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Volumn 31, Issue 1, 2013, Pages 45-51

Immunosignaturing: A critical review

Author keywords

Antibody profiling; Biomarker discovery; Health monitoring; Immunodiagnostics; Peptide microarray

Indexed keywords

BIO-MARKER DISCOVERY; COMPLEX INTERACTION; CRITICAL REVIEW; HEALTH MONITORING; IMMUNE SYSTEMS; IMMUNODIAGNOSTICS;

EID: 84871680408     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2012.10.012     Document Type: Review
Times cited : (51)

References (66)
  • 1
    • 37749031255 scopus 로고    scopus 로고
    • Next-generation sequencing transforms today's biology
    • Schuster S.C. Next-generation sequencing transforms today's biology. Nat. Methods 2008, 5:16-18.
    • (2008) Nat. Methods , vol.5 , pp. 16-18
    • Schuster, S.C.1
  • 3
    • 2542640080 scopus 로고    scopus 로고
    • Mass spectrometry as a diagnostic and a cancer biomarker discovery tool
    • Diamandis E.P. Mass spectrometry as a diagnostic and a cancer biomarker discovery tool. Mol. Cell. Proteomics 2004, 3:367-378.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 367-378
    • Diamandis, E.P.1
  • 4
    • 33747432967 scopus 로고    scopus 로고
    • Identification of biomarkers from mess spectrometry data using a "common" peak approach
    • Fushiki T., et al. Identification of biomarkers from mess spectrometry data using a "common" peak approach. BMC Bioinform. 2006, 7:358.
    • (2006) BMC Bioinform. , vol.7 , pp. 358
    • Fushiki, T.1
  • 5
    • 0027688060 scopus 로고
    • Memory in idiotypic networks due to competition between proliferation and differentiation
    • Sulzer B., et al. Memory in idiotypic networks due to competition between proliferation and differentiation. Bull. Math. Biol. 1993, 55:1133-1182.
    • (1993) Bull. Math. Biol. , vol.55 , pp. 1133-1182
    • Sulzer, B.1
  • 6
    • 34447550255 scopus 로고    scopus 로고
    • Managing and exploiting stress in the antibody factory
    • Cenci S., Sitia R. Managing and exploiting stress in the antibody factory. FEBS Lett. 2007, 581:3652-3657.
    • (2007) FEBS Lett. , vol.581 , pp. 3652-3657
    • Cenci, S.1    Sitia, R.2
  • 7
    • 8644253628 scopus 로고    scopus 로고
    • Cell division rates of primary human precursor B cells in culture reflect in vivo rates
    • Cooperman J., et al. Cell division rates of primary human precursor B cells in culture reflect in vivo rates. Stem Cells 2004, 22:1111-1120.
    • (2004) Stem Cells , vol.22 , pp. 1111-1120
    • Cooperman, J.1
  • 8
    • 0025339171 scopus 로고
    • The bulk of the peripheral B-cell pool in mice is stable and not rapidly renewed from the bone marrow
    • Forster I., Rajewsky K. The bulk of the peripheral B-cell pool in mice is stable and not rapidly renewed from the bone marrow. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:4781-4784.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4781-4784
    • Forster, I.1    Rajewsky, K.2
  • 9
    • 0035887189 scopus 로고    scopus 로고
    • Homeostasis of peripheral B cells in the absence of B cell influx from the bone marrow
    • Hao Z., Rajewsky K. Homeostasis of peripheral B cells in the absence of B cell influx from the bone marrow. J. Exp. Med. 2001, 194:1151-1164.
    • (2001) J. Exp. Med. , vol.194 , pp. 1151-1164
    • Hao, Z.1    Rajewsky, K.2
  • 10
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: history, character, and diagnostic prospects
    • Anderson N.L., Anderson N.G. The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1:845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 11
    • 81455150067 scopus 로고    scopus 로고
    • Mathematical model identifies blood biomarker-based early cancer detection strategies and limitations
    • Hori S.S., Gambhir S.S. Mathematical model identifies blood biomarker-based early cancer detection strategies and limitations. Sci. Transl. Med. 2012, 3:109ra116.
    • (2012) Sci. Transl. Med. , vol.3
    • Hori, S.S.1    Gambhir, S.S.2
  • 12
    • 68049122014 scopus 로고    scopus 로고
    • The preclinical natural history of serous ovarian cancer: defining the target for early detection
    • Brown P.O., Palmer C. The preclinical natural history of serous ovarian cancer: defining the target for early detection. PLoS Med. 2009, 6:e1000114.
    • (2009) PLoS Med. , vol.6
    • Brown, P.O.1    Palmer, C.2
  • 13
    • 35349014634 scopus 로고    scopus 로고
    • Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies
    • Acierno J.P., et al. Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies. J. Mol. Biol. 2007, 374:130-146.
    • (2007) J. Mol. Biol. , vol.374 , pp. 130-146
    • Acierno, J.P.1
  • 14
    • 0030176302 scopus 로고    scopus 로고
    • The effect of pH, hydrogen peroxide and temperature on the stability of human monoclonal antibody
    • Usami A., et al. The effect of pH, hydrogen peroxide and temperature on the stability of human monoclonal antibody. J. Pharm. Biomed. Anal. 1996, 14:1133-1140.
    • (1996) J. Pharm. Biomed. Anal. , vol.14 , pp. 1133-1140
    • Usami, A.1
  • 15
    • 84857974112 scopus 로고    scopus 로고
    • Evaluation of biological sample preparation for immunosignature-based diagnostics
    • Chase B.A., et al. Evaluation of biological sample preparation for immunosignature-based diagnostics. Clin. Vaccine Immunol. 2012, 19:352-358.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 352-358
    • Chase, B.A.1
  • 16
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability
    • Harn N., et al. Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J. Pharm. Sci. 2007, 96:532-546.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 532-546
    • Harn, N.1
  • 17
    • 0141858715 scopus 로고    scopus 로고
    • The specificity of cross-reactivity: promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness
    • James L.C., Tawfik D.S. The specificity of cross-reactivity: promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness. Protein Sci. 2003, 12:2183-2193.
    • (2003) Protein Sci. , vol.12 , pp. 2183-2193
    • James, L.C.1    Tawfik, D.S.2
  • 18
    • 0346494733 scopus 로고    scopus 로고
    • Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics
    • Wang L.F., Yu M. Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics. Curr. Drug Targets 2004, 5:1-15.
    • (2004) Curr. Drug Targets , vol.5 , pp. 1-15
    • Wang, L.F.1    Yu, M.2
  • 19
    • 78049282755 scopus 로고    scopus 로고
    • Humoral 'reactome' profiles using peptide microarray chips
    • Valentini D., et al. Humoral 'reactome' profiles using peptide microarray chips. Trends Immunol. 2010, 31:399-400.
    • (2010) Trends Immunol. , vol.31 , pp. 399-400
    • Valentini, D.1
  • 20
    • 84859859148 scopus 로고    scopus 로고
    • Physical characterization of the 'immunosignaturing effect'
    • M111.011593
    • Stafford P., et al. Physical characterization of the 'immunosignaturing effect'. Mol. Cell. Proteomics 2012, 11. M111.011593.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Stafford, P.1
  • 21
    • 84868666605 scopus 로고    scopus 로고
    • On silico peptide microarrays for high-resolution mapping of antibody epitopes and diverse protein-protein interactions
    • Price J.V., et al. On silico peptide microarrays for high-resolution mapping of antibody epitopes and diverse protein-protein interactions. Nat. Med. 2012, 18:1434-1440.
    • (2012) Nat. Med. , vol.18 , pp. 1434-1440
    • Price, J.V.1
  • 22
    • 0036921994 scopus 로고    scopus 로고
    • Phage display: practicalities and prospects
    • Willats W.G.T. Phage display: practicalities and prospects. Plant Mol. Biol. 2002, 50:837-854.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 837-854
    • Willats, W.G.T.1
  • 24
    • 0031981377 scopus 로고    scopus 로고
    • Functional diversity and clonal frequencies of reactivity in the available antibody repertoire
    • Nobrega A., et al. Functional diversity and clonal frequencies of reactivity in the available antibody repertoire. Eur. J. Immunol. 1998, 28:1204-1215.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1204-1215
    • Nobrega, A.1
  • 25
    • 84871702330 scopus 로고    scopus 로고
    • Feasibility of an early Alzheimer's disease immunosignature diagnostic test
    • Restrepo L., et al. Feasibility of an early Alzheimer's disease immunosignature diagnostic test. J. Neuroimmunol. 2011, 10.1016/j.jneuroim.2012.09.014.
    • (2011) J. Neuroimmunol.
    • Restrepo, L.1
  • 26
    • 80051532205 scopus 로고    scopus 로고
    • Application of immunosignatures to the assessment of Alzheimer's disease
    • Restrepo L., et al. Application of immunosignatures to the assessment of Alzheimer's disease. Ann. Neurol. 2011, 70:286-295.
    • (2011) Ann. Neurol. , vol.70 , pp. 286-295
    • Restrepo, L.1
  • 27
    • 84862901532 scopus 로고    scopus 로고
    • Immunosignaturing can detect products from molecular markers in brain cancer
    • (in press)
    • Hughes, A. et al. (2012) Immunosignaturing can detect products from molecular markers in brain cancer. PLoS ONE (in press).
    • (2012) PLoS ONE
    • Hughes, A.1
  • 28
    • 80051799620 scopus 로고    scopus 로고
    • Statistical methods for analyzing immunosignatures
    • Brown J., et al. Statistical methods for analyzing immunosignatures. BMC Bioinform. 2011, 12:349.
    • (2011) BMC Bioinform. , vol.12 , pp. 349
    • Brown, J.1
  • 29
    • 84881606847 scopus 로고    scopus 로고
    • Immunosignaturing microarrays distinguish antibody profiles of related pancreatic diseases
    • Kukreja M., et al. Immunosignaturing microarrays distinguish antibody profiles of related pancreatic diseases. Proteomics Bioinform. 2012, S6.
    • (2012) Proteomics Bioinform. , vol.S6
    • Kukreja, M.1
  • 30
    • 77953025997 scopus 로고    scopus 로고
    • A general method for characterization of humoral immunity induced by a vaccine or infection
    • Legutki J.B., et al. A general method for characterization of humoral immunity induced by a vaccine or infection. Vaccine 2010, 28:4529-4537.
    • (2010) Vaccine , vol.28 , pp. 4529-4537
    • Legutki, J.B.1
  • 31
    • 79953228541 scopus 로고    scopus 로고
    • Exploring antibody recognition of sequence space through random-sequence peptide microarrays
    • M110.000786
    • Halperin R.F., et al. Exploring antibody recognition of sequence space through random-sequence peptide microarrays. Mol. Cell. Proteomics 2011, 10. M110.000786.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Halperin, R.F.1
  • 32
    • 84855243121 scopus 로고    scopus 로고
    • GuiTope: an application for mapping random-sequence peptides to protein sequences
    • Halperin R., et al. GuiTope: an application for mapping random-sequence peptides to protein sequences. BMC Bioinform. 2012, 13:1.
    • (2012) BMC Bioinform. , vol.13 , pp. 1
    • Halperin, R.1
  • 34
    • 80053174264 scopus 로고    scopus 로고
    • Segmentation and intensity estimation for microarray images with saturated pixels
    • Yang Y., et al. Segmentation and intensity estimation for microarray images with saturated pixels. BMC Bioinform. 2011, 12:462.
    • (2011) BMC Bioinform. , vol.12 , pp. 462
    • Yang, Y.1
  • 35
    • 80051799620 scopus 로고    scopus 로고
    • Statistical methods for analyzing immunosignatures
    • Brown J.R., et al. Statistical methods for analyzing immunosignatures. BMC Bioinform. 2011, 12:349.
    • (2011) BMC Bioinform. , vol.12 , pp. 349
    • Brown, J.R.1
  • 36
    • 84862491822 scopus 로고    scopus 로고
    • Comparative study of classification algorithms for immunosignaturing data
    • Kukreja M., et al. Comparative study of classification algorithms for immunosignaturing data. BMC Bioinform. 2012, 13:139.
    • (2012) BMC Bioinform. , vol.13 , pp. 139
    • Kukreja, M.1
  • 37
    • 84862901532 scopus 로고    scopus 로고
    • Immunosignaturing can detect products from molecular markers in brain cancer
    • Hughes A.K., et al. Immunosignaturing can detect products from molecular markers in brain cancer. PLoS ONE 2012, 7:e40201.
    • (2012) PLoS ONE , vol.7
    • Hughes, A.K.1
  • 38
    • 0038712135 scopus 로고    scopus 로고
    • Disregulated expression of the Th2 cytokine gene in patients with intraoral squamous cell carcinoma
    • Agarwal A., et al. Disregulated expression of the Th2 cytokine gene in patients with intraoral squamous cell carcinoma. Immunol. Invest. 2003, 32:17-30.
    • (2003) Immunol. Invest. , vol.32 , pp. 17-30
    • Agarwal, A.1
  • 39
    • 33750341091 scopus 로고    scopus 로고
    • MIMOX: a web tool for phage display based epitope mapping
    • Huang J., et al. MIMOX: a web tool for phage display based epitope mapping. BMC Bioinform. 2006, 7:451.
    • (2006) BMC Bioinform. , vol.7 , pp. 451
    • Huang, J.1
  • 40
    • 0036463587 scopus 로고    scopus 로고
    • Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences
    • Mackey A.J., et al. Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences. Mol. Cell. Proteomics 2002, 1:139-147.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 139-147
    • Mackey, A.J.1
  • 41
    • 33646150213 scopus 로고    scopus 로고
    • Discontinuous epitope prediction based on mimotope analysis
    • Moreau V., et al. Discontinuous epitope prediction based on mimotope analysis. Bioinformatics 2006, 22:1088-1095.
    • (2006) Bioinformatics , vol.22 , pp. 1088-1095
    • Moreau, V.1
  • 42
    • 40549137774 scopus 로고    scopus 로고
    • Phage display of peptides in ligand selection for use in affinity chromatography
    • Casey J.L., et al. Phage display of peptides in ligand selection for use in affinity chromatography. Methods Mol. Biol. 2008, 421:111-124.
    • (2008) Methods Mol. Biol. , vol.421 , pp. 111-124
    • Casey, J.L.1
  • 43
    • 84859149826 scopus 로고    scopus 로고
    • Autoreactive antibodies raised by self derived de novo peptides can identify unrelated antigens on protein microarrays. Are autoantibodies really autoantibodies?
    • Kroening K., et al. Autoreactive antibodies raised by self derived de novo peptides can identify unrelated antigens on protein microarrays. Are autoantibodies really autoantibodies?. Exp. Mol. Pathol. 2012, 92:304-311.
    • (2012) Exp. Mol. Pathol. , vol.92 , pp. 304-311
    • Kroening, K.1
  • 44
    • 0032499710 scopus 로고    scopus 로고
    • Identification of multiple cancer/testis antigens by allogeneic antibody screening of a melanoma cell line library
    • Chen Y.T., et al. Identification of multiple cancer/testis antigens by allogeneic antibody screening of a melanoma cell line library. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:6919-6923.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6919-6923
    • Chen, Y.T.1
  • 45
    • 0033858931 scopus 로고    scopus 로고
    • Antibodies in diagnostics - from immunoassays to protein chips
    • Borrebaeck C.A.K. Antibodies in diagnostics - from immunoassays to protein chips. Immunol. Today 2000, 21:379-382.
    • (2000) Immunol. Today , vol.21 , pp. 379-382
    • Borrebaeck, C.A.K.1
  • 46
    • 0034429848 scopus 로고    scopus 로고
    • Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays
    • Butler J.E. Solid supports in enzyme-linked immunosorbent assay and other solid-phase immunoassays. Methods 2000, 22:4-23.
    • (2000) Methods , vol.22 , pp. 4-23
    • Butler, J.E.1
  • 47
    • 0027364064 scopus 로고
    • The immunochemistry of sandwich ELISAs - VI. Greater than 90% of monoclonal and 75% of polyclonal anti-fluorescyl capture antibodies (CAbs) are denatured by passive adsorption
    • Butler J.E., et al. The immunochemistry of sandwich ELISAs - VI. Greater than 90% of monoclonal and 75% of polyclonal anti-fluorescyl capture antibodies (CAbs) are denatured by passive adsorption. Mol. Immunol. 1993, 30:1165-1175.
    • (1993) Mol. Immunol. , vol.30 , pp. 1165-1175
    • Butler, J.E.1
  • 48
    • 0036303521 scopus 로고    scopus 로고
    • Towards proteome-wide production of monoclonal antibody by phage display
    • Liu B., et al. Towards proteome-wide production of monoclonal antibody by phage display. J. Mol. Biol. 2002, 315:1063-1073.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1063-1073
    • Liu, B.1
  • 49
    • 63449121086 scopus 로고    scopus 로고
    • Generation and validation of affinity reagents on a proteome-wide level
    • Uhlen M., Hober S. Generation and validation of affinity reagents on a proteome-wide level. J. Mol. Recognit. 2009, 22:57-64.
    • (2009) J. Mol. Recognit. , vol.22 , pp. 57-64
    • Uhlen, M.1    Hober, S.2
  • 50
    • 77955495015 scopus 로고    scopus 로고
    • Immune response biomarker profiling application on protoarray protein microarrays
    • Humana Press, A.J. Rai (Ed.)
    • Schweitzer B., et al. Immune response biomarker profiling application on protoarray protein microarrays. The Urinary Proteome 2010, 243-252. Humana Press. A.J. Rai (Ed.).
    • (2010) The Urinary Proteome , pp. 243-252
    • Schweitzer, B.1
  • 51
    • 0037434981 scopus 로고    scopus 로고
    • Disease proteomics
    • Hanash S. Disease proteomics. Nature 2003, 422:226-232.
    • (2003) Nature , vol.422 , pp. 226-232
    • Hanash, S.1
  • 52
    • 78650938957 scopus 로고    scopus 로고
    • Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening
    • Reddy M.M., et al. Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening. Cell 2011, 144:132-142.
    • (2011) Cell , vol.144 , pp. 132-142
    • Reddy, M.M.1
  • 53
    • 4444326138 scopus 로고    scopus 로고
    • Recent advances in peptide-based microarray technologies
    • Panicker R.C., et al. Recent advances in peptide-based microarray technologies. Comb. Chem. High Throughput Screen. 2004, 7:547-556.
    • (2004) Comb. Chem. High Throughput Screen. , vol.7 , pp. 547-556
    • Panicker, R.C.1
  • 54
    • 77952038163 scopus 로고    scopus 로고
    • Exploring peptide space for enzyme modulators
    • Fu J., et al. Exploring peptide space for enzyme modulators. J. Am. Chem. Soc. 2010, 132:6419-6424.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6419-6424
    • Fu, J.1
  • 55
    • 79954473035 scopus 로고    scopus 로고
    • Peptide-modified surfaces for enzyme immobilization
    • Fu J., et al. Peptide-modified surfaces for enzyme immobilization. PLoS ONE 2011, 6:e18692.
    • (2011) PLoS ONE , vol.6
    • Fu, J.1
  • 56
    • 77956285399 scopus 로고    scopus 로고
    • Discovery of high-affinity protein binding ligands - backwards
    • Diehnelt C.W., et al. Discovery of high-affinity protein binding ligands - backwards. PLoS ONE 2010, 5:e10728.
    • (2010) PLoS ONE , vol.5
    • Diehnelt, C.W.1
  • 57
    • 67149144312 scopus 로고    scopus 로고
    • Peptide microarrays for carbohydrate recognition
    • Boltz K.W., et al. Peptide microarrays for carbohydrate recognition. Analyst 2009, 134:650-652.
    • (2009) Analyst , vol.134 , pp. 650-652
    • Boltz, K.W.1
  • 58
    • 84859635358 scopus 로고    scopus 로고
    • Current advances in peptide and small molecule microarray technologies
    • Foong Y.M., et al. Current advances in peptide and small molecule microarray technologies. Curr. Opin. Chem. Biol. 2012, 16:234-242.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 234-242
    • Foong, Y.M.1
  • 59
    • 65549111163 scopus 로고    scopus 로고
    • Bacterial glycoprofiling by using random sequence peptide microarrays
    • Morales Betanzos C., et al. Bacterial glycoprofiling by using random sequence peptide microarrays. Chembiochem 2009, 10:877-888.
    • (2009) Chembiochem , vol.10 , pp. 877-888
    • Morales Betanzos, C.1
  • 60
    • 0035017737 scopus 로고    scopus 로고
    • Peptide and small molecule microarray for high throughput cell adhesion and functional assays
    • Falsey J.R., et al. Peptide and small molecule microarray for high throughput cell adhesion and functional assays. Bioconjug. Chem. 2001, 12:346-353.
    • (2001) Bioconjug. Chem. , vol.12 , pp. 346-353
    • Falsey, J.R.1
  • 61
    • 25844440962 scopus 로고    scopus 로고
    • IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2
    • Shreffler W.G., et al. IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2. J. Allergy Clin. Immunol. 2005, 116:893-899.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 893-899
    • Shreffler, W.G.1
  • 62
    • 73949152574 scopus 로고    scopus 로고
    • Epitope mapping of human chromogranin A by peptide microarrays
    • Humana Press, M. Cretich, M. Chiari (Eds.)
    • Cretich M., et al. Epitope mapping of human chromogranin A by peptide microarrays. Peptide Microarrays 2009, 221-232. Humana Press. M. Cretich, M. Chiari (Eds.).
    • (2009) Peptide Microarrays , pp. 221-232
    • Cretich, M.1
  • 63
    • 64349108978 scopus 로고    scopus 로고
    • Association energetics of cross-reactive and specific antibodies
    • Mohan S., et al. Association energetics of cross-reactive and specific antibodies. Biochemistry 2009, 48:1390-1398.
    • (2009) Biochemistry , vol.48 , pp. 1390-1398
    • Mohan, S.1
  • 64
    • 34547460183 scopus 로고    scopus 로고
    • Molecular evolution of affinity and flexibility in the immune system
    • Thorpe I.F., Brooks C.L. Molecular evolution of affinity and flexibility in the immune system. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:8821-8826.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8821-8826
    • Thorpe, I.F.1    Brooks, C.L.2
  • 65
    • 35448975223 scopus 로고    scopus 로고
    • Properties and function of polyreactive antibodies and polyreactive antigen-binding B cells
    • Zhou Z.H., et al. Properties and function of polyreactive antibodies and polyreactive antigen-binding B cells. J. Autoimmun. 2007, 29:219-228.
    • (2007) J. Autoimmun. , vol.29 , pp. 219-228
    • Zhou, Z.H.1
  • 66
    • 84871703853 scopus 로고    scopus 로고
    • Immunosignaturing: challenges and opportunities
    • Department of Genetics, Genomics & Bioinformatics, UCR
    • Stafford P. Immunosignaturing: challenges and opportunities. Bioinformatics and Proteomics 2010, Department of Genetics, Genomics & Bioinformatics, UCR.
    • (2010) Bioinformatics and Proteomics
    • Stafford, P.1


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