메뉴 건너뛰기




Volumn 13, Issue 23-24, 2008, Pages 1075-1081

Recent developments in microwave-assisted protein chemistries - can this be integrated into the drug discovery and validation process?

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN; MONOCLONAL ANTIBODY; MYOGLOBIN; TRYPSIN;

EID: 55749112818     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2008.08.007     Document Type: Review
Times cited : (25)

References (36)
  • 1
    • 36448943427 scopus 로고    scopus 로고
    • A deubiquitinase that regulates type I interferon production
    • Kayagaki N., et al. A deubiquitinase that regulates type I interferon production. Science 318 (2007) 1628-1632
    • (2007) Science , vol.318 , pp. 1628-1632
    • Kayagaki, N.1
  • 2
    • 2342447397 scopus 로고    scopus 로고
    • The ubiquitin ligase COP1 is a critical negative regulator of p53
    • Dornan D., et al. The ubiquitin ligase COP1 is a critical negative regulator of p53. Nature 429 (2004) 86-92
    • (2004) Nature , vol.429 , pp. 86-92
    • Dornan, D.1
  • 3
    • 34248335027 scopus 로고    scopus 로고
    • Utilizing the activation mechanism of serine proteases to engineer hepatocyte growth factor into a Met antagonist
    • Kirchhofer D., et al. Utilizing the activation mechanism of serine proteases to engineer hepatocyte growth factor into a Met antagonist. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 5306-5311
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5306-5311
    • Kirchhofer, D.1
  • 4
    • 33344475312 scopus 로고    scopus 로고
    • Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity
    • Edosada C.Y., et al. Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity. FEBS Lett. 580 (2006) 1581-1586
    • (2006) FEBS Lett. , vol.580 , pp. 1581-1586
    • Edosada, C.Y.1
  • 5
    • 35348971600 scopus 로고    scopus 로고
    • Targeted mass spectrometric strategy for global mapping of ubiquitination on proteins
    • Mollah S., et al. Targeted mass spectrometric strategy for global mapping of ubiquitination on proteins. Rapid Commun. Mass Spectrom. 21 (2007) 3357-3364
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3357-3364
    • Mollah, S.1
  • 6
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1
  • 7
    • 0042386240 scopus 로고    scopus 로고
    • Protein identification: the origins of peptide mass fingerprinting
    • Henzel W.J., et al. Protein identification: the origins of peptide mass fingerprinting. J. Am. Soc. Mass Spectrom. 14 (2003) 931-942
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 931-942
    • Henzel, W.J.1
  • 8
    • 0000312004 scopus 로고
    • Protein sequencing by tandem mass spectrometry
    • Hunt D.F., et al. Protein sequencing by tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 6233-6237
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6233-6237
    • Hunt, D.F.1
  • 9
  • 10
    • 0033081238 scopus 로고    scopus 로고
    • Protein identification using 20-minute Edman cycles and sequence mixture analysis
    • Henzel W.J., et al. Protein identification using 20-minute Edman cycles and sequence mixture analysis. Anal. Biochem. 267 (1999) 148-160
    • (1999) Anal. Biochem. , vol.267 , pp. 148-160
    • Henzel, W.J.1
  • 11
    • 17044393960 scopus 로고    scopus 로고
    • UPLC: An introduction and review
    • Schwartz M.E. UPLC: An introduction and review. J. Liq. Chrom. Rel. Technol. 28 (2005) 1253-1263
    • (2005) J. Liq. Chrom. Rel. Technol. , vol.28 , pp. 1253-1263
    • Schwartz, M.E.1
  • 12
    • 18344364097 scopus 로고    scopus 로고
    • The Orbitrap: a new mass spectrometer
    • Hu Q., et al. The Orbitrap: a new mass spectrometer. J. Mass Spectrom. 40 (2005) 430-443
    • (2005) J. Mass Spectrom. , vol.40 , pp. 430-443
    • Hu, Q.1
  • 13
    • 24044553566 scopus 로고    scopus 로고
    • Multiple reaction monitoring to identify sites of protein phosphorylation with high sensitivity
    • Unwin R.D., et al. Multiple reaction monitoring to identify sites of protein phosphorylation with high sensitivity. Mol. Cell Proteomics 4 (2005) 1134-1144
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1134-1144
    • Unwin, R.D.1
  • 14
    • 33846811132 scopus 로고    scopus 로고
    • An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-TOF instrument
    • Pringle S.D., et al. An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-TOF instrument. Int. J. Mass Spectrom. 261 (2007) 1-12
    • (2007) Int. J. Mass Spectrom. , vol.261 , pp. 1-12
    • Pringle, S.D.1
  • 15
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1
  • 16
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret A. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sci. 7 (1998) 706-719
    • (1998) Protein Sci. , vol.7 , pp. 706-719
    • Ducret, A.1
  • 17
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., et al. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75 (2003) 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1
  • 18
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., and Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4 (2007) 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 19
    • 0035813244 scopus 로고    scopus 로고
    • Microwave assisted organic synthesis - a review
    • Lidstrom P., et al. Microwave assisted organic synthesis - a review. Tetrahedron 57 (2001) 9225-9283
    • (2001) Tetrahedron , vol.57 , pp. 9225-9283
    • Lidstrom, P.1
  • 20
    • 34548050212 scopus 로고    scopus 로고
    • Microwave-assisted proteomics
    • Lill J.R., et al. Microwave-assisted proteomics. Mass Spectrom. Rev. 26 (2007) 657-671
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 657-671
    • Lill, J.R.1
  • 21
    • 34047208469 scopus 로고    scopus 로고
    • Microwave energy: a versatile tool for the biosciences
    • Collins J.M., and Leadbeater N.E. Microwave energy: a versatile tool for the biosciences. Org. Biomol. Chem. 5 (2007) 1141-1150
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 1141-1150
    • Collins, J.M.1    Leadbeater, N.E.2
  • 22
    • 37049027551 scopus 로고    scopus 로고
    • Applications of microwave-assisted proteomics in biotechnology
    • Sandoval W., et al. Applications of microwave-assisted proteomics in biotechnology. Comb. Chem. High Throughput Screen. 10 (2007) 751-765
    • (2007) Comb. Chem. High Throughput Screen. , vol.10 , pp. 751-765
    • Sandoval, W.1
  • 23
    • 33750610771 scopus 로고
    • A rapid and novel means of protein hydrolysis by microwave irradiation using Teflon-Pyrex tubes
    • Villafranca J.J. (Ed), Academic Press, San Diego
    • Chiou S.-H., and Wang K.-T. A rapid and novel means of protein hydrolysis by microwave irradiation using Teflon-Pyrex tubes. In: Villafranca J.J. (Ed). Current Research in Protein Chemistry: Techniques, Structure, and Function (1990), Academic Press, San Diego 3-10
    • (1990) Current Research in Protein Chemistry: Techniques, Structure, and Function , pp. 3-10
    • Chiou, S.-H.1    Wang, K.-T.2
  • 24
    • 0030635970 scopus 로고    scopus 로고
    • Hydrolysis of samples for amino acid analysis
    • Smith B.J. (Ed), Humana Press, Totowa
    • Davidson I. Hydrolysis of samples for amino acid analysis. In: Smith B.J. (Ed). Methods in Molecular Biology (1996), Humana Press, Totowa 119-129
    • (1996) Methods in Molecular Biology , pp. 119-129
    • Davidson, I.1
  • 25
    • 33644867597 scopus 로고    scopus 로고
    • Rapid kinetic-based screening of human Fab fragments
    • Steukers M., et al. Rapid kinetic-based screening of human Fab fragments. J. Immunol. Methods 310 (2006) 126-135
    • (2006) J. Immunol. Methods , vol.310 , pp. 126-135
    • Steukers, M.1
  • 26
    • 0031876578 scopus 로고    scopus 로고
    • An efficient route to human bispecific IgG
    • Merchant A.M., et al. An efficient route to human bispecific IgG. Nat. Biotechnol. 16 (1998) 677-681
    • (1998) Nat. Biotechnol. , vol.16 , pp. 677-681
    • Merchant, A.M.1
  • 27
    • 1942502345 scopus 로고    scopus 로고
    • A revival of bispecific antibodies
    • Kufer P., et al. A revival of bispecific antibodies. Trends Biotechnol. 22 (2004) 238-244
    • (2004) Trends Biotechnol. , vol.22 , pp. 238-244
    • Kufer, P.1
  • 28
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies; prospects and challenges for immunoconjugates
    • Wu A.M., and Senter P.D. Arming antibodies; prospects and challenges for immunoconjugates. Nat. Biotechnol. 23 (2005) 1137-1146
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 29
    • 21444439732 scopus 로고    scopus 로고
    • Generation of high-affinity human antibodies by combining donor-derived and synthetic complimentarity-determining region diversity
    • Hoet R.M., et al. Generation of high-affinity human antibodies by combining donor-derived and synthetic complimentarity-determining region diversity. Nat. Biotechnol. 23 (2005) 344-348
    • (2005) Nat. Biotechnol. , vol.23 , pp. 344-348
    • Hoet, R.M.1
  • 30
    • 33750632035 scopus 로고    scopus 로고
    • Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation
    • Sandoval W.N., et al. Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation. Int. J. Mass Spectrom. 259 (2007) 117-123
    • (2007) Int. J. Mass Spectrom. , vol.259 , pp. 117-123
    • Sandoval, W.N.1
  • 31
    • 25144468506 scopus 로고    scopus 로고
    • Characterization of oligosaccharide moieties of intact glycoproteins by microwave-assisted partial acid hydrolysis and mass spectrometry
    • Lee B.-S., et al. Characterization of oligosaccharide moieties of intact glycoproteins by microwave-assisted partial acid hydrolysis and mass spectrometry. Rapid Commun. Mass Spectrom. 19 (2005) 2629-2635
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2629-2635
    • Lee, B.-S.1
  • 33
    • 34248637584 scopus 로고    scopus 로고
    • Positional proteomics: preparation of amino-terminal peptides as a strategy for proteome simplification and characterization
    • McDonald L., et al. Positional proteomics: preparation of amino-terminal peptides as a strategy for proteome simplification and characterization. Nat. Protoc. 1 (2006) 1790-1798
    • (2006) Nat. Protoc. , vol.1 , pp. 1790-1798
    • McDonald, L.1
  • 34
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka J.E.P., et al. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9528-9533
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1
  • 35
    • 5044222901 scopus 로고    scopus 로고
    • Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis
    • Zhong H., et al. Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis. Nat. Biotechnol. 22 (2004) 1291-1296
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1291-1296
    • Zhong, H.1
  • 36
    • 55749110049 scopus 로고    scopus 로고
    • Zhu-Shimoni, J. et al. Trace levels of leached Protein A in bioprocess samples without interference from the large excess of rhMAb IgG. (in press)
    • Zhu-Shimoni, J. et al. Trace levels of leached Protein A in bioprocess samples without interference from the large excess of rhMAb IgG. (in press)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.