메뉴 건너뛰기




Volumn 404, Issue 4, 2012, Pages 1057-1067

Advancing formaldehyde cross-linking towards quantitative proteomic applications

Author keywords

FFPE; Formaldehyde cross linking; Mass spectrometry; Protein protein interactions

Indexed keywords

FFPE; FORMALDEHYDE CROSS-LINKING; LIVING CELL; PROTEIN-PROTEIN INTERACTIONS;

EID: 84865577612     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-012-6065-9     Document Type: Review
Times cited : (53)

References (77)
  • 1
    • 0022112084 scopus 로고
    • Formaldehyde fixation
    • 10.1177/33.8.3894502 1:STN:280:DyaL2M3mt1Oiug%3D%3D
    • CH Fox FB Johnson J Whiting PP Roller 1985 Formaldehyde fixation J Histochem Cytochem 33 8 845 853 10.1177/33.8.3894502 1:STN:280: DyaL2M3mt1Oiug%3D%3D
    • (1985) J Histochem Cytochem , vol.33 , Issue.8 , pp. 845-853
    • Fox, C.H.1    Johnson, F.B.2    Whiting, J.3    Roller, P.P.4
  • 2
    • 79953072078 scopus 로고    scopus 로고
    • The use of formalin fixed wax embedded tissue for proteomic analysis
    • 10.1136/jcp.2010.086835 1:CAS:528:DC%2BC3MXlvFGqt7Y%3D
    • LD Ralton GI Murray 2011 The use of formalin fixed wax embedded tissue for proteomic analysis J Clin Pathol 64 4 297 302 10.1136/jcp.2010.086835 1:CAS:528:DC%2BC3MXlvFGqt7Y%3D
    • (2011) J Clin Pathol , vol.64 , Issue.4 , pp. 297-302
    • Ralton, L.D.1    Murray, G.I.2
  • 3
    • 0023948705 scopus 로고
    • Mapping protein-DNA interactions in vivo with formaldehyde: Evidence that histone H4 is retained on a highly transcribed gene
    • 10.1016/S0092-8674(88)90469-2 1:CAS:528:DyaL1cXkvVOgsrk%3D
    • MJ Solomon PL Larsen A Varshavsky 1988 Mapping protein-DNA interactions in vivo with formaldehyde: evidence that histone H4 is retained on a highly transcribed gene Cell 53 6 937 947 10.1016/S0092-8674(88)90469-2 1:CAS:528:DyaL1cXkvVOgsrk%3D
    • (1988) Cell , vol.53 , Issue.6 , pp. 937-947
    • Solomon, M.J.1    Larsen, P.L.2    Varshavsky, A.3
  • 4
    • 79952113220 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in biomedical research: Emerging technologies and future strategies
    • 10.1017/S1462399410001614
    • GM Walsh JC Rogalski C Klockenbusch J Kast 2010 Mass spectrometry-based proteomics in biomedical research: emerging technologies and future strategies Expert Rev Mol Med 12 e30 10.1017/S1462399410001614
    • (2010) Expert Rev Mol Med , vol.12 , pp. 30
    • Walsh, G.M.1    Rogalski, J.C.2    Klockenbusch, C.3    Kast, J.4
  • 5
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • 10.1007/s00216-007-1486-6 1:CAS:528:DC%2BD2sXhtVyntbfF
    • M Bantscheff M Schirle G Sweetman J Rick B Kuster 2007 Quantitative mass spectrometry in proteomics: a critical review Anal Bioanal Chem 389 4 1017 1031 10.1007/s00216-007-1486-6 1:CAS:528:DC%2BD2sXhtVyntbfF
    • (2007) Anal Bioanal Chem , vol.389 , Issue.4 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3    Rick, J.4    Kuster, B.5
  • 6
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • 10.1074/mcp.M200025-MCP200 1:CAS:528:DC%2BD38XlslWhsrk%3D
    • SE Ong B Blagoev I Kratchmarova DB Kristensen H Steen A Pandey M Mann 2002 Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol Cell Proteomics 1 5 376 386 10.1074/mcp.M200025-MCP200 1:CAS:528:DC%2BD38XlslWhsrk%3D
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 8
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • 10.1021/ac0262560 1:CAS:528:DC%2BD3sXhslSmtbw%3D
    • A Thompson J Schafer K Kuhn S Kienle J Schwarz G Schmidt T Neumann R Johnstone AK Mohammed C Hamon 2003 Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS Anal Chem 75 8 1895 1904 10.1021/ac0262560 1:CAS:528:DC%2BD3sXhslSmtbw%3D
    • (2003) Anal Chem , vol.75 , Issue.8 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3    Kienle, S.4    Schwarz, J.5    Schmidt, G.6    Neumann, T.7    Johnstone, R.8    Mohammed, A.K.9    Hamon, C.10
  • 10
    • 46849099222 scopus 로고    scopus 로고
    • Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions
    • 10.1002/jms.1415 1:CAS:528:DC%2BD1cXnvFCmu7g%3D
    • BW Sutherland J Toews J Kast 2008 Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions J Mass Spectrom 43 6 699 715 10.1002/jms.1415 1:CAS:528:DC%2BD1cXnvFCmu7g%3D
    • (2008) J Mass Spectrom , vol.43 , Issue.6 , pp. 699-715
    • Sutherland, B.W.1    Toews, J.2    Kast, J.3
  • 13
    • 44149119998 scopus 로고    scopus 로고
    • Mass spectrometric identification of formaldehyde-induced peptide modifications under in vivo protein cross-linking conditions
    • 10.1016/j.aca.2008.04.049 1:CAS:528:DC%2BD1cXms1yjur0%3D
    • J Toews JC Rogalski TJ Clark J Kast 2008 Mass spectrometric identification of formaldehyde-induced peptide modifications under in vivo protein cross-linking conditions Anal Chim Acta 618 2 168 183 10.1016/j.aca.2008.04.049 1:CAS:528:DC%2BD1cXms1yjur0%3D
    • (2008) Anal Chim Acta , vol.618 , Issue.2 , pp. 168-183
    • Toews, J.1    Rogalski, J.C.2    Clark, T.J.3    Kast, J.4
  • 14
    • 77956173802 scopus 로고    scopus 로고
    • Accessibility governs the relative reactivity of basic residues in formaldehyde-induced protein modifications
    • 10.1016/j.aca.2010.07.040 1:CAS:528:DC%2BC3cXhtV2hu77J
    • J Toews JC Rogalski J Kast 2010 Accessibility governs the relative reactivity of basic residues in formaldehyde-induced protein modifications Anal Chim Acta 676 1-2 60 67 10.1016/j.aca.2010.07.040 1:CAS:528:DC%2BC3cXhtV2hu77J
    • (2010) Anal Chim Acta , vol.676 , Issue.12 , pp. 60-67
    • Toews, J.1    Rogalski, J.C.2    Kast, J.3
  • 15
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • 10.1038/nprot.2009.21 1:CAS:528:DC%2BD1MXjvFyjs7g%3D
    • PJ Boersema R Raijmakers S Lemeer S Mohammed AJ Heck 2009 Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics Nat Protoc 4 4 484 494 10.1038/nprot.2009.21 1:CAS:528:DC%2BD1MXjvFyjs7g%3D
    • (2009) Nat Protoc , vol.4 , Issue.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 16
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • 10.1021/pr100234w 1:CAS:528:DC%2BC3cXmsFSnsrk%3D
    • P Ostasiewicz DF Zielinska M Mann JR Wisniewski 2010 Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry J Proteome Res 9 7 3688 3700 10.1021/pr100234w 1:CAS:528: DC%2BC3cXmsFSnsrk%3D
    • (2010) J Proteome Res , vol.9 , Issue.7 , pp. 3688-3700
    • Ostasiewicz, P.1    Zielinska, D.F.2    Mann, M.3    Wisniewski, J.R.4
  • 19
    • 12344310514 scopus 로고    scopus 로고
    • Reversing the effects of formalin fixation with citraconic anhydride and heat: A universal antigen retrieval method
    • 1:CAS:528:DC%2BD2MXot12hug%3D%3D
    • S Namimatsu M Ghazizadeh Y Sugisaki 2005 Reversing the effects of formalin fixation with citraconic anhydride and heat: a universal antigen retrieval method J Histochem Cytochem 53 1 3 11 1:CAS:528:DC%2BD2MXot12hug%3D%3D
    • (2005) J Histochem Cytochem , vol.53 , Issue.1 , pp. 3-11
    • Namimatsu, S.1    Ghazizadeh, M.2    Sugisaki, Y.3
  • 20
    • 1242293694 scopus 로고    scopus 로고
    • Integrating histology and imaging mass spectrometry
    • 10.1021/ac0351264 1:CAS:528:DC%2BD2cXhtFCksL8%3D
    • P Chaurand SA Schwartz D Billheimer BJ Xu A Crecelius RM Caprioli 2004 Integrating histology and imaging mass spectrometry Anal Chem 76 4 1145 1155 10.1021/ac0351264 1:CAS:528:DC%2BD2cXhtFCksL8%3D
    • (2004) Anal Chem , vol.76 , Issue.4 , pp. 1145-1155
    • Chaurand, P.1    Schwartz, S.A.2    Billheimer, D.3    Xu, B.J.4    Crecelius, A.5    Caprioli, R.M.6
  • 21
    • 0030884713 scopus 로고    scopus 로고
    • Emerging tandem-mass-spectrometry techniques for the rapid identification of proteins
    • 10.1016/S0167-7799(97)01110-4 1:CAS:528:DyaK2sXmslCksLw%3D
    • AR Dongre JK Eng JR Yates 3rd 1997 Emerging tandem-mass-spectrometry techniques for the rapid identification of proteins Trends Biotechnol 15 10 418 425 10.1016/S0167-7799(97)01110-4 1:CAS:528:DyaK2sXmslCksLw%3D
    • (1997) Trends Biotechnol , vol.15 , Issue.10 , pp. 418-425
    • Dongre, A.R.1    Eng, J.K.2    Yates III, J.R.3
  • 22
    • 77956108790 scopus 로고    scopus 로고
    • MTRAQ-based quantification of potential endometrial carcinoma biomarkers from archived formalin-fixed paraffin-embedded tissues
    • 10.1002/pmic.201000082 1:CAS:528:DC%2BC3cXhtV2gsb3E
    • LV DeSouza O Krakovska MM Darfler DB Krizman AD Romaschin TJ Colgan KW Siu 2010 mTRAQ-based quantification of potential endometrial carcinoma biomarkers from archived formalin-fixed paraffin-embedded tissues Proteomics 10 17 3108 3116 10.1002/pmic.201000082 1:CAS:528:DC%2BC3cXhtV2gsb3E
    • (2010) Proteomics , vol.10 , Issue.17 , pp. 3108-3116
    • Desouza, L.V.1    Krakovska, O.2    Darfler, M.M.3    Krizman, D.B.4    Romaschin, A.D.5    Colgan, T.J.6    Siu, K.W.7
  • 23
    • 84856407461 scopus 로고    scopus 로고
    • Peptide extraction from formalin-fixed paraffin-embedded tissue
    • Chapter 23:Unit23 25
    • Heaton KJ, Master SR (2011) Peptide extraction from formalin-fixed paraffin-embedded tissue. Curr Protoc Protein Sci Chapter 23:Unit23 25
    • (2011) Curr Protoc Protein Sci
    • Heaton, K.J.1    Master, S.R.2
  • 24
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • 10.1038/nmeth.1322 1:CAS:528:DC%2BD1MXks12ksb0%3D
    • JR Wisniewski A Zougman N Nagaraj M Mann 2009 Universal sample preparation method for proteome analysis Nat Methods 6 5 359 362 10.1038/nmeth.1322 1:CAS:528:DC%2BD1MXks12ksb0%3D
    • (2009) Nat Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 25
    • 33846629961 scopus 로고    scopus 로고
    • Quantitative protein analysis from formalin-fixed tissues: Implications for translational clinical research and nanoscale molecular diagnosis
    • 10.1002/path.2107 1:CAS:528:DC%2BD2sXisFyksb4%3D
    • KF Becker C Schott S Hipp V Metzger P Porschewski R Beck J Nahrig I Becker H Hofler 2007 Quantitative protein analysis from formalin-fixed tissues: implications for translational clinical research and nanoscale molecular diagnosis J Pathol 211 3 370 378 10.1002/path.2107 1:CAS:528: DC%2BD2sXisFyksb4%3D
    • (2007) J Pathol , vol.211 , Issue.3 , pp. 370-378
    • Becker, K.F.1    Schott, C.2    Hipp, S.3    Metzger, V.4    Porschewski, P.5    Beck, R.6    Nahrig, J.7    Becker, I.8    Hofler, H.9
  • 26
    • 79955448303 scopus 로고    scopus 로고
    • Initial development and validation of a novel extraction method for quantitative mining of the formalin-fixed, paraffin-embedded tissue proteome for biomarker investigations
    • 10.1021/pr100812d 1:CAS:528:DC%2BC3cXhs1SrsbzM
    • NJ Nirmalan C Hughes J Peng T McKenna J Langridge DA Cairns P Harnden PJ Selby RE Banks 2011 Initial development and validation of a novel extraction method for quantitative mining of the formalin-fixed, paraffin-embedded tissue proteome for biomarker investigations J Proteome Res 10 2 896 906 10.1021/pr100812d 1:CAS:528:DC%2BC3cXhs1SrsbzM
    • (2011) J Proteome Res , vol.10 , Issue.2 , pp. 896-906
    • Nirmalan, N.J.1    Hughes, C.2    Peng, J.3    McKenna, T.4    Langridge, J.5    Cairns, D.A.6    Harnden, P.7    Selby, P.J.8    Banks, R.E.9
  • 28
    • 75349102311 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of formalin fixed paraffin embedded oral HPV lesions from HIV patients
    • 10.2174/1875039700801010040 1:CAS:528:DC%2BD1cXlslegu7g%3D
    • MR Jain T Liu J Hu M Darfler V Fitzhugh J Rinaggio H Li 2008 Quantitative proteomic analysis of formalin fixed paraffin embedded oral HPV lesions from HIV patients Open Proteomics J 1 40 45 10.2174/1875039700801010040 1:CAS:528:DC%2BD1cXlslegu7g%3D
    • (2008) Open Proteomics J , vol.1 , pp. 40-45
    • Jain, M.R.1    Liu, T.2    Hu, J.3    Darfler, M.4    Fitzhugh, V.5    Rinaggio, J.6    Li, H.7
  • 29
    • 77952764025 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of formalin-fixed and paraffin-embedded nasopharyngeal carcinoma using iTRAQ labeling, two-dimensional liquid chromatography, and tandem mass spectrometry
    • 10.1369/jhc.2010.955526 1:CAS:528:DC%2BC3cXms1Sjs70%3D
    • Z Xiao G Li Y Chen M Li F Peng C Li F Li Y Yu Y Ouyang Z Chen 2010 Quantitative proteomic analysis of formalin-fixed and paraffin-embedded nasopharyngeal carcinoma using iTRAQ labeling, two-dimensional liquid chromatography, and tandem mass spectrometry J Histochem Cytochem 58 6 517 527 10.1369/jhc.2010.955526 1:CAS:528:DC%2BC3cXms1Sjs70%3D
    • (2010) J Histochem Cytochem , vol.58 , Issue.6 , pp. 517-527
    • Xiao, Z.1    Li, G.2    Chen, Y.3    Li, M.4    Peng, F.5    Li, C.6    Li, F.7    Yu, Y.8    Ouyang, Y.9    Chen, Z.10
  • 30
    • 79952392534 scopus 로고    scopus 로고
    • Differential proteomic analysis of late-stage and recurrent breast cancer from formalin-fixed paraffin-embedded tissues
    • 10.1021/pr101073s 1:CAS:528:DC%2BC3MXnvVSlsw%3D%3D
    • NW Bateman M Sun R Bhargava BL Hood MM Darfler AJ Kovatich JA Hooke DB Krizman TP Conrads 2011 Differential proteomic analysis of late-stage and recurrent breast cancer from formalin-fixed paraffin-embedded tissues J Proteome Res 10 3 1323 1332 10.1021/pr101073s 1:CAS:528:DC%2BC3MXnvVSlsw%3D%3D
    • (2011) J Proteome Res , vol.10 , Issue.3 , pp. 1323-1332
    • Bateman, N.W.1    Sun, M.2    Bhargava, R.3    Hood, B.L.4    Darfler, M.M.5    Kovatich, A.J.6    Hooke, J.A.7    Krizman, D.B.8    Conrads, T.P.9
  • 31
    • 77954834510 scopus 로고    scopus 로고
    • The current state of chromatin immunoprecipitation
    • 10.1007/s12033-009-9239-8 1:CAS:528:DC%2BC3cXktVWqtLc%3D
    • P Collas 2010 The current state of chromatin immunoprecipitation Mol Biotechnol 45 1 87 100 10.1007/s12033-009-9239-8 1:CAS:528:DC%2BC3cXktVWqtLc%3D
    • (2010) Mol Biotechnol , vol.45 , Issue.1 , pp. 87-100
    • Collas, P.1
  • 32
    • 17644392168 scopus 로고    scopus 로고
    • Multiple and simultaneous detection of specific bacteria in enriched bacterial communities using a DNA microarray chip with randomly generated genomic DNA probes
    • 10.1021/ac048703c 1:CAS:528:DC%2BD2MXit1ahurg%3D
    • BC Kim JH Park MB Gu 2005 Multiple and simultaneous detection of specific bacteria in enriched bacterial communities using a DNA microarray chip with randomly generated genomic DNA probes Anal Chem 77 8 2311 2317 10.1021/ac048703c 1:CAS:528:DC%2BD2MXit1ahurg%3D
    • (2005) Anal Chem , vol.77 , Issue.8 , pp. 2311-2317
    • Kim, B.C.1    Park, J.H.2    Gu, M.B.3
  • 34
    • 50849090969 scopus 로고    scopus 로고
    • Genome-wide analysis of transcription factor binding sites based on ChIP-Seq data
    • 10.1038/nmeth.1246 1:CAS:528:DC%2BD1cXhtVGgsb3F
    • A Valouev DS Johnson A Sundquist C Medina E Anton S Batzoglou RM Myers A Sidow 2008 Genome-wide analysis of transcription factor binding sites based on ChIP-Seq data Nat Methods 5 9 829 834 10.1038/nmeth.1246 1:CAS:528: DC%2BD1cXhtVGgsb3F
    • (2008) Nat Methods , vol.5 , Issue.9 , pp. 829-834
    • Valouev, A.1    Johnson, D.S.2    Sundquist, A.3    Medina, C.4    Anton, E.5    Batzoglou, S.6    Myers, R.M.7    Sidow, A.8
  • 35
    • 34250159524 scopus 로고    scopus 로고
    • Genome-wide mapping of in vivo protein-DNA interactions
    • 10.1126/science.1141319 1:CAS:528:DC%2BD2sXmtFSjtrg%3D
    • DS Johnson A Mortazavi RM Myers B Wold 2007 Genome-wide mapping of in vivo protein-DNA interactions Science 316 5830 1497 1502 10.1126/science.1141319 1:CAS:528:DC%2BD2sXmtFSjtrg%3D
    • (2007) Science , vol.316 , Issue.5830 , pp. 1497-1502
    • Johnson, D.S.1    Mortazavi, A.2    Myers, R.M.3    Wold, B.4
  • 36
    • 34548231009 scopus 로고    scopus 로고
    • Co-immunoprecipitations revisited: An update on experimental concepts and their implementation for sensitive interactome investigations of endogenous proteins
    • 10.1007/s00216-007-1385-x 1:CAS:528:DC%2BD2sXpsFSjt7g%3D
    • K Markham Y Bai G Schmitt-Ulms 2007 Co-immunoprecipitations revisited: an update on experimental concepts and their implementation for sensitive interactome investigations of endogenous proteins Anal Bioanal Chem 389 2 461 473 10.1007/s00216-007-1385-x 1:CAS:528:DC%2BD2sXpsFSjt7g%3D
    • (2007) Anal Bioanal Chem , vol.389 , Issue.2 , pp. 461-473
    • Markham, K.1    Bai, Y.2    Schmitt-Ulms, G.3
  • 37
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • 10.1007/s00216-009-3405-5 1:CAS:528:DC%2BC3cXmt1eiug%3D%3D
    • A Sinz 2010 Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry Anal Bioanal Chem 397 8 3433 3440 10.1007/s00216-009-3405-5 1:CAS:528:DC%2BC3cXmt1eiug%3D%3D
    • (2010) Anal Bioanal Chem , vol.397 , Issue.8 , pp. 3433-3440
    • Sinz, A.1
  • 38
    • 0017075525 scopus 로고
    • Chemical probes of extended biological structures: Synthesis and properties of the cleavable protein cross-linking reagent [35S] dithiobis(succinimidyl propionate)
    • 10.1016/0022-2836(76)90011-5 1:CAS:528:DyaE28XksF2isbs%3D
    • AJ Lomant G Fairbanks 1976 Chemical probes of extended biological structures: synthesis and properties of the cleavable protein cross-linking reagent [35S]dithiobis(succinimidyl propionate) J Mol Biol 104 1 243 261 10.1016/0022-2836(76)90011-5 1:CAS:528:DyaE28XksF2isbs%3D
    • (1976) J Mol Biol , vol.104 , Issue.1 , pp. 243-261
    • Lomant, A.J.1    Fairbanks, G.2
  • 39
    • 10644254712 scopus 로고    scopus 로고
    • Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry
    • 10.1002/pmic.200400856 1:CAS:528:DC%2BD2cXhtFarsb7N
    • J Vasilescu X Guo J Kast 2004 Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry Proteomics 4 12 3845 3854 10.1002/pmic.200400856 1:CAS:528:DC%2BD2cXhtFarsb7N
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3845-3854
    • Vasilescu, J.1    Guo, X.2    Kast, J.3
  • 40
    • 77955394572 scopus 로고    scopus 로고
    • Optimization of formaldehyde cross-linking for protein interaction analysis of non-tagged integrin beta1
    • 10.1155/2010/927585
    • C Klockenbusch J Kast 2010 Optimization of formaldehyde cross-linking for protein interaction analysis of non-tagged integrin beta1 J Biomed Biotechnol 2010 927585 10.1155/2010/927585
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 927585
    • Klockenbusch, C.1    Kast, J.2
  • 42
    • 82355165051 scopus 로고    scopus 로고
    • Time-controlled transcardiac perfusion crosslinking for in vivo interactome studies
    • 10.1007/978-1-61779-364-6-16
    • AH Jeon G Schmitt-Ulms 2012 Time-controlled transcardiac perfusion crosslinking for in vivo interactome studies Methods Mol Biol 803 231 246 10.1007/978-1-61779-364-6-16
    • (2012) Methods Mol Biol , vol.803 , pp. 231-246
    • Jeon, A.H.1    Schmitt-Ulms, G.2
  • 43
    • 77953167152 scopus 로고    scopus 로고
    • Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS
    • 10.1074/mcp.M900490-MCP200 1:CAS:528:DC%2BC3cXpsFCrtL4%3D
    • T Nittis L Guittat RD LeDuc B Dao JP Duxin H Rohrs RR Townsend SA Stewart 2010 Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS Mol Cell Proteomics 9 6 1144 1156 10.1074/mcp.M900490-MCP200 1:CAS:528: DC%2BC3cXpsFCrtL4%3D
    • (2010) Mol Cell Proteomics , vol.9 , Issue.6 , pp. 1144-1156
    • Nittis, T.1    Guittat, L.2    Leduc, R.D.3    Dao, B.4    Duxin, J.P.5    Rohrs, H.6    Townsend, R.R.7    Stewart, S.A.8
  • 44
    • 26844556166 scopus 로고    scopus 로고
    • I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions
    • 10.1021/pr050225e 1:CAS:528:DC%2BD2MXovFWhsbY%3D
    • AJ Tackett JA DeGrasse MD Sekedat M Oeffinger MP Rout BT Chait 2005 I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions J Proteome Res 4 5 1752 1756 10.1021/pr050225e 1:CAS:528:DC%2BD2MXovFWhsbY%3D
    • (2005) J Proteome Res , vol.4 , Issue.5 , pp. 1752-1756
    • Tackett, A.J.1    Degrasse, J.A.2    Sekedat, M.D.3    Oeffinger, M.4    Rout, M.P.5    Chait, B.T.6
  • 45
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: Quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26S proteasome-interacting network
    • 1:CAS:528:DC%2BD28XitVagsbo%3D
    • C Guerrero C Tagwerker P Kaiser L Huang 2006 An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26S proteasome-interacting network Mol Cell Proteomics 5 2 366 378 1:CAS:528:DC%2BD28XitVagsbo%3D
    • (2006) Mol Cell Proteomics , vol.5 , Issue.2 , pp. 366-378
    • Guerrero, C.1    Tagwerker, C.2    Kaiser, P.3    Huang, L.4
  • 46
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • 1:CAS:528:DyaK1cXntlers7k%3D
    • PI Higgs PS Myers K Postle 1998 Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers J Bacteriol 180 22 6031 6038 1:CAS:528:DyaK1cXntlers7k%3D
    • (1998) J Bacteriol , vol.180 , Issue.22 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 47
    • 0027282061 scopus 로고
    • Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
    • 1:CAS:528:DyaK3sXlsFGrtbw%3D
    • JT Skare BM Ahmer CL Seachord RP Darveau K Postle 1993 Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA J Biol Chem 268 22 16302 16308 1:CAS:528:DyaK3sXlsFGrtbw%3D
    • (1993) J Biol Chem , vol.268 , Issue.22 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 48
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • 1:CAS:528:DyaK2sXjtFKhsbY%3D
    • RA Larsen D Foster-Hartnett MA McIntosh K Postle 1997 Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions J Bacteriol 179 10 3213 3221 1:CAS:528:DyaK2sXjtFKhsbY%3D
    • (1997) J Bacteriol , vol.179 , Issue.10 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 49
    • 0034099903 scopus 로고    scopus 로고
    • Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae
    • 1:CAS:528:DC%2BD3cXitVans7k%3D
    • G Layh-Schmitt A Podtelejnikov M Mann 2000 Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae Microbiology 146 Pt 3 741 747 1:CAS:528:DC%2BD3cXitVans7k%3D
    • (2000) Microbiology , vol.146 , Issue.PART 3 , pp. 741-747
    • Layh-Schmitt, G.1    Podtelejnikov, A.2    Mann, M.3
  • 51
    • 77955817279 scopus 로고    scopus 로고
    • Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing
    • 10.1096/fj.09-146357 1:CAS:528:DC%2BC3cXhtVeisbfJ
    • H Okada W Zhang C Peterhoff JC Hwang RA Nixon SH Ryu TW Kim 2010 Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing FASEB J 24 8 2783 2794 10.1096/fj.09-146357 1:CAS:528:DC%2BC3cXhtVeisbfJ
    • (2010) FASEB J , vol.24 , Issue.8 , pp. 2783-2794
    • Okada, H.1    Zhang, W.2    Peterhoff, C.3    Hwang, J.C.4    Nixon, R.A.5    Ryu, S.H.6    Kim, T.W.7
  • 52
    • 67449088488 scopus 로고    scopus 로고
    • Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins
    • 10.1074/mcp.M800193-MCP200 1:CAS:528:DC%2BD1MXmtlGqur4%3D
    • MP Bousquet-Dubouch E Baudelet F Guerin M Matondo S Uttenweiler-Joseph O Burlet-Schiltz B Monsarrat 2009 Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins Mol Cell Proteomics 8 5 1150 1164 10.1074/mcp.M800193-MCP200 1:CAS:528:DC%2BD1MXmtlGqur4%3D
    • (2009) Mol Cell Proteomics , vol.8 , Issue.5 , pp. 1150-1164
    • Bousquet-Dubouch, M.P.1    Baudelet, E.2    Guerin, F.3    Matondo, M.4    Uttenweiler-Joseph, S.5    Burlet-Schiltz, O.6    Monsarrat, B.7
  • 53
    • 82555186441 scopus 로고    scopus 로고
    • Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links
    • 10.1093/bib/bbq087 1:CAS:528:DC%2BC3MXhsFant7bL
    • SL Mayne HG Patterton 2011 Bioinformatics tools for the structural elucidation of multi-subunit protein complexes by mass spectrometric analysis of protein-protein cross-links Brief Bioinform 12 6 660 671 10.1093/bib/bbq087 1:CAS:528:DC%2BC3MXhsFant7bL
    • (2011) Brief Bioinform , vol.12 , Issue.6 , pp. 660-671
    • Mayne, S.L.1    Patterton, H.G.2
  • 54
    • 77952027769 scopus 로고    scopus 로고
    • XComb: A cross-linked peptide database approach to protein-protein interaction analysis
    • 10.1021/pr9011816 1:CAS:528:DC%2BC3cXkvVKrurk%3D
    • A Panchaud P Singh SA Shaffer DR Goodlett 2010 xComb: a cross-linked peptide database approach to protein-protein interaction analysis J Proteome Res 9 5 2508 2515 10.1021/pr9011816 1:CAS:528:DC%2BC3cXkvVKrurk%3D
    • (2010) J Proteome Res , vol.9 , Issue.5 , pp. 2508-2515
    • Panchaud, A.1    Singh, P.2    Shaffer, S.A.3    Goodlett, D.R.4
  • 55
    • 79952430498 scopus 로고    scopus 로고
    • Xlink-identifier: An automated data analysis platform for confident identifications of chemically cross-linked peptides using tandem mass spectrometry
    • 10.1021/pr100848a 1:CAS:528:DC%2BC3MXhvFGqtro%3D
    • X Du SM Chowdhury NP Manes S Wu MU Mayer JN Adkins GA Anderson RD Smith 2011 Xlink-identifier: an automated data analysis platform for confident identifications of chemically cross-linked peptides using tandem mass spectrometry J Proteome Res 10 3 923 931 10.1021/pr100848a 1:CAS:528: DC%2BC3MXhvFGqtro%3D
    • (2011) J Proteome Res , vol.10 , Issue.3 , pp. 923-931
    • Du, X.1    Chowdhury, S.M.2    Manes, N.P.3    Wu, S.4    Mayer, M.U.5    Adkins, J.N.6    Anderson, G.A.7    Smith, R.D.8
  • 56
    • 79952118292 scopus 로고    scopus 로고
    • Protein identification by spectral networks analysis
    • 10.1007/978-1-60761-977-2-11 1:CAS:528:DC%2BC3cXhs1WrsL%2FF
    • N Bandeira 2011 Protein identification by spectral networks analysis Methods Mol Biol 694 151 168 10.1007/978-1-60761-977-2-11 1:CAS:528: DC%2BC3cXhs1WrsL%2FF
    • (2011) Methods Mol Biol , vol.694 , pp. 151-168
    • Bandeira, N.1
  • 57
    • 80053020998 scopus 로고    scopus 로고
    • Isocratic method for affinity enrichment of covalently-linked peptides in cyanogen bromide cleavage of proteins
    • Shi T, Liu J, Yan C, Wang X (2011) Isocratic method for affinity enrichment of covalently-linked peptides in cyanogen bromide cleavage of proteins. Proteomics
    • (2011) Proteomics
    • Shi, T.1    Liu, J.2    Yan, C.3    Wang, X.4
  • 58
    • 84857097692 scopus 로고    scopus 로고
    • Optimizing the enrichment of cross-linked products for mass spectrometric protein analysis
    • 10.1002/rcm.6150 1:CAS:528:DC%2BC38Xit1Sktbk%3D
    • R Fritzsche CH Ihling M Gotze A Sinz 2012 Optimizing the enrichment of cross-linked products for mass spectrometric protein analysis Rapid Commun Mass Spectrom 26 6 653 658 10.1002/rcm.6150 1:CAS:528:DC%2BC38Xit1Sktbk%3D
    • (2012) Rapid Commun Mass Spectrom , vol.26 , Issue.6 , pp. 653-658
    • Fritzsche, R.1    Ihling, C.H.2    Gotze, M.3    Sinz, A.4
  • 59
    • 79961213851 scopus 로고    scopus 로고
    • Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry
    • 10.1021/pr200260n 1:CAS:528:DC%2BC3MXnvFansL0%3D
    • MA Lauber JP Reilly 2011 Structural analysis of a prokaryotic ribosome using a novel amidinating cross-linker and mass spectrometry J Proteome Res 10 8 3604 3616 10.1021/pr200260n 1:CAS:528:DC%2BC3MXnvFansL0%3D
    • (2011) J Proteome Res , vol.10 , Issue.8 , pp. 3604-3616
    • Lauber, M.A.1    Reilly, J.P.2
  • 60
    • 84857966803 scopus 로고    scopus 로고
    • Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography
    • 014126
    • A Leitner R Reischl T Walzthoeni F Herzog S Bohn F Forster R Aebersold 2012 Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography Mol Cell Proteomics 11 3 M111 014126
    • (2012) Mol Cell Proteomics , vol.11 , Issue.3 , pp. 111
    • Leitner, A.1    Reischl, R.2    Walzthoeni, T.3    Herzog, F.4    Bohn, S.5    Forster, F.6    Aebersold, R.7
  • 61
    • 36049005354 scopus 로고    scopus 로고
    • Interactome and interface protocol (2IP): A novel strategy for high sensitivity topology mapping of protein complexes
    • 10.1002/pmic.200700688 1:CAS:528:DC%2BD2sXhtlOgurrJ
    • R Weerasekera YM She KA Markham Y Bai N Opalka S Orlicky F Sicheri T Kislinger G Schmitt-Ulms 2007 Interactome and interface protocol (2IP): a novel strategy for high sensitivity topology mapping of protein complexes Proteomics 7 21 3835 3852 10.1002/pmic.200700688 1:CAS:528:DC%2BD2sXhtlOgurrJ
    • (2007) Proteomics , vol.7 , Issue.21 , pp. 3835-3852
    • Weerasekera, R.1    She, Y.M.2    Markham, K.A.3    Bai, Y.4    Opalka, N.5    Orlicky, S.6    Sicheri, F.7    Kislinger, T.8    Schmitt-Ulms, G.9
  • 62
    • 80955137946 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation and high-throughput sequencing from paraffin-embedded pathology tissue
    • 10.1038/nprot.2011.406 1:CAS:528:DC%2BC3MXhsFyltb3O
    • M Fanelli S Amatori I Barozzi S Minucci 2011 Chromatin immunoprecipitation and high-throughput sequencing from paraffin-embedded pathology tissue Nat Protoc 6 12 1905 1919 10.1038/nprot.2011.406 1:CAS:528:DC%2BC3MXhsFyltb3O
    • (2011) Nat Protoc , vol.6 , Issue.12 , pp. 1905-1919
    • Fanelli, M.1    Amatori, S.2    Barozzi, I.3    Minucci, S.4
  • 63
    • 77956314944 scopus 로고    scopus 로고
    • Citric acid antigen retrieval (CAAR) for tryptic peptide imaging directly on archived formalin-fixed paraffin-embedded tissue
    • 10.1021/pr9011766 1:CAS:528:DC%2BC3cXptlWgtL4%3D
    • JO Gustafsson MK Oehler SR McColl P Hoffmann 2010 Citric acid antigen retrieval (CAAR) for tryptic peptide imaging directly on archived formalin-fixed paraffin-embedded tissue J Proteome Res 9 9 4315 4328 10.1021/pr9011766 1:CAS:528:DC%2BC3cXptlWgtL4%3D
    • (2010) J Proteome Res , vol.9 , Issue.9 , pp. 4315-4328
    • Gustafsson, J.O.1    Oehler, M.K.2    McColl, S.R.3    Hoffmann, P.4
  • 64
    • 80054825298 scopus 로고    scopus 로고
    • Proteomic analysis of formalin-fixed paraffin-embedded tissue by MALDI imaging mass spectrometry
    • 10.1038/nprot.2011.388 1:CAS:528:DC%2BC3MXhtl2qu7bI
    • R Casadonte RM Caprioli 2011 Proteomic analysis of formalin-fixed paraffin-embedded tissue by MALDI imaging mass spectrometry Nat Protoc 6 11 1695 1709 10.1038/nprot.2011.388 1:CAS:528:DC%2BC3MXhtl2qu7bI
    • (2011) Nat Protoc , vol.6 , Issue.11 , pp. 1695-1709
    • Casadonte, R.1    Caprioli, R.M.2
  • 65
    • 68549098247 scopus 로고    scopus 로고
    • Generation of high-quality protein extracts from formalin-fixed, paraffin-embedded tissues
    • 10.1002/pmic.200800971 1:CAS:528:DC%2BD1MXhtVWkurjP
    • MF Addis A Tanca D Pagnozzi S Crobu G Fanciulli P Cossu-Rocca S Uzzau 2009 Generation of high-quality protein extracts from formalin-fixed, paraffin-embedded tissues Proteomics 9 15 3815 3823 10.1002/pmic.200800971 1:CAS:528:DC%2BD1MXhtVWkurjP
    • (2009) Proteomics , vol.9 , Issue.15 , pp. 3815-3823
    • Addis, M.F.1    Tanca, A.2    Pagnozzi, D.3    Crobu, S.4    Fanciulli, G.5    Cossu-Rocca, P.6    Uzzau, S.7
  • 66
    • 77956327955 scopus 로고    scopus 로고
    • Formalin-fixed paraffin-embedded (FFPE) proteome analysis using gel-free and gel-based proteomics
    • 10.1021/pr1004168 1:CAS:528:DC%2BC3cXpt1Cltbo%3D
    • O Azimzadeh Z Barjaktarovic M Aubele J Calzada-Wack H Sarioglu MJ Atkinson S Tapio 2010 Formalin-fixed paraffin-embedded (FFPE) proteome analysis using gel-free and gel-based proteomics J Proteome Res 9 9 4710 4720 10.1021/pr1004168 1:CAS:528:DC%2BC3cXpt1Cltbo%3D
    • (2010) J Proteome Res , vol.9 , Issue.9 , pp. 4710-4720
    • Azimzadeh, O.1    Barjaktarovic, Z.2    Aubele, M.3    Calzada-Wack, J.4    Sarioglu, H.5    Atkinson, M.J.6    Tapio, S.7
  • 67
    • 62849124399 scopus 로고    scopus 로고
    • Development and validation of a novel protein extraction methodology for quantitation of protein expression in formalin-fixed paraffin-embedded tissues using western blotting
    • 10.1002/path.2504 1:CAS:528:DC%2BD1MXjvFOmu7Y%3D
    • NJ Nirmalan P Harnden PJ Selby RE Banks 2009 Development and validation of a novel protein extraction methodology for quantitation of protein expression in formalin-fixed paraffin-embedded tissues using western blotting J Pathol 217 4 497 506 10.1002/path.2504 1:CAS:528:DC%2BD1MXjvFOmu7Y%3D
    • (2009) J Pathol , vol.217 , Issue.4 , pp. 497-506
    • Nirmalan, N.J.1    Harnden, P.2    Selby, P.J.3    Banks, R.E.4
  • 68
    • 78650087646 scopus 로고    scopus 로고
    • Elevated pressure improves the extraction and identification of proteins recovered from formalin-fixed, paraffin-embedded tissue surrogates
    • 10.1371/journal.pone.0014253
    • CB Fowler IE Chesnick CD Moore TJ O'Leary JT Mason 2010 Elevated pressure improves the extraction and identification of proteins recovered from formalin-fixed, paraffin-embedded tissue surrogates PLoS One 5 12 e14253 10.1371/journal.pone.0014253
    • (2010) PLoS One , vol.5 , Issue.12 , pp. 14253
    • Fowler, C.B.1    Chesnick, I.E.2    Moore, C.D.3    O'Leary, T.J.4    Mason, J.T.5
  • 71
    • 78651516681 scopus 로고    scopus 로고
    • Proteomic analysis of formalin-fixed, paraffin-embedded lung neuroendocrine tumor samples from hospital archives
    • 10.1016/j.jprot.2010.12.001 1:CAS:528:DC%2BC3MXhtVWqs7w%3D
    • A Tanca MF Addis D Pagnozzi P Cossu-Rocca R Tonelli G Falchi A Eccher T Roggio G Fanciulli S Uzzau 2011 Proteomic analysis of formalin-fixed, paraffin-embedded lung neuroendocrine tumor samples from hospital archives J Proteomics 74 3 359 370 10.1016/j.jprot.2010.12.001 1:CAS:528: DC%2BC3MXhtVWqs7w%3D
    • (2011) J Proteomics , vol.74 , Issue.3 , pp. 359-370
    • Tanca, A.1    Addis, M.F.2    Pagnozzi, D.3    Cossu-Rocca, P.4    Tonelli, R.5    Falchi, G.6    Eccher, A.7    Roggio, T.8    Fanciulli, G.9    Uzzau, S.10
  • 72
    • 39749160439 scopus 로고    scopus 로고
    • Proteomic analysis of laser-captured paraffin-embedded tissues: A molecular portrait of head and neck cancer progression
    • 10.1158/1078-0432.CCR-07-1497 1:CAS:528:DC%2BD1cXhvF2gtbk%3D
    • V Patel BL Hood AA Molinolo NH Lee TP Conrads JC Braisted DB Krizman TD Veenstra JS Gutkind 2008 Proteomic analysis of laser-captured paraffin-embedded tissues: a molecular portrait of head and neck cancer progression Clin Cancer Res 14 4 1002 1014 10.1158/1078-0432.CCR-07-1497 1:CAS:528:DC%2BD1cXhvF2gtbk%3D
    • (2008) Clin Cancer Res , vol.14 , Issue.4 , pp. 1002-1014
    • Patel, V.1    Hood, B.L.2    Molinolo, A.A.3    Lee, N.H.4    Conrads, T.P.5    Braisted, J.C.6    Krizman, D.B.7    Veenstra, T.D.8    Gutkind, J.S.9
  • 73
    • 69249119365 scopus 로고    scopus 로고
    • Mapping the local protein interactome of the NuA3 histone acetyltransferase
    • 10.1002/pro.212 1:CAS:528:DC%2BD1MXhtVKnt7rO
    • SK Smart SG Mackintosh RD Edmondson SD Taverna AJ Tackett 2009 Mapping the local protein interactome of the NuA3 histone acetyltransferase Protein Sci 18 9 1987 1997 10.1002/pro.212 1:CAS:528:DC%2BD1MXhtVKnt7rO
    • (2009) Protein Sci , vol.18 , Issue.9 , pp. 1987-1997
    • Smart, S.K.1    MacKintosh, S.G.2    Edmondson, R.D.3    Taverna, S.D.4    Tackett, A.J.5
  • 76
    • 77950642747 scopus 로고    scopus 로고
    • Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy
    • 10.1021/pr1000175 1:CAS:528:DC%2BC3cXivFGiur8%3D
    • RM Kaake T Milenkovic N Przulj P Kaiser L Huang 2010 Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy J Proteome Res 9 4 2016 2029 10.1021/pr1000175 1:CAS:528:DC%2BC3cXivFGiur8%3D
    • (2010) J Proteome Res , vol.9 , Issue.4 , pp. 2016-2029
    • Kaake, R.M.1    Milenkovic, T.2    Przulj, N.3    Kaiser, P.4    Huang, L.5
  • 77
    • 79955780957 scopus 로고    scopus 로고
    • Membrane-SPINE: An improved method to identify protein-protein interaction partners of membrane proteins in vivo
    • 10.1002/pmic.201000558
    • VS Muller PR Jungblut TF Meyer S Hunke 2011 Membrane-SPINE: an improved method to identify protein-protein interaction partners of membrane proteins in vivo Proteomics 11 10 2124 2128 10.1002/pmic.201000558
    • (2011) Proteomics , vol.11 , Issue.10 , pp. 2124-2128
    • Muller, V.S.1    Jungblut, P.R.2    Meyer, T.F.3    Hunke, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.