2501 SSFDQQDWDYSIAEKMHPIRPQFRELPPLPPSRASFGGGASRPSR SSSGYVVPKRLGDMREYNAHPQLHVPPNSPLPPLPTHLQSSRPSR SSRGEGNNIISSRPFLSNSDPWSNKLTGRWGPLPPLPNDSRPSR SSDNWARRVHASELIYTDLSPQILLAQRQLPPTPGRDPSHSRPSR SSYNDLGTRPVSEVIKYDYFPQYSQHVITPDGSYSTRPLPSRPSR SSESPLMYNRVGALQSLTSVQSMMHFALQRRLPRTPPPASRPSR PQYARIVSYRFRALPSPPSASRPSR RPLPPLP 7 Phage display (common panning) PMID:7929027 Src SH3 domain of Proto-oncogene tyrosine-protein kinase Src Not determined. Not determined. Not determined. T9 M13 phage display library (X22) 2502 STAPWGLRVAHEGGVLKRPLPIPPVTRPSR STNVWVTGSVIARGAQSRPLPIPPETRPSR STNDVDWMHMWNSGGPHRRLPPTPATRPSR STRWSHSWPGYVGGANPSPATRPLPWPSR STAHSLWDWGTFSGVSHKSRLPPLPTRPSR STAVSFRFMPGGGEAFYSTRPVPPITRPSR STMYGVSWLSSGSGGILAPPVPPRNTRPSR RPLPPLP 7 Phage display (common panning) PMID:7929027 Src SH3 domain of Proto-oncogene tyrosine-protein kinase Src Not determined. Not determined. Not determined. T12 M13 phage display library (X36) 2503 LASRPLPLLPNSAPGQ LTGRPLPALPPPFSDF PAYRPLPRLPDLSVIY RALRVRPLPPVPGTSL DAPGSLPFRPLPPVPT LKWRALPPLPETDTPY ISQRALPPLPLMSDPA LTSRPLPDIPVRPSKS NTNRPLPPTPDGLDVR MKDRVLPPIPTVESAV LQSRPLPLPPQSSYPI FINRRLPALPPDNSLL FRALPLPPTPDNPFAG LYSAIAPDPPPRNSSS 14 Phage display (common panning) 3 PMID:8643668 Src SH3 domain of Proto-oncogene tyrosine-protein kinase Src Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2504 ITMRPLPALPGHGQIH LPRRPLPDLPMAAGKG LGSRPLPPTPRQWPEV STIRPLPAIPRDTLLT RSGRPLPPIPEVGHNV IGSRPLPWTPDDLGSA LAQRELPGLPAGAGVS IPGRALPELPPQRALP FVGRELPPTPRTVIPW DPRSALPALPLTPLQT SPHDVLPALPDSHSKS 11 Phage display (common panning) 3 PMID:8643668 SH3 domain of tyrosine-protein kinase Yes Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2505 PPWWAPPPIPNSPQVL PPKFSPPPPPYWQLHA PPHWAPPAPPAMSPPI PPTWTPPKPPGWGVVF PPSFAPPAAPPRHSFG PTYPPPPPPDTAKGA GPRWSPPPVPLPTSLD APTWSPPALPNVAKYK PPDYAAPAIPSSLWVD IKGPRFPVPPVPLNGV PPAWSPPHRPVAFGST APKKPAPPVPMMAHVM 12 Phage display (common panning) 3 PMID:8643668 SH3 domain of tyrosine-protein kinase ABL1 Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2506 LTPQSKPPLPPKPSAV SSHNSRPPLPEKPSWL PVKPPLPAKPWWLPPL TERPPLPQRPDWLSYS LGEFSKPPIPQKPTWM YPQFRPPVPPKPSLMQ VTRPPLPPKPGHMADF VSLGLKPPVPPKPMQL LLGPPVPPKPQTLFSF YKPEVPARPIWLSEL GAGAARPLVPKKPLFL 11 Phage display (common panning) 3 PMID:8643668 SH3 domain of cortactin Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2507 YDASSAPQRPPLPVRKSBR EYVNASPERPPIPGRKSRP WNGIAIPGRPEIPPRASRP SMIFIYPERPSPPPRFSRP GVEEWNPERPQIPLRLSRP WVVDSRPDIPLRRSLP WVPLGRPEIPLRKSLP GGTVGRPPIPERKSVD YSHAGRPEVPPRQSKP FSAAARPDIPSRASTP LYIPKRPEVPPRRHEA NNISARPPLPSRQNPP MAGTPRPAVPQRMNPP 13 Phage display (common panning) 3 PMID:8643668 SH3 domain of apoptosis-stimulating of p53 protein 2 Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2508 MPPPVPPRPPGTLQVA LSYSPPPVPPRPDSTL VLAPPVPPRPGNTFFT YRPPVAPRPPSSLSVD LQCPDCPRVPPRPIPI VPPLVAPRPPSTLNSL LTPPPFPKRPRWTLPE YWPHRPPLAPPQTTLG 8 Phage display (common panning) 3 PMID:8643668 SH3 domains of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 and gamma-2 Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2509 GQPAGDPDPPPLPAKF FEQTGVPLLPPKSFKY IFGDPPPPIPMKGRSL SNQGSIPVLPIKRVQY NYVNALPPGPPLPAKN SSDPERPVLPPKLWSV HFGPSKPPLPIKTRIT DWKVPEPPVPKLPLKQ ATSEGLPILPSKVGSY NANVSAPRAPAFPVKT EMVLGPPVPPKRGTVV AGSRHPPTLPPKESGG SVAADPPRLPAKSRPQ P-x-L-P-x-K 13 Phage display (common panning) 3 PMID:8643668 SH3 domain of Crk N Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2510 KWDSLLPALPPAFTVE RWDQVLPELPTSKGQI RFDFPLPTHPNLQKAH RLDSPLPALPPTVMQN RWGAPLPPLPEYSWST YWDMPLPRLPGEEPSL RFDYNLPDVPLSLGTA TKKPNAPLPPLPAYMG KWDLDLPPEPMSLGNY YYQRPLPPLPLSHFES YYRKPLPNLPRGQTDD YFDKPLPESPGALMSL YFSRALPGLPERQEAH SLWDPLPPIPQSKTSV SYYDPLPKLPDPGDLG KLYYPLPPVPFKDTKH DPYDALPETPSMKASQ 17 Phage display (common panning) 3 PMID:8643668 SH3 domain of Grb2 N Not determined. Not determined. Not determined. X6PX2PX6 M13 phage display library 2511 SRLDYLKSSLLHLGSR[0.43] SRVDELKLKLSTLVSR[6.1] SRVDYLKDKLISLASR[NT] SRVADVKRKILGLASR[NT] SRVEELRGALLSLKSR[NT] SRLELLKESMRSLASR[NT] SREAWRGRLWDLAKSR[NT] SRVGELKEMMRTLASR[NT] SRLTELKEKLSQLNSR[NT] SRRPEFLKQEIRKASR[NT] 10 Phage display (common panning) 3 PMID:9722581 Troponin C, skeletal muscle Not determined. Not determined. Not determined. X12 M13 phage display ibrary Surface plasmon resonance (SPR) Equilibrium binding constants (μM) for troponin C-binding peptides in the presence of calcium were determined. NT denotes not tested. Nondenaturing polyacrylamide gel electrophoresis demonstrated that pT5 (SRLDYLKSSLLHLGSR) formed a stable complex with troponin C in the presence of calcium. It also showned that the pT5 peptide inhibited the maximal calcium-activated tension of rabbit psoas muscle fibers. 2512 KDYQRNRGPSKFTGLQPSVL 1 Phage display (common panning) 4 PMID:21669956 Purified serum IgG from goat-1 (G1) infection with Map Not determined. Not determined. Not determined. X20 fUSE5 phage display library 2513 VPVRHTPVRDNRLVGFRSSS YVPIVTFYSEISMHSSRAIP EARHVELCPDFKYYPFFCVP 3 Phage display (subtractive panning) 5 PMID:21669956 Purified serum IgG from goat-2 (G2) infection with Map Not determined. Not determined. Not determined. X20 fUSE5 phage display library A pre-clearance step was introduced using serum IgG from goat-2 (G2) prior to (pre-challenge) infection with Map. 2514 VFAEFLPLFSKFGSRMHILK PVLRSGRCAELIQIGFRCRA 2 Phage display (common panning) 4 PMID:16177378 Apical membrane antigen 1, AMA1 Anti-AMA1 monoclonal antibody 4G2dc1 Not determined. Not determined. X20 fUSE5 phage display library 2515 GGWYSFDSPYLMSITEMRLR 1 Phage display (subtractive panning) 3 PMID:16517852 Anti-EBV monoclonal antibody gp125 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2516 YTDSSMAVTLMKFASNFLF 1 Phage display (subtractive panning) 3 PMID:16517852 Anti-EBV monoclonal antibody F1 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2517 DNYWSFSDSTYWTLRYSSG 1 Phage display (subtractive panning) 3 PMID:16517852 Anti-EBV monoclonal antibody A2 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2518 SKLLYNYGACRTGCYMAGR ELISSCLVWSARGCLFGGGI VMDECVFSSISVLFCNHMLH 3 Phage display (subtractive panning) 3 PMID:16517852 Anti-EBV monoclonal antibody A3 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2519 GGWYSFDSPYLMSITEMRLR 1 Phage display (subtractive panning) 4 PMID:16517852 Anti-EBV monoclonal antibody gp125 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2520 YTDSSMAVTLMKFASNFLF 1 Phage display (subtractive panning) 4 PMID:16517852 Anti-EBV monoclonal antibody F1 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2521 DNYWSFSDSTYWTLRYSSG 1 Phage display (subtractive panning) 4 PMID:16517852 Anti-EBV monoclonal antibody A2 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2522 SKLLYNYGACRTGCYMAGR ELISSCLVWSARGCLFGGGI VMDECVFSSISVLFCNHMLH 3 Phage display (subtractive panning) 4 PMID:16517852 Anti-EBV monoclonal antibody A3 Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library Coated wells were blocked with 5% BLOTTO (milk powder diluted in phosphate-buffered saline [PBS]), and the 20-mer phage peptide library was preincubated in 1% BLOTTO for 15 min to remove any milk-binding phage before it was added to the MAb-coated wells. To assess their diagnostic value, a panel of 62 individual EBV IgM sera for their reactivities was screened with the peptides alone. For all peptides, there was a clear distinction between the EBV-positive and the EBV-negative samples, resulting in 100% specificity. The sensitivities were 88%, 85%, 71%, and 54% for peptides F1 (YTDSSMAVTLMKFASNFLF), A3 (SKLLYNYGACRTGCYMAGR, ELISSCLVWSARGCLFGGGI and VMDECVFSSISVLFCNHMLH), gp125 (GGWYSFDSPYLMSITEMRLR), and A2 (DNYWSFSDSTYWTLRYSSG), respectively. Any combination of peptides increased the sensitivity, indicating that individual peptides react with different subsets of antibodies. Furthermore, when the F1 and the gp125 peptides were coupled to bovine serum albumin and screened against 216 serum samples, there were dramatic improvements in sensitivities (95% and 92%, respectively) and little cross-reactivity with the other peptides encountered during acute viral infections, including rheumatoid factor. This study shows the potential for the use of peptide mimotopes as alternatives to the complex antigens used in current serodiagnostics for EBV infection. 2523 DGPSYHVAFKNSRGLRHS 1 Phage display (subtractive panning) 4-6 PMID:19073711 Purified serum IgG from an EBV-infected patient Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library The 20-mer phage peptide library was preincubated in BLOTTO to remove any milk-binding phage before it was added to the purified human anti-EBV IgG preparations-coated wells. 2524 NGALYPRFFPDYSILMFPII DQFAQAYRGDRNFFNELTST RQFSKFKDASDRYGNYLHFF SSSIKIWNKLGWNTVIAGTR FVNAFQNANFMRPRELFALA SANLNFFSPDFGLYTPNASA AITCAHTLSIKSRRCQYVFK AASYASRTVGFASVYWFSRP RLRGDYNVGPIRFGWPVAPN MSDFDRKVYTFNFITDPQHL GVTDFDFKVFSSTFPKIFLS TPNTVRDFYYNVSLPSYMLI 12 Phage display (subtractive panning) 4-6 PMID:19073711 Purified serum IgG from an EBV-immunised rabbit Epstein-Barr virus, EBV Not determined. Not determined. X20 fUSE5 phage display library The 20-mer phage peptide library was preincubated in BLOTTO to remove any milk-binding phage before it was added to the purified rabbit anti-EBV IgG preparations-coated wells. 2525 LPPNPTK(2) DPGATPP(1) TLTPPPL(1) PQSSPPH(1) TNRLHPP(1) TRLPPLS(1) LPLSGND(1) APPGRPT(1) AKALPHT(1) APRHNTQ(1) AAPLHNK(1) [TLAH]-P-P 11 Phage display (subtractive panning) 3 http://d.g.wanfangdata.com.cn/Periodical_zglx-e200504001.aspx Endoglucanase isozyme AgEGl, IsoA Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) The phage display library was incubated first with native polyacrylamide gel slices to remove phage clones binding to polyacrylamide gel.