메뉴 건너뛰기




Volumn 1834, Issue 11, 2013, Pages 2396-2407

Colon tumour secretopeptidome: Insights into endogenous proteolytic cleavage events in the colon tumour microenvironment

Author keywords

Ectodomain; Low molecular weight; Peptidome; Proteolysis; Proteolytic cleavage; Secretome

Indexed keywords

CELL MEMBRANE PROTEIN; CELL SURFACE PROTEIN; PEPTIDE FRAGMENT;

EID: 84884651647     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.05.006     Document Type: Article
Times cited : (34)

References (93)
  • 1
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • DOI 10.1038/nrc2228, PII NRC2228
    • C. Lopez-Otin, and L.M. Matrisian Emerging roles of proteases in tumour suppression Nat. Rev. Cancer 7 10 2007 800 808 (Pubitemid 47463671)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 3
    • 0037304947 scopus 로고    scopus 로고
    • Intramembrane-cleaving proteases: Controlled liberation of proteins and bioactive peptides
    • DOI 10.1016/S0962-8924(02)00041-7, PII S0962892402000417
    • A. Weihofen, and B. Martoglio Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides Trends Cell Biol. 13 2 2003 71 78 (Pubitemid 36135888)
    • (2003) Trends in Cell Biology , vol.13 , Issue.2 , pp. 71-78
    • Weihofen, A.1    Martoglio, B.2
  • 4
    • 78751490759 scopus 로고    scopus 로고
    • Cancer cells cut homophilic cell adhesion molecules and run
    • S.E. Craig, and S.M. Brady-Kalnay Cancer cells cut homophilic cell adhesion molecules and run Cancer Res. 71 2 2011 303 309
    • (2011) Cancer Res. , vol.71 , Issue.2 , pp. 303-309
    • Craig, S.E.1    Brady-Kalnay, S.M.2
  • 6
    • 29244479537 scopus 로고    scopus 로고
    • The shed ectodomain of Nr-CAM stimulates cell proliferation and motility, and confers cell transformation
    • DOI 10.1158/0008-5472.CAN-05-2647
    • M. Conacci-Sorrell, A. Kaplan, S. Raveh, N. Gavert, T. Sakurai, and A. Ben-Ze'ev The shed ectodomain of Nr-CAM stimulates cell proliferation and motility, and confers cell transformation Cancer Res. 65 24 2005 11605 11612 (Pubitemid 41821720)
    • (2005) Cancer Research , vol.65 , Issue.24 , pp. 11605-11612
    • Conacci-Sorrell, M.1    Kaplan, A.2    Raveh, S.3    Gavert, N.4    Sakurai, T.5    Ben-Ze'ev, A.6
  • 7
    • 49649103585 scopus 로고    scopus 로고
    • The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation
    • A.J. Najy, K.C. Day, and M.L. Day The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation J. Biol. Chem. 283 26 2008 18393 18401
    • (2008) J. Biol. Chem. , vol.283 , Issue.26 , pp. 18393-18401
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 9
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • J. Arribas, and A. Borroto Protein ectodomain shedding Chem. Rev. 102 12 2002 4627 4638
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 10
    • 0036007414 scopus 로고    scopus 로고
    • Shedding light on sheddases: Role in growth and development
    • DOI 10.1002/bies.10037
    • F. Kheradmand, and Z. Werb Shedding light on sheddases: role in growth and development Bioessays 24 1 2002 8 12 (Pubitemid 34108414)
    • (2002) BioEssays , vol.24 , Issue.1 , pp. 8-12
    • Kheradmand, F.1    Werb, Z.2
  • 11
    • 33746928340 scopus 로고    scopus 로고
    • Emerging roles for ectodomain shedding in the regulation of inflammatory responses
    • DOI 10.1189/jlb.0106038
    • K.J. Garton, P.J. Gough, and E.W. Raines Emerging roles for ectodomain shedding in the regulation of inflammatory responses J. Leukoc. Biol. 79 6 2006 1105 1116 (Pubitemid 44835543)
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.6 , pp. 1105-1116
    • Garton, K.J.1    Gough, P.J.2    Raines, E.W.3
  • 12
    • 56749133149 scopus 로고    scopus 로고
    • The ADAMs: Signalling scissors in the tumour microenvironment
    • G. Murphy The ADAMs: signalling scissors in the tumour microenvironment Nat. Rev. Cancer 8 12 2008 929 941
    • (2008) Nat. Rev. Cancer , vol.8 , Issue.12 , pp. 929-941
    • Murphy, G.1
  • 16
    • 0031426654 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells
    • DOI 10.1083/jcb.139.7.1861
    • A. Lochter, S. Galosy, J. Muschler, N. Freedman, Z. Werb, and M.J. Bissell Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells J. Cell Biol. 139 7 1997 1861 1872 (Pubitemid 28079248)
    • (1997) Journal of Cell Biology , vol.139 , Issue.7 , pp. 1861-1872
    • Lochter, A.1    Galosy, S.2    Muschler, J.3    Freedman, N.4    Werb, Z.5    Bissell, M.J.6
  • 18
    • 0038771182 scopus 로고    scopus 로고
    • RIPped out by presenilin-dependent gamma-secretase
    • M. Medina, and C.G. Dotti RIPped out by presenilin-dependent gamma-secretase Cell. Signal. 15 9 2003 829 841
    • (2003) Cell. Signal. , vol.15 , Issue.9 , pp. 829-841
    • Medina, M.1    Dotti, C.G.2
  • 19
    • 65249188697 scopus 로고    scopus 로고
    • Intramembrane proteolysis
    • M.S. Wolfe Intramembrane proteolysis Chem. Rev. 109 4 2009 1599 1612
    • (2009) Chem. Rev. , vol.109 , Issue.4 , pp. 1599-1612
    • Wolfe, M.S.1
  • 20
    • 66249133368 scopus 로고    scopus 로고
    • How intramembrane proteases bury hydrolytic reactions in the membrane
    • E. Erez, D. Fass, and E. Bibi How intramembrane proteases bury hydrolytic reactions in the membrane Nature 459 7245 2009 371 378
    • (2009) Nature , vol.459 , Issue.7245 , pp. 371-378
    • Erez, E.1    Fass, D.2    Bibi, E.3
  • 21
    • 0141817915 scopus 로고    scopus 로고
    • The Notch Ligands, Jagged and Delta, Are Sequentially Processed by α-Secretase and Presenilin/γ-Secretase and Release Signaling Fragments
    • DOI 10.1074/jbc.M302659200
    • M.J. LaVoie, and D.J. Selkoe The Notch ligands, Jagged and Delta, are sequentially processed by alpha-secretase and presenilin/gamma-secretase and release signaling fragments J. Biol. Chem. 278 36 2003 34427 34437 (Pubitemid 37553289)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 34427-34437
    • LaVoie, M.J.1    Selkoe, D.J.2
  • 22
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ™ labeling reveals a diverse MMP-2 substrate degradome
    • DOI 10.1074/mcp.M600341-MCP200
    • R.A. Dean, and C.M. Overall Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome Mol. Cell. Proteomics 6 4 2007 611 623 (Pubitemid 46630094)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.4 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 23
    • 49549113643 scopus 로고    scopus 로고
    • Global mapping of the topography and magnitude of proteolytic events in apoptosis
    • M.M. Dix, G.M. Simon, and B.F. Cravatt Global mapping of the topography and magnitude of proteolytic events in apoptosis Cell 134 4 2008 679 691
    • (2008) Cell , vol.134 , Issue.4 , pp. 679-691
    • Dix, M.M.1    Simon, G.M.2    Cravatt, B.F.3
  • 24
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • DOI 10.1038/nbt810
    • K. Gevaert, M. Goethals, L. Martens, J. Van Damme, A. Staes, G.R. Thomas, and J. Vandekerckhove Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides Nat. Biotechnol. 21 5 2003 566 569 (Pubitemid 36532024)
    • (2003) Nature Biotechnology , vol.21 , Issue.5 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 27
    • 79955784642 scopus 로고    scopus 로고
    • Broad coverage identification of multiple proteolytic cleavage site sequences in complex high molecular weight proteins using quantitative proteomics as a complement to Edman sequencing
    • M110.003533
    • A. Doucet, and C.M. Overall Broad coverage identification of multiple proteolytic cleavage site sequences in complex high molecular weight proteins using quantitative proteomics as a complement to Edman sequencing Mol. Cell. Proteomics 10 5 2011 M110.003533
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.5
    • Doucet, A.1    Overall, C.M.2
  • 28
    • 0036733748 scopus 로고    scopus 로고
    • Peptidomics-based approach reveals the secretion of the 29-residue COOH-terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines
    • K. Sasaki, K. Sato, Y. Akiyama, K. Yanagihara, M. Oka, and K. Yamaguchi Peptidomics-based approach reveals the secretion of the 29-residue COOH terminal fragment of the putative tumor suppressor protein DMBT1 from pancreatic adenocarcinoma cell lines Cancer Res. 62 17 2002 4894 4898 (Pubitemid 34984410)
    • (2002) Cancer Research , vol.62 , Issue.17 , pp. 4894-4898
    • Sasaki, K.1    Sato, K.2    Akiyama, Y.3    Yanagihara, K.4    Oka, M.5    Yamaguchi, K.6
  • 29
    • 13244268302 scopus 로고    scopus 로고
    • A proteomic approach to characterize protein shedding
    • DOI 10.1002/pmic.200400912
    • M. Ahram, J.N. Adkins, D.L. Auberry, D.S. Wunschel, and D.L. Springer A proteomic approach to characterize protein shedding Proteomics 5 1 2005 123 131 (Pubitemid 40189644)
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 123-131
    • Ahram, M.1    Adkins, J.N.2    Auberry, D.L.3    Wunschel, D.S.4    Springer, D.L.5
  • 31
    • 0021910637 scopus 로고
    • A colon cancer cell line (LIM1215) derived from a patient with inherited nonpolyposis colorectal cancer
    • R.H. Whitehead, F.A. Macrae, D.J. St John, and J. Ma A colon cancer cell line (LIM1215) derived from a patient with inherited nonpolyposis colorectal cancer J. Natl. Cancer Inst. 74 4 1985 759 765 (Pubitemid 15118229)
    • (1985) Journal of the National Cancer Institute , vol.74 , Issue.4 , pp. 759-765
    • Whitehead, R.H.1    Macrae, F.A.2    St. John, D.J.B.3    Ma, J.4
  • 32
    • 0023265494 scopus 로고
    • A new colon carcinoma cell line (LIM1863) that grows as organoids with spontaneous differentiation into crypt-like structures in vitro
    • R.H. Whitehead, J.K. Jones, A. Gabriel, and R.E. Lukies A new colon carcinoma cell line (LIM1863) that grows as organoids with spontaneous differentiation into crypt-like structures in vitro Cancer Res. 47 10 1987 2683 2689 (Pubitemid 17090078)
    • (1987) Cancer Research , vol.47 , Issue.10 , pp. 2683-2689
    • Whitehead, R.H.1    Jones, J.K.2    Gabriel, A.3    Lukies, R.E.4
  • 35
    • 72149117946 scopus 로고    scopus 로고
    • A centrifugal ultrafiltration strategy for isolating the low-molecular weight (
    • D.W. Greening, and R.J. Simpson A centrifugal ultrafiltration strategy for isolating the low-molecular weight (
    • (2010) J. Proteomics , vol.73 , Issue.3 , pp. 637-648
    • Greening, D.W.1    Simpson, R.J.2
  • 36
    • 84858037808 scopus 로고    scopus 로고
    • Comparison of ultracentrifugation, density gradient separation, and immunoaffinity capture methods for isolating human colon cancer cell line LIM1863-derived exosomes
    • B.J. Tauro, D.W. Greening, R.A. Mathias, H. Ji, S. Mathivanan, A.M. Scott, and R.J. Simpson Comparison of ultracentrifugation, density gradient separation, and immunoaffinity capture methods for isolating human colon cancer cell line LIM1863-derived exosomes Methods 56 2 2012 293 304
    • (2012) Methods , vol.56 , Issue.2 , pp. 293-304
    • Tauro, B.J.1    Greening, D.W.2    Mathias, R.A.3    Ji, H.4    Mathivanan, S.5    Scott, A.M.6    Simpson, R.J.7
  • 37
    • 38949168230 scopus 로고    scopus 로고
    • Comparison of human platelet-membrane cytoskeletal proteins with the plasma proteome: Towards understanding the platelet-plasma nexus
    • D.W. Greening, K.M. Glenister, E.A. Kapp, R.L. Moritz, R.L. Sparrow, G.W. Lynch, and R.J. Simpson Comparison of human platelet-membrane cytoskeletal proteins with the plasma proteome: towards understanding the platelet-plasma nexus Proteomics Clin. Appl. 2 63-77 2008
    • (2008) Proteomics Clin. Appl. , vol.2 , Issue.6377
    • Greening, D.W.1    Glenister, K.M.2    Kapp, E.A.3    Moritz, R.L.4    Sparrow, R.L.5    Lynch, G.W.6    Simpson, R.J.7
  • 38
    • 43049127826 scopus 로고    scopus 로고
    • PeptideAtlas: A resource for target selection for emerging targeted proteomics workflows
    • DOI 10.1038/embor.2008.56, PII EMBOR200856
    • E.W. Deutsch, H. Lam, and R. Aebersold PeptideAtlas: a resource for target selection for emerging targeted proteomics workflows EMBO Rep. 9 5 2008 429 434 (Pubitemid 351627279)
    • (2008) EMBO Reports , vol.9 , Issue.5 , pp. 429-434
    • Deutsch, E.W.1    Lam, H.2    Aebersold, R.3
  • 41
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • J.D. Bendtsen, H. Nielsen, G. von Heijne, and S. Brunak Improved prediction of signal peptides: SignalP 3.0 J. Mol. Biol. 340 4 2004 783 795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 43
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 45
    • 67049118923 scopus 로고    scopus 로고
    • Accurate and sensitive peptide identification with Mascot Percolator
    • M. Brosch, L. Yu, T. Hubbard, and J. Choudhary Accurate and sensitive peptide identification with Mascot Percolator J. Proteome Res. 8 6 2009 3176 3181
    • (2009) J. Proteome Res. , vol.8 , Issue.6 , pp. 3176-3181
    • Brosch, M.1    Yu, L.2    Hubbard, T.3    Choudhary, J.4
  • 46
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • DOI 10.1038/nmeth1113, PII NMETH1113
    • L. Kall, J.D. Canterbury, J. Weston, W.S. Noble, and M.J. MacCoss Semi-supervised learning for peptide identification from shotgun proteomics datasets Nat. Methods 4 11 2007 923 925 (Pubitemid 350042380)
    • (2007) Nature Methods , vol.4 , Issue.11 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 48
    • 17444419756 scopus 로고    scopus 로고
    • Prediction of peptide retention at different HPLC conditions from multiple linear regression models
    • DOI 10.1021/pr049780r
    • T. Baczek, P. Wiczling, M. Marszall, Y.V. Heyden, and R. Kaliszan Prediction of peptide retention at different HPLC conditions from multiple linear regression models J. Proteome Res. 4 2 2005 555 563 (Pubitemid 40548163)
    • (2005) Journal of Proteome Research , vol.4 , Issue.2 , pp. 555-563
    • Baczek, T.1    Wiczling, P.2    Marszall, M.3    Heyden, Y.V.4    Kaliszan, R.5
  • 49
    • 0242611620 scopus 로고    scopus 로고
    • Characterizing degradation products of peptides containing N-terminal Cys residues by (off-line high-performance liquid chromatography)/matrix-assisted laser desorption/ionization quadrupole time-of-flight measurements
    • O.V. Krokhin, W. Ens, and K.G. Standing Characterizing degradation products of peptides containing N-terminal Cys residues by (off-line high-performance liquid chromatography)/matrix-assisted laser desorption/ionization quadrupole time-of-flight measurements Rapid Commun. Mass Spectrom. 17 22 2003 2528 2534 (Pubitemid 37413277)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.22 , pp. 2528-2534
    • Krokhin, O.V.1    Ens, W.2    Standing, K.G.3
  • 50
    • 5744223586 scopus 로고    scopus 로고
    • An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: Its application to protein peptide mapping by off-line HPLC-MALDI MS
    • DOI 10.1074/mcp.M400031-MCP200
    • O.V. Krokhin, R. Craig, V. Spicer, W. Ens, K.G. Standing, R.C. Beavis, and J.A. Wilkins An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: its application to protein peptide mapping by off-line HPLC-MALDI MS Mol. Cell. Proteomics 3 9 2004 908 919 (Pubitemid 39377699)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.9 , pp. 908-919
    • Krokhin, O.V.1    Craig, R.2    Spicer, V.3    Ens, W.4    Standing, K.G.5    Beavis, R.C.6    Wilkins, J.A.7
  • 51
    • 84869886372 scopus 로고    scopus 로고
    • Identifying mutated proteins secreted by colon cancer cell lines using mass spectrometry
    • Spec No. (141-149
    • S. Mathivanan, H. Ji, B.J. Tauro, Y.S. Chen, and R.J. Simpson Identifying mutated proteins secreted by colon cancer cell lines using mass spectrometry J. Proteomics 76 2012 Spec No. (141-149
    • (2012) J. Proteomics , vol.76
    • Mathivanan, S.1    Ji, H.2    Tauro, B.J.3    Chen, Y.S.4    Simpson, R.J.5
  • 56
    • 68849110472 scopus 로고    scopus 로고
    • Concomitant mutations and splice variants in KRAS and BRAF demonstrate complex perturbation of the Ras/Raf signalling pathway in advanced colorectal cancer
    • R. Seth, S. Crook, S. Ibrahem, W. Fadhil, D. Jackson, and M. Ilyas Concomitant mutations and splice variants in KRAS and BRAF demonstrate complex perturbation of the Ras/Raf signalling pathway in advanced colorectal cancer Gut 58 9 2009 1234 1241
    • (2009) Gut , vol.58 , Issue.9 , pp. 1234-1241
    • Seth, R.1    Crook, S.2    Ibrahem, S.3    Fadhil, W.4    Jackson, D.5    Ilyas, M.6
  • 59
    • 84862178250 scopus 로고    scopus 로고
    • The many roles of PTK7: A versatile regulator of cell-cell communication
    • H. Peradziryi, N.S. Tolwinski, and A. Borchers The many roles of PTK7: a versatile regulator of cell-cell communication Arch. Biochem. Biophys. 524 1 2012 71 76
    • (2012) Arch. Biochem. Biophys. , vol.524 , Issue.1 , pp. 71-76
    • Peradziryi, H.1    Tolwinski, N.S.2    Borchers, A.3
  • 61
    • 84871911898 scopus 로고    scopus 로고
    • Reprint of "on the size of the active site in proteases. I. Papain"
    • I. Schechter Reprint of "on the size of the active site in proteases. I. Papain" Biochem. Biophys. Res. Commun. 425 3 2012 497 502
    • (2012) Biochem. Biophys. Res. Commun. , vol.425 , Issue.3 , pp. 497-502
    • Schechter, I.1
  • 62
    • 0014405092 scopus 로고
    • On the active site of proteases. 3. Mapping the active site of papain; Specific peptide inhibitors of papain
    • I. Schechter, and A. Berger On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain Biochem. Biophys. Res. Commun. 32 5 1968 898 902
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , Issue.5 , pp. 898-902
    • Schechter, I.1    Berger, A.2
  • 65
    • 0033768442 scopus 로고    scopus 로고
    • Organ-specific expression of the intestinal epithelium-related antigen A33, a cell surface target for antibody-based imaging and treatment in gastrointestinal cancer
    • J. Sakamoto, H. Kojima, J. Kato, H. Hamashima, and H. Suzuki Organ-specific expression of the intestinal epithelium-related antigen A33, a cell surface target for antibody-based imaging and treatment in gastrointestinal cancer Cancer Chemother. Pharmacol. 46 Suppl. 2000 S27 S32
    • (2000) Cancer Chemother. Pharmacol. , vol.46 , Issue.SUPPL.
    • Sakamoto, J.1    Kojima, H.2    Kato, J.3    Hamashima, H.4    Suzuki, H.5
  • 67
    • 0034333498 scopus 로고    scopus 로고
    • The murine A33 antigen is expressed at two distinct sites during development, the ICM of the blastocyst and the intestinal epithelium
    • H.E. Abud, C.N. Johnstone, N.C. Tebbutt, and J.K. Heath The murine A33 antigen is expressed at two distinct sites during development, the ICM of the blastocyst and the intestinal epithelium Mech. Dev. 98 1-2 2000 111 114
    • (2000) Mech. Dev. , vol.98 , Issue.12 , pp. 111-114
    • Abud, H.E.1    Johnstone, C.N.2    Tebbutt, N.C.3    Heath, J.K.4
  • 68
    • 0031945841 scopus 로고    scopus 로고
    • Current concepts in mucosal immunity. III. Ontogeny and function of gamma delta T cells in the intestine
    • M.F. Kagnoff Current concepts in mucosal immunity. III. Ontogeny and function of gamma delta T cells in the intestine Am. J. Physiol. 274 3 Pt 1 1998 G455 G458
    • (1998) Am. J. Physiol. , vol.274 , Issue.3 PART 1
    • Kagnoff, M.F.1
  • 71
    • 0019156135 scopus 로고
    • Shedding from normal and cancer-cell surfaces
    • P.H. Black Shedding from normal and cancer-cell surfaces N. Engl. J. Med. 303 24 1980 1415 1416 (Pubitemid 11197535)
    • (1980) New England Journal of Medicine , vol.303 , Issue.24 , pp. 1415-1416
    • Black, P.H.1
  • 74
    • 68449094056 scopus 로고    scopus 로고
    • Disruption of E-cadherin by matrix metalloproteinase directly mediates epithelial-mesenchymal transition downstream of transforming growth factor-beta1 in renal tubular epithelial cells
    • G. Zheng, J.G. Lyons, T.K. Tan, Y. Wang, T.T. Hsu, D. Min, L. Succar, G.K. Rangan, M. Hu, B.R. Henderson, S.I. Alexander, and D.C. Harris Disruption of E-cadherin by matrix metalloproteinase directly mediates epithelial- mesenchymal transition downstream of transforming growth factor-beta1 in renal tubular epithelial cells Am. J. Pathol. 175 2 2009 580 591
    • (2009) Am. J. Pathol. , vol.175 , Issue.2 , pp. 580-591
    • Zheng, G.1    Lyons, J.G.2    Tan, T.K.3    Wang, Y.4    Hsu, T.T.5    Min, D.6    Succar, L.7    Rangan, G.K.8    Hu, M.9    Henderson, B.R.10    Alexander, S.I.11    Harris, D.C.12
  • 75
    • 0034285732 scopus 로고    scopus 로고
    • Medical billing outsourcing: Is it worth the risk?
    • D. Steinberger Medical billing outsourcing: is it worth the risk? J. Ophthalmic Nurs. Technol. 19 5 2000 218 219
    • (2000) J. Ophthalmic Nurs. Technol. , vol.19 , Issue.5 , pp. 218-219
    • Steinberger, D.1
  • 76
    • 33745477470 scopus 로고    scopus 로고
    • Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis
    • DOI 10.1128/MCB.02380-05
    • J.J. Bech-Serra, B. Santiago-Josefat, C. Esselens, P. Saftig, J. Baselga, J. Arribas, and F. Canals Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis Mol. Cell. Biol. 26 13 2006 5086 5095 (Pubitemid 43955821)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.13 , pp. 5086-5095
    • Bech-Serra, J.J.1    Santiago-Josefat, B.2    Esselens, C.3    Saftig, P.4    Baselga, J.5    Arribas, J.6    Canals, F.7
  • 77
    • 0033923006 scopus 로고    scopus 로고
    • Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type I matrix metalloproteinase (MTI-MMP) correlate with melanoma progression
    • DOI 10.1002/1096-9896(2000)9999:9999<::AID-PATH632>3.0.CO;2-#
    • U.B. Hofmann, J.R. Westphal, A.J. Zendman, J.C. Becker, D.J. Ruiter, and G.N. van Muijen Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type 1 matrix metalloproteinase (MT1-MMP) correlate with melanoma progression J. Pathol. 191 3 2000 245 256 (Pubitemid 30441247)
    • (2000) Journal of Pathology , vol.191 , Issue.3 , pp. 245-256
    • Hofmann, U.B.1    Westphal, J.R.2    Zendman, A.J.W.3    Becker, J.C.4    Ruiter, D.J.5    Van Muijen, G.N.P.6
  • 80
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • DOI 10.1101/gad.1451806
    • K. Hotary, X.Y. Li, E. Allen, S.L. Stevens, and S.J. Weiss A cancer cell metalloprotease triad regulates the basement membrane transmigration program Genes Dev. 20 19 2006 2673 2686 (Pubitemid 44498378)
    • (2006) Genes and Development , vol.20 , Issue.19 , pp. 2673-2686
    • Hotary, K.1    Li, X.-Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 81
    • 0037688169 scopus 로고    scopus 로고
    • Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
    • DOI 10.1023/A:1023003616848
    • S. Netzel-Arnett, J.D. Hooper, R. Szabo, E.L. Madison, J.P. Quigley, T.H. Bugge, and T.M. Antalis Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer Cancer Metastasis Rev. 22 2-3 2003 237 258 (Pubitemid 36561060)
    • (2003) Cancer and Metastasis Reviews , vol.22 , Issue.2-3 , pp. 237-258
    • Netzel-Arnett, S.1    Hooper, J.D.2    Szabo, R.3    Madison, E.L.4    Quigley, J.P.5    Bugge, T.H.6    Antalis, T.M.7
  • 82
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • DOI 10.1093/embo-reports/kve180
    • M. Sastre, H. Steiner, K. Fuchs, A. Capell, G. Multhaup, M.M. Condron, D.B. Teplow, and C. Haass Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch EMBO Rep. 2 9 2001 835 841 (Pubitemid 32982753)
    • (2001) EMBO Reports , vol.2 , Issue.9 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 83
    • 54949110552 scopus 로고    scopus 로고
    • Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements
    • M.L. Hemming, J.E. Elias, S.P. Gygi, and D.J. Selkoe Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements PLoS Biol. 6 10 2008 e257
    • (2008) PLoS Biol. , vol.6 , Issue.10 , pp. 257
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 84
    • 33745209256 scopus 로고    scopus 로고
    • Mannose-6-phosphate/insulin-like growth factor II receptor expression and tumor development
    • E. Hebert Mannose-6-phosphate/insulin-like growth factor II receptor expression and tumor development Biosci. Rep. 26 1 2006 7 17
    • (2006) Biosci. Rep. , vol.26 , Issue.1 , pp. 7-17
    • Hebert, E.1
  • 85
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • DOI 10.1038/nrm1050
    • P. Ghosh, N.M. Dahms, and S. Kornfeld Mannose 6-phosphate receptors: new twists in the tale Nat. Rev. Mol. Cell Biol. 4 3 2003 202 212 (Pubitemid 36288042)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 86
    • 1442299204 scopus 로고    scopus 로고
    • The insulin-like growth factor-II/mannose-6-phosphate receptor: Structure, distribution and function in the central nervous system
    • DOI 10.1016/j.brainresrev.2003.11.002, PII S0165017303002571
    • C. Hawkes, and S. Kar The insulin-like growth factor-II/mannose-6- phosphate receptor: structure, distribution and function in the central nervous system Brain Res. Rev. 44 2-3 2004 117 140 (Pubitemid 38293429)
    • (2004) Brain Research Reviews , vol.44 , Issue.2-3 , pp. 117-140
    • Hawkes, C.1    Kar, S.2
  • 87
    • 28844439793 scopus 로고    scopus 로고
    • Interaction of nuclear receptors with the Wnt/β-catenin/Tcf signaling axis: Wnt you like to know?
    • DOI 10.1210/er.2003-0034
    • D.J. Mulholland, S. Dedhar, G.A. Coetzee, and C.C. Nelson Interaction of nuclear receptors with the Wnt/beta-catenin/Tcf signaling axis: Wnt you like to know? Endocr. Rev. 26 7 2005 898 915 (Pubitemid 41770157)
    • (2005) Endocrine Reviews , vol.26 , Issue.7 , pp. 898-915
    • Mulholland, D.J.1    Dedhar, S.2    Coetzee, G.A.3    Nelson, C.C.4
  • 89
    • 77954051527 scopus 로고    scopus 로고
    • Identification of beta-secretase (BACE1) substrates using quantitative proteomics
    • M.L. Hemming, J.E. Elias, S.P. Gygi, and D.J. Selkoe Identification of beta-secretase (BACE1) substrates using quantitative proteomics PLoS One 4 12 2009 e8477
    • (2009) PLoS One , vol.4 , Issue.12 , pp. 8477
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 90
    • 84885686338 scopus 로고    scopus 로고
    • Stoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomics
    • A.H. Smits, P.W. Jansen, I. Poser, A.A. Hyman, and M. Vermeulen Stoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomics Nucleic Acids Res. 2012
    • (2012) Nucleic Acids Res.
    • Smits, A.H.1    Jansen, P.W.2    Poser, I.3    Hyman, A.A.4    Vermeulen, M.5
  • 91
    • 0019264751 scopus 로고
    • Shedding from the cell surface of normal and cancer cells
    • P.H. Black Shedding from the cell surface of normal and cancer cells Adv. Cancer Res. 32 1980 75 199
    • (1980) Adv. Cancer Res. , vol.32 , pp. 75-199
    • Black, P.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.