메뉴 건너뛰기




Volumn 15, Issue 7, 2016, Pages 2337-2345

Establishing a proteomics-based monocyte assay to assess differential innate immune activation responses

Author keywords

activation; differentiation; label free proteomics; THP 1 cell line; TLR ligands

Indexed keywords

EPIDERMAL GROWTH FACTOR; ISOASPARTIC ACID; PROTEOME; LIPOPEPTIDE; PAM(3)CSK(4) PEPTIDE; PHORBOL 13 ACETATE 12 MYRISTATE;

EID: 84977079069     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.6b00422     Document Type: Article
Times cited : (7)

References (61)
  • 1
    • 0035795985 scopus 로고    scopus 로고
    • An overview of the immune system
    • Parkin, J.; Cohen, B. An overview of the immune system Lancet 2001, 357 (9270) 1777-1789 10.1016/S0140-6736(00)04904-7
    • (2001) Lancet , vol.357 , Issue.9270 , pp. 1777-1789
    • Parkin, J.1    Cohen, B.2
  • 2
    • 84861474688 scopus 로고    scopus 로고
    • Signaling in innate immunity and inflammation
    • Newton, K.; Dixit, V. M. Signaling in innate immunity and inflammation Cold Spring Harbor Perspect. Biol. 2012, 4 (3) a006049 10.1101/cshperspect.a006049
    • (2012) Cold Spring Harbor Perspect. Biol. , vol.4 , Issue.3 , pp. a006049
    • Newton, K.1    Dixit, V.M.2
  • 3
    • 81855202393 scopus 로고    scopus 로고
    • Innate immunity and transplantation tolerance: The potential role of TLRs/NLRs in GVHD
    • Shin, O. S.; Harris, J. B. Innate immunity and transplantation tolerance: the potential role of TLRs/NLRs in GVHD Korean J. Hematol. 2011, 46 (2) 69-79 10.5045/kjh.2011.46.2.69
    • (2011) Korean J. Hematol. , vol.46 , Issue.2 , pp. 69-79
    • Shin, O.S.1    Harris, J.B.2
  • 4
    • 0142031430 scopus 로고    scopus 로고
    • Role of Toll-Like Receptors in Pathogen Recognition Role of Toll-Like Receptors in Pathogen Recognition
    • Janssens, S.; Beyaert, R. Role of Toll-Like Receptors in Pathogen Recognition Role of Toll-Like Receptors in Pathogen Recognition Clin. Microbiol. Rev. 2003, 16 (4) 637-646 10.1128/CMR.16.4.637-646.2003
    • (2003) Clin. Microbiol. Rev. , vol.16 , Issue.4 , pp. 637-646
    • Janssens, S.1    Beyaert, R.2
  • 5
    • 33947694370 scopus 로고    scopus 로고
    • TLR signaling
    • Kawai, T.; Akira, S. TLR signaling Semin. Immunol. 2007, 19 (1) 24-32 10.1016/j.smim.2006.12.004
    • (2007) Semin. Immunol. , vol.19 , Issue.1 , pp. 24-32
    • Kawai, T.1    Akira, S.2
  • 6
    • 34548459868 scopus 로고    scopus 로고
    • Structure and function of Toll receptors and their ligands
    • Gay, N. J.; Gangloff, M. Structure and function of Toll receptors and their ligands Annu. Rev. Biochem. 2007, 76, 141-165 10.1146/annurev.biochem.76.060305.151318
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 141-165
    • Gay, N.J.1    Gangloff, M.2
  • 7
    • 84949187162 scopus 로고    scopus 로고
    • Toll-like receptors
    • Takeda, K.; Akira, S. Toll-like receptors Curr. Protoc. Immunol. 2015, 109, 14.12.1-14.12.10 10.1002/0471142735.im1412s109
    • (2015) Curr. Protoc. Immunol. , vol.109 , pp. 14121-141210
    • Takeda, K.1    Akira, S.2
  • 8
    • 79251563125 scopus 로고    scopus 로고
    • Current views of toll-like receptor signaling pathways
    • Yamamoto, M.; Takeda, K. Current views of toll-like receptor signaling pathways Gastroenterol. Res. Pract. 2010, 2010, 240365 10.1155/2010/240365
    • (2010) Gastroenterol. Res. Pract. , vol.2010 , pp. 240365
    • Yamamoto, M.1    Takeda, K.2
  • 9
    • 84867277240 scopus 로고    scopus 로고
    • Toll-like receptors, signaling adapters and regulation of the pro-inflammatory response by PI3K
    • Troutman, T. D.; Bazan, J. F.; Pasare, C. Toll-like receptors, signaling adapters and regulation of the pro-inflammatory response by PI3K Cell Cycle 2012, 11 (19) 3559-3567 10.4161/cc.21572
    • (2012) Cell Cycle , vol.11 , Issue.19 , pp. 3559-3567
    • Troutman, T.D.1    Bazan, J.F.2    Pasare, C.3
  • 10
    • 2542448243 scopus 로고    scopus 로고
    • CD1: Antigen presentation and T cell function
    • Brigl, M.; Brenner, M. B. CD1: antigen presentation and T cell function Annu. Rev. Immunol. 2004, 22, 817-890 10.1146/annurev.immunol.22.012703.104608
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 817-890
    • Brigl, M.1    Brenner, M.B.2
  • 11
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R. N. MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation Cell 1994, 76 (2) 287-299 10.1016/0092-8674(94)90336-0
    • (1994) Cell , vol.76 , Issue.2 , pp. 287-299
    • Germain, R.N.1
  • 14
    • 85191983349 scopus 로고    scopus 로고
    • From Monocytes to M1/M2Macrophages: Phenotypical vs. Functional Differentiation
    • Italiani, P.; Boraschi, D. From Monocytes to M1/M2Macrophages: Phenotypical vs. Functional Differentiation Front. Immunol. 2014, 5, 514 10.3389/fimmu.2014.00514
    • (2014) Front. Immunol. , vol.5 , pp. 514
    • Italiani, P.1    Boraschi, D.2
  • 15
    • 79251500322 scopus 로고    scopus 로고
    • Measurement of the unfolded protein response (UPR) in monocytes
    • Carroll, T. P.; Greene, C. M.; McElvaney, N. G. Measurement of the unfolded protein response (UPR) in monocytes Methods Enzymol. 2011, 489 (C) 83-95 10.1016/B978-0-12-385116-1.00005-4
    • (2011) Methods Enzymol. , vol.489 , Issue.C , pp. 83-95
    • Carroll, T.P.1    Greene, C.M.2    McElvaney, N.G.3
  • 16
    • 0015116634 scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin G
    • Engvall, E.; Perlmann, P. Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin G Immunochemistry 1971, 8 (9) 871-874 10.1016/0019-2791(71)90454-X
    • (1971) Immunochemistry , vol.8 , Issue.9 , pp. 871-874
    • Engvall, E.1    Perlmann, P.2
  • 17
    • 0034760702 scopus 로고    scopus 로고
    • Enzyme-linked immunospot assays provide a sensitive tool for detection of cytokine secretion by monocytes
    • Kouwenhoven, M.; Ozenci, V.; Teleshova, N.; Hussein, Y.; Huang, Y. M.; Eusebio, A.; Link, H. Enzyme-linked immunospot assays provide a sensitive tool for detection of cytokine secretion by monocytes Clin. Diagn. Lab. Immunol. 2001, 8 (6) 1248-1257 10.1128/CDLI.8.6.1248-1257.2001
    • (2001) Clin. Diagn. Lab. Immunol. , vol.8 , Issue.6 , pp. 1248-1257
    • Kouwenhoven, M.1    Ozenci, V.2    Teleshova, N.3    Hussein, Y.4    Huang, Y.M.5    Eusebio, A.6    Link, H.7
  • 18
    • 85047379040 scopus 로고    scopus 로고
    • Polymerase Chain Reaction (PCR)
    • Winter, P. C. Polymerase Chain Reaction (PCR) Curr. Sci. 2005, 199 (December) 1-5 10.1038/npg.els.0005339
    • (2005) Curr. Sci. , vol.199 , Issue.DEC. , pp. 1-5
    • Winter, P.C.1
  • 19
    • 84870893908 scopus 로고    scopus 로고
    • The polymerase chain reaction
    • Powledge, T. M. The polymerase chain reaction Adv. Physiol. Educ. 2004, 28 (1-4) 44-50 10.1152/advan.00002.2004
    • (2004) Adv. Physiol. Educ. , vol.28 , Issue.14 , pp. 44-50
    • Powledge, T.M.1
  • 20
    • 1542618524 scopus 로고    scopus 로고
    • Monitoring of monocyte functional state after extracorporeal circulation: A flow cytometry study
    • Sbrana, S.; Parri, M. S.; De Filippis, R.; Gianetti, J.; Clerico, A. Monitoring of monocyte functional state after extracorporeal circulation: a flow cytometry study Cytometry 2004, 58 (1) 17-24 10.1002/cyto.b.10061
    • (2004) Cytometry , vol.58 , Issue.1 , pp. 17-24
    • Sbrana, S.1    Parri, M.S.2    De Filippis, R.3    Gianetti, J.4    Clerico, A.5
  • 21
    • 0033884049 scopus 로고    scopus 로고
    • Flow cytometry: Principles and clinical applications in hematology
    • Brown, M.; Wittwer, C. Flow cytometry: Principles and clinical applications in hematology Clin. Chem. 2000, 46 (8 II) 1221-1229
    • (2000) Clin. Chem. , vol.46 , Issue.8 , pp. 1221-1229
    • Brown, M.1    Wittwer, C.2
  • 23
    • 30944457268 scopus 로고    scopus 로고
    • LPS-induced ROS generation and changes in glutathione level and their relation to the maturation of human monocyte-derived dendritic cells
    • Yamada, H.; Arai, T.; Endo, N.; Yamashita, K.; Fukuda, K.; Sasada, M.; Uchiyama, T. LPS-induced ROS generation and changes in glutathione level and their relation to the maturation of human monocyte-derived dendritic cells Life Sci. 2006, 78 (9) 926-933 10.1016/j.lfs.2005.05.106
    • (2006) Life Sci. , vol.78 , Issue.9 , pp. 926-933
    • Yamada, H.1    Arai, T.2    Endo, N.3    Yamashita, K.4    Fukuda, K.5    Sasada, M.6    Uchiyama, T.7
  • 25
    • 0033534720 scopus 로고    scopus 로고
    • Monocyte adherence induced by lipopolysaccharide involves CD14, LFA-1, and cytohesin-1. Regulation by rho and phosphatidylinositol 3-kinase
    • Hmama, Z.; Knutson, K. L.; Herrera-Velit, P.; Nandan, D.; Reiner, N. E. Monocyte adherence induced by lipopolysaccharide involves CD14, LFA-1, and cytohesin-1. Regulation by rho and phosphatidylinositol 3-kinase J. Biol. Chem. 1999, 274 (2) 1050-1057 10.1074/jbc.274.2.1050
    • (1999) J. Biol. Chem. , vol.274 , Issue.2 , pp. 1050-1057
    • Hmama, Z.1    Knutson, K.L.2    Herrera-Velit, P.3    Nandan, D.4    Reiner, N.E.5
  • 26
    • 77957045079 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced expression of cell surface receptors and cell activation of neutrophils and monocytes in whole human blood
    • Gomes, N. E.; Brunialti, M. K. C.; Mendes, M. E.; Freudenberg, M.; Galanos, C.; Salomão, R. Lipopolysaccharide-induced expression of cell surface receptors and cell activation of neutrophils and monocytes in whole human blood Braz. J. Med. Biol. Res. 2010, 43 (9) 853-859 10.1590/S0100-879X2010007500078
    • (2010) Braz. J. Med. Biol. Res. , vol.43 , Issue.9 , pp. 853-859
    • Gomes, N.E.1    Brunialti, M.K.C.2    Mendes, M.E.3    Freudenberg, M.4    Galanos, C.5    Salomão, R.6
  • 27
    • 0018871095 scopus 로고
    • Establishment and characterization of a human acute monocytic leukemia cell line (THP-1)
    • Tsuchiya, S.; Yamabe, M.; Yamaguchi, Y.; Kobayashi, Y.; Konno, T.; Tada, K. Establishment and characterization of a human acute monocytic leukemia cell line (THP-1) Int. J. Cancer 1980, 26 (2) 171-176 10.1002/ijc.2910260208
    • (1980) Int. J. Cancer , vol.26 , Issue.2 , pp. 171-176
    • Tsuchiya, S.1    Yamabe, M.2    Yamaguchi, Y.3    Kobayashi, Y.4    Konno, T.5    Tada, K.6
  • 28
    • 0025963002 scopus 로고
    • The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation
    • Auwerx, J. The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation Experientia 1991, 47, 22-31 10.1007/BF02041244
    • (1991) Experientia , vol.47 , pp. 22-31
    • Auwerx, J.1
  • 29
    • 84859396928 scopus 로고    scopus 로고
    • Monocyte/macrophage proteomics: Recent findings and biomedical applications
    • Castagna, A.; Polati, R.; Bossi, A. M.; Girelli, D. Monocyte/macrophage proteomics: recent findings and biomedical applications Expert Rev. Proteomics 2012, 9 (2) 201-215 10.1586/epr.12.11
    • (2012) Expert Rev. Proteomics , vol.9 , Issue.2 , pp. 201-215
    • Castagna, A.1    Polati, R.2    Bossi, A.M.3    Girelli, D.4
  • 30
    • 33644511721 scopus 로고    scopus 로고
    • Proteome analysis of human monocytic THP-1 cells primed with oxidized low-density lipoproteins
    • Kang, J. H.; Kim, H. T.; Choi, M.-S.; Lee, W. H.; Huh, T.-L.; Park, Y. B.; Moon, B. J.; Kwon, O.-S. Proteome analysis of human monocytic THP-1 cells primed with oxidized low-density lipoproteins Proteomics 2006, 6 (4) 1261-1273 10.1002/pmic.200500290
    • (2006) Proteomics , vol.6 , Issue.4 , pp. 1261-1273
    • Kang, J.H.1    Kim, H.T.2    Choi, M.-S.3    Lee, W.H.4    Huh, T.-L.5    Park, Y.B.6    Moon, B.J.7    Kwon, O.-S.8
  • 31
    • 0030013991 scopus 로고    scopus 로고
    • Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1, 25-dihydroxyvitamin by binding
    • Schwende, H.; Fitzke, E.; Ambs, P.; Dieter, P. Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1, 25-dihydroxyvitamin by binding J. Leukocyte Biol. 1996, 59 (April) 555-561
    • (1996) J. Leukocyte Biol. , vol.59 , Issue.APR. , pp. 555-561
    • Schwende, H.1    Fitzke, E.2    Ambs, P.3    Dieter, P.4
  • 32
    • 0035908090 scopus 로고    scopus 로고
    • On the role of the innate immunity in autoimmune disease
    • Bachmann, M. F.; Kopf, M. On the role of the innate immunity in autoimmune disease J. Exp. Med. 2001, 193 (12) F47-F50 10.1084/jem.193.12.F47
    • (2001) J. Exp. Med. , vol.193 , Issue.12 , pp. F47-F50
    • Bachmann, M.F.1    Kopf, M.2
  • 33
    • 32944474237 scopus 로고    scopus 로고
    • Innate immunity gone awry: Linking microbial infections to chronic inflammation and cancer
    • Karin, M.; Lawrence, T.; Nizet, V. Innate immunity gone awry: Linking microbial infections to chronic inflammation and cancer Cell 2006, 124 (4) 823-835 10.1016/j.cell.2006.02.016
    • (2006) Cell , vol.124 , Issue.4 , pp. 823-835
    • Karin, M.1    Lawrence, T.2    Nizet, V.3
  • 34
  • 35
    • 77953251575 scopus 로고    scopus 로고
    • Innate immunity and rheumatoid arthritis
    • Gierut, A.; Perlman, H.; Pope, R. M. Innate immunity and rheumatoid arthritis Rheum Dis Clin North Am. 2010, 36, 271-296 10.1016/j.rdc.2010.03.004
    • (2010) Rheum Dis Clin North Am. , vol.36 , pp. 271-296
    • Gierut, A.1    Perlman, H.2    Pope, R.M.3
  • 36
    • 61349104286 scopus 로고    scopus 로고
    • The role of innate immune responses in autoimmune disease development
    • Waldner, H. The role of innate immune responses in autoimmune disease development Autoimmun. Rev. 2009, 8, 400-404 10.1016/j.autrev.2008.12.019
    • (2009) Autoimmun. Rev. , vol.8 , pp. 400-404
    • Waldner, H.1
  • 37
    • 79953162113 scopus 로고    scopus 로고
    • Smoking, citrullination and genetic variability in the immunopathogenesis of rheumatoid arthritis
    • Klareskog, L.; Malmström, V.; Lundberg, K.; Padyukov, L.; Alfredsson, L. Smoking, citrullination and genetic variability in the immunopathogenesis of rheumatoid arthritis Semin. Immunol. 2011, 23 (2) 92-98 10.1016/j.smim.2011.01.014
    • (2011) Semin. Immunol. , vol.23 , Issue.2 , pp. 92-98
    • Klareskog, L.1    Malmström, V.2    Lundberg, K.3    Padyukov, L.4    Alfredsson, L.5
  • 40
    • 0033988464 scopus 로고    scopus 로고
    • Isoaspartate in peptides and proteins: Formation, significance, and analysis
    • Aswad, D. W.; Paranandi, M. V.; Schurter, B. T. Isoaspartate in peptides and proteins: formation, significance, and analysis J. Pharm. Biomed. Anal. 2000, 21 (6) 1129-1136 10.1016/S0731-7085(99)00230-7
    • (2000) J. Pharm. Biomed. Anal. , vol.21 , Issue.6 , pp. 1129-1136
    • Aswad, D.W.1    Paranandi, M.V.2    Schurter, B.T.3
  • 41
    • 80155190078 scopus 로고    scopus 로고
    • Alzheimer's disease and mild cognitive impairment are associated with elevated levels of isoaspartyl residues in blood plasma proteins
    • Yang, H.; Lyutvinskiy, Y.; Soininen, H.; Zubarev, R. A. Alzheimer's disease and mild cognitive impairment are associated with elevated levels of isoaspartyl residues in blood plasma proteins J. Alzheimer's Dis. 2011, 27 (1) 113-118 10.3233/JAD-2011-110626
    • (2011) J. Alzheimer's Dis. , vol.27 , Issue.1 , pp. 113-118
    • Yang, H.1    Lyutvinskiy, Y.2    Soininen, H.3    Zubarev, R.A.4
  • 42
    • 84929921146 scopus 로고    scopus 로고
    • Immune attack: The role of inflammation in Alzheimer disease
    • Heppner, F. L.; Ransohoff, R. M.; Becher, B. Immune attack: the role of inflammation in Alzheimer disease Nat. Rev. Neurosci. 2015, 16 (6) 358-372 10.1038/nrn3880
    • (2015) Nat. Rev. Neurosci. , vol.16 , Issue.6 , pp. 358-372
    • Heppner, F.L.1    Ransohoff, R.M.2    Becher, B.3
  • 43
    • 84881096228 scopus 로고    scopus 로고
    • In silico instrumental response correction improves precision of label-free proteomics and accuracy of proteomics-based predictive models
    • Lyutvinskiy, Y.; Yang, H.; Rutishauser, D.; Zubarev, R. a. In silico instrumental response correction improves precision of label-free proteomics and accuracy of proteomics-based predictive models Mol. Cell. Proteomics 2013, 12, 2324-2331 10.1074/mcp.O112.023804
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2324-2331
    • Lyutvinskiy, Y.1    Yang, H.2    Rutishauser, D.3    Zubarev, R.A.4
  • 44
    • 84941078404 scopus 로고    scopus 로고
    • Proteomics reveals a role for attachment in monocyte differentiation into efficient pro-inflammatory macrophages
    • Tarasova, N. K.; Ytterberg, A. J.; Lundberg, K.; Zhang, X.-M.; Harris, R. A.; Zubarev, R. A. Proteomics reveals a role for attachment in monocyte differentiation into efficient pro-inflammatory macrophages J. Proteome Res. 2015, 14 (9) 3940-3947 10.1021/acs.jproteome.5b00659
    • (2015) J. Proteome Res. , vol.14 , Issue.9 , pp. 3940-3947
    • Tarasova, N.K.1    Ytterberg, A.J.2    Lundberg, K.3    Zhang, X.-M.4    Harris, R.A.5    Zubarev, R.A.6
  • 45
    • 0001677717 scopus 로고
    • Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
    • Benjamini, Y.; Hochberg, Y. Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing J. R. Stat. Soc. Ser. B 1995, 57 (1) 289-300 10.2307/2346101
    • (1995) J. R. Stat. Soc. Ser. B , vol.57 , Issue.1 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 46
    • 0014083515 scopus 로고
    • The heterogeneity of thymine methyl group origin in DNA pyrimidine isostichs of developing sea urchin embryos
    • Scarano, E.; Iaccarino, M.; Grippo, P.; Parisi, E. The heterogeneity of thymine methyl group origin in DNA pyrimidine isostichs of developing sea urchin embryos Proc. Natl. Acad. Sci. U. S. A. 1967, 57 (5) 1394-1400 10.1073/pnas.57.5.1394
    • (1967) Proc. Natl. Acad. Sci. U. S. A. , vol.57 , Issue.5 , pp. 1394-1400
    • Scarano, E.1    Iaccarino, M.2    Grippo, P.3    Parisi, E.4
  • 47
    • 2942594082 scopus 로고    scopus 로고
    • Cytosine methylation and CpG, TpG (CpA) and TpA frequencies
    • Jabbari, K.; Bernardi, G. Cytosine methylation and CpG, TpG (CpA) and TpA frequencies Gene 2004, 333, 143-149 10.1016/j.gene.2004.02.043
    • (2004) Gene , vol.333 , pp. 143-149
    • Jabbari, K.1    Bernardi, G.2
  • 48
    • 42949093707 scopus 로고    scopus 로고
    • Toll-like receptor 9-dependent immune activation by unmethylated CpG motifs in Aspergillus fumigatus DNA
    • Ramirez-Ortiz, Z. G.; Specht, C. A.; Wang, J. P.; Lee, C. K.; Bartholomeu, D. C.; Gazzinelli, R. T.; Levitz, S. M. Toll-like receptor 9-dependent immune activation by unmethylated CpG motifs in Aspergillus fumigatus DNA Infect. Immun. 2008, 76 (5) 2123-2129 10.1128/IAI.00047-08
    • (2008) Infect. Immun. , vol.76 , Issue.5 , pp. 2123-2129
    • Ramirez-Ortiz, Z.G.1    Specht, C.A.2    Wang, J.P.3    Lee, C.K.4    Bartholomeu, D.C.5    Gazzinelli, R.T.6    Levitz, S.M.7
  • 49
    • 84887856706 scopus 로고    scopus 로고
    • CpG-oligodeoxynucleotide-induced TLR9 activation regulates macrophage TREM-1 expression and shedding
    • Molad, Y.; Pokroy-Shapira, E.; Carmon, V. CpG-oligodeoxynucleotide-induced TLR9 activation regulates macrophage TREM-1 expression and shedding Innate Immun. 2013, 19 (6) 623-630 10.1177/1753425913476970
    • (2013) Innate Immun. , vol.19 , Issue.6 , pp. 623-630
    • Molad, Y.1    Pokroy-Shapira, E.2    Carmon, V.3
  • 50
    • 2342492317 scopus 로고    scopus 로고
    • Review of epidermal growth factor receptor biology
    • Herbst, R. S. Review of epidermal growth factor receptor biology Int. J. Radiat. Oncol., Biol., Phys. 2004, 59 (2) S21-S26 10.1016/j.ijrobp.2003.11.041
    • (2004) Int. J. Radiat. Oncol., Biol., Phys. , vol.59 , Issue.2 , pp. S21-S26
    • Herbst, R.S.1
  • 51
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter, G.; Cohen, S. Epidermal growth factor J. Biol. Chem. 1990, 265 (14) 7709-7712
    • (1990) J. Biol. Chem. , vol.265 , Issue.14 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 52
    • 0026629665 scopus 로고
    • Topical use of human recombinant epidermal growth factor (h-EGF) in venous ulcers
    • Falanga, V.; Eaglstein, W. H.; Bucalo, B.; Katz, M. H.; Harris, B.; Carson, P. Topical use of human recombinant epidermal growth factor (h-EGF) in venous ulcers J. Dermatol. Surg. Oncol. 1992, 18 (7) 604-606 10.1111/j.1524-4725.1992.tb03514.x
    • (1992) J. Dermatol. Surg. Oncol. , vol.18 , Issue.7 , pp. 604-606
    • Falanga, V.1    Eaglstein, W.H.2    Bucalo, B.3    Katz, M.H.4    Harris, B.5    Carson, P.6
  • 53
    • 84922496604 scopus 로고    scopus 로고
    • Aggregation of nanoparticles in endosomes and lysosomes produces surface-enhanced Raman spectroscopy
    • Lucas, L. J.; Chen, X. K.; Smith, A. J.; Korbelik, M.; Zeng, H.; Lee, P. W. K.; Hewitt, K. C. Aggregation of nanoparticles in endosomes and lysosomes produces surface-enhanced Raman spectroscopy J. Nanophotonics 2015, 9 (1) 093094 10.1117/1.JNP.9.093094
    • (2015) J. Nanophotonics , vol.9 , Issue.1 , pp. 093094
    • Lucas, L.J.1    Chen, X.K.2    Smith, A.J.3    Korbelik, M.4    Zeng, H.5    Lee, P.W.K.6    Hewitt, K.C.7
  • 54
    • 34250354402 scopus 로고    scopus 로고
    • Altered immunogenicity of isoaspartate containing proteins
    • Doyle, H. a; Gee, R. J.; Mamula, M. J. Altered immunogenicity of isoaspartate containing proteins Autoimmunity 2007, 40 (March) 131-137 10.1080/08916930601165180
    • (2007) Autoimmunity , vol.40 , Issue.MAR. , pp. 131-137
    • Doyle, H.A.1    Gee, R.J.2    Mamula, M.J.3
  • 55
    • 0033529490 scopus 로고    scopus 로고
    • Isoaspartyl post-translational modification triggers autoimmune responses to self-proteins
    • Mamula, M. J.; Gee, R. J.; Elliott, J. I.; Sette, A.; Southwood, S.; Jones, P. J.; Blier, P. R. Isoaspartyl post-translational modification triggers autoimmune responses to self-proteins J. Biol. Chem. 1999, 274 (32) 22321-22327 10.1074/jbc.274.32.22321
    • (1999) J. Biol. Chem. , vol.274 , Issue.32 , pp. 22321-22327
    • Mamula, M.J.1    Gee, R.J.2    Elliott, J.I.3    Sette, A.4    Southwood, S.5    Jones, P.J.6    Blier, P.R.7
  • 57
    • 0242472763 scopus 로고    scopus 로고
    • Western array analysis of human atherosclerotic plaques: Downregulation of apoptosis-linked gene 2
    • Martinet, W.; Schrijvers, D. M.; De Meyer, G. R. Y.; Herman, A. G.; Kockx, M. M. Western array analysis of human atherosclerotic plaques: Downregulation of apoptosis-linked gene 2 Cardiovasc. Res. 2003, 60 (2) 259-267 10.1016/S0008-6363(03)00537-6
    • (2003) Cardiovasc. Res. , vol.60 , Issue.2 , pp. 259-267
    • Martinet, W.1    Schrijvers, D.M.2    De Meyer, G.R.Y.3    Herman, A.G.4    Kockx, M.M.5
  • 58
    • 82555185587 scopus 로고    scopus 로고
    • Propofol inhibits the activation of p38 through up-regulating the expression of Annexin A1 to exert its anti-inflammation effect
    • Tang, J.; Chen, X.; Tu, W.; Guo, Y.; Zhao, Z.; Xue, Q.; Lin, C.; Xiao, J.; Sun, X.; Tao, T.; Gu, M.; Liu, Y. Propofol inhibits the activation of p38 through up-regulating the expression of Annexin A1 to exert its anti-inflammation effect PLoS One 2011, 6 (12) e27890 10.1371/journal.pone.0027890
    • (2011) PLoS One , vol.6 , Issue.12 , pp. e27890
    • Tang, J.1    Chen, X.2    Tu, W.3    Guo, Y.4    Zhao, Z.5    Xue, Q.6    Lin, C.7    Xiao, J.8    Sun, X.9    Tao, T.10    Gu, M.11    Liu, Y.12
  • 60
    • 0041367295 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in proteins: Unwanted alterations or surreptitious signals?
    • Reissner, K. J.; Aswad, D. W. Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell. Mol. Life Sci. 2003, 60 (7) 1281-1295 10.1007/s00018-003-2287-5
    • (2003) Cell. Mol. Life Sci. , vol.60 , Issue.7 , pp. 1281-1295
    • Reissner, K.J.1    Aswad, D.W.2
  • 61
    • 0034664688 scopus 로고    scopus 로고
    • Isoaspartate formation and neurodegeneration in Alzheimer's disease
    • Shimizu, T.; Watanabe, A.; Ogawara, M.; Mori, H.; Shirasawa, T. Isoaspartate formation and neurodegeneration in Alzheimer's disease Arch. Biochem. Biophys. 2000, 381 (2) 225-234 10.1006/abbi.2000.1955
    • (2000) Arch. Biochem. Biophys. , vol.381 , Issue.2 , pp. 225-234
    • Shimizu, T.1    Watanabe, A.2    Ogawara, M.3    Mori, H.4    Shirasawa, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.