomarkers for distinguishing pre-malignant and malignant oral lesions. PLoS One, 5, 2010, e11148, 10.1371/journal.pone.0011148.
    • (2010) PLoS One , vol.5
    • de Jong, E.P.1    Xie, H.2    Onsongo, G.3    Stone, M.D.4    Chen, X.-B.5    Kooren, J.A.6
  • 74
    • 84946594100 scopus 로고    scopus 로고
    • Insights into immune responses in oral cancer through proteomic analysis of saliva and salivary extracellular vesicles
    • Winck, F.V., Ribeiro, A.C.P., Domingues, R.R., Ling, L.Y., Riaño-Pachón, D.M., Rivera, C., et al. Insights into immune responses in oral cancer through proteomic analysis of saliva and salivary extracellular vesicles. Sci. Rep., 5, 2015, 16305, 10.1038/srep16305.
    • (2015) Sci. Rep. , vol.5 , pp. 16305
    • Winck, F.V.1    Ribeiro, A.C.P.2    Domingues, R.R.3    Ling, L.Y.4    Riaño-Pachón, D.M.5    Rivera, C.6
  • 75
    • 84942987797 scopus 로고    scopus 로고
    • Saliva proteome profiling reveals potential salivary biomarkers for detection of oral cavity squamous cell carcinoma
    • Wu, C.-C., Chu, H.-W., Hsu, C.-W., Chang, K.-P., Liu, H.-P., Saliva proteome profiling reveals potential salivary biomarkers for detection of oral cavity squamous cell carcinoma. Proteomics 15 (2015), 3394–3404, 10.1002/pmic.201500157.
    • (2015) Proteomics , vol.15 , pp. 3394-3404
    • Wu, C.-C.1    Chu, H.-W.2    Hsu, C.-W.3    Chang, K.-P.4    Liu, H.-P.5
  • 77
    • 84878233934 scopus 로고    scopus 로고
    • Quantitative salivary proteomic differences in oral chronic graft-versus-host disease
    • Bassim, C.W., Ambatipudi, K.S., Mays, J.W., Edwards, D.A., Swatkoski, S., Fassil, H., et al. Quantitative salivary proteomic differences in oral chronic graft-versus-host disease. J. Clin. Immunol. 32 (2012), 1390–1399, 10.1007/s10875-012-9738-4.
    • (2012) J. Clin. Immunol. , vol.32 , pp. 1390-1399
    • Bassim, C.W.1    Ambatipudi, K.S.2    Mays, J.W.3    Edwards, D.A.4    Swatkoski, S.5    Fassil, H.6
  • 78
    • 84867824228 scopus 로고    scopus 로고
    • Quantitative proteomics of parotid saliva in primary Sjögren's syndrome
    • Ambatipudi, K.S., Swatkoski, S., Moresco, J.J., Tu, P.G., Coca, A., Anolik, J.H., et al. Quantitative proteomics of parotid saliva in primary Sjögren's syndrome. Proteomics 12 (2012), 3113–3120, 10.1002/pmic.201200208.
    • (2012) Proteomics , vol.12 , pp. 3113-3120
    • Ambatipudi, K.S.1    Swatkoski, S.2    Moresco, J.J.3    Tu, P.G.4    Coca, A.5    Anolik, J.H.6
  • 80
    • 84876010113 scopus 로고    scopus 로고
    • Selected reaction monitoring to differentiate and relatively quantitate isomers of sulfated and unsulfated core 1 O-glycans from salivary MUC7 protein in rheumatoid arthritis
    • Flowers, S.A., Ali, L., Lane, C.S., Olin, M., Karlsson, N.G., Selected reaction monitoring to differentiate and relatively quantitate isomers of sulfated and unsulfated core 1 O-glycans from salivary MUC7 protein in rheumatoid arthritis. Mol. Cell. Proteomics 12 (2013), 921–931, 10.1074/mcp.M113.028878.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 921-931
    • Flowers, S.A.1    Ali, L.2    Lane, C.S.3    Olin, M.4    Karlsson, N.G.5
  • 81
    • 80855127433 scopus 로고    scopus 로고
    • MALDI-TOF and SELDI-TOF analysis: “tandem” techniques to identify potential biomarker in fibromyalgia
    • Giacomelli, C., Bazzichi, L., Giusti, L., Ciregia, F., Baldini, C., Da Valle, Y., et al. MALDI-TOF and SELDI-TOF analysis: “tandem” techniques to identify potential biomarker in fibromyalgia. Reumatismo 63 (2011), 165–170, 10.4081/reumatismo.2011.165.
    • (2011) Reumatismo , vol.63 , pp. 165-170
    • Giacomelli, C.1    Bazzichi, L.2    Giusti, L.3    Ciregia, F.4    Baldini, C.5    Da Valle, Y.6
  • 82
    • 74149084375 scopus 로고    scopus 로고
    • Identification of a truncated cystatin SA-I as a saliva biomarker for oral squamous cell carcinoma using the SELDI ProteinChip platform
    • Shintani, S., Hamakawa, H., Ueyama, Y., Hatori, M., Toyoshima, T., Identification of a truncated cystatin SA-I as a saliva biomarker for oral squamous cell carcinoma using the SELDI ProteinChip platform. Int. J. Oral Maxillofac. Surg. 39 (2010), 68–74, 10.1016/j.ijom.2009.10.001.
    • (2010) Int. J. Oral Maxillofac. Surg. , vol.39 , pp. 68-74
    • Shintani, S.1    Hamakawa, H.2    Ueyama, Y.3    Hatori, M.4    Toyoshima, T.5
  • 84
    • 33749639880 scopus 로고    scopus 로고
    • Identification of parotid salivary biomarkers in Sjögren's syndrome by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry and two-dimensional difference gel electrophoresis
    • Ryu, O.H., Atkinson, J.C., Hoehn, G.T., Illei, G.G., Hart, T.C., Identification of parotid salivary biomarkers in Sjögren's syndrome by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry and two-dimensional difference gel electrophoresis. Rheumatology 45 (2006), 1077–1086, 10.1093/rheumatology/kei212.
    • (2006) Rheumatology , vol.45 , pp. 1077-1086
    • Ryu, O.H.1    Atkinson, J.C.2    Hoehn, G.T.3    Illei, G.G.4    Hart, T.C.5
  • 85
    • 33645728160 scopus 로고    scopus 로고
    • The use of surface-enhanced laser desorption / ionization time-of-flight mass spectrometry to detect putative breast cancer markers in saliva: a feasibility study
    • Bigler, L., Streckfus, C.F., Bigler, L.R., Zwick, M., The use of surface-enhanced laser desorption / ionization time-of-flight mass spectrometry to detect putative breast cancer markers in saliva: a feasibility study. J. Oral Pathol. Med. 125 (2006), 292–300, 10.1111/j.1600-0714.2006.00427.x.
    • (2006) J. Oral Pathol. Med. , vol.125 , pp. 292-300
    • Bigler, L.1    Streckfus, C.F.2    Bigler, L.R.3    Zwick, M.4
  • 86
    • 84975781062 scopus 로고    scopus 로고
    • Expression of salivary biomarkers in patients with Oral Mucositis: evaluation by SELDI-TOF/MS
    • (n/a–n/a)
    • Ardito, F., Giuliani, M., Perrone, D., Giannatempo, G., Di Fede, O., Favia, G., et al. Expression of salivary biomarkers in patients with Oral Mucositis: evaluation by SELDI-TOF/MS. Oral Dis., 2015, 10.1111/odi.12405 (n/a–n/a).
    • (2015) Oral Dis.
    • Ardito, F.1    Giuliani, M.2    Perrone, D.3    Giannatempo, G.4    Di Fede, O.5    Favia, G.6
  • 87
    • 0025941162 scopus 로고
    • Changing trends in oral cancer in the United States to 1985: a Connecticut study., J. Oral Maxillofac. Surg., 1935
    • J.K. Chen, E. Eisenberg, D.J. Krutchkoff, R. V Katz, Changing trends in oral cancer in the United States, 1935 to 1985: a Connecticut study., J. Oral Maxillofac. Surg. 49 (1991) 1152–8.
    • (1991) , vol.49 , pp. 1152-8
    • Chen, J.K.1    Eisenberg, E.2    Krutchkoff, D.J.3    Katz, R.V.4
  • 88
    • 0029034064 scopus 로고
    • Cancer incidence and mortality in young adults in Vaud, Switzerland, 1974–1992
    • Levi, F., La Vecchia, C., Randimbison, L., Te, V.C., Cancer incidence and mortality in young adults in Vaud, Switzerland, 1974–1992. Int. J. Cancer 61 (1995), 606–610.
    • (1995) Int. J. Cancer , vol.61 , pp. 606-610
    • Levi, F.1    La Vecchia, C.2    Randimbison, L.3    Te, V.C.4
  • 89
    • 77950272369 scopus 로고    scopus 로고
    • Antimicrobial peptides present in mammalian skin and gut are multifunctional defence molecules
    • Metz-Boutigue, M.-H., Shooshtarizadeh, P., Prevost, G., Haikel, Y., Chich, J.-F., Antimicrobial peptides present in mammalian skin and gut are multifunctional defence molecules. Curr. Pharm. Des. 16 (2010), 1024–1039.
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 1024-1039
    • Metz-Boutigue, M.-H.1    Shooshtarizadeh, P.2    Prevost, G.3    Haikel, Y.4    Chich, J.-F.5
  • 90
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides: the ancient arm of the human immune system
    • Wiesner, J., Vilcinskas, A., Antimicrobial peptides: the ancient arm of the human immune system. Virulence 1 (2010), 440–464, 10.4161/viru.1.5.12983.
    • (2010) Virulence , vol.1 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2
  • 91
    • 84942293774 scopus 로고    scopus 로고
    • Highly abundant defense proteins in human sweat as revealed by targeted proteomics and label-free quantification mass spectrometry
    • Csősz, É., Emri, G., Kalló, G., Tsaprailis, G., Tőzsér, J., Highly abundant defense proteins in human sweat as revealed by targeted proteomics and label-free quantification mass spectrometry. J. Eur. Acad. Dermatol. Venereol. 29 (2015), 2024–2031, 10.1111/jdv.13221.
    • (2015) J. Eur. Acad. Dermatol. Venereol. , vol.29 , pp. 2024-2031
    • Csősz, É.1    Emri, G.2    Kalló, G.3    Tsaprailis, G.4    Tőzsér, J.5
  • 92
    • 59349120490 scopus 로고    scopus 로고
    • Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications
    • Hassan, M.I., Waheed, A., Yadav, S., Singh, T.P., Ahmad, F., Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications. Cell. Mol. Life Sci. 66 (2009), 447–459, 10.1007/s00018-008-8463-x.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 447-459
    • Hassan, M.I.1    Waheed, A.2    Yadav, S.3    Singh, T.P.4    Ahmad, F.5
  • 93
    • 77449142191 scopus 로고    scopus 로고
    • The clusterin paradigm in prostate and breast carcinogenesis
    • Rizzi, F., Bettuzzi, S., The clusterin paradigm in prostate and breast carcinogenesis. Endocr. Relat. Cancer 17 (2010), R1–17, 10.1677/ERC-09-0140.
    • (2010) Endocr. Relat. Cancer , vol.17 , pp. R1-17
    • Rizzi, F.1    Bettuzzi, S.2
  • 94
    • 47349099698 scopus 로고    scopus 로고
    • Apolipoprotein D is involved in the mechanisms regulating protection from oxidative stress
    • Ganfornina, M.D., Do Carmo, S., Lora, J.M., Torres-Schumann, S., Vogel, M., Allhorn, M., et al. Apolipoprotein D is involved in the mechanisms regulating protection from oxidative stress. Aging Cell 7 (2008), 506–515, 10.1111/j.1474-9726.2008.00395.x.
    • (2008) Aging Cell , vol.7 , pp. 506-515
    • Ganfornina, M.D.1    Do Carmo, S.2    Lora, J.M.3    Torres-Schumann, S.4    Vogel, M.5    Allhorn, M.6
  • 95
    • 0842289185 scopus 로고    scopus 로고
    • Human serum albumin and its N-terminal tetrapeptide (DAHK) block oxidant-induced neuronal death
    • Gum, E.T., Swanson, R.A., Alano, C., Liu, J., Hong, S., Weinstein, P.R., et al. Human serum albumin and its N-terminal tetrapeptide (DAHK) block oxidant-induced neuronal death. Stroke 35 (2004), 590–595, 10.1161/01.STR.0000110790.05859.DA.
    • (2004) Stroke , vol.35 , pp. 590-595
    • Gum, E.T.1    Swanson, R.A.2    Alano, C.3    Liu, J.4    Hong, S.5    Weinstein, P.R.6
  • 96
    • 84922676516 scopus 로고    scopus 로고
    • Quantitative proteomics of the human skin secretome reveal a reduction in immune defense mediators in ectodermal dysplasia patients
    • Burian, M., Velic, A., Matic, K., Günther, S., Kraft, B., Gonser, L., et al. Quantitative proteomics of the human skin secretome reveal a reduction in immune defense mediators in ectodermal dysplasia patients. J. Investig. Dermatol. 135 (2015), 759–767, 10.1038/jid.2014.462.
    • (2015) J. Investig. Dermatol. , vol.135 , pp. 759-767
    • Burian, M.1    Velic, A.2    Matic, K.3    Günther, S.4    Kraft, B.5    Gonser, L.6
  • 97
    • 84859621668 scopus 로고    scopus 로고
    • Proteomic analysis of eccrine sweat: implications for the discovery of schizophrenia biomarker proteins
    • Raiszadeh, M.M., Ross, M.M., Russo, P.S., Schaepper, M.A., Zhou, W., Deng, J., et al. Proteomic analysis of eccrine sweat: implications for the discovery of schizophrenia biomarker proteins. J. Proteome Res. 11 (2012), 2127–2139, 10.1021/pr2007957.
    • (2012) J. Proteome Res. , vol.11 , pp. 2127-2139
    • Raiszadeh, M.M.1    Ross, M.M.2    Russo, P.S.3    Schaepper, M.A.4    Zhou, W.5    Deng, J.6
  • 98
    • 0021252832 scopus 로고
    • Electrophoretic patterns of proteins in cystic fibrosis sweat
    • Penneys, N.S., Haft, J., Rubin, R., Electrophoretic patterns of proteins in cystic fibrosis sweat. J. Investig. Dermatol. 83 (1984), 238–239.
    • (1984) J. Investig. Dermatol. , vol.83 , pp. 238-239
    • Penneys, N.S.1    Haft, J.2    Rubin, R.3
  • 99
    • 20444384801 scopus 로고    scopus 로고
    • Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo
    • Rieg, S., Steffen, H., Seeber, S., Humeny, A., Kalbacher, H., Dietz, K., et al. Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo. J. Immunol. 174 (2005), 8003–8010, 10.1016/S0093-3619(08)70018-2.
    • (2005) J. Immunol. , vol.174 , pp. 8003-8010
    • Rieg, S.1    Steffen, H.2    Seeber, S.3    Humeny, A.4    Kalbacher, H.5    Dietz, K.6
  • 100
    • 0018360724 scopus 로고
    • Total free amino acids, ammonia, and protein in the sweat of children
    • Alexiou, D., Anagnostopoulos, A., Papadatos, C., Total free amino acids, ammonia, and protein in the sweat of children. Am. J. Clin. Nutr. 32 (1979), 750–752.
    • (1979) Am. J. Clin. Nutr. , vol.32 , pp. 750-752
    • Alexiou, D.1    Anagnostopoulos, A.2    Papadatos, C.3
  • 101
    • 0033665646 scopus 로고    scopus 로고
    • Variations in regional sweat composition in normal human males
    • Patterson, M.J., Galloway, S.D., Nimmo, M.A., Variations in regional sweat composition in normal human males. Exp. Physiol. 85 (2000), 869–875.
    • (2000) Exp. Physiol. , vol.85 , pp. 869-875
    • Patterson, M.J.1    Galloway, S.D.2    Nimmo, M.A.3
  • 102
    • 84893137825 scopus 로고    scopus 로고
    • Regional variations in transepidermal water loss, eccrine sweat gland density, sweat secretion rates and electrolyte composition in resting and exercising humans
    • Taylor, N.A., Machado-Moreira, C.A., Regional variations in transepidermal water loss, eccrine sweat gland density, sweat secretion rates and electrolyte composition in resting and exercising humans. Extreme Physiology & Medicine, 2, 2013, 4, 10.1186/2046-7648-2-4.
    • (2013) Extreme Physiology & Medicine , vol.2 , pp. 4
    • Taylor, N.A.1    Machado-Moreira, C.A.2
  • 103
    • 0022461784 scopus 로고
    • Total protein concentration in selectively collected secretions from the middle and inferior meatus of the nose
    • Sueno, K., Nakaima, N., Shingaki, K., Ura, M., Noda, Y., Kosugi, T., et al. Total protein concentration in selectively collected secretions from the middle and inferior meatus of the nose. Auris Nasus Larynx 13:Suppl 1 (1986), S85–S88.
    • (1986) Auris Nasus Larynx , vol.13 , pp. S85-S88
    • Sueno, K.1    Nakaima, N.2    Shingaki, K.3    Ura, M.4    Noda, Y.5    Kosugi, T.6
  • 105
    • 0032968506 scopus 로고    scopus 로고
    • Innate antimicrobial activity of nasal secretions
    • Cole, A.M., Dewan, P., Ganz, T., Innate antimicrobial activity of nasal secretions. Infect. Immun. 67 (1999), 3267–3275.
    • (1999) Infect. Immun. , vol.67 , pp. 3267-3275
    • Cole, A.M.1    Dewan, P.2    Ganz, T.3
  • 107
    • 84924357946 scopus 로고    scopus 로고
    • Proteomic analysis of pediatric sinonasal secretions shows increased MUC5B mucin in CRS
    • Saieg, A., Brown, K.J., Pena, M.T., Rose, M.C., Preciado, D., Proteomic analysis of pediatric sinonasal secretions shows increased MUC5B mucin in CRS. Pediatr. Res. 77 (2015), 356–362, 10.1038/pr.2014.187.
    • (2015) Pediatr. Res. , vol.77 , pp. 356-362
    • Saieg, A.1    Brown, K.J.2    Pena, M.T.3    Rose, M.C.4    Preciado, D.5
  • 108
    • 3042663342 scopus 로고    scopus 로고
    • Analysis of the sinusitis nasal lavage fluid proteome using capillary liquid chromatography interfaced to electrospray ionization-quadrupole time of flight- tandem mass spectrometry
    • Casado, B., Pannell, L.K., Viglio, S., Iadarola, P., Baraniuk, J.N., Analysis of the sinusitis nasal lavage fluid proteome using capillary liquid chromatography interfaced to electrospray ionization-quadrupole time of flight- tandem mass spectrometry. Electrophoresis 25 (2004), 1386–1393, 10.1002/elps.200305862.
    • (2004) Electrophoresis , vol.25 , pp. 1386-1393
    • Casado, B.1    Pannell, L.K.2    Viglio, S.3    Iadarola, P.4    Baraniuk, J.N.5
  • 109
    • 78649985806 scopus 로고    scopus 로고
    • A pathway-based approach to find novel markers of local glucocorticoid treatment in intermittent allergic rhinitis
    • Wang, H., Chavali, S., Mobini, R., Muraro, A., Barbon, F., Boldrin, D., et al. A pathway-based approach to find novel markers of local glucocorticoid treatment in intermittent allergic rhinitis. Allergy 66 (2011), 132–140, 10.1111/j.1398-9995.2010.02444.x.
    • (2011) Allergy , vol.66 , pp. 132-140
    • Wang, H.1    Chavali, S.2    Mobini, R.3    Muraro, A.4    Barbon, F.5    Boldrin, D.6
  • 110
    • 84868094595 scopus 로고    scopus 로고
    • Brain insulin signaling and Alzheimer's disease: current evidence and future directions
    • Schiöth, H.B., Craft, S., Brooks, S.J., Frey, W.H., Benedict, C., Brain insulin signaling and Alzheimer's disease: current evidence and future directions. Mol. Neurobiol. 46 (2012), 4–10, 10.1007/s12035-011-8229-6.
    • (2012) Mol. Neurobiol. , vol.46 , pp. 4-10
    • Schiöth, H.B.1    Craft, S.2    Brooks, S.J.3    Frey, W.H.4    Benedict, C.5
  • 111
    • 84874971833 scopus 로고    scopus 로고
    • Lactoferrin-modified PEG-co-PCL nanoparticles for enhanced brain delivery of NAP peptide following intranasal administration
    • Liu, Z., Jiang, M., Kang, T., Miao, D., Gu, G., Song, Q., et al. Lactoferrin-modified PEG-co-PCL nanoparticles for enhanced brain delivery of NAP peptide following intranasal administration. Biomaterials 34 (2013), 3870–3881, 10.1016/j.biomaterials.2013.02.003.
    • (2013) Biomaterials , vol.34 , pp. 3870-3881
    • Liu, Z.1    Jiang, M.2    Kang, T.3    Miao, D.4    Gu, G.5    Song, Q.6
  • 112
    • 77953915771 scopus 로고    scopus 로고
    • Noninvasive diagnosis of intraamniotic infection: proteomic biomarkers in vaginal fluid
    • (32.e1–8)
    • Hitti, J., Lapidus, J.A., Lu, X., Reddy, A.P., Jacob, T., Dasari, S., et al. Noninvasive diagnosis of intraamniotic infection: proteomic biomarkers in vaginal fluid. Am. J. Obstet. Gynecol., 203, 2010, 10.1016/j.ajog.2010.03.037 (32.e1–8).
    • (2010) Am. J. Obstet. Gynecol. , vol.203
    • Hitti, J.1    Lapidus, J.A.2    Lu, X.3    Reddy, A.P.4    Jacob, T.5    Dasari, S.6
  • 114
    • 0032710330 scopus 로고    scopus 로고
    • Vaginal lactobacilli, microbial flora, and risk of human immunodeficiency virus type 1 and sexually transmitted disease acquisition
    • Martin, H.L., Richardson, B.A., Nyange, P.M., Lavreys, L., Hillier, S.L., Chohan, B., et al. Vaginal lactobacilli, microbial flora, and risk of human immunodeficiency virus type 1 and sexually transmitted disease acquisition. J. Infect. Dis. 180 (1999), 1863–1868, 10.1086/315127.
    • (1999) J. Infect. Dis. , vol.180 , pp. 1863-1868
    • Martin, H.L.1    Richardson, B.A.2    Nyange, P.M.3    Lavreys, L.4    Hillier, S.L.5    Chohan, B.6
  • 115
    • 34249739205 scopus 로고    scopus 로고
    • Bacterial flora of the female genital tract: function and immune regulation
    • Witkin, S.S., Linhares, I.M., Giraldo, P., Bacterial flora of the female genital tract: function and immune regulation. Best Pract. Res. Clin. Obstet. Gynaecol. 21 (2007), 347–354, 10.1016/j.bpobgyn.2006.12.004.
    • (2007) Best Pract. Res. Clin. Obstet. Gynaecol. , vol.21 , pp. 347-354
    • Witkin, S.S.1    Linhares, I.M.2    Giraldo, P.3
  • 116
    • 78649799773 scopus 로고    scopus 로고
    • Use of cervicovaginal fluid for the identification of biomarkers for pathologies of the female genital tract
    • Zegels, G., Van Raemdonck, G.A., Tjalma, W.A., Van Ostade, X.W., Use of cervicovaginal fluid for the identification of biomarkers for pathologies of the female genital tract. Proteome Sci., 8, 2010, 63, 10.1186/1477-5956-8-63.
    • (2010) Proteome Sci. , vol.8 , pp. 63
    • Zegels, G.1    Van Raemdonck, G.A.2    Tjalma, W.A.3    Van Ostade, X.W.4
  • 117
    • 34547172207 scopus 로고    scopus 로고
    • Proteomic analysis of human cervico-vaginal fluid
    • Shaw, J.L.V., Smith, C.R., Diamandis, E.P., Proteomic analysis of human cervico-vaginal fluid. J. Proteome Res. 6 (2007), 2859–2865, 10.1021/pr0701658.
    • (2007) J. Proteome Res. , vol.6 , pp. 2859-2865
    • Shaw, J.L.V.1    Smith, C.R.2    Diamandis, E.P.3
  • 118
    • 33846591828 scopus 로고    scopus 로고
    • Proteomic analysis of cervical-vaginal fluid: identification of novel biomarkers for detection of intra-amniotic infection
    • Gravett, M.G., Thomas, A., Schneider, K.A., Reddy, A.P., Dasari, S., Jacob, T., et al. Proteomic analysis of cervical-vaginal fluid: identification of novel biomarkers for detection of intra-amniotic infection. J. Proteome Res. 6 (2007), 89–96, 10.1021/pr060149v.
    • (2007) J. Proteome Res. , vol.6 , pp. 89-96
    • Gravett, M.G.1    Thomas, A.2    Schneider, K.A.3    Reddy, A.P.4    Dasari, S.5    Jacob, T.6
  • 119
    • 84898947649 scopus 로고    scopus 로고
    • Human epididymis protein 4 and secretory leukocyte protease inhibitor in vaginal fluid: relation to vaginal components and bacterial composition
    • Orfanelli, T., Jayaram, A., Doulaveris, G., Forney, L.J., Ledger, W.J., Witkin, S.S., Human epididymis protein 4 and secretory leukocyte protease inhibitor in vaginal fluid: relation to vaginal components and bacterial composition. Reproductive Sciences (Thousand Oaks, Calif.) 21 (2014), 538–542, 10.1177/1933719113503416.
    • (2014) Reproductive Sciences (Thousand Oaks, Calif.) , vol.21 , pp. 538-542
    • Orfanelli, T.1    Jayaram, A.2    Doulaveris, G.3    Forney, L.J.4    Ledger, W.J.5    Witkin, S.S.6
  • 120
    • 29144497972 scopus 로고    scopus 로고
    • Proteomic analysis using protein chips to detect biomarkers in cervical and amniotic fluid in women with intra-amniotic inflammation., J. Proteome Res. 4 2236–42. doi:.
    • U. Rüetschi, A. Rosén, G. Karlsson, H. Zetterberg, L. Rymo, H. Hagberg, et al., Proteomic analysis using protein chips to detect biomarkers in cervical and amniotic fluid in women with intra-amniotic inflammation., J. Proteome Res. 4 2236–42. doi: http://dx.doi.org/10.1021/pr050139e.
    • Rüetschi, U.1    Rosén, A.2    Karlsson, G.3    Zetterberg, H.4    Rymo, L.5    Hagberg, H.6
  • 121
    • 34248196045 scopus 로고    scopus 로고
    • Identification of novel protein biomarkers of preterm birth in human cervical-vaginal fluid
    • Pereira, L., Reddy, A.P., Jacob, T., Thomas, A., Schneider, K.A., Dasari, S., et al. Identification of novel protein biomarkers of preterm birth in human cervical-vaginal fluid. J. Proteome Res. 6 (2007), 1269–1276, 10.1021/pr0605421.
    • (2007) J. Proteome Res. , vol.6 , pp. 1269-1276
    • Pereira, L.1    Reddy, A.P.2    Jacob, T.3    Thomas, A.4    Schneider, K.A.5    Dasari, S.6
  • 122
    • 52049107191 scopus 로고    scopus 로고
    • Proteomic analysis of human cervico-vaginal fluid displays differential protein expression in association with labor onset at term
    • Di Quinzio, M.K.W., Georgiou, H.M., Holdsworth-Carson, S.J., Ayhan, M., Heng, Y.J., Walker, S.P., et al. Proteomic analysis of human cervico-vaginal fluid displays differential protein expression in association with labor onset at term. J. Proteome Res. 7 (2008), 1916–1921, 10.1021/pr7006413.
    • (2008) J. Proteome Res. , vol.7 , pp. 1916-1921
    • Di Quinzio, M.K.W.1    Georgiou, H.M.2    Holdsworth-Carson, S.J.3    Ayhan, M.4    Heng, Y.J.5    Walker, S.P.6
  • 123
    • 77949839899 scopus 로고    scopus 로고
    • Temporal proteomic analysis of human cervicovaginal fluid with impending term labor
    • Heng, Y.J., Di Quinzio, M.K.W., Permezel, M., Ayhan, M., Rice, G.E., Georgiou, H.M., Temporal proteomic analysis of human cervicovaginal fluid with impending term labor. J. Proteome Res. 9 (2010), 1344–1350, 10.1021/pr900892f.
    • (2010) J. Proteome Res. , vol.9 , pp. 1344-1350
    • Heng, Y.J.1    Di Quinzio, M.K.W.2    Permezel, M.3    Ayhan, M.4    Rice, G.E.5    Georgiou, H.M.6
  • 125
    • 66749133422 scopus 로고    scopus 로고
    • Identification and quantification of preterm birth biomarkers in human cervicovaginal fluid by liquid chromatography/tandem mass spectrometry
    • Shah, S.J., Yu, K.H., Sangar, V., Parry, S.I., Blair, I.A., Identification and quantification of preterm birth biomarkers in human cervicovaginal fluid by liquid chromatography/tandem mass spectrometry. J. Proteome Res. 8 (2009), 2407–2417, 10.1021/pr8010342.
    • (2009) J. Proteome Res. , vol.8 , pp. 2407-2417
    • Shah, S.J.1    Yu, K.H.2    Sangar, V.3    Parry, S.I.4    Blair, I.A.5
  • 126
    • 84933055854 scopus 로고    scopus 로고
    • Identification of protein biomarkers for cervical cancer using human cervicovaginal fluid
    • Van Raemdonck, G.A.A., Tjalma, W.A.A., Coen, E.P., Depuydt, C.E., Van Ostade, X.W.M., Identification of protein biomarkers for cervical cancer using human cervicovaginal fluid. PLoS One, 9, 2014, e106488, 10.1371/journal.pone.0106488.
    • (2014) PLoS One , vol.9
    • Van Raemdonck, G.A.A.1    Tjalma, W.A.A.2    Coen, E.P.3    Depuydt, C.E.4    Van Ostade, X.W.M.5
  • 127
    • 84899840430 scopus 로고    scopus 로고
    • Increased Serpin A5 levels in the cervicovaginal fluid of HIV-1 exposed seronegatives suggest that a subtle balance between serine proteases and their inhibitors may determine susceptibility to HIV-1 infection
    • Van Raemdonck, G., Zegels, G., Coen, E., Vuylsteke, B., Jennes, W., Van Ostade, X., Increased Serpin A5 levels in the cervicovaginal fluid of HIV-1 exposed seronegatives suggest that a subtle balance between serine proteases and their inhibitors may determine susceptibility to HIV-1 infection. Virology 458–459 (2014), 11–21, 10.1016/j.virol.2014.04.015.
    • (2014) Virology , vol.458-459 , pp. 11-21
    • Van Raemdonck, G.1    Zegels, G.2    Coen, E.3    Vuylsteke, B.4    Jennes, W.5    Van Ostade, X.6
  • 128
    • 3142677421 scopus 로고    scopus 로고
    • Protein reabsorption in renal proximal tubule-function and dysfunction in kidney pathophysiology
    • Christensen, E.I., Gburek, J., Protein reabsorption in renal proximal tubule-function and dysfunction in kidney pathophysiology. Pediatric Nephrology (Berlin, Germany) 19 (2004), 714–721, 10.1007/s00467-004-1494-0.
    • (2004) Pediatric Nephrology (Berlin, Germany) , vol.19 , pp. 714-721
    • Christensen, E.I.1    Gburek, J.2
  • 129
    • 1442275722 scopus 로고    scopus 로고
    • Why do we not all have proteinuria? An update of our current understanding of the glomerular barrier
    • Haraldsson, B., Sörensson, J., Why do we not all have proteinuria? An update of our current understanding of the glomerular barrier. News Physiol. Sci. 19 (2004), 7–10.
    • (2004) News Physiol. Sci. , vol.19 , pp. 7-10
    • Haraldsson, B.1    Sörensson, J.2
  • 131
    • 70449312786 scopus 로고
    • Investigation into methods of collection of urine for culture from men and women
    • (accessed February 15, 2016)
    • Clarke, S.H., Investigation into methods of collection of urine for culture from men and women. Br. Med. J. 2 (1960), 1491–1493 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2097631&tool=pmcentrez&rendertype=abstract (accessed February 15, 2016).
    • (1960) Br. Med. J. , vol.2 , pp. 1491-1493
    • Clarke, S.H.1
  • 132
    • 0003511692 scopus 로고    scopus 로고
    • Fundamentals of Urine and Body Fluid Analysis
    • 3rd ed Elsevier/Saunders St. Louis, Mo
    • Brunzel, N.A., Fundamentals of Urine and Body Fluid Analysis. 3rd ed, 2013, Elsevier/Saunders, St. Louis, Mo.
    • (2013)
    • Brunzel, N.A.1
  • 133
    • 0024058029 scopus 로고
    • Collection of urine specimens in general practice: to clean or not to clean?
    • Bradbury, S.M., Collection of urine specimens in general practice: to clean or not to clean?. J. R. Coll. Gen. Pract. 38 (1988), 363–365.
    • (1988) J. R. Coll. Gen. Pract. , vol.38 , pp. 363-365
    • Bradbury, S.M.1
  • 134
    • 0029908225 scopus 로고    scopus 로고
    • Megalin/gp330 mediates uptake of albumin in renal proximal tubule
    • (accessed January 24, 2016)
    • Cui, S., Verroust, P.J., Moestrup, S.K., Christensen, E.I., Megalin/gp330 mediates uptake of albumin in renal proximal tubule. Am. J. Physiol. 271 (1996), F900–F907 http://www.ncbi.nlm.nih.gov/pubmed/8898021 (accessed January 24, 2016).
    • (1996) Am. J. Physiol. , vol.271 , pp. F900-F907
    • Cui, S.1    Verroust, P.J.2    Moestrup, S.K.3    Christensen, E.I.4
  • 135
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun, T., Shen, R.-F., Knepper, M.A., Identification and proteomic profiling of exosomes in human urine. Proc. Natl. Acad. Sci. 101 (2004), 13368–13373, 10.1073/pnas.0403453101.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.-F.2    Knepper, M.A.3
  • 137
    • 11144356366 scopus 로고    scopus 로고
    • Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots
    • Pieper, R., Gatlin, C.L., McGrath, A.M., Makusky, A.J., Mondal, M., Seonarain, M., et al. Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots. Proteomics 4 (2004), 1159–1174, 10.1002/pmic.200300661.
    • (2004) Proteomics , vol.4 , pp. 1159-1174
    • Pieper, R.1    Gatlin, C.L.2    McGrath, A.M.3    Makusky, A.J.4    Mondal, M.5    Seonarain, M.6
  • 138
    • 33645464362 scopus 로고    scopus 로고
    • Concanavalin A-captured glycoproteins in healthy human urine
    • Wang, L., Li, F., Sun, W., Wu, S., Wang, X., Zhang, L., et al. Concanavalin A-captured glycoproteins in healthy human urine. Mol. Cell. Proteomics 5 (2006), 560–562, 10.1074/mcp.D500013-MCP200.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 560-562
    • Wang, L.1    Li, F.2    Sun, W.3    Wu, S.4    Wang, X.5    Zhang, L.6
  • 139
    • 29544433936 scopus 로고    scopus 로고
    • Human urine proteome analysis by three separation approaches
    • Sun, W., Li, F., Wu, S., Wang, X., Zheng, D., Wang, J., et al. Human urine proteome analysis by three separation approaches. Proteomics 5 (2005), 4994–5001, 10.1002/pmic.200401334.
    • (2005) Proteomics , vol.5 , pp. 4994-5001
    • Sun, W.1    Li, F.2    Wu, S.3    Wang, X.4    Zheng, D.5    Wang, J.6
  • 141
    • 33847635745 scopus 로고    scopus 로고
    • Prediction of diabetic nephropathy using urine proteomic profiling 10 years prior to development of nephropathy
    • Otu, H.H., Can, H., Spentzos, D., Nelson, R.G., Hanson, R.L., Looker, H.C., et al. Prediction of diabetic nephropathy using urine proteomic profiling 10 years prior to development of nephropathy. Diabetes Care 30 (2007), 638–643, 10.2337/dc06-1656.
    • (2007) Diabetes Care , vol.30 , pp. 638-643
    • Otu, H.H.1    Can, H.2    Spentzos, D.3    Nelson, R.G.4    Hanson, R.L.5    Looker, H.C.6
  • 142
    • 50849092540 scopus 로고    scopus 로고
    • CE-MS analysis of the human urinary proteome for biomarker discovery and disease diagnostics
    • Coon, J.J., Zürbig, P., Dakna, M., Dominiczak, A.F., Decramer, S., Fliser, D., et al. CE-MS analysis of the human urinary proteome for biomarker discovery and disease diagnostics. Proteomics Clin. Appl., 2, 2008, 964, 10.1002/prca.200800024.
    • (2008) Proteomics Clin. Appl. , vol.2 , pp. 964
    • Coon, J.J.1    Zürbig, P.2    Dakna, M.3    Dominiczak, A.F.4    Decramer, S.5    Fliser, D.6
  • 143
    • 10644231668 scopus 로고    scopus 로고
    • Proteomic analysis of voided urine after prostatic massage from patients with prostate cancer: a pilot study
    • Rehman, I., Azzouzi, A.R., Catto, J.W.F., Allen, S., Cross, S.S., Feeley, K., et al. Proteomic analysis of voided urine after prostatic massage from patients with prostate cancer: a pilot study. Urology 64 (2004), 1238–1243, 10.1016/j.urology.2004.06.063.
    • (2004) Urology , vol.64 , pp. 1238-1243
    • Rehman, I.1    Azzouzi, A.R.2    Catto, J.W.F.3    Allen, S.4    Cross, S.S.5    Feeley, K.6
  • 145
    • 68049101085 scopus 로고    scopus 로고
    • Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction
    • Quintana, L.F., Campistol, J.M., Alcolea, M.P., Bañon-Maneus, E., Sol-González, A., Cutillas, P.R., Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction. Mol. Cell. Proteomics 8 (2009), 1658–1673, 10.1074/mcp.M900059-MCP200.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1658-1673
    • Quintana, L.F.1    Campistol, J.M.2    Alcolea, M.P.3    Bañon-Maneus, E.4    Sol-González, A.5    Cutillas, P.R.6
  • 146
    • 79960869429 scopus 로고    scopus 로고
    • Identification of β2-microglobulin as a urinary biomarker for chronic allograft nephropathy using proteomic methods
    • Johnston, O., Cassidy, H., O'Connell, S., O'Riordan, A., Gallagher, W., Maguire, P.B., et al. Identification of β2-microglobulin as a urinary biomarker for chronic allograft nephropathy using proteomic methods. Proteomics Clin. Appl. 5 (2011), 422–431, 10.1002/prca.201000160.
    • (2011) Proteomics Clin. Appl. , vol.5 , pp. 422-431
    • Johnston, O.1    Cassidy, H.2    O'Connell, S.3    O'Riordan, A.4    Gallagher, W.5    Maguire, P.B.6
  • 147
    • 84928266354 scopus 로고    scopus 로고
    • Label-free quantitative urinary proteomics identifies the arginase pathway as a new player in congenital obstructive nephropathy
    • Lacroix, C., Caubet, C., Gonzalez-de-Peredo, A., Breuil, B., Bouyssié, D., Stella, A., et al. Label-free quantitative urinary proteomics identifies the arginase pathway as a new player in congenital obstructive nephropathy. Mol. Cell. Proteomics 13 (2014), 3421–3434, 10.1074/mcp.M114.040121.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3421-3434
    • Lacroix, C.1    Caubet, C.2    Gonzalez-de-Peredo, A.3    Breuil, B.4    Bouyssié, D.5    Stella, A.6
  • 148
  • 149
    • 2342642123 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionization-time of flight-mass spectrometry (SELDI-TOF-MS): a new proteomic urinary test for patients with urolithiasis
    • Cadieux, P.A., Beiko, D.T., Watterson, J.D., Burton, J.P., Howard, J.C., Knudsen, B.E., et al. Surface-enhanced laser desorption/ionization-time of flight-mass spectrometry (SELDI-TOF-MS): a new proteomic urinary test for patients with urolithiasis. J. Clin. Lab. Anal. 18 (2004), 170–175, 10.1002/jcla.20018.
    • (2004) J. Clin. Lab. Anal. , vol.18 , pp. 170-175
    • Cadieux, P.A.1    Beiko, D.T.2    Watterson, J.D.3    Burton, J.P.4    Howard, J.C.5    Knudsen, B.E.6
  • 150
    • 27144531588 scopus 로고    scopus 로고
    • Proteome analysis of gelatin-bound urinary proteins from patients with bladder cancers
    • Saito, M., Kimoto, M., Araki, T., Shimada, Y., Fujii, R., Oofusa, K., et al. Proteome analysis of gelatin-bound urinary proteins from patients with bladder cancers. Eur. Urol. 48 (2005), 865–871, 10.1016/j.eururo.2005.04.028.
    • (2005) Eur. Urol. , vol.48 , pp. 865-871
    • Saito, M.1    Kimoto, M.2    Araki, T.3    Shimada, Y.4    Fujii, R.5    Oofusa, K.6
  • 151
    • 0030832166 scopus 로고    scopus 로고
    • Proteome profiling of bladder squamous cell carcinomas: identification of markers that define their degree of differentiation
    • (accessed January 27, 2016)
    • Ostergaard, M., Rasmussen, H.H., Nielsen, H.V., Vorum, H., Orntoft, T.F., Wolf, H., et al. Proteome profiling of bladder squamous cell carcinomas: identification of markers that define their degree of differentiation. Cancer Res. 57 (1997), 4111–4117 http://www.ncbi.nlm.nih.gov/pubmed/9307301 (accessed January 27, 2016).
    • (1997) Cancer Res. , vol.57 , pp. 4111-4117
    • Ostergaard, M.1    Rasmussen, H.H.2    Nielsen, H.V.3    Vorum, H.4    Orntoft, T.F.5    Wolf, H.6
  • 152
    • 11144356519 scopus 로고    scopus 로고
    • Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine
    • Kageyama, S., Isono, T., Iwaki, H., Wakabayashi, Y., Okada, Y., Kontani, K., et al. Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine. Clin. Chem. 50 (2004), 857–866, 10.1373/clinchem.2003.027425.
    • (2004) Clin. Chem. , vol.50 , pp. 857-866
    • Kageyama, S.1    Isono, T.2    Iwaki, H.3    Wakabayashi, Y.4    Okada, Y.5    Kontani, K.6
  • 153
    • 84877917326 scopus 로고    scopus 로고
    • Identification of potential bladder cancer markers in urine by abundant-protein depletion coupled with quantitative proteomics
    • Chen, C.-L., Lin, T.-S., Tsai, C.-H., Wu, C.-C., Chung, T., Chien, K.-Y., et al. Identification of potential bladder cancer markers in urine by abundant-protein depletion coupled with quantitative proteomics. J. Proteomics 85 (2013), 28–43, 10.1016/j.jprot.2013.04.024.
    • (2013) J. Proteomics , vol.85 , pp. 28-43
    • Chen, C.-L.1    Lin, T.-S.2    Tsai, C.-H.3    Wu, C.-C.4    Chung, T.5    Chien, K.-Y.6
  • 154
    • 78149375285 scopus 로고    scopus 로고
    • Discovery of novel bladder cancer biomarkers by comparative urine proteomics using iTRAQ technology
    • Chen, Y.-T., Chen, C.-L., Chen, H.-W., Chung, T., Wu, C.-C., Chen, C.-D., et al. Discovery of novel bladder cancer biomarkers by comparative urine proteomics using iTRAQ technology. J. Proteome Res. 9 (2010), 5803–5815, 10.1021/pr100576x.
    • (2010) J. Proteome Res. , vol.9 , pp. 5803-5815
    • Chen, Y.-T.1    Chen, C.-L.2    Chen, H.-W.3    Chung, T.4    Wu, C.-C.5    Chen, C.-D.6
  • 155
    • 77951096890 scopus 로고    scopus 로고
    • Urinary proteomics as a novel tool for biomarker discovery in kidney diseases
    • Wu, J., Chen, Y., Gu, W., Urinary proteomics as a novel tool for biomarker discovery in kidney diseases. J. Zhejiang Univ. Sci. B 11 (2010), 227–237, 10.1631/jzus.B0900327.
    • (2010) J. Zhejiang Univ. Sci. B , vol.11 , pp. 227-237
    • Wu, J.1    Chen, Y.2    Gu, W.3
  • 156
    • 79956044485 scopus 로고    scopus 로고
    • Urinary glycoprotein biomarker discovery for bladder cancer detection using LC/MS-MS and label-free quantification
    • Yang, N., Feng, S., Shedden, K., Xie, X., Liu, Y., Rosser, C.J., et al. Urinary glycoprotein biomarker discovery for bladder cancer detection using LC/MS-MS and label-free quantification. Clin. Cancer Res. 17 (2011), 3349–3359, 10.1158/1078-0432.CCR-10-3121.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 3349-3359
    • Yang, N.1    Feng, S.2    Shedden, K.3    Xie, X.4    Liu, Y.5    Rosser, C.J.6
  • 157
    • 84862832755 scopus 로고    scopus 로고
    • Multiplexed quantification of 63 proteins in human urine by multiple reaction monitoring-based mass spectrometry for discovery of potential bladder cancer biomarkers
    • Chen, Y.-T., Chen, H.-W., Domanski, D., Smith, D.S., Liang, K.-H., Wu, C.-C., et al. Multiplexed quantification of 63 proteins in human urine by multiple reaction monitoring-based mass spectrometry for discovery of potential bladder cancer biomarkers. J. Proteomics 75 (2012), 3529–3545, 10.1016/j.jprot.2011.12.031.
    • (2012) J. Proteomics , vol.75 , pp. 3529-3545
    • Chen, Y.-T.1    Chen, H.-W.2    Domanski, D.3    Smith, D.S.4    Liang, K.-H.5    Wu, C.-C.6
  • 158
    • 84891713377 scopus 로고    scopus 로고
    • Urine screening by Seldi-Tof, followed by biomarker identification, in a Brazilian cohort of patients with renal cell carcinoma (RCC)., Int. Braz J Urol. 39
    • G. Alves, D.A. Pereira, V. Sandim, A.A. Ornellas, N. Escher, C. Melle, et al., Urine screening by Seldi-Tof, followed by biomarker identification, in a Brazilian cohort of patients with renal cell carcinoma (RCC)., Int. Braz J Urol. 39 228–39.
    • Alves, G.1    Pereira, D.A.2    Sandim, V.3    Ornellas, A.A.4    Escher, N.5    Melle, C.6
  • 159
    • 45349089587 scopus 로고    scopus 로고
    • Proteomic evaluation of urine from renal cell carcinoma using SELDI-TOF-MS and tree analysis pattern
    • Wu, D.-L., Zhang, W.-H., Wang, W.-J., Jing, S.-B., Xu, Y.-M., Proteomic evaluation of urine from renal cell carcinoma using SELDI-TOF-MS and tree analysis pattern. Technol. Cancer Res. Treat. 7 (2008), 155–160.
    • (2008) Technol. Cancer Res. Treat. , vol.7 , pp. 155-160
    • Wu, D.-L.1    Zhang, W.-H.2    Wang, W.-J.3    Jing, S.-B.4    Xu, Y.-M.5
  • 160
    • 19744380300 scopus 로고    scopus 로고
    • ProteinChip technology reveals distinctive protein expression profiles in the urine of bladder cancer patients
    • Mueller, J., Von Eggeling, F., Driesch, D., Schubert, J., Melle, C., Junker, K., ProteinChip technology reveals distinctive protein expression profiles in the urine of bladder cancer patients. Eur. Urol. 47 (2005), 885–894, 10.1016/j.eururo.2005.02.016.
    • (2005) Eur. Urol. , vol.47 , pp. 885-894
    • Mueller, J.1    Von Eggeling, F.2    Driesch, D.3    Schubert, J.4    Melle, C.5    Junker, K.6
  • 161
    • 0035074699 scopus 로고    scopus 로고
    • Development of a novel proteomic approach for the detection of transitional cell carcinoma of the bladder in urine
    • Vlahou, A., Schellhammer, P.F., Mendrinos, S., Patel, K., Kondylis, F.I., Gong, L., et al. Development of a novel proteomic approach for the detection of transitional cell carcinoma of the bladder in urine. Am. J. Pathol. 158 (2001), 1491–1502, 10.1016/S0002-9440(10)64100-4.
    • (2001) Am. J. Pathol. , vol.158 , pp. 1491-1502
    • Vlahou, A.1    Schellhammer, P.F.2    Mendrinos, S.3    Patel, K.4    Kondylis, F.I.5    Gong, L.6
  • 162
    • 77049102608 scopus 로고    scopus 로고
    • An approach to molecular imaging of atherosclerosis, thrombosis, and vascular inflammation using microparticles of iron oxide
    • McAteer, M.A., Akhtar, A.M., von Zur Muhlen, C., Choudhury, R.P., An approach to molecular imaging of atherosclerosis, thrombosis, and vascular inflammation using microparticles of iron oxide. Atherosclerosis 209 (2010), 18–27, 10.1016/j.atherosclerosis.2009.10.009.
    • (2010) Atherosclerosis , vol.209 , pp. 18-27
    • McAteer, M.A.1    Akhtar, A.M.2    von Zur Muhlen, C.3    Choudhury, R.P.4
  • 163
    • 60849126133 scopus 로고    scopus 로고
    • Evaluation of urine proteome pattern analysis for its potential to reflect coronary artery atherosclerosis in symptomatic patients
    • von Zur Muhlen, C., Schiffer, E., Zuerbig, P., Kellmann, M., Brasse, M., Meert, N., et al. Evaluation of urine proteome pattern analysis for its potential to reflect coronary artery atherosclerosis in symptomatic patients. J. Proteome Res. 8 (2009), 335–345, 10.1021/pr800615t.
    • (2009) J. Proteome Res. , vol.8 , pp. 335-345
    • von Zur Muhlen, C.1    Schiffer, E.2    Zuerbig, P.3    Kellmann, M.4    Brasse, M.5    Meert, N.6
  • 164
    • 72549085929 scopus 로고    scopus 로고
    • Two-dimensional differential in-gel electrophoresis proteomic approaches reveal urine candidate biomarkers in pediatric obstructive sleep apnea
    • Gozal, D., Jortani, S., Snow, A.B., Kheirandish-Gozal, L., Bhattacharjee, R., Kim, J., et al. Two-dimensional differential in-gel electrophoresis proteomic approaches reveal urine candidate biomarkers in pediatric obstructive sleep apnea. Am. J. Respir. Crit. Care Med. 180 (2009), 1253–1261, 10.1164/rccm.200905-0765OC.
    • (2009) Am. J. Respir. Crit. Care Med. , vol.180 , pp. 1253-1261
    • Gozal, D.1    Jortani, S.2    Snow, A.B.3    Kheirandish-Gozal, L.4    Bhattacharjee, R.5    Kim, J.6
  • 165
    • 31544440478 scopus 로고    scopus 로고
    • Proteomic-based discovery and characterization of glycosylated eosinophil-derived neurotoxin and COOH-terminal osteopontin fragments for ovarian cancer in urine
    • Ye, B., Skates, S., Mok, S.C., Horick, N.K., Rosenberg, H.F., Vitonis, A., et al. Proteomic-based discovery and characterization of glycosylated eosinophil-derived neurotoxin and COOH-terminal osteopontin fragments for ovarian cancer in urine. Clin. Cancer Res. 12 (2006), 432–441, 10.1158/1078-0432.CCR-05-0461.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 432-441
    • Ye, B.1    Skates, S.2    Mok, S.C.3    Horick, N.K.4    Rosenberg, H.F.5    Vitonis, A.6
  • 166
    • 84953298807 scopus 로고    scopus 로고
    • Proteomic analysis of urine to identify breast cancer biomarker candidates using a label-free LC-MS/MS approach
    • Beretov, J., Wasinger, V.C., Millar, E.K.A., Schwartz, P., Graham, P.H., Li, Y., Proteomic analysis of urine to identify breast cancer biomarker candidates using a label-free LC-MS/MS approach. PLoS One, 10, 2015, e0141876, 10.1371/journal.pone.0141876.
    • (2015) PLoS One , vol.10
    • Beretov, J.1    Wasinger, V.C.2    Millar, E.K.A.3    Schwartz, P.4    Graham, P.H.5    Li, Y.6
  • 167
    • 84872826514 scopus 로고    scopus 로고
    • Identification of novel biomarkers for sepsis prognosis via urinary proteomic analysis using iTRAQ labeling and 2D-LC-MS/MS
    • Su, L., Cao, L., Zhou, R., Jiang, Z., Xiao, K., Kong, W., et al. Identification of novel biomarkers for sepsis prognosis via urinary proteomic analysis using iTRAQ labeling and 2D-LC-MS/MS. PLoS One, 8, 2013, e54237, 10.1371/journal.pone.0054237.
    • (2013) PLoS One , vol.8
    • Su, L.1    Cao, L.2    Zhou, R.3    Jiang, Z.4    Xiao, K.5    Kong, W.6
  • 168
    • 84874849330 scopus 로고    scopus 로고
    • Urinary proteomics analysis for sepsis biomarkers with iTRAQ labeling and two-dimensional liquid chromatography-tandem mass spectrometry
    • Su, L., Zhou, R., Liu, C., Wen, B., Xiao, K., Kong, W., et al. Urinary proteomics analysis for sepsis biomarkers with iTRAQ labeling and two-dimensional liquid chromatography-tandem mass spectrometry. J. Trauma Acute Care Surg. 74 (2013), 940–945, 10.1097/TA.0b013e31828272c5.
    • (2013) J. Trauma Acute Care Surg. , vol.74 , pp. 940-945
    • Su, L.1    Zhou, R.2    Liu, C.3    Wen, B.4    Xiao, K.5    Kong, W.6
  • 169
    • 0000415976 scopus 로고
    • Constancy of urinary creatinine excretion
    • Vestergaard, P., Leverett, R., Constancy of urinary creatinine excretion. J. Lab. Clin. Med. 51 (1958), 211–218.
    • (1958) J. Lab. Clin. Med. , vol.51 , pp. 211-218
    • Vestergaard, P.1    Leverett, R.2
  • 170
    • 23144461504 scopus 로고    scopus 로고
    • Pilot study of capillary electrophoresis coupled to mass spectrometry as a tool to define potential prostate cancer biomarkers in urine
    • Theodorescu, D., Fliser, D., Wittke, S., Mischak, H., Krebs, R., Walden, M., et al. Pilot study of capillary electrophoresis coupled to mass spectrometry as a tool to define potential prostate cancer biomarkers in urine. Electrophoresis 26 (2005), 2797–2808, 10.1002/elps.200400208.
    • (2005) Electrophoresis , vol.26 , pp. 2797-2808
    • Theodorescu, D.1    Fliser, D.2    Wittke, S.3    Mischak, H.4    Krebs, R.5    Walden, M.6
  • 171
    • 67649544381 scopus 로고    scopus 로고
    • Biomarker discovery in neurodegenerative diseases: a proteomic approach
    • Shi, M., Caudle, W.M., Zhang, J., Biomarker discovery in neurodegenerative diseases: a proteomic approach. Neurobiol. Dis. 35 (2009), 157–164, 10.1016/j.nbd.2008.09.004.
    • (2009) Neurobiol. Dis. , vol.35 , pp. 157-164
    • Shi, M.1    Caudle, W.M.2    Zhang, J.3
  • 173
    • 84908047315 scopus 로고    scopus 로고
    • Urine sample preparation for proteomic analysis
    • Olszowy, P., Buszewski, B., Urine sample preparation for proteomic analysis. J. Sep. Sci. 37 (2014), 2920–2928, 10.1002/jssc.201400331.
    • (2014) J. Sep. Sci. , vol.37 , pp. 2920-2928
    • Olszowy, P.1    Buszewski, B.2
  • 174
    • 84958645720 scopus 로고    scopus 로고
    • Biomarker discovery in mass spectrometry-based urinary proteomics
    • Thomas, S., Hao, L., Ricke, W.A., Li, L., Biomarker discovery in mass spectrometry-based urinary proteomics. Proteomics Clin. Appl. 10:4 (2016), 358–370, 10.1002/prca.201500102.
    • (2016) Proteomics Clin. Appl. , vol.10 , Issue.4 , pp. 358-370
    • Thomas, S.1    Hao, L.2    Ricke, W.A.3    Li, L.4
  • 175
  • 176
    • 79956196909 scopus 로고    scopus 로고
    • Urine proteomics and biomarkers in renal disease
    • Kim, M.J., Frankel, A.H., Tam, F.W.K., Urine proteomics and biomarkers in renal disease. Nephron Exp. Nephrol. 119 (2011), e1–e7, 10.1159/000324223.
    • (2011) Nephron Exp. Nephrol. , vol.119 , pp. e1-e7
    • Kim, M.J.1    Frankel, A.H.2    Tam, F.W.K.3
  • 177
    • 0042905861 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in innate immunity
    • Ganz, T., The role of antimicrobial peptides in innate immunity. Integr. Comp. Biol. 43 (2003), 300–304, 10.1093/icb/43.2.300.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 300-304
    • Ganz, T.1
  • 178
    • 84888867050 scopus 로고    scopus 로고
    • Structure and function of the human skin microbiome
    • Schommer, N.N., Gallo, R.L., Structure and function of the human skin microbiome. Trends Microbiol. 21 (2013), 660–668, 10.1016/j.tim.2013.10.001.
    • (2013) Trends Microbiol. , vol.21 , pp. 660-668
    • Schommer, N.N.1    Gallo, R.L.2
  • 179
    • 84946206131 scopus 로고    scopus 로고
    • Relative quantification of human β-defensins by a proteomics approach based on selected reaction monitoring
    • Kalló, G., Chatterjee, A., Tóth, M., Rajnavölgyi, É., Csutak, A., Tőzsér, J., et al. Relative quantification of human β-defensins by a proteomics approach based on selected reaction monitoring. Rapid Commun. Mass Spectrom. 29 (2015), 1623–1631, 10.1002/rcm.7259.
    • (2015) Rapid Commun. Mass Spectrom. , vol.29 , pp. 1623-1631
    • Kalló, G.1    Chatterjee, A.2    Tóth, M.3    Rajnavölgyi, É.4    Csutak, A.5    Tőzsér, J.6
  • 180
    • 35848948624 scopus 로고    scopus 로고
    • Antimicrobial peptides, innate immunity, and the normally sterile urinary tract
    • Zasloff, M., Antimicrobial peptides, innate immunity, and the normally sterile urinary tract. J. Am. Soc. Nephrol. 18 (2007), 2810–2816, 10.1681/ASN.2007050611.
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 2810-2816
    • Zasloff, M.1
  • 181
    • 0026100932 scopus 로고
    • Cell walls of normal and lysozyme-damaged blastoconidia of Candida albicans: localization of surface factor 4 antigen and vicinal-glycol staining
    • Marquis, G., Garzon, S., Strykowski, H., Auger, P., Cell walls of normal and lysozyme-damaged blastoconidia of Candida albicans: localization of surface factor 4 antigen and vicinal-glycol staining. Infect. Immun. 59 (1991), 1312–1318.
    • (1991) Infect. Immun. , vol.59 , pp. 1312-1318
    • Marquis, G.1    Garzon, S.2    Strykowski, H.3    Auger, P.4
  • 182
    • 0033013458 scopus 로고    scopus 로고
    • Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin
    • Lee-Huang, S., Huang, P.L., Sun, Y., Kung, H.F., Blithe, D.L., Chen, H.C., Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 2678–2681.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2678-2681
    • Lee-Huang, S.1    Huang, P.L.2    Sun, Y.3    Kung, H.F.4    Blithe, D.L.5    Chen, H.C.6
  • 183
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T.H., Smith, K.D., Sato, S., Rodriguez, D.J., Holmes, M.A., Strong, R.K., et al. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432 (2004), 917–921, 10.1038/nature03104.
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6
  • 184
    • 18744397511 scopus 로고    scopus 로고
    • An iron delivery pathway mediated by a lipocalin
    • Yang, J., Goetz, D., Li, J.Y., Wang, W., Mori, K., Setlik, D., et al. An iron delivery pathway mediated by a lipocalin. Mol. Cell 10 (2002), 1045–1056.
    • (2002) Mol. Cell , vol.10 , pp. 1045-1056
    • Yang, J.1    Goetz, D.2    Li, J.Y.3    Wang, W.4    Mori, K.5    Setlik, D.6
  • 185
    • 64849105312 scopus 로고    scopus 로고
    • Lacritin and other new proteins of the lacrimal functional unit
    • McKown, R.L., Wang, N., Raab, R.W., Karnati, R., Zhang, Y., Williams, P.B., et al. Lacritin and other new proteins of the lacrimal functional unit. Exp. Eye Res. 88 (2009), 848–858, 10.1016/j.exer.2008.09.002.
    • (2009) Exp. Eye Res. , vol.88 , pp. 848-858
    • McKown, R.L.1    Wang, N.2    Raab, R.W.3    Karnati, R.4    Zhang, Y.5    Williams, P.B.6
  • 186
    • 33748101108 scopus 로고    scopus 로고
    • Restricted epithelial proliferation by lacritin via PKCalpha-dependent NFAT and mTOR pathways
    • Wang, J., Wang, N., Xie, J., Walton, S.C., McKown, R.L., Raab, R.W., et al. Restricted epithelial proliferation by lacritin via PKCalpha-dependent NFAT and mTOR pathways. J. Cell Biol. 174 (2006), 689–700, 10.1083/jcb.200605140.
    • (2006) J. Cell Biol. , vol.174 , pp. 689-700
    • Wang, J.1    Wang, N.2    Xie, J.3    Walton, S.C.4    McKown, R.L.5    Raab, R.W.6
  • 189
    • 84931567071 scopus 로고    scopus 로고
    • Contribution of epigenetics in diabetic retinopathy
    • Kowluru, R.A., Mishra, M., Contribution of epigenetics in diabetic retinopathy. Sci. China Life Sci. 58 (2015), 556–563, 10.1007/s11427-015-4853-0.
    • (2015) Sci. China Life Sci. , vol.58 , pp. 556-563
    • Kowluru, R.A.1    Mishra, M.2
  • 190
    • 77955013602 scopus 로고    scopus 로고
    • Diabetic retinopathy
    • Cheung, N., Mitchell, P., Wong, T.Y., Diabetic retinopathy. Lancet 376 (2010), 124–136, 10.1016/S0140-6736(09)62124-3.
    • (2010) Lancet , vol.376 , pp. 124-136
    • Cheung, N.1    Mitchell, P.2    Wong, T.Y.3
  • 191
    • 84890318972 scopus 로고    scopus 로고
    • Effects of diabetes on the eye
    • Lutty, G.A., Effects of diabetes on the eye. Invest. Ophthalmol. Vis. Sci. 54 (2013), 81–87, 10.1167/iovs.13-12979.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 81-87
    • Lutty, G.A.1
  • 192
    • 0028366839 scopus 로고
    • The rationale of argon green laser photocoagulation for diabetic maculopathy
    • Dastur, Y.K., The rationale of argon green laser photocoagulation for diabetic maculopathy. J. Postgrad. Med. 40 (1994), 13–17.
    • (1994) J. Postgrad. Med. , vol.40 , pp. 13-17
    • Dastur, Y.K.1
  • 193
    • 84871418985 scopus 로고    scopus 로고
    • Transfer of extracellular vesicles during immune cell-cell interactions
    • Gutiérrez-vázquez, C., Villarroya-beltri, C., Mittelbrunn, M., Transfer of extracellular vesicles during immune cell-cell interactions. Immunol. Rev. 251 (2013), 125–142, 10.1111/imr.12013.Transfer.
    • (2013) Immunol. Rev. , vol.251 , pp. 125-142
    • Gutiérrez-vázquez, C.1    Villarroya-beltri, C.2    Mittelbrunn, M.3
  • 194
    • 84908885164 scopus 로고    scopus 로고
    • Extracellular vesicles as emerging intercellular communicasomes
    • Yoon, Y.J., Kim, O.Y., Gho, Y.S., Extracellular vesicles as emerging intercellular communicasomes. BMB Rep. 47 (2014), 531–539, 10.5483/BMBRep.2014.47.10.164.
    • (2014) BMB Rep. , vol.47 , pp. 531-539
    • Yoon, Y.J.1    Kim, O.Y.2    Gho, Y.S.3
  • 195
    • 84900552714 scopus 로고    scopus 로고
    • Extracellular membrane vesicles as a mechanism of cell-to-cell communication: advantages and disadvantages
    • Turturici, G., Tinnirello, R., Sconzo, G., Geraci, F., Extracellular membrane vesicles as a mechanism of cell-to-cell communication: advantages and disadvantages. Am. J. Physiol. Cell Physiol. 306 (2014), C621–C633, 10.1152/ajpcell.00228.2013.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.306 , pp. C621-C633
    • Turturici, G.1    Tinnirello, R.2    Sconzo, G.3    Geraci, F.4
  • 196
    • 84949934993 scopus 로고    scopus 로고
    • As we wait: coping with an imperfect nomenclature for extracellular vesicles
    • Gould, S.J., Raposo, G., As we wait: coping with an imperfect nomenclature for extracellular vesicles. Journal of Extracellular Vesicles 2 (2013), 3–5, 10.3402/jev.v2i0.20389.
    • (2013) Journal of Extracellular Vesicles , vol.2 , pp. 3-5
    • Gould, S.J.1    Raposo, G.2
  • 197
    • 22044446912 scopus 로고    scopus 로고
    • Exosomal-like vesicles are present in human blood plasma
    • Caby, M.-P., Lankar, D., Claude, V.-S., Raposo, G., Bonnerot, C., Exosomal-like vesicles are present in human blood plasma. Int. Immunol. 17 (2005), 879–887, 10.1093/intimm/dxh267.
    • (2005) Int. Immunol. , vol.17 , pp. 879-887
    • Caby, M.-P.1    Lankar, D.2    Claude, V.-S.3    Raposo, G.4    Bonnerot, C.5
  • 198
    • 67349142591 scopus 로고    scopus 로고
    • Prostate cancer-derived urine exosomes: a novel approach to biomarkers for prostate cancer
    • Nilsson, J., Skog, J., Nordstrand, A., Baranov, V., Mincheva-Nilsson, L., Breakefield, X.O., et al. Prostate cancer-derived urine exosomes: a novel approach to biomarkers for prostate cancer. Br. J. Cancer 100 (2009), 1603–1607, 10.1038/sj.bjc.6605058.
    • (2009) Br. J. Cancer , vol.100 , pp. 1603-1607
    • Nilsson, J.1    Skog, J.2    Nordstrand, A.3    Baranov, V.4    Mincheva-Nilsson, L.5    Breakefield, X.O.6
  • 199
    • 79958048581 scopus 로고    scopus 로고
    • Body fluid derived exosomes as a novel template for clinical diagnostics
    • Keller, S., Ridinger, J., Rupp, A.-K., Janssen, J.W.G., Altevogt, P., Body fluid derived exosomes as a novel template for clinical diagnostics. J. Transl. Med., 9, 2011, 86, 10.1186/1479-5876-9-86.
    • (2011) J. Transl. Med. , vol.9 , pp. 86
    • Keller, S.1    Ridinger, J.2    Rupp, A.-K.3    Janssen, J.W.G.4    Altevogt, P.5
  • 201
    • 78149360255 scopus 로고    scopus 로고
    • Proinflammatory exosomes in bronchoalveolar lavage fluid of patients with sarcoidosis
    • Qazi, K.R., Torregrosa Paredes, P., Dahlberg, B., Grunewald, J., Eklund, A., Gabrielsson, S., Proinflammatory exosomes in bronchoalveolar lavage fluid of patients with sarcoidosis. Thorax 65 (2010), 1016–1024, 10.1136/thx.2009.132027.
    • (2010) Thorax , vol.65 , pp. 1016-1024
    • Qazi, K.R.1    Torregrosa Paredes, P.2    Dahlberg, B.3    Grunewald, J.4    Eklund, A.5    Gabrielsson, S.6
  • 202
    • 34548619487 scopus 로고    scopus 로고
    • Exosomes with immune modulatory features are present in human breast milk
    • Admyre, C., Johansson, S.M., Qazi, K.R., Filén, J.-J., Lahesmaa, R., Norman, M., et al. Exosomes with immune modulatory features are present in human breast milk. J. Immunol. 179 (2007), 1969–1978, 10.4049/jimmunol.179.3.1969.
    • (2007) J. Immunol. , vol.179 , pp. 1969-1978
    • Admyre, C.1    Johansson, S.M.2    Qazi, K.R.3    Filén, J.-J.4    Lahesmaa, R.5    Norman, M.6
  • 204
    • 84926489794 scopus 로고    scopus 로고
    • Proteomics of microparticles with SILAC quantification (PROMIS-Quan): a novel proteomic method for plasma biomarker quantification
    • Harel, M., Oren-Giladi, P., Kaidar-Person, O., Shaked, Y., Geiger, T., Proteomics of microparticles with SILAC quantification (PROMIS-Quan): a novel proteomic method for plasma biomarker quantification. Molecular & Cellular Proteomics: MCP. 14 (2015), 1127–1136, 10.1074/mcp.M114.043364.
    • (2015) Molecular & Cellular Proteomics: MCP. , vol.14 , pp. 1127-1136
    • Harel, M.1    Oren-Giladi, P.2    Kaidar-Person, O.3    Shaked, Y.4    Geiger, T.5
  • 207
    • 84934270711 scopus 로고    scopus 로고
    • Emerging roles of exosomes in normal and pathological conditions: new insights for diagnosis and therapeutic applications
    • De Toro, J., Herschlik, L., Waldner, C., Mongini, C., Emerging roles of exosomes in normal and pathological conditions: new insights for diagnosis and therapeutic applications. Front. Immunol., 6, 2015, 203, 10.3389/fimmu.2015.00203.
    • (2015) Front. Immunol. , vol.6 , pp. 203
    • De Toro, J.1    Herschlik, L.2    Waldner, C.3    Mongini, C.4
  • 209
    • 77957557995 scopus 로고    scopus 로고
    • Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome
    • Rood, I.M., Deegens, J.K.J., Merchant, M.L., Tamboer, W.P.M., Wilkey, D.W., Wetzels, J.F.M., et al. Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome. Kidney Int. 78 (2010), 810–816, 10.1038/ki.2010.262.
    • (2010) Kidney Int. , vol.78 , pp. 810-816
    • Rood, I.M.1    Deegens, J.K.J.2    Merchant, M.L.3    Tamboer, W.P.M.4    Wilkey, D.W.5    Wetzels, J.F.M.6
  • 210
    • 79958078403 scopus 로고    scopus 로고
    • Proteomic analysis of urinary exosomes from patients of early IgA nephropathy and thin basement membrane nephropathy
    • Moon, P.G., Lee, J.E., You, S., Kim, T.K., Cho, J.H., Kim, I.S., et al. Proteomic analysis of urinary exosomes from patients of early IgA nephropathy and thin basement membrane nephropathy. Proteomics 11 (2011), 2459–2475, 10.1002/pmic.201000443.
    • (2011) Proteomics , vol.11 , pp. 2459-2475
    • Moon, P.G.1    Lee, J.E.2    You, S.3    Kim, T.K.4    Cho, J.H.5    Kim, I.S.6
  • 211
    • 52049112613 scopus 로고    scopus 로고
    • Isolation and identification of potential urinary microparticle biomarkers of bladder cancer
    • Smalley, D.M., Sheman, N.E., Nelson, K., Theodorescu, D., Isolation and identification of potential urinary microparticle biomarkers of bladder cancer. J. Proteome Res. 7 (2008), 2088–2096, 10.1021/pr700775x.
    • (2008) J. Proteome Res. , vol.7 , pp. 2088-2096
    • Smalley, D.M.1    Sheman, N.E.2    Nelson, K.3    Theodorescu, D.4
  • 212
    • 84870936601 scopus 로고    scopus 로고
    • Comparative and targeted proteomic analyses of urinary microparticles from bladder cancer and hernia patients
    • Chen, C.L., Lai, Y.F., Tang, P., Chien, K.Y., Yu, J.S., Tsai, C.H., et al. Comparative and targeted proteomic analyses of urinary microparticles from bladder cancer and hernia patients. J. Proteome Res. 11 (2012), 5611–5629, 10.1021/pr3008732.
    • (2012) J. Proteome Res. , vol.11 , pp. 5611-5629
    • Chen, C.L.1    Lai, Y.F.2    Tang, P.3    Chien, K.Y.4    Yu, J.S.5    Tsai, C.H.6


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