메뉴 건너뛰기




Volumn 80, Issue , 2013, Pages 160-170

Evaluating the potential nonthermal microwave effects of microwave-assisted proteolytic reactions

Author keywords

Enzyme; Mass spectrometry; Microwave; Nonthermal effect; Protein digestion

Indexed keywords

ACETAMIDE DERIVATIVE; N METHYLIODOACETAMIDE; UNCLASSIFIED DRUG; CYTOCHROME; ENZYME; IODOACETAMIDE; N-METHYLIODOACETAMIDE; PEPTIDE; PROTEIN; TRYPSIN;

EID: 84874001843     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.01.005     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 0037013893 scopus 로고    scopus 로고
    • Microwave-assisted reactions in organic synthesis-are there any nonthermal microwave effects?
    • Kuhnert N. Microwave-assisted reactions in organic synthesis-are there any nonthermal microwave effects?. Angew Chem Int Ed 2002, 41:1863-1866.
    • (2002) Angew Chem Int Ed , vol.41 , pp. 1863-1866
    • Kuhnert, N.1
  • 2
    • 14644427257 scopus 로고    scopus 로고
    • Microwaves in organic synthesis. Thermal and non-thermal microwave effects
    • de la Hoz A., Diaz-Ortiz A., Moreno A. Microwaves in organic synthesis. Thermal and non-thermal microwave effects. Chem Soc Rev 2005, 34:164-178.
    • (2005) Chem Soc Rev , vol.34 , pp. 164-178
    • de la Hoz, A.1    Diaz-Ortiz, A.2    Moreno, A.3
  • 3
    • 33644853780 scopus 로고    scopus 로고
    • The impact of microwave synthesis on drug discovery
    • Kappe C.O., Dallinger D. The impact of microwave synthesis on drug discovery. Nat Rev Drug Discov 2006, 5:51-63.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 51-63
    • Kappe, C.O.1    Dallinger, D.2
  • 4
    • 4444332221 scopus 로고    scopus 로고
    • Microwave-assisted synthesis of single-crystalline tellurium nanorods and nanowires in ionic liquids
    • Zhu Y.-J., Wang W.-W., Qi R.-J., Hu X.-L. Microwave-assisted synthesis of single-crystalline tellurium nanorods and nanowires in ionic liquids. Angew Chem Int Ed 2004, 43:1410-1414.
    • (2004) Angew Chem Int Ed , vol.43 , pp. 1410-1414
    • Zhu, Y.-J.1    Wang, W.-W.2    Qi, R.-J.3    Hu, X.-L.4
  • 5
    • 0036838857 scopus 로고    scopus 로고
    • Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes
    • Pramanik B.N., Mirza U.A., Ing Y.H., Liu Y.H., Bartner P.L., Weber P.C., et al. Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes. Protein Sci 2002, 11:2676-2687.
    • (2002) Protein Sci , vol.11 , pp. 2676-2687
    • Pramanik, B.N.1    Mirza, U.A.2    Ing, Y.H.3    Liu, Y.H.4    Bartner, P.L.5    Weber, P.C.6
  • 7
    • 12444335586 scopus 로고    scopus 로고
    • Microwave-assisted synthesis of metallic nanostructures in solution
    • Tsuji M., Hashimoto M., Nishizawa Y., Kubokawa M., Tsuji T. Microwave-assisted synthesis of metallic nanostructures in solution. Chem Eur J 2005, 11:440-452.
    • (2005) Chem Eur J , vol.11 , pp. 440-452
    • Tsuji, M.1    Hashimoto, M.2    Nishizawa, Y.3    Kubokawa, M.4    Tsuji, T.5
  • 8
    • 34547211227 scopus 로고    scopus 로고
    • The influence of microwave irradiation on lipase-catalyzed kinetic resolution of racemic secondary alcohols
    • Bachu P., Gibson J.S., Sperry J., Brimble M.A. The influence of microwave irradiation on lipase-catalyzed kinetic resolution of racemic secondary alcohols. Tetrahedron Asymmetry 2007, 18:1618-1624.
    • (2007) Tetrahedron Asymmetry , vol.18 , pp. 1618-1624
    • Bachu, P.1    Gibson, J.S.2    Sperry, J.3    Brimble, M.A.4
  • 9
    • 50149112426 scopus 로고    scopus 로고
    • Investigating the existence of nonthermal/specific microwave effects using silicon carbide heating elements as power modulators
    • Razzaq T., Kremsner J.M., Kappe C.O. Investigating the existence of nonthermal/specific microwave effects using silicon carbide heating elements as power modulators. J Org Chem 2008, 73:6321-6329.
    • (2008) J Org Chem , vol.73 , pp. 6321-6329
    • Razzaq, T.1    Kremsner, J.M.2    Kappe, C.O.3
  • 10
    • 70349149840 scopus 로고    scopus 로고
    • Kinetic resolution of rac-1-phenylethanol with immobilized lipases: a critical comparison of microwave and conventional heating protocols
    • de Souza R.O.M.A., Antunes O.A.C., Kroutil W., Kappe C.O. Kinetic resolution of rac-1-phenylethanol with immobilized lipases: a critical comparison of microwave and conventional heating protocols. J Org Chem 2009, 74:6157-6162.
    • (2009) J Org Chem , vol.74 , pp. 6157-6162
    • de Souza, R.O.M.A.1    Antunes, O.A.C.2    Kroutil, W.3    Kappe, C.O.4
  • 11
    • 84863295837 scopus 로고    scopus 로고
    • Theoretical verification of nonthermal microwave effects on intramolecular reactions
    • Kanno M., Nakamura K., Kanai E., Hoki K., Kono H., Tanaka M. Theoretical verification of nonthermal microwave effects on intramolecular reactions. J Phys Chem A 2012, 116:2177-2183.
    • (2012) J Phys Chem A , vol.116 , pp. 2177-2183
    • Kanno, M.1    Nakamura, K.2    Kanai, E.3    Hoki, K.4    Kono, H.5    Tanaka, M.6
  • 12
    • 74249084980 scopus 로고    scopus 로고
    • Microwave effect for glycosylation promoted by solid super acid in supercritical carbon dioxide
    • Hinou H., Saito N., Ogawa M., Maeda T., Nishimura S.-I. Microwave effect for glycosylation promoted by solid super acid in supercritical carbon dioxide. Int J Mol Sci 2009, 10:5285-5295.
    • (2009) Int J Mol Sci , vol.10 , pp. 5285-5295
    • Hinou, H.1    Saito, N.2    Ogawa, M.3    Maeda, T.4    Nishimura, S.-I.5
  • 13
    • 37549015931 scopus 로고    scopus 로고
    • Nonthermal microwave effects revisited: on the importance of internal temperature monitoring and agitation in microwave chemistry
    • Herrero M.A., Kremsner J.M., Kappe C.O. Nonthermal microwave effects revisited: on the importance of internal temperature monitoring and agitation in microwave chemistry. J Org Chem 2008, 73:36-47.
    • (2008) J Org Chem , vol.73 , pp. 36-47
    • Herrero, M.A.1    Kremsner, J.M.2    Kappe, C.O.3
  • 14
    • 50849111740 scopus 로고    scopus 로고
    • A new glycosylation method part 3: study of microwave effects at low temperatures to control reaction pathways and reduce byproducts
    • Shimizu H., Yoshimura Y., Hinou H., Nishimura S.-I. A new glycosylation method part 3: study of microwave effects at low temperatures to control reaction pathways and reduce byproducts. Tetrahedron 2008, 64:10091-10096.
    • (2008) Tetrahedron , vol.64 , pp. 10091-10096
    • Shimizu, H.1    Yoshimura, Y.2    Hinou, H.3    Nishimura, S.-I.4
  • 15
    • 42949090771 scopus 로고    scopus 로고
    • Non-thermal effects in the microwave induced unfolding of proteins observed by chaperone binding
    • George D.F., Bilek M.M., McKenzie D.R. Non-thermal effects in the microwave induced unfolding of proteins observed by chaperone binding. Bioelectromagnetics 2008, 29:324-330.
    • (2008) Bioelectromagnetics , vol.29 , pp. 324-330
    • George, D.F.1    Bilek, M.M.2    McKenzie, D.R.3
  • 16
    • 0034173371 scopus 로고    scopus 로고
    • Microwave-enhanced folding and denaturation of globular proteins
    • Bohr H., Bohr J. Microwave-enhanced folding and denaturation of globular proteins. Phys Rev E 2000, 61:4310.
    • (2000) Phys Rev E , vol.61 , pp. 4310
    • Bohr, H.1    Bohr, J.2
  • 17
    • 0037716964 scopus 로고    scopus 로고
    • Microwave radiation can alter protein conformation without bulk heating
    • de Pomerai D.I., Smith B., Dawe A., North K., Smith T., Archer D.B., et al. Microwave radiation can alter protein conformation without bulk heating. FEBS Lett 2003, 543:93-97.
    • (2003) FEBS Lett , vol.543 , pp. 93-97
    • de Pomerai, D.I.1    Smith, B.2    Dawe, A.3    North, K.4    Smith, T.5    Archer, D.B.6
  • 18
    • 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
  • 19
    • 82955233601 scopus 로고    scopus 로고
    • Advances in mass spectrometry for the identification of pathogens
    • Ho Y.-P., Reddy P.M. Advances in mass spectrometry for the identification of pathogens. Mass Spectrom Rev 2011, 30:1203-1224.
    • (2011) Mass Spectrom Rev , vol.30 , pp. 1203-1224
    • Ho, Y.-P.1    Reddy, P.M.2
  • 20
    • 77950549715 scopus 로고    scopus 로고
    • Identification of pathogens by mass spectrometry
    • Ho Y.-P., Reddy P.M. Identification of pathogens by mass spectrometry. Clin Chem 2010, 56:525-536.
    • (2010) Clin Chem , vol.56 , pp. 525-536
    • Ho, Y.-P.1    Reddy, P.M.2
  • 21
    • 0034212611 scopus 로고    scopus 로고
    • Thermal denaturation: a useful technique in peptide mass mapping
    • Park Z.Y., Russell D.H. Thermal denaturation: a useful technique in peptide mass mapping. Anal Chem 2000, 72:2667-2670.
    • (2000) Anal Chem , vol.72 , pp. 2667-2670
    • Park, Z.Y.1    Russell, D.H.2
  • 22
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-aqueous solvent systems: applications for peptide mass mapping using mass spectrometry
    • Russell W.K., Park Z.Y., Russell D.H. Proteolysis in mixed organic-aqueous solvent systems: applications for peptide mass mapping using mass spectrometry. Anal Chem 2001, 73:2682-2685.
    • (2001) Anal Chem , vol.73 , pp. 2682-2685
    • Russell, W.K.1    Park, Z.Y.2    Russell, D.H.3
  • 23
    • 26844475051 scopus 로고    scopus 로고
    • Ultra fast trypsin digestion of proteins by high intensity focused ultrasound
    • Lopez-Ferrer D., Capelo J.L., Vazquez J. Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J Proteome Res 2005, 4:1569-1574.
    • (2005) J Proteome Res , vol.4 , pp. 1569-1574
    • Lopez-Ferrer, D.1    Capelo, J.L.2    Vazquez, J.3
  • 24
    • 0142135898 scopus 로고    scopus 로고
    • Dual-function microanalytical device by in situ photolithographic grafting of porous polymer monolith: integrating solid-phase extraction and enzymatic digestion for peptide mass mapping
    • Peterson D.S., Rohr T., Svec F., Frechet J.M.J. Dual-function microanalytical device by in situ photolithographic grafting of porous polymer monolith: integrating solid-phase extraction and enzymatic digestion for peptide mass mapping. Anal Chem 2003, 75:5328-5335.
    • (2003) Anal Chem , vol.75 , pp. 5328-5335
    • Peterson, D.S.1    Rohr, T.2    Svec, F.3    Frechet, J.M.J.4
  • 25
    • 15444379768 scopus 로고    scopus 로고
    • Blending protein separation and peptide analysis through real-time proteolytic digestion
    • Slysz G.W., Schriemer D.C. Blending protein separation and peptide analysis through real-time proteolytic digestion. Anal Chem 2005, 77:1572-1579.
    • (2005) Anal Chem , vol.77 , pp. 1572-1579
    • Slysz, G.W.1    Schriemer, D.C.2
  • 26
    • 16344395716 scopus 로고    scopus 로고
    • A new application of microwave technology to proteomics
    • Juan H.F., Chang S.C., Huang H.C., Chen S.T. A new application of microwave technology to proteomics. Proteomics 2005, 5:840-842.
    • (2005) Proteomics , vol.5 , pp. 840-842
    • Juan, H.F.1    Chang, S.C.2    Huang, H.C.3    Chen, S.T.4
  • 27
    • 25644450260 scopus 로고    scopus 로고
    • Assessment of microwave-assisted enzymatic digestion by measuring glycated hemoglobin A1c by mass spectrometry
    • Vesper H.W., Mi L.C., Enada A., Myers G.L. Assessment of microwave-assisted enzymatic digestion by measuring glycated hemoglobin A1c by mass spectrometry. Rapid Commun Mass Spectrom 2005, 19:2865-2870.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 2865-2870
    • Vesper, H.W.1    Mi, L.C.2    Enada, A.3    Myers, G.L.4
  • 28
    • 33645714858 scopus 로고    scopus 로고
    • Microwave-assisted protein preparation and enzymatic digestion in proteomics
    • Sun W., Gao S., Wang L., Chen Y., Wu S., Wang X., et al. Microwave-assisted protein preparation and enzymatic digestion in proteomics. Mol Cell Proteomics 2006, 5:769-776.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 769-776
    • Sun, W.1    Gao, S.2    Wang, L.3    Chen, Y.4    Wu, S.5    Wang, X.6
  • 29
    • 36849066250 scopus 로고    scopus 로고
    • Development of microwave-assisted protein digestion based on trypsin-immobilized magnetic microspheres for highly efficient proteolysis followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis
    • Lin S., Lin Z.X., Yao G.P., Deng C.H., Yang P.Y., Zhang X.M. Development of microwave-assisted protein digestion based on trypsin-immobilized magnetic microspheres for highly efficient proteolysis followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis. Rapid Commun Mass Spectrom 2007, 21:3910-3918.
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 3910-3918
    • Lin, S.1    Lin, Z.X.2    Yao, G.P.3    Deng, C.H.4    Yang, P.Y.5    Zhang, X.M.6
  • 30
    • 79953198925 scopus 로고    scopus 로고
    • Microwave assisted acid cleavage for denaturation and proteolysis of intact human adenovirus
    • Fenselau C., Laine O., Swatkoski S. Microwave assisted acid cleavage for denaturation and proteolysis of intact human adenovirus. Int J Mass Spectrom 2011, 301:7-11.
    • (2011) Int J Mass Spectrom , vol.301 , pp. 7-11
    • Fenselau, C.1    Laine, O.2    Swatkoski, S.3
  • 31
    • 54049111767 scopus 로고    scopus 로고
    • Extension of microwave-accelerated residue-specific acid cleavage to proteins with carbohydrate side chains and disulfide linkages
    • Li J.X., Shefcheck K., Callahan J., Fenselau C. Extension of microwave-accelerated residue-specific acid cleavage to proteins with carbohydrate side chains and disulfide linkages. Int J Mass Spectrom 2008, 278:109-113.
    • (2008) Int J Mass Spectrom , vol.278 , pp. 109-113
    • Li, J.X.1    Shefcheck, K.2    Callahan, J.3    Fenselau, C.4
  • 32
    • 39749157207 scopus 로고    scopus 로고
    • Evaluation of microwave-accelerated residue-specific acid cleavage for proteomic applications
    • Swatkoski S., Gutierrez P., Wynne C., Petrov A., Dinman J.D., Edwards N., et al. Evaluation of microwave-accelerated residue-specific acid cleavage for proteomic applications. J Proteome Res 2008, 7:579-586.
    • (2008) J Proteome Res , vol.7 , pp. 579-586
    • Swatkoski, S.1    Gutierrez, P.2    Wynne, C.3    Petrov, A.4    Dinman, J.D.5    Edwards, N.6
  • 33
    • 5044222901 scopus 로고    scopus 로고
    • Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis
    • Zhong H., Zhang Y., Wen Z., Li L. Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis. Nat Biotechnol 2004, 22:1291-1296.
    • (2004) Nat Biotechnol , vol.22 , pp. 1291-1296
    • Zhong, H.1    Zhang, Y.2    Wen, Z.3    Li, L.4
  • 34
    • 15744374025 scopus 로고    scopus 로고
    • Microwave-assisted acid hydrolysis of proteins combined with liquid chromatography MALDI MS/MS for protein identification
    • Zhong H., Marcus S.L., Li L. Microwave-assisted acid hydrolysis of proteins combined with liquid chromatography MALDI MS/MS for protein identification. J Am Soc Mass Spectrom 2005, 16:471-481.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 471-481
    • Zhong, H.1    Marcus, S.L.2    Li, L.3
  • 35
    • 32144458961 scopus 로고    scopus 로고
    • Microwave-assisted specific chemical digestion for rapid protein identification
    • Hua L., Low T.Y., Sze S.K. Microwave-assisted specific chemical digestion for rapid protein identification. Proteomics 2006, 6:586-591.
    • (2006) Proteomics , vol.6 , pp. 586-591
    • Hua, L.1    Low, T.Y.2    Sze, S.K.3
  • 36
    • 33947427539 scopus 로고    scopus 로고
    • Acceleration of microwave-assisted enzymatic digestion reactions by magnetite beads
    • Chen W.-Y., Chen Y.-C. Acceleration of microwave-assisted enzymatic digestion reactions by magnetite beads. Anal Chem 2007, 79:2394-2401.
    • (2007) Anal Chem , vol.79 , pp. 2394-2401
    • Chen, W.-Y.1    Chen, Y.-C.2
  • 37
    • 43949131094 scopus 로고    scopus 로고
    • Fast and efficient proteolysis by microwave-assisted protein digestion using trypsin-immobilized magnetic silica microspheres
    • Lin S., Yao G., Qi D., Li Y., Deng C., Yang P., et al. Fast and efficient proteolysis by microwave-assisted protein digestion using trypsin-immobilized magnetic silica microspheres. Anal Chem 2008, 80:3655-3665.
    • (2008) Anal Chem , vol.80 , pp. 3655-3665
    • Lin, S.1    Yao, G.2    Qi, D.3    Li, Y.4    Deng, C.5    Yang, P.6
  • 38
    • 44449121455 scopus 로고    scopus 로고
    • Novel microwave-assisted digestion by trypsin-immobilized magnetic nanoparticles for proteomic analysis
    • Lin S., Yun D., Qi D., Deng C., Li Y., Zhang X. Novel microwave-assisted digestion by trypsin-immobilized magnetic nanoparticles for proteomic analysis. J Proteome Res 2008, 7:1297-1307.
    • (2008) J Proteome Res , vol.7 , pp. 1297-1307
    • Lin, S.1    Yun, D.2    Qi, D.3    Deng, C.4    Li, Y.5    Zhang, X.6
  • 39
    • 71949114466 scopus 로고    scopus 로고
    • Quantum dots - electrospray ionization mass spectrometry: 3-mercaptopropanic acid capped CdS quantum dots as accelerating and enrichment probes for microwave tryptic digestion of proteins
    • Shirvas K., Kailasa S.K., Wu H.F. Quantum dots - electrospray ionization mass spectrometry: 3-mercaptopropanic acid capped CdS quantum dots as accelerating and enrichment probes for microwave tryptic digestion of proteins. Rapid Commun Mass Spectrom 2009, 23:3603-3607.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 3603-3607
    • Shirvas, K.1    Kailasa, S.K.2    Wu, H.F.3
  • 40
    • 66449135386 scopus 로고    scopus 로고
    • Quantum dots laser desorption/ionization MS: multifunctional CdSe quantum dots as the matrix, concentrating probes and acceleration for microwave enzymatic digestion for peptide analysis and high resolution detection of proteins in a linear MALDI-TOF MS
    • Shrivas K., Kailasa S.K., Wu H.F. Quantum dots laser desorption/ionization MS: multifunctional CdSe quantum dots as the matrix, concentrating probes and acceleration for microwave enzymatic digestion for peptide analysis and high resolution detection of proteins in a linear MALDI-TOF MS. Proteomics 2009, 9:2656-2667.
    • (2009) Proteomics , vol.9 , pp. 2656-2667
    • Shrivas, K.1    Kailasa, S.K.2    Wu, H.F.3
  • 41
    • 67650891650 scopus 로고    scopus 로고
    • Cysteine-capped ZnSe quantum dots as affinity and accelerating probes for microwave enzymatic digestion of proteins via direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis
    • Shastri L.A., Kailasa S.K., Wu H.F. Cysteine-capped ZnSe quantum dots as affinity and accelerating probes for microwave enzymatic digestion of proteins via direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis. Rapid Commun Mass Spectrom 2009, 23:2247-2252.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 2247-2252
    • Shastri, L.A.1    Kailasa, S.K.2    Wu, H.F.3
  • 42
    • 78650707514 scopus 로고    scopus 로고
    • On particle ionization/enrichment of multifunctional nanoprobes: washing/separation-free, acceleration and enrichment of microwave-assisted tryptic digestion of proteins via bare TiO2 nanoparticles in ESI-MS and comparing to MALDI-MS
    • Wu H.F., Agrawal K., Shrivas K., Lee Y.H. On particle ionization/enrichment of multifunctional nanoprobes: washing/separation-free, acceleration and enrichment of microwave-assisted tryptic digestion of proteins via bare TiO2 nanoparticles in ESI-MS and comparing to MALDI-MS. J Mass Spectrom 2010, 45:1402-1408.
    • (2010) J Mass Spectrom , vol.45 , pp. 1402-1408
    • Wu, H.F.1    Agrawal, K.2    Shrivas, K.3    Lee, Y.H.4
  • 43
    • 15744364177 scopus 로고    scopus 로고
    • Microwave-assisted enzyme-catalyzed reactions in various solvent systems
    • Lin S.-S., Wu C.-H., Sun M.-C., Sun C.-M., Ho Y.-P. Microwave-assisted enzyme-catalyzed reactions in various solvent systems. J Am Soc Mass Spectrom 2005, 16:581-588.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 581-588
    • Lin, S.-S.1    Wu, C.-H.2    Sun, M.-C.3    Sun, C.-M.4    Ho, Y.-P.5
  • 44
    • 76749088472 scopus 로고    scopus 로고
    • Digestion completeness of microwave-assisted and conventional trypsin-catalyzed reactions
    • Reddy P.M., Hsu W.Y., Hu J.F., Ho Y.P. Digestion completeness of microwave-assisted and conventional trypsin-catalyzed reactions. J Am Soc Mass Spectrom 2010, 21:421-424.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 421-424
    • Reddy, P.M.1    Hsu, W.Y.2    Hu, J.F.3    Ho, Y.P.4
  • 45
    • 0027983518 scopus 로고
    • Modification of cysteine residues with n-methyl iodoacetamide
    • Ramseier U., Chang J.Y. Modification of cysteine residues with n-methyl iodoacetamide. Anal Biochem 1994, 221:231-233.
    • (1994) Anal Biochem , vol.221 , pp. 231-233
    • Ramseier, U.1    Chang, J.Y.2
  • 46
    • 40449135495 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization-MS-based relative quantification of peptides and proteins using iodoacetamide and N-methyliodoacetamide as labeling reagents
    • Sun M.-C., Chen C.-D., Huang Y.-S., Wu Z.-S., Ho Y.-P. Matrix-assisted laser desorption/ionization-MS-based relative quantification of peptides and proteins using iodoacetamide and N-methyliodoacetamide as labeling reagents. J Sep Sci 2008, 31:538-547.
    • (2008) J Sep Sci , vol.31 , pp. 538-547
    • Sun, M.-C.1    Chen, C.-D.2    Huang, Y.-S.3    Wu, Z.-S.4    Ho, Y.-P.5
  • 47
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis J., Thomas H., Sebela M., Shevchenko A. Fast-response proteomics by accelerated in-gel digestion of proteins. Anal Chem 2003, 75:1300-1306.
    • (2003) Anal Chem , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 48
    • 84866041597 scopus 로고    scopus 로고
    • Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols
    • Damm M., Nusshold C., Cantillo D., Rechberger G.N., Gruber K., Sattler W., et al. Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols. J Proteomics 2012, 75:5533-5543.
    • (2012) J Proteomics , vol.75 , pp. 5533-5543
    • Damm, M.1    Nusshold, C.2    Cantillo, D.3    Rechberger, G.N.4    Gruber, K.5    Sattler, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.