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Volumn 8, Issue 5-6, 2014, Pages 338-350

Ensembles of protein termini and specific proteolytic signatures as candidate biomarkers of disease

Author keywords

Biomarker; Neo peptides; Neoepitope antibody; Posttranslational modification; Protein termini; Proteolysis

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BIOLOGICAL MARKER; EPITOPE; FIBRIN; FIBRINOGEN; GLYCOSYLATED HEMOGLOBIN; PROTEIN; PROTEOME; TAU PROTEIN;

EID: 84902082685     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201300104     Document Type: Review
Times cited : (28)

References (83)
  • 1
    • 22544449287 scopus 로고    scopus 로고
    • Genomic medicine: bringing biomarkers to clinical medicine
    • Seo, D., Ginsburg, G. S., Genomic medicine: bringing biomarkers to clinical medicine. Curr. Opin. Chem. Biol. 2005, 9, 381-386.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 381-386
    • Seo, D.1    Ginsburg, G.S.2
  • 2
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: the long and uncertain path to clinical utility
    • Rifai, N., Gillette, M. A., Carr, S. A., Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat. Biotechnol. 2006, 24, 971-983.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 3
    • 77954827460 scopus 로고    scopus 로고
    • The path to personalized medicine
    • Hamburg, M. A., Collins, F. S., The path to personalized medicine. N. Engl. J Med. 2010, 363, 301-304.
    • (2010) N. Engl. J Med. , vol.363 , pp. 301-304
    • Hamburg, M.A.1    Collins, F.S.2
  • 4
    • 84863534126 scopus 로고    scopus 로고
    • Proteome and computational analyses reveal new insights into the mechanisms of hepatitis C virus-mediated liver disease posttransplantation
    • Diamond, D. L., Krasnoselsky, A. L., Burnum, K. E., Monroe, M. E. et al., Proteome and computational analyses reveal new insights into the mechanisms of hepatitis C virus-mediated liver disease posttransplantation. Hepatology 2012, 56, 28-38.
    • (2012) Hepatology , vol.56 , pp. 28-38
    • Diamond, D.L.1    Krasnoselsky, A.L.2    Burnum, K.E.3    Monroe, M.E.4
  • 5
    • 84874285978 scopus 로고    scopus 로고
    • In vivo quantitative proteomics of somatosensory cortical synapses shows which protein levels are modulated by sensory deprivation
    • Butko, M. T., Savas, J. N., Friedman, B., Delahunty, C. et al., In vivo quantitative proteomics of somatosensory cortical synapses shows which protein levels are modulated by sensory deprivation. Proc. Natl. Acad. Sci. 2013, 110, E726-E735.
    • (2013) Proc. Natl. Acad. Sci. , vol.110
    • Butko, M.T.1    Savas, J.N.2    Friedman, B.3    Delahunty, C.4
  • 6
    • 84860508745 scopus 로고    scopus 로고
    • Proteomic portrait of human breast cancer progression identifies novel prognostic markers
    • Geiger, T., Madden, S. F., Gallagher, W. M., Cox, J., Mann, M., Proteomic portrait of human breast cancer progression identifies novel prognostic markers. Cancer Res. 2012, 72, 2428-2439.
    • (2012) Cancer Res. , vol.72 , pp. 2428-2439
    • Geiger, T.1    Madden, S.F.2    Gallagher, W.M.3    Cox, J.4    Mann, M.5
  • 7
    • 84872593231 scopus 로고    scopus 로고
    • Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation
    • Auf dem Keller, U., Prudova, A., Eckhard, U., Fingleton, B., Overall, C. M., Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation. Sci. Signal. 2013, 6, rs2.
    • (2013) Sci. Signal. , vol.6
    • Auf dem Keller, U.1    Prudova, A.2    Eckhard, U.3    Fingleton, B.4    Overall, C.M.5
  • 8
    • 78649315174 scopus 로고    scopus 로고
    • Mass-spectrometry-based clinical proteomics-a review and prospective
    • Parker, C. E., Pearson, T. W., Anderson, N. L., Borchers, C. H., Mass-spectrometry-based clinical proteomics-a review and prospective. Analyst 2010, 135, 1830-1838.
    • (2010) Analyst , vol.135 , pp. 1830-1838
    • Parker, C.E.1    Pearson, T.W.2    Anderson, N.L.3    Borchers, C.H.4
  • 9
    • 84872008110 scopus 로고    scopus 로고
    • The riddle of protein diagnostics: future bleak or bright?
    • Anderson, N. L., Ptolemy, A. S., Rifai, N., The riddle of protein diagnostics: future bleak or bright? Clin. Chem. 2013, 59, 194-197.
    • (2013) Clin. Chem. , vol.59 , pp. 194-197
    • Anderson, N.L.1    Ptolemy, A.S.2    Rifai, N.3
  • 10
    • 84871983086 scopus 로고    scopus 로고
    • Quantitative analysis of peptides and proteins in biomedicine by targeted mass spectrometry
    • Gillette, M. A., Carr, S. A., Quantitative analysis of peptides and proteins in biomedicine by targeted mass spectrometry. Nat. Methods 2013, 10, 28-34.
    • (2013) Nat. Methods , vol.10 , pp. 28-34
    • Gillette, M.A.1    Carr, S.A.2
  • 11
    • 84872017894 scopus 로고    scopus 로고
    • Unleashing the power of proteomics to develop blood-based cancer markers
    • Taguchi, A., Hanash, S. M., Unleashing the power of proteomics to develop blood-based cancer markers. Clin. Chem. 2013, 59, 119-126.
    • (2013) Clin. Chem. , vol.59 , pp. 119-126
    • Taguchi, A.1    Hanash, S.M.2
  • 12
    • 84876903149 scopus 로고    scopus 로고
    • Computational biomarker pipeline from discovery to clinical implementation: plasma proteomic biomarkers for cardiac transplantation
    • Cohen Freue, G. V., Meredith, A., Smith, D., Bergman, A. et al., Computational biomarker pipeline from discovery to clinical implementation: plasma proteomic biomarkers for cardiac transplantation. PLoS Comput. Biol. 2013, 9, e1002963.
    • (2013) PLoS Comput. Biol. , vol.9
    • Cohen Freue, G.V.1    Meredith, A.2    Smith, D.3    Bergman, A.4
  • 13
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen, O. N., Interpreting the protein language using proteomics. Nat. Rev. Mol. Cell Biol. 2006, 7, 391-403.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 391-403
    • Jensen, O.N.1
  • 14
    • 84875255239 scopus 로고    scopus 로고
    • Protein TAILS: when termini tell tales of proteolysis and function
    • Lange, P. F., Overall, C. M., Protein TAILS: when termini tell tales of proteolysis and function. Curr. Opin. Chem. Biol. 2013, 17, 73-82.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 73-82
    • Lange, P.F.1    Overall, C.M.2
  • 15
    • 33750619876 scopus 로고    scopus 로고
    • Posttranslational protein modifications current implications for cancer detection, prevention, and therapeutics
    • Krueger, K. E., Srivastava, S., Posttranslational protein modifications current implications for cancer detection, prevention, and therapeutics. Mol. Cell. Proteomics 2006, 5, 1799-1810.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1799-1810
    • Krueger, K.E.1    Srivastava, S.2
  • 16
    • 64549125924 scopus 로고    scopus 로고
    • Multiple reaction monitoring for quantitative biomarker analysis in proteomics and metabolomics
    • Kitteringham, N. R., Jenkins, R. E., Lane, C. S., Elliott, V. L., Park, B. K., Multiple reaction monitoring for quantitative biomarker analysis in proteomics and metabolomics. J. Chromatogr. B 2009, 877, 1229-1239.
    • (2009) J. Chromatogr. B , vol.877 , pp. 1229-1239
    • Kitteringham, N.R.1    Jenkins, R.E.2    Lane, C.S.3    Elliott, V.L.4    Park, B.K.5
  • 17
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: multifunctional enzymes in life and disease
    • López-Otín, C., Bond, J. S., Proteases: multifunctional enzymes in life and disease. J. Biol. Chem. 2008, 283, 30433-30437.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30433-30437
    • López-Otín, C.1    Bond, J.S.2
  • 18
    • 84876019734 scopus 로고    scopus 로고
    • Missing the target: matrix metalloproteinase antitargets in inflammation and cancer
    • Dufour, A., Overall, C. M., Missing the target: matrix metalloproteinase antitargets in inflammation and cancer. Trends Pharmacol. Sci. 2013, 34, 233-242.
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 233-242
    • Dufour, A.1    Overall, C.M.2
  • 19
    • 84859366447 scopus 로고    scopus 로고
    • Protease signalling: the cutting edge
    • Turk, B., Turk, D., Turk, V., Protease signalling: the cutting edge. EMBO J. 2012, 31, 1630-1643.
    • (2012) EMBO J. , vol.31 , pp. 1630-1643
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 20
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • O'Brien, R. J., Wong, P. C., Amyloid precursor protein processing and Alzheimer's disease. Annu. Rev. Neurosci. 2011, 34, 185-204.
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 21
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and γ-secretases in cell biology and disease
    • De Strooper, B., Annaert, W., Novel research horizons for presenilins and γ-secretases in cell biology and disease. Annu. Rev. Cell. Dev. Biol. 2010, 26, 235-260.
    • (2010) Annu. Rev. Cell. Dev. Biol. , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 22
    • 0028982454 scopus 로고
    • Reduction of beta-amyloid peptide42 in the cerebrospinal fluid of patients with Alzheimer's disease
    • Motter, R., Vigo-Pelfrey, C., Kholodenko, D., Barbour, R. et al., Reduction of beta-amyloid peptide42 in the cerebrospinal fluid of patients with Alzheimer's disease. Ann. Neurol. 1995, 38, 643-648.
    • (1995) Ann. Neurol. , vol.38 , pp. 643-648
    • Motter, R.1    Vigo-Pelfrey, C.2    Kholodenko, D.3    Barbour, R.4
  • 23
    • 0002683274 scopus 로고    scopus 로고
    • Development of a specific diagnostic test for measurement of β-amyloid (1-42)[βA4 (l-42)] in CSF
    • Vanderstichele, H., Blennow, K., D'Heuvaert, N., Buyse, M.-A. et al., Development of a specific diagnostic test for measurement of β-amyloid (1-42)[βA4 (l-42)] in CSF. Adv. Behavioral Biol. 1998, 49, 773-778.
    • (1998) Adv. Behavioral Biol. , vol.49 , pp. 773-778
    • Vanderstichele, H.1    Blennow, K.2    D'Heuvaert, N.3    Buyse, M.-A.4
  • 24
    • 84878439275 scopus 로고    scopus 로고
    • Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid- 1-42 and proteins as Alzheimer disease biomarkers
    • Kang, J. H., Korecka, M., Toledo, J. B., Trojanowski, J. Q., Shaw, L. M., Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid- 1-42 and proteins as Alzheimer disease biomarkers. Clin. Chem. 2013, 59, 903-916.
    • (2013) Clin. Chem. , vol.59 , pp. 903-916
    • Kang, J.H.1    Korecka, M.2    Toledo, J.B.3    Trojanowski, J.Q.4    Shaw, L.M.5
  • 25
    • 84867722073 scopus 로고    scopus 로고
    • Characterization of plasma β-secretase (BACE1) activity and soluble amyloid precursor proteins as potential biomarkers for Alzheimer's disease
    • Wu, G., Sankaranarayanan, S., Wong, J., Tugusheva, K. et al., Characterization of plasma β-secretase (BACE1) activity and soluble amyloid precursor proteins as potential biomarkers for Alzheimer's disease. J. Neurosci. Res. 2012, 90, 2247-2258.
    • (2012) J. Neurosci. Res. , vol.90 , pp. 2247-2258
    • Wu, G.1    Sankaranarayanan, S.2    Wong, J.3    Tugusheva, K.4
  • 26
    • 84858113047 scopus 로고    scopus 로고
    • Age and diagnostic performance of Alzheimer disease CSF biomarkers
    • Mattsson, N., Rosen, E., Hansson, O., Andreasen, N. et al., Age and diagnostic performance of Alzheimer disease CSF biomarkers. Neurology 2012, 78, 468-476.
    • (2012) Neurology , vol.78 , pp. 468-476
    • Mattsson, N.1    Rosen, E.2    Hansson, O.3    Andreasen, N.4
  • 27
    • 84900196508 scopus 로고    scopus 로고
    • Edwards, D., Hoyer-Hansen, G., Blasi, F., Sloane, B. F. (Eds), Springer, New York
    • Cox, J. H., Overall, C. M., Edwards, D., Hoyer-Hansen, G., Blasi, F., Sloane, B. F. (Eds), The cancer degradome. Springer, New York 2008, pp. 519-539.
    • (2008) The cancer degradome , pp. 519-539
    • Cox, J.H.1    Overall, C.M.2
  • 28
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3
    • McQuibban, G. A., Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 2000, 289, 1202-1206.
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1
  • 29
    • 0141653868 scopus 로고    scopus 로고
    • HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration
    • Zhang, K., McQuibban, G. A., Silva, C., Butler, G. S. et al., HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration. Nat. Neurosci. 2003, 6, 1064-1071.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1064-1071
    • Zhang, K.1    McQuibban, G.A.2    Silva, C.3    Butler, G.S.4
  • 30
    • 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. 2010, 56, 177-185.
    • (2010) Clin. Chem. , vol.56 , pp. 177-185
    • Anderson, N.L.1
  • 31
    • 0025318519 scopus 로고
    • Coagulation disturbances in cancer of the breast and colon measured with specific monoclonal antibody enzyme immunoassay for fibrin-fibrinogen degradation products
    • McCulloch, P., Nieuwenhuizen, W., Douglas, J., Lowe, G. D. O., George, W. D., Coagulation disturbances in cancer of the breast and colon measured with specific monoclonal antibody enzyme immunoassay for fibrin-fibrinogen degradation products. Pathophysiol. Haemos. Thromb. 1990, 20, 73-80.
    • (1990) Pathophysiol. Haemos. Thromb. , vol.20 , pp. 73-80
    • McCulloch, P.1    Nieuwenhuizen, W.2    Douglas, J.3    Lowe, G.D.O.4    George, W.D.5
  • 32
    • 80052290625 scopus 로고    scopus 로고
    • TopFIND, a knowledgebase linking protein termini with function
    • Lange, P. F., Overall, C. M., TopFIND, a knowledgebase linking protein termini with function. Nat. Methods 2011, 8, 703-704.
    • (2011) Nat. Methods , vol.8 , pp. 703-704
    • Lange, P.F.1    Overall, C.M.2
  • 33
    • 84896969045 scopus 로고    scopus 로고
    • Annotating N termini for the Human Proteome Project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome
    • in press.
    • Lange, P. F., Huesgen, P. F., Nguyen, K., Overall, C. M., Annotating N termini for the Human Proteome Project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J. Proteome Res. 2014. in press.
    • (2014) J. Proteome Res.
    • Lange, P.F.1    Huesgen, P.F.2    Nguyen, K.3    Overall, C.M.4
  • 35
    • 40549132858 scopus 로고    scopus 로고
    • Tools for analyzing and predicting N-terminal protein modifications
    • Meinnel, T., Giglione, C., Tools for analyzing and predicting N-terminal protein modifications. Proteomics 2008, 8, 626-649.
    • (2008) Proteomics , vol.8 , pp. 626-649
    • Meinnel, T.1    Giglione, C.2
  • 36
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky, A., The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011, 20, 1298-1345.
    • (2011) Protein Sci. , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 37
    • 0019513273 scopus 로고
    • Nonenzymatic glycosylation of proterelevance to diabetes
    • Bunn, H. F., Nonenzymatic glycosylation of proterelevance to diabetes. Am. J. Med. 1981, 70, 325-330.
    • (1981) Am. J. Med. , vol.70 , pp. 325-330
    • Bunn, H.F.1
  • 38
    • 0025027476 scopus 로고
    • Effect of long-term monitoring of glycosylated hemoglobin levels in insulin-dependent diabetes mellitus
    • Larsen, M. L., Hørder, M., Mogensen, E. F., Effect of long-term monitoring of glycosylated hemoglobin levels in insulin-dependent diabetes mellitus. N. Engl. J. Med. 1990, 323, 1021-1025.
    • (1990) N. Engl. J. Med. , vol.323 , pp. 1021-1025
    • Larsen, M.L.1    Hørder, M.2    Mogensen, E.F.3
  • 39
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct β-amyloid peptide species, A β N3 (pE), in senile plaques
    • Saido, T. C., Iwatsubo, T., Mann, D., Shimada, H. et al., Dominant and differential deposition of distinct β-amyloid peptide species, A β N3 (pE), in senile plaques. Neuron 1995, 14, 457-466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.3    Shimada, H.4
  • 40
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging
    • Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L. et al., Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging. Proc. Natl. Acad. Sci. USA 1994, 91, 8378-8382.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8378-8382
    • Näslund, J.1    Schierhorn, A.2    Hellman, U.3    Lannfelt, L.4
  • 41
    • 33947305482 scopus 로고    scopus 로고
    • Characterization of Aβ11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Aβ species in the pathogenesis of Alzheimer's disease
    • Liu, K., Solano, I., Mann, D., Lemere, C. et al., Characterization of Aβ11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Aβ species in the pathogenesis of Alzheimer's disease. Acta. Neuropathol. 2006, 112, 163-174.
    • (2006) Acta. Neuropathol. , vol.112 , pp. 163-174
    • Liu, K.1    Solano, I.2    Mann, D.3    Lemere, C.4
  • 42
    • 84866893131 scopus 로고    scopus 로고
    • The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species
    • Bien, J., Jefferson, T., Čaušević, M., Jumpertz, T. et al., The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species. J. Biol. Chem. 2012, 287, 33304-33313.
    • (2012) J. Biol. Chem. , vol.287 , pp. 33304-33313
    • Bien, J.1    Jefferson, T.2    Čaušević, M.3    Jumpertz, T.4
  • 43
    • 53549099647 scopus 로고    scopus 로고
    • Glutaminyl cyclase inhibition attenuates pyroglutamate Aβ and Alzheimer's disease-like pathology
    • Schilling, S., Zeitschel, U., Hoffmann, T., Heiser, U. et al., Glutaminyl cyclase inhibition attenuates pyroglutamate Aβ and Alzheimer's disease-like pathology. Nat. Med. 2008, 14, 1106-1111.
    • (2008) Nat. Med. , vol.14 , pp. 1106-1111
    • Schilling, S.1    Zeitschel, U.2    Hoffmann, T.3    Heiser, U.4
  • 44
    • 0031969223 scopus 로고    scopus 로고
    • Alzheimer's disease as proteolytic disorders: anabolism and catabolism of beta-amyloid
    • Saido, T. C., Alzheimer's disease as proteolytic disorders: anabolism and catabolism of beta-amyloid. Neurobiol. Aging 1998, 19, S69-S75.
    • (1998) Neurobiol. Aging , vol.19
    • Saido, T.C.1
  • 45
    • 33749617597 scopus 로고    scopus 로고
    • On the seeding and oligomerization of pGlu-amyloid peptides (in vitro)
    • Schilling, S., Lauber, T., Schaupp, M., Manhart, S. et al., On the seeding and oligomerization of pGlu-amyloid peptides (in vitro). Biochemistry 2006, 45, 12393-12399.
    • (2006) Biochemistry , vol.45 , pp. 12393-12399
    • Schilling, S.1    Lauber, T.2    Schaupp, M.3    Manhart, S.4
  • 46
    • 84862227658 scopus 로고    scopus 로고
    • TopFIND 2.0 - linking protein termini with proteolytic processing and modifications altering protein function
    • Lange, P. F., Huesgen, P. F., Overall, C. M., TopFIND 2.0 - linking protein termini with proteolytic processing and modifications altering protein function. Nucl. Acids Res. 2012, 40, D351-D361.
    • (2012) Nucl. Acids Res. , vol.40
    • Lange, P.F.1    Huesgen, P.F.2    Overall, C.M.3
  • 47
  • 48
    • 33745954240 scopus 로고    scopus 로고
    • Diagnostics and biomarker development: priming the pipeline
    • Phillips, K. A., Van Bebber, S., Issa, A. M., Diagnostics and biomarker development: priming the pipeline. Nat. Rev. Drug Discov. 2006, 5, 463-469.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 463-469
    • Phillips, K.A.1    Van Bebber, S.2    Issa, A.M.3
  • 49
    • 84859847988 scopus 로고    scopus 로고
    • N- and C-terminal degradomics: new approaches to reveal biological roles for plant proteases from substrate identification
    • Huesgen, P. F., Overall, C. M., N- and C-terminal degradomics: new approaches to reveal biological roles for plant proteases from substrate identification. Physiol. Plant 2012, 145, 5-17.
    • (2012) Physiol. Plant , vol.145 , pp. 5-17
    • Huesgen, P.F.1    Overall, C.M.2
  • 50
    • 84890577781 scopus 로고    scopus 로고
    • Proteolytic post-translational modification of proteins: Proteomic tools and methodology
    • Rogers, L. D., Overal, C. M., Proteolytic post-translational modification of proteins: Proteomic tools and methodology. Mol. Cell. Proteomics 2013, 12, 3532-3542.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3532-3542
    • Rogers, L.D.1    Overal, C.M.2
  • 51
    • 84875266403 scopus 로고    scopus 로고
    • Contemporary positional proteomics strategies to study protein processing
    • Plasman, K., Van Damme, P., Gevaert, K., Contemporary positional proteomics strategies to study protein processing. Cell 2013, 17, 66-72.
    • (2013) Cell , vol.17 , pp. 66-72
    • Plasman, K.1    Van Damme, P.2    Gevaert, K.3
  • 52
    • 77749320923 scopus 로고    scopus 로고
    • Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products
    • Kleifeld, O., Doucet, A., Auf dem Keller, U., Prudova, A. et al., Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products. Nat. Biotechnol. 2010, 28, 281-288.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 281-288
    • Kleifeld, O.1    Doucet, A.2    Auf dem Keller, U.3    Prudova, A.4
  • 53
    • 77954693076 scopus 로고    scopus 로고
    • Proteome-wide analysis of protein carboxy termini: C terminomics
    • Schilling, O., Barré, O., Huesgen, P. F., Overall, C. M., Proteome-wide analysis of protein carboxy termini: C terminomics. Nat. Methods 2010, 7, 508-511.
    • (2010) Nat. Methods , vol.7 , pp. 508-511
    • Schilling, O.1    Barré, O.2    Huesgen, P.F.3    Overall, C.M.4
  • 54
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K., Goethals, M., Martens, L., Van Damme, J. et al., Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 2003, 21, 566-569.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4
  • 55
    • 77949502598 scopus 로고    scopus 로고
    • Sampling the N-terminal proteome of human blood
    • Wildes, D., Wells, J. A., Sampling the N-terminal proteome of human blood. Proc. Natl. Acad. Sci. 2010, 107, 4561-4566.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 4561-4566
    • Wildes, D.1    Wells, J.A.2
  • 56
    • 84897055735 scopus 로고    scopus 로고
    • The Human Proteome Organization Chromosome 6 Consortium: integrating chromosome-centric and biology/disease driven strategies
    • doi: 10.1016/j.jprot.2013.08.001. [Epub ahead of print]
    • Borchers, C. H., Kast, J., Foster, L. J., Siu, K. W. M. et al., The Human Proteome Organization Chromosome 6 Consortium: integrating chromosome-centric and biology/disease driven strategies. J. Proteomics 2013. doi: 10.1016/j.jprot.2013.08.001. [Epub ahead of print]
    • (2013) J. Proteomics
    • Borchers, C.H.1    Kast, J.2    Foster, L.J.3    Siu, K.W.M.4
  • 57
    • 79960269601 scopus 로고    scopus 로고
    • A pipeline that integrates the discovery and verification of plasma protein biomarkers reveals candidate markers for cardiovascular disease
    • Addona, T. A., Shi, X., Keshishian, H., Mani, D. R. et al., A pipeline that integrates the discovery and verification of plasma protein biomarkers reveals candidate markers for cardiovascular disease. Nat. Biotechnol. 2011, 29, 635-643.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 635-643
    • Addona, T.A.1    Shi, X.2    Keshishian, H.3    Mani, D.R.4
  • 58
    • 79960214321 scopus 로고    scopus 로고
    • A targeted proteomics-based pipeline for verification of biomarkers in plasma
    • Whiteaker, J. R., Lin, C., Kennedy, J., Hou, L. et al., A targeted proteomics-based pipeline for verification of biomarkers in plasma. Nat. Biotechnol. 2011, 29, 625-634.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 625-634
    • Whiteaker, J.R.1    Lin, C.2    Kennedy, J.3    Hou, L.4
  • 59
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L., Hunter, C. L., Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 2006, 5, 573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 60
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange, V., Picotti, P., Domon, B., Aebersold, R., Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 2008, 4, 222.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 61
    • 84897097267 scopus 로고    scopus 로고
    • Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags
    • doi: 10.1016/j.jprot.2013.09.006. [Epub ahead of print].
    • Fahlmann, R. P., Chen, W., Overall, C. M., Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags. J. Proteomics 2013. doi: 10.1016/j.jprot.2013.09.006. [Epub ahead of print].
    • (2013) J. Proteomics
    • Fahlmann, R.P.1    Chen, W.2    Overall, C.M.3
  • 62
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona, T. A., Abbatiello, S. E., Schilling, B., Skates, S. J. et al., Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat. Biotechnol. 2009, 27, 633-641.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 633-641
    • Addona, T.A.1    Abbatiello, S.E.2    Schilling, B.3    Skates, S.J.4
  • 63
    • 84884373799 scopus 로고    scopus 로고
    • Design, implementation and multisite evaluation of a system suitability protocol for the quantitative assessment of instrument performance in liquid chromatography-multiple reaction monitoring-MS (LC-MRM-MS)
    • Abbatiello, S. E., Mani, D. R., Schilling, B., MacLean, B. et al., Design, implementation and multisite evaluation of a system suitability protocol for the quantitative assessment of instrument performance in liquid chromatography-multiple reaction monitoring-MS (LC-MRM-MS). Mol. Cell. Proteomics 2013, 12, 2623-2639.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2623-2639
    • Abbatiello, S.E.1    Mani, D.R.2    Schilling, B.3    MacLean, B.4
  • 64
    • 84888295045 scopus 로고    scopus 로고
    • Method and platform standardization in MRM-based quantitative plasma proteomics
    • Percy, A. J., Chambers, A. G., Yang, J., Jackson, A. M. et al., Method and platform standardization in MRM-based quantitative plasma proteomics. J. Proteomics 2013, 95, 66-76.
    • (2013) J. Proteomics , vol.95 , pp. 66-76
    • Percy, A.J.1    Chambers, A.G.2    Yang, J.3    Jackson, A.M.4
  • 65
    • 65749097654 scopus 로고    scopus 로고
    • Chapter 13. Characterizing proteolytic processing of chemokines by mass spectrometry, biochemistry, neo-epitope antibodies and functional assays
    • Starr, A. E., Overall, C. M., Chapter 13. Characterizing proteolytic processing of chemokines by mass spectrometry, biochemistry, neo-epitope antibodies and functional assays. Meth. Enzymol. 2009, 461, 281-307.
    • (2009) Meth. Enzymol. , vol.461 , pp. 281-307
    • Starr, A.E.1    Overall, C.M.2
  • 66
    • 0026714961 scopus 로고
    • Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin
    • Hughes, C. E., Caterson, B., White, R. J., Roughley, P. J., Mort, J. S., Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin. J. Biol. Chem. 1992, 267, 16011-16014.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16011-16014
    • Hughes, C.E.1    Caterson, B.2    White, R.J.3    Roughley, P.J.4    Mort, J.S.5
  • 67
    • 2542640080 scopus 로고    scopus 로고
    • Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: opportunities and potential limitations
    • Diamandis, E. P., Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: opportunities and potential limitations. Mol. Cell. Proteomics 2004, 3, 367-378.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 367-378
    • Diamandis, E.P.1
  • 68
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach
    • Gauci, S., Helbig, A. O., Slijper, M., Krijgsveld, J. et al., Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. 2009, 81, 4493-4501.
    • (2009) Anal. Chem. , vol.81 , pp. 4493-4501
    • Gauci, S.1    Helbig, A.O.2    Slijper, M.3    Krijgsveld, J.4
  • 69
    • 80053404377 scopus 로고    scopus 로고
    • Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates
    • Kleifeld, O., Doucet, A., Prudova, A., Keller, U. A. D. et al., Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates. Nat. Protoc. 2011, 6, 1578-1611.
    • (2011) Nat. Protoc. , vol.6 , pp. 1578-1611
    • Kleifeld, O.1    Doucet, A.2    Prudova, A.3    Keller, U.A.D.4
  • 70
    • 84855877960 scopus 로고    scopus 로고
    • Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics
    • Burkhart, J. M., Schumbrutzki, C., Wortelkamp, S., Sickmann, A., Zahedi, R. P., Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics. J. Proteomics 2012, 75, 1454-1462.
    • (2012) J. Proteomics , vol.75 , pp. 1454-1462
    • Burkhart, J.M.1    Schumbrutzki, C.2    Wortelkamp, S.3    Sickmann, A.4    Zahedi, R.P.5
  • 71
    • 77957344363 scopus 로고    scopus 로고
    • A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin
    • Proc, J. L., Kuzyk, M. A., Hardie, D. B., Yang, J. et al., A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin. J. Proteome Res. 2010, 9, 5422-5437.
    • (2010) J. Proteome Res. , vol.9 , pp. 5422-5437
    • Proc, J.L.1    Kuzyk, M.A.2    Hardie, D.B.3    Yang, J.4
  • 72
    • 84860854049 scopus 로고    scopus 로고
    • Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics
    • Shi, T., Su, D., Liu, T., Tang, K. et al., Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics. Proteomics 2012, 12, 1074-1092.
    • (2012) Proteomics , vol.12 , pp. 1074-1092
    • Shi, T.1    Su, D.2    Liu, T.3    Tang, K.4
  • 73
    • 31044436630 scopus 로고    scopus 로고
    • Differential exoprotease activities confer tumor-specific serum peptidome patterns
    • Villanueva, J., Shaffer, D. R., Philip, J., Chaparro, C. A. et al., Differential exoprotease activities confer tumor-specific serum peptidome patterns. J. Clin. Invest. 2006, 116, 271-284.
    • (2006) J. Clin. Invest. , vol.116 , pp. 271-284
    • Villanueva, J.1    Shaffer, D.R.2    Philip, J.3    Chaparro, C.A.4
  • 74
    • 66449083773 scopus 로고    scopus 로고
    • Developing multiplexed assays for troponin I and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry
    • Kuhn, E., Addona, T., Keshishian, H., Burgess, M. et al., Developing multiplexed assays for troponin I and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry. Clin. Chem. 2009, 55, 1108-1117.
    • (2009) Clin. Chem. , vol.55 , pp. 1108-1117
    • Kuhn, E.1    Addona, T.2    Keshishian, H.3    Burgess, M.4
  • 75
    • 76649109590 scopus 로고    scopus 로고
    • An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers
    • Whiteaker, J. R., Zhao, L., Anderson, L., Paulovich, A. G., An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers. Mol. Cell. Proteomics 2010, 9, 184-196.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 184-196
    • Whiteaker, J.R.1    Zhao, L.2    Anderson, L.3    Paulovich, A.G.4
  • 76
    • 54049129625 scopus 로고    scopus 로고
    • Pivotal evaluation of the accuracy of a biomarker used for classification or prediction: standards for study design
    • Pepe, M. S., Feng, Z., Janes, H., Bossuyt, P. M., Potter, J. D., Pivotal evaluation of the accuracy of a biomarker used for classification or prediction: standards for study design. J. Natl. Cancer Inst. 2008, 100, 1432-1438.
    • (2008) J. Natl. Cancer Inst. , vol.100 , pp. 1432-1438
    • Pepe, M.S.1    Feng, Z.2    Janes, H.3    Bossuyt, P.M.4    Potter, J.D.5
  • 77
    • 55349134214 scopus 로고    scopus 로고
    • The interface between biomarker discovery and clinical validation: the tar pit of the protein biomarker pipeline
    • Paulovich, A. G., Whiteaker, J. R., Hoofnagle, A. N., Wang, P., The interface between biomarker discovery and clinical validation: the tar pit of the protein biomarker pipeline. Prot. Clin. Appl. 2008, 2, 1386-1402.
    • (2008) Prot. Clin. Appl. , vol.2 , pp. 1386-1402
    • Paulovich, A.G.1    Whiteaker, J.R.2    Hoofnagle, A.N.3    Wang, P.4
  • 78
    • 84869790085 scopus 로고    scopus 로고
    • Measurement of hemoglobin A1c A new twist on the path to harmony
    • Sacks, D. B., Measurement of hemoglobin A1c A new twist on the path to harmony. Diabetes Care 2012, 35, 2674-2680.
    • (2012) Diabetes Care , vol.35 , pp. 2674-2680
    • Sacks, D.B.1
  • 80
    • 65949116587 scopus 로고    scopus 로고
    • Activity assays and immunoassays for plasma Renin and proreninformation provided and precautions necessary for accurate measurement
    • Campbell, D. J., Nussberger, J., Stowasser, M., Danser, A. H. J. et al., Activity assays and immunoassays for plasma Renin and proreninformation provided and precautions necessary for accurate measurement. Clin. Chem. 2009, 55, 867-877.
    • (2009) Clin. Chem. , vol.55 , pp. 867-877
    • Campbell, D.J.1    Nussberger, J.2    Stowasser, M.3    Danser, A.H.J.4
  • 81
    • 84872176550 scopus 로고    scopus 로고
    • Mass-encoded synthetic biomarkers for multiplexed urinary monitoring of disease
    • Kwong, G. A., Maltzahn von, G., Murugappan, G., Abudayyeh, O. et al., Mass-encoded synthetic biomarkers for multiplexed urinary monitoring of disease. Nat. Biotechnol. 2012, 31, 63-70.
    • (2012) Nat. Biotechnol. , vol.31 , pp. 63-70
    • Kwong, G.A.1    Maltzahn von, G.2    Murugappan, G.3    Abudayyeh, O.4
  • 82
    • 84876376320 scopus 로고    scopus 로고
    • Coagulation assays and anticoagulant monitoring
    • Funk, D. M. A., Coagulation assays and anticoagulant monitoring. Hematology 2012, 2012, 460-465.
    • (2012) Hematology , vol.2012 , pp. 460-465
    • Funk, D.M.A.1
  • 83
    • 83055180536 scopus 로고    scopus 로고
    • Functional imaging of proteases: recent advances in the design and application of substrate-based and activity-based probes
    • Edgington, L. E., Verdoes, M., Bogyo, M., Functional imaging of proteases: recent advances in the design and application of substrate-based and activity-based probes. Curr. Opin. Chem. Biol. 2011, 15, 798-805.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 798-805
    • Edgington, L.E.1    Verdoes, M.2    Bogyo, M.3


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