메뉴 건너뛰기




Volumn 11, Issue 1, 2013, Pages 18-28

Interactome Mapping: Using Protein Microarray Technology to Reconstruct Diverse Protein Networks

Author keywords

Biomarker; Interactome; Protein microarray; Protein network; Serum profiling; Systems biology

Indexed keywords

ACYLTRANSFERASE; ARABIDOPSIS PROTEIN; AUTOANTIGEN; CELL EXTRACT; CELL PROTEIN; GLYCAN; LATENCY ASSOCIATED NUCLEAR ANTIGEN; LECTIN; MITOGEN ACTIVATED PROTEIN KINASE; UBIQUITIN PROTEIN LIGASE E3;

EID: 84875381367     PISSN: 16720229     EISSN: 22103244     Source Type: Journal    
DOI: 10.1016/j.gpb.2012.12.005     Document Type: Review
Times cited : (26)

References (73)
  • 2
    • 0036615479 scopus 로고    scopus 로고
    • Biophysical characterization of proteins in the post-genomic era of proteomics
    • Neet K.E., Lee J.C. Biophysical characterization of proteins in the post-genomic era of proteomics. Mol Cell Proteomics 2002, 1:415-420.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 415-420
    • Neet, K.E.1    Lee, J.C.2
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 20144381803 scopus 로고    scopus 로고
    • Integration with the human genome of peptide sequences obtained by high-throughput mass spectrometry
    • Desiere F., Deutsch E.W., Nesvizhskii A.I., Mallick P., King N.L., Eng J.K., et al. Integration with the human genome of peptide sequences obtained by high-throughput mass spectrometry. Genome Biol 2005, 6:R9.
    • (2005) Genome Biol , vol.6
    • Desiere, F.1    Deutsch, E.W.2    Nesvizhskii, A.I.3    Mallick, P.4    King, N.L.5    Eng, J.K.6
  • 6
    • 10944228461 scopus 로고    scopus 로고
    • Global analysis of protein function using protein microarrays
    • Smith M.G., Jona G., Ptacek J., Devgan G., Zhu H., Zhu X., et al. Global analysis of protein function using protein microarrays. Mech Ageing Dev 2005, 126:171-175.
    • (2005) Mech Ageing Dev , vol.126 , pp. 171-175
    • Smith, M.G.1    Jona, G.2    Ptacek, J.3    Devgan, G.4    Zhu, H.5    Zhu, X.6
  • 7
    • 84866409532 scopus 로고    scopus 로고
    • Applications of functional protein microarrays in basic and clinical research
    • Zhu H., Qian J. Applications of functional protein microarrays in basic and clinical research. Adv Genet 2012, 79:123-155.
    • (2012) Adv Genet , vol.79 , pp. 123-155
    • Zhu, H.1    Qian, J.2
  • 8
    • 71049156699 scopus 로고    scopus 로고
    • Identification of novel serological biomarkers for inflammatory bowel disease using Escherichia coli proteome chip
    • Chen C.S., Sullivan S., Anderson T., Tan A.C., Alex P.J., Brant S.R., et al. Identification of novel serological biomarkers for inflammatory bowel disease using Escherichia coli proteome chip. Mol Cell Proteomics 2009, 8:1765-1776.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1765-1776
    • Chen, C.S.1    Sullivan, S.2    Anderson, T.3    Tan, A.C.4    Alex, P.J.5    Brant, S.R.6
  • 9
    • 53049096773 scopus 로고    scopus 로고
    • Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers
    • Tao S.C., Li Y., Zhou J., Qian J., Schnaar R.L., Zhang Y., et al. Lectin microarrays identify cell-specific and functionally significant cell surface glycan markers. Glycobiology 2008, 18:761-769.
    • (2008) Glycobiology , vol.18 , pp. 761-769
    • Tao, S.C.1    Li, Y.2    Zhou, J.3    Qian, J.4    Schnaar, R.L.5    Zhang, Y.6
  • 10
    • 0347335769 scopus 로고    scopus 로고
    • Protein microarrays: new tools for pharmaceutical development
    • Kumble K.D. Protein microarrays: new tools for pharmaceutical development. Anal Bioanal Chem 2003, 377:812-819.
    • (2003) Anal Bioanal Chem , vol.377 , pp. 812-819
    • Kumble, K.D.1
  • 12
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H., Bilgin M., Bangham R., Hall D., Casamayor A., Bertone P., et al. Global analysis of protein activities using proteome chips. Science 2001, 293:2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3    Hall, D.4    Casamayor, A.5    Bertone, P.6
  • 13
    • 33645225281 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome diagnostics using a coronavirus protein microarray
    • Zhu H., Hu S., Jona G., Zhu X., Kreiswirth N., Willey B.M., et al. Severe acute respiratory syndrome diagnostics using a coronavirus protein microarray. Proc Natl Acad Sci U S A 2006, 103:4011-4016.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4011-4016
    • Zhu, H.1    Hu, S.2    Jona, G.3    Zhu, X.4    Kreiswirth, N.5    Willey, B.M.6
  • 14
    • 84861302962 scopus 로고    scopus 로고
    • SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function
    • Li R., Wang L., Liao G., Guzzo C.M., Matunis M.J., Zhu H., et al. SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function. J Virol 2012, 86:5412-5421.
    • (2012) J Virol , vol.86 , pp. 5412-5421
    • Li, R.1    Wang, L.2    Liao, G.3    Guzzo, C.M.4    Matunis, M.J.5    Zhu, H.6
  • 15
    • 58149498875 scopus 로고    scopus 로고
    • MAPK target networks in Arabidopsis thaliana revealed using functional protein microarrays
    • Popescu S.C., Popescu G.V., Bachan S., Zhang Z., Gerstein M., Snyder M., et al. MAPK target networks in Arabidopsis thaliana revealed using functional protein microarrays. Genes Dev 2009, 23:80-92.
    • (2009) Genes Dev , vol.23 , pp. 80-92
    • Popescu, S.C.1    Popescu, G.V.2    Bachan, S.3    Zhang, Z.4    Gerstein, M.5    Snyder, M.6
  • 16
    • 84862321638 scopus 로고    scopus 로고
    • Rapid identification of monospecific monoclonal antibodies using a human proteome microarray
    • Jeong J.S., Jiang L., Albino E., Marrero J., Rho H.S., Hu J., et al. Rapid identification of monospecific monoclonal antibodies using a human proteome microarray. Mol Cell Proteomics 2012, 11:1-10.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1-10
    • Jeong, J.S.1    Jiang, L.2    Albino, E.3    Marrero, J.4    Rho, H.S.5    Hu, J.6
  • 17
    • 9344247454 scopus 로고    scopus 로고
    • Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips
    • Huang J., Zhu H., Haggarty S.J., Spring D.R., Hwang H., Jin F., et al. Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips. Proc Natl Acad Sci U S A 2004, 101:16594-16599.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16594-16599
    • Huang, J.1    Zhu, H.2    Haggarty, S.J.3    Spring, D.R.4    Hwang, H.5    Jin, F.6
  • 18
    • 70350340058 scopus 로고    scopus 로고
    • Profiling the human protein-DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling
    • Hu S., Xie Z., Onishi A., Yu X., Jiang L., Lin J., et al. Profiling the human protein-DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling. Cell 2009, 139:610-622.
    • (2009) Cell , vol.139 , pp. 610-622
    • Hu, S.1    Xie, Z.2    Onishi, A.3    Yu, X.4    Jiang, L.5    Lin, J.6
  • 20
    • 28444460297 scopus 로고    scopus 로고
    • Global analysis of protein phosphorylation in yeast
    • Ptacek J., Devgan G., Michaud G., Zhu H., Zhu X., Fasolo J., et al. Global analysis of protein phosphorylation in yeast. Nature 2005, 438:679-684.
    • (2005) Nature , vol.438 , pp. 679-684
    • Ptacek, J.1    Devgan, G.2    Michaud, G.3    Zhu, H.4    Zhu, X.5    Fasolo, J.6
  • 21
    • 62449196769 scopus 로고    scopus 로고
    • Large-scale detection of ubiquitination substrates using cell extracts and protein microarrays
    • Merbl Y., Kirschner M.W. Large-scale detection of ubiquitination substrates using cell extracts and protein microarrays. Proc Natl Acad Sci U S A 2009, 106:2543-2548.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2543-2548
    • Merbl, Y.1    Kirschner, M.W.2
  • 23
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • Lin Y.Y., Lu J.Y., Zhang J., Walter W., Dang W., Wan J., et al. Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 2009, 136:1073-1084.
    • (2009) Cell , vol.136 , pp. 1073-1084
    • Lin, Y.Y.1    Lu, J.Y.2    Zhang, J.3    Walter, W.4    Dang, W.5    Wan, J.6
  • 25
    • 73649129599 scopus 로고    scopus 로고
    • Novel autoimmune hepatitis-specific autoantigens identified using protein microarray technology
    • Song Q., Liu G., Hu S., Zhang Y., Tao Y., Han Y., et al. Novel autoimmune hepatitis-specific autoantigens identified using protein microarray technology. J Proteome Res 2010, 9:30-39.
    • (2010) J Proteome Res , vol.9 , pp. 30-39
    • Song, Q.1    Liu, G.2    Hu, S.3    Zhang, Y.4    Tao, Y.5    Han, Y.6
  • 27
    • 0034502592 scopus 로고    scopus 로고
    • Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6
    • Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K. Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6. Plant J 2000, 24:655-665.
    • (2000) Plant J , vol.24 , pp. 655-665
    • Ichimura, K.1    Mizoguchi, T.2    Yoshida, R.3    Yuasa, T.4    Shinozaki, K.5
  • 30
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S., Utley R.T., Savard J., Clarke A., Grant P., Brandl C.J., et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J 1999, 18:5108-5119.
    • (1999) EMBO J , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5    Brandl, C.J.6
  • 31
    • 80052939858 scopus 로고    scopus 로고
    • Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction
    • Lu J.Y., Lin Y.Y., Sheu J.C., Wu J.T., Lee F.J., Chen Y., et al. Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction. Cell 2011, 146:969-979.
    • (2011) Cell , vol.146 , pp. 969-979
    • Lu, J.Y.1    Lin, Y.Y.2    Sheu, J.C.3    Wu, J.T.4    Lee, F.J.5    Chen, Y.6
  • 32
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 33
    • 84867186480 scopus 로고    scopus 로고
    • Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways
    • Chen Y., Zhao W., Yang J.S., Cheng Z., Luo H., Lu Z., et al. Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Mol Cell Proteomics 2012, 11:1048-1062.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1048-1062
    • Chen, Y.1    Zhao, W.2    Yang, J.S.3    Cheng, Z.4    Luo, H.5    Lu, Z.6
  • 34
    • 84855449701 scopus 로고    scopus 로고
    • Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1
    • Zhang T., Wang S., Lin Y., Xu W., Ye D., Xiong Y., et al. Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1. Cell Metab 2012, 15:75-87.
    • (2012) Cell Metab , vol.15 , pp. 75-87
    • Zhang, T.1    Wang, S.2    Lin, Y.3    Xu, W.4    Ye, D.5    Xiong, Y.6
  • 35
    • 80054896036 scopus 로고    scopus 로고
    • Conserved herpesvirus kinases target the DNA damage response pathway and TIP60 histone acetyltransferase to promote virus replication
    • Li R., Zhu J., Xie Z., Liao G., Liu J., Chen M.R., et al. Conserved herpesvirus kinases target the DNA damage response pathway and TIP60 histone acetyltransferase to promote virus replication. Cell Host Microbe 2011, 10:390-400.
    • (2011) Cell Host Microbe , vol.10 , pp. 390-400
    • Li, R.1    Zhu, J.2    Xie, Z.3    Liao, G.4    Liu, J.5    Chen, M.R.6
  • 36
    • 84861321790 scopus 로고    scopus 로고
    • A protein array screen for Kaposi's sarcoma-associated herpesvirus LANA interactors links LANA to TIP60, PP2A activity and telomere shortening
    • Shamay M., Liu J., Li R., Liao G., Shen L., Greenway M., et al. A protein array screen for Kaposi's sarcoma-associated herpesvirus LANA interactors links LANA to TIP60, PP2A activity and telomere shortening. J Virol 2012, 86:5179-5191.
    • (2012) J Virol , vol.86 , pp. 5179-5191
    • Shamay, M.1    Liu, J.2    Li, R.3    Liao, G.4    Shen, L.5    Greenway, M.6
  • 37
    • 84929281641 scopus 로고    scopus 로고
    • Cambridge University Press, Cambridge, A. Arvin, G. Campadelli-Fiume, E. Mocarski, P.S. Moore, B. Roizman, R. Whitley (Eds.)
    • Human herpesviruses: biology, therapy and immunoprophylaxis 2007, Cambridge University Press, Cambridge. A. Arvin, G. Campadelli-Fiume, E. Mocarski, P.S. Moore, B. Roizman, R. Whitley (Eds.).
    • (2007) Human herpesviruses: biology, therapy and immunoprophylaxis
  • 38
    • 38149065307 scopus 로고    scopus 로고
    • Conserved herpesvirus protein kinases
    • Gershburg E., Pagano J.S. Conserved herpesvirus protein kinases. Biochim Biophys Acta 2008, 1784:203-212.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 203-212
    • Gershburg, E.1    Pagano, J.S.2
  • 39
    • 33845366594 scopus 로고    scopus 로고
    • Analysis of the structure-activity relationship of four herpesviral UL97 subfamily protein kinases reveals partial but not full functional conservation
    • Romaker D., Schregel V., Maurer K., Auerochs S., Marzi A., Sticht H., et al. Analysis of the structure-activity relationship of four herpesviral UL97 subfamily protein kinases reveals partial but not full functional conservation. J Med Chem 2006, 49:7044-7053.
    • (2006) J Med Chem , vol.49 , pp. 7044-7053
    • Romaker, D.1    Schregel, V.2    Maurer, K.3    Auerochs, S.4    Marzi, A.5    Sticht, H.6
  • 40
    • 77950850768 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral production
    • Meng Q., Hagemeier S.R., Fingeroth J.D., Gershburg E., Pagano J.S., Kenney S.C. The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral production. J Virol 2010, 84:4534-4542.
    • (2010) J Virol , vol.84 , pp. 4534-4542
    • Meng, Q.1    Hagemeier, S.R.2    Fingeroth, J.D.3    Gershburg, E.4    Pagano, J.S.5    Kenney, S.C.6
  • 41
    • 34248339596 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus
    • Gershburg E., Raffa S., Torrisi M.R., Pagano J.S. Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J Virol 2007, 81:5407-5412.
    • (2007) J Virol , vol.81 , pp. 5407-5412
    • Gershburg, E.1    Raffa, S.2    Torrisi, M.R.3    Pagano, J.S.4
  • 42
    • 0036143222 scopus 로고    scopus 로고
    • Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the l-riboside benzimidazole 1263W94
    • Gershburg E., Pagano J.S. Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the l-riboside benzimidazole 1263W94. J Virol 2002, 76:998-1003.
    • (2002) J Virol , vol.76 , pp. 998-1003
    • Gershburg, E.1    Pagano, J.S.2
  • 43
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau J.R., Lima C.D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat Rev Mol Cell Biol 2010, 11:861-871.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 44
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson E.S. Protein modification by SUMO. Annu Rev Biochem 2004, 73:355-382.
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 45
    • 84865293571 scopus 로고    scopus 로고
    • Mechanisms of Kaposi's sarcoma-associated herpesvirus latency and reactivation
    • Ye F., Lei X., Gao S.J. Mechanisms of Kaposi's sarcoma-associated herpesvirus latency and reactivation. Adv Virol 2011, 2011:193860.
    • (2011) Adv Virol , vol.2011 , pp. 193860
    • Ye, F.1    Lei, X.2    Gao, S.J.3
  • 46
    • 0037321704 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus permits replication of terminal repeat-containing plasmids
    • Grundhoff A., Ganem D. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus permits replication of terminal repeat-containing plasmids. J Virol 2003, 77:2779-2783.
    • (2003) J Virol , vol.77 , pp. 2779-2783
    • Grundhoff, A.1    Ganem, D.2
  • 47
    • 0036827642 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells
    • Hu J., Garber A.C., Renne R. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells. J Virol 2002, 76:11677-11687.
    • (2002) J Virol , vol.76 , pp. 11677-11687
    • Hu, J.1    Garber, A.C.2    Renne, R.3
  • 48
    • 33644651607 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi sarcoma-associated herpesvirus induces B cell hyperplasia and lymphoma
    • Fakhari F.D., Jeong J.H., Kanan Y., Dittmer D.P. The latency-associated nuclear antigen of Kaposi sarcoma-associated herpesvirus induces B cell hyperplasia and lymphoma. J Clin Invest 2006, 116:735-742.
    • (2006) J Clin Invest , vol.116 , pp. 735-742
    • Fakhari, F.D.1    Jeong, J.H.2    Kanan, Y.3    Dittmer, D.P.4
  • 49
    • 0346336776 scopus 로고    scopus 로고
    • Transcriptional coactivation of c-Jun by the KSHV-encoded LANA
    • An J., Sun Y., Rettig M.B. Transcriptional coactivation of c-Jun by the KSHV-encoded LANA. Blood 2004, 103:222-228.
    • (2004) Blood , vol.103 , pp. 222-228
    • An, J.1    Sun, Y.2    Rettig, M.B.3
  • 50
    • 33746787632 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus latent protein LANA interacts with HIF-1 alpha to upregulate RTA expression during hypoxia: latency control under low oxygen conditions
    • Cai Q., Lan K., Verma S.C., Si H., Lin D., Robertson E.S. Kaposi's sarcoma-associated herpesvirus latent protein LANA interacts with HIF-1 alpha to upregulate RTA expression during hypoxia: latency control under low oxygen conditions. J Virol 2006, 80:7965-7975.
    • (2006) J Virol , vol.80 , pp. 7965-7975
    • Cai, Q.1    Lan, K.2    Verma, S.C.3    Si, H.4    Lin, D.5    Robertson, E.S.6
  • 51
    • 77953028751 scopus 로고    scopus 로고
    • Human I-mfa domain proteins specifically interact with KSHV LANA and affect its regulation of Wnt signaling-dependent transcription
    • Kusano S., Eizuru Y. Human I-mfa domain proteins specifically interact with KSHV LANA and affect its regulation of Wnt signaling-dependent transcription. Biochem Biophys Res Commun 2010, 396:608-613.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 608-613
    • Kusano, S.1    Eizuru, Y.2
  • 52
    • 0036828167 scopus 로고    scopus 로고
    • Protein interactions targeting the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus to cell chromosomes
    • Krithivas A., Fujimuro M., Weidner M., Young D.B., Hayward S.D. Protein interactions targeting the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus to cell chromosomes. J Virol 2002, 76:11596-11604.
    • (2002) J Virol , vol.76 , pp. 11596-11604
    • Krithivas, A.1    Fujimuro, M.2    Weidner, M.3    Young, D.B.4    Hayward, S.D.5
  • 54
    • 80052472658 scopus 로고    scopus 로고
    • Ribosomal protein S6 interacts with the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus
    • Chen W., Dittmer D.P. Ribosomal protein S6 interacts with the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus. J Virol 2011, 85:9495-9505.
    • (2011) J Virol , vol.85 , pp. 9495-9505
    • Chen, W.1    Dittmer, D.P.2
  • 55
    • 84871458375 scopus 로고    scopus 로고
    • Functional protein microarray as molecular decathlete: a versatile player in clinical proteomics
    • Zhu H., Cox E., Qian J. Functional protein microarray as molecular decathlete: a versatile player in clinical proteomics. Proteomics Clin Appl 2012, 6:548-562.
    • (2012) Proteomics Clin Appl , vol.6 , pp. 548-562
    • Zhu, H.1    Cox, E.2    Qian, J.3
  • 56
    • 28544440424 scopus 로고    scopus 로고
    • Biomarker discovery using protein microarray technology platforms: antibody-antigen complex profiling
    • Mattoon D., Michaud G., Merkel J., Schweitzer B. Biomarker discovery using protein microarray technology platforms: antibody-antigen complex profiling. Expert Rev Proteomics 2005, 2:879-889.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 879-889
    • Mattoon, D.1    Michaud, G.2    Merkel, J.3    Schweitzer, B.4
  • 57
    • 33644528470 scopus 로고    scopus 로고
    • Autoimmune hepatitis, from mechanisms to therapy
    • Manns M.P., Vogel A. Autoimmune hepatitis, from mechanisms to therapy. Hepatology 2006, 43:S132-S144.
    • (2006) Hepatology , vol.43
    • Manns, M.P.1    Vogel, A.2
  • 58
    • 34250335677 scopus 로고    scopus 로고
    • The molecular biology of SARS coronavirus
    • Satija N., Lal S.K. The molecular biology of SARS coronavirus. Ann N Y Acad Sci 2007, 1102:26-38.
    • (2007) Ann N Y Acad Sci , vol.1102 , pp. 26-38
    • Satija, N.1    Lal, S.K.2
  • 59
    • 34249977081 scopus 로고    scopus 로고
    • Pathophysiology of inflammatory bowel disease: an overview
    • Thoreson R., Cullen J.J. Pathophysiology of inflammatory bowel disease: an overview. Surg Clin North Am 2007, 87:575-585.
    • (2007) Surg Clin North Am , vol.87 , pp. 575-585
    • Thoreson, R.1    Cullen, J.J.2
  • 60
    • 31844441031 scopus 로고    scopus 로고
    • Serologic markers in inflammatory bowel disease
    • Bossuyt X. Serologic markers in inflammatory bowel disease. Clin Chem 2006, 52:171-181.
    • (2006) Clin Chem , vol.52 , pp. 171-181
    • Bossuyt, X.1
  • 61
    • 0022262016 scopus 로고
    • Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives
    • Hakomori S. Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives. Cancer Res 1985, 45:2405-2414.
    • (1985) Cancer Res , vol.45 , pp. 2405-2414
    • Hakomori, S.1
  • 62
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: new wine in an old bottle
    • Hakomori S. Glycosylation defining cancer malignancy: new wine in an old bottle. Proc Natl Acad Sci U S A 2002, 99:10231-10233.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 64
    • 0035380645 scopus 로고    scopus 로고
    • Proteome and glycosylation mapping identifies post-translational modifications associated with aggressive breast cancer
    • Dwek M.V., Ross H.A., Leathem A.J. Proteome and glycosylation mapping identifies post-translational modifications associated with aggressive breast cancer. Proteomics 2001, 1:756-762.
    • (2001) Proteomics , vol.1 , pp. 756-762
    • Dwek, M.V.1    Ross, H.A.2    Leathem, A.J.3
  • 65
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • Kung L.A., Tao S.C., Qian J., Smith M.G., Snyder M., Zhu H. Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes. Mol Syst Biol 2009, 5:308.
    • (2009) Mol Syst Biol , vol.5 , pp. 308
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5    Zhu, H.6
  • 66
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: glycoproteomics and glycan profiling
    • Hirabayashi J. Lectin-based structural glycomics: glycoproteomics and glycan profiling. Glycoconj J 2004, 21:35-40.
    • (2004) Glycoconj J , vol.21 , pp. 35-40
    • Hirabayashi, J.1
  • 67
    • 33646380883 scopus 로고    scopus 로고
    • Application of lectin microarray to crude samples: differential glycan profiling of LEC mutants
    • Ebe Y., Kuno A., Uchiyama N., Koseki-Kuno S., Yamada M., Sato T., et al. Application of lectin microarray to crude samples: differential glycan profiling of LEC mutants. J Biochem 2006, 139:323-327.
    • (2006) J Biochem , vol.139 , pp. 323-327
    • Ebe, Y.1    Kuno, A.2    Uchiyama, N.3    Koseki-Kuno, S.4    Yamada, M.5    Sato, T.6
  • 68
    • 28544452519 scopus 로고    scopus 로고
    • Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling
    • Kuno A., Uchiyama N., Koseki-Kuno S., Ebe Y., Takashima S., Yamada M., et al. Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling. Nat Methods 2005, 2:851-856.
    • (2005) Nat Methods , vol.2 , pp. 851-856
    • Kuno, A.1    Uchiyama, N.2    Koseki-Kuno, S.3    Ebe, Y.4    Takashima, S.5    Yamada, M.6
  • 69
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 2011, 146:1016-1028.
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1    Luo, H.2    Lee, S.3    Jin, F.4    Yang, J.S.5    Montellier, E.6
  • 70
    • 0141789934 scopus 로고    scopus 로고
    • Optical real-time monitoring of the laser molecular-beam epitaxial growth of perovskite oxide thin films by an oblique-incidence reflectance-difference technique
    • Chen F., Lv H., Chen Z., Zhao T., Yang G. Optical real-time monitoring of the laser molecular-beam epitaxial growth of perovskite oxide thin films by an oblique-incidence reflectance-difference technique. J Opt Soc Am B 2000, 18:1031-1035.
    • (2000) J Opt Soc Am B , vol.18 , pp. 1031-1035
    • Chen, F.1    Lv, H.2    Chen, Z.3    Zhao, T.4    Yang, G.5
  • 71
    • 1642619447 scopus 로고    scopus 로고
    • Label-free detection of microarrays of biomolecules by oblique-incidence reflectivity difference microscopy
    • Landry J.P., Zhu X.D., Gregg J.P. Label-free detection of microarrays of biomolecules by oblique-incidence reflectivity difference microscopy. Opt Lett 2004, 29:581-583.
    • (2004) Opt Lett , vol.29 , pp. 581-583
    • Landry, J.P.1    Zhu, X.D.2    Gregg, J.P.3
  • 72
    • 78349276459 scopus 로고    scopus 로고
    • Detection of the specific binding on protein microarrays by oblique-incidence reflectivity difference method
    • Lu H., Wen J., Wang X., Yuan K., Li W., Lv H., et al. Detection of the specific binding on protein microarrays by oblique-incidence reflectivity difference method. J Opt 2010, 12:1-5.
    • (2010) J Opt , vol.12 , pp. 1-5
    • Lu, H.1    Wen, J.2    Wang, X.3    Yuan, K.4    Li, W.5    Lv, H.6
  • 73
    • 78649364162 scopus 로고    scopus 로고
    • Label-free and high-throughput detection of protein microarrays by oblique-incidence reflectivity difference method
    • Wang X., Lu H., Wen J., Yuan K., Lv H., Jin K., et al. Label-free and high-throughput detection of protein microarrays by oblique-incidence reflectivity difference method. Chinese Phys Lett 2010, 27:1-4.
    • (2010) Chinese Phys Lett , vol.27 , pp. 1-4
    • Wang, X.1    Lu, H.2    Wen, J.3    Yuan, K.4    Lv, H.5    Jin, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.