메뉴 건너뛰기




Volumn 16, Issue 7, 2009, Pages 763-772

Useful Tools for Biomolecule Isolation, Detection, and Identification: Acylhydrazone-Based Cleavable Linkers (DOI:10.1016/j.chembiol.2009.06.005);Useful Tools for Biomolecule Isolation, Detection, and Identification: Acylhydrazone-Based Cleavable Linkers

Author keywords

CHEMBIO

Indexed keywords


EID: 67651091698     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2009.08.007     Document Type: Erratum
Times cited : (62)

References (50)
  • 2
    • 1342286046 scopus 로고    scopus 로고
    • Design and synthesis of a photocleavable biotinylated nucleotide for DNA analysis by mass spectrometry
    • Bai X., Kim S., Li Z., Turro N.J., and Ju J. Design and synthesis of a photocleavable biotinylated nucleotide for DNA analysis by mass spectrometry. Nucleic Acids Res. 32 (2004) 535-541
    • (2004) Nucleic Acids Res. , vol.32 , pp. 535-541
    • Bai, X.1    Kim, S.2    Li, Z.3    Turro, N.J.4    Ju, J.5
  • 3
    • 0031184172 scopus 로고    scopus 로고
    • Application of reversible biotinylated label for directed immobilization of synthetic peptides and proteins: isolation of ligates from crude cell lysates
    • Ball H.L., and Mascagni P. Application of reversible biotinylated label for directed immobilization of synthetic peptides and proteins: isolation of ligates from crude cell lysates. J. Pept. Sci. 3 (1997) 252-260
    • (1997) J. Pept. Sci. , vol.3 , pp. 252-260
    • Ball, H.L.1    Mascagni, P.2
  • 4
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions
    • Berggard T., Linse S., and James P. Methods for the detection and analysis of protein-protein interactions. Proteomics 7 (2007) 2833-2842
    • (2007) Proteomics , vol.7 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 5
    • 1542268868 scopus 로고    scopus 로고
    • Addition of carbon nucleophiles to cyclic N-acyliminium ions in SDS/water
    • Camilo N.S., and Pilli R.A. Addition of carbon nucleophiles to cyclic N-acyliminium ions in SDS/water. Tetrahedron Lett. 45 (2004) 2821-2823
    • (2004) Tetrahedron Lett. , vol.45 , pp. 2821-2823
    • Camilo, N.S.1    Pilli, R.A.2
  • 6
    • 0019876606 scopus 로고
    • The amino acid sequence of yeast enolase
    • Chin C.C.Q., Brewer J.M., and Wold F. The amino acid sequence of yeast enolase. J. Biol. Chem. 256 (1981) 1377-1384
    • (1981) J. Biol. Chem. , vol.256 , pp. 1377-1384
    • Chin, C.C.Q.1    Brewer, J.M.2    Wold, F.3
  • 8
    • 34347218266 scopus 로고    scopus 로고
    • Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging
    • Dieterich D.C., Lee J.J., Link A.J., Graumann J., Tirrell D.A., and Schuman E.M. Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging. Nat. Protoc. 2 (2007) 532-540
    • (2007) Nat. Protoc. , vol.2 , pp. 532-540
    • Dieterich, D.C.1    Lee, J.J.2    Link, A.J.3    Graumann, J.4    Tirrell, D.A.5    Schuman, E.M.6
  • 9
    • 33845461876 scopus 로고    scopus 로고
    • Nucleophilic catalysis of hydrazone formation and transimination: Implications for dynamic covalent chemistry
    • Dirksen A., Dirksen S., Hackeng T.M., and Dawson P.E. Nucleophilic catalysis of hydrazone formation and transimination: Implications for dynamic covalent chemistry. J. Am. Chem. Soc. 128 (2006) 15602-15603
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15602-15603
    • Dirksen, A.1    Dirksen, S.2    Hackeng, T.M.3    Dawson, P.E.4
  • 11
    • 0022262433 scopus 로고
    • Synthetic tools for adrenocorticotropin receptor identification
    • Finn F.M., Stehle C.J., and Hofmann K. Synthetic tools for adrenocorticotropin receptor identification. Biochemistry 24 (1985) 1960-1965
    • (1985) Biochemistry , vol.24 , pp. 1960-1965
    • Finn, F.M.1    Stehle, C.J.2    Hofmann, K.3
  • 12
    • 4644349577 scopus 로고    scopus 로고
    • Novel chemoselective linkage chemistry toward controlled loading of ligands to proteins through in situ real-time quantification of conjugate formation
    • Flinn N.S., Quibell M., Turnell W.G., Monk T.P., and Ramjee M.K. Novel chemoselective linkage chemistry toward controlled loading of ligands to proteins through in situ real-time quantification of conjugate formation. Bioconjug. Chem. 15 (2004) 1010-1020
    • (2004) Bioconjug. Chem. , vol.15 , pp. 1010-1020
    • Flinn, N.S.1    Quibell, M.2    Turnell, W.G.3    Monk, T.P.4    Ramjee, M.K.5
  • 13
    • 35648998466 scopus 로고    scopus 로고
    • Proteomics evaluation of chemically cleavable activity-based probes
    • Fonovic M., Verhelst S.H., Sorum M.T., and Bogyo M. Proteomics evaluation of chemically cleavable activity-based probes. Mol. Cell. Proteomics 6 (2007) 1761-1770
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1761-1770
    • Fonovic, M.1    Verhelst, S.H.2    Sorum, M.T.3    Bogyo, M.4
  • 14
    • 14544272334 scopus 로고    scopus 로고
    • 2/water: An efficient system for deprotection of oximes and imines to carbonyls under neutral conditions in water
    • 2/water: An efficient system for deprotection of oximes and imines to carbonyls under neutral conditions in water. J. Org. Chem. 70 (2005) 1934-1936
    • (2005) J. Org. Chem. , vol.70 , pp. 1934-1936
    • Gogoi, P.1    Hazarika, P.2    Konwar, D.3
  • 15
    • 0035852702 scopus 로고    scopus 로고
    • Double-level "orthogonal" dynamic combinatorial libraries on transition metal template
    • Goral V., Nelen M.I., Eliseev A.V., and Lehn J.M. Double-level "orthogonal" dynamic combinatorial libraries on transition metal template. Proc. Natl. Acad. Sci. USA 98 (2001) 1347-1352
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1347-1352
    • Goral, V.1    Nelen, M.I.2    Eliseev, A.V.3    Lehn, J.M.4
  • 16
    • 0025288944 scopus 로고
    • Avidin and streptavidin
    • Green N.M. Avidin and streptavidin. Methods Enzymol. 184 (1990) 51-67
    • (1990) Methods Enzymol. , vol.184 , pp. 51-67
    • Green, N.M.1
  • 17
    • 0037108987 scopus 로고    scopus 로고
    • Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation
    • Hirsch J.D., Eslamizar L., Filanoski B.J., Malekzadeh N., Haugland R.P., Beechem J.M., and Haugland R.P. Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation. Anal. Biochem. 308 (2002) 343-357
    • (2002) Anal. Biochem. , vol.308 , pp. 343-357
    • Hirsch, J.D.1    Eslamizar, L.2    Filanoski, B.J.3    Malekzadeh, N.4    Haugland, R.P.5    Beechem, J.M.6    Haugland, R.P.7
  • 18
    • 0019876624 scopus 로고
    • The primary structures of two yeast enolase genes. Homology between the 5′ noncoding flanking regions of yeast enolase and glyceraldehyde-3- phosphate dehydrogenase genes
    • Holland M.J., Holland J.P., Thill G.P., and Jackson K.A. The primary structures of two yeast enolase genes. Homology between the 5′ noncoding flanking regions of yeast enolase and glyceraldehyde-3- phosphate dehydrogenase genes. J. Biol. Chem. 256 (1981) 1385-1395
    • (1981) J. Biol. Chem. , vol.256 , pp. 1385-1395
    • Holland, M.J.1    Holland, J.P.2    Thill, G.P.3    Jackson, K.A.4
  • 19
    • 14944364973 scopus 로고    scopus 로고
    • The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures
    • Holmberg A., Blomstergren A., Nord O., Lukacs M., Lundeberg J., and Uhlen M. The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures. Electrophoresis 26 (2005) 501-510
    • (2005) Electrophoresis , vol.26 , pp. 501-510
    • Holmberg, A.1    Blomstergren, A.2    Nord, O.3    Lukacs, M.4    Lundeberg, J.5    Uhlen, M.6
  • 21
    • 0033004596 scopus 로고    scopus 로고
    • Disruption of the streptavidin interaction with biotinylated nucleic acid probes by 2-mercaptoethanol
    • Jenne A., and Famulok M. Disruption of the streptavidin interaction with biotinylated nucleic acid probes by 2-mercaptoethanol. Biotechniques 26 (1999) 249-254
    • (1999) Biotechniques , vol.26 , pp. 249-254
    • Jenne, A.1    Famulok, M.2
  • 22
    • 33947707837 scopus 로고    scopus 로고
    • Design, synthesis and characterization of pH-sensitive PEG-PE conjugates for stimuli-sensitive pharmaceutical nanocarriers: The effect of substitutes at the hydrazone linkage on the pH-stability of PEG-PE conjugates
    • Kale A.A., and Torchilin V.P. Design, synthesis and characterization of pH-sensitive PEG-PE conjugates for stimuli-sensitive pharmaceutical nanocarriers: The effect of substitutes at the hydrazone linkage on the pH-stability of PEG-PE conjugates. Bioconjug. Chem. 18 (2007) 363-370
    • (2007) Bioconjug. Chem. , vol.18 , pp. 363-370
    • Kale, A.A.1    Torchilin, V.P.2
  • 23
    • 0028875782 scopus 로고
    • Synthesis of the carbonic acid benzotriazol-1-yl-ester-(2-biotinylamino)-9h-fluoren-9-ylmethyl ester: A convenient transient-biotinylation reagent for use in affinity chromatography
    • Kazmierski W.M., and McDermed J. Synthesis of the carbonic acid benzotriazol-1-yl-ester-(2-biotinylamino)-9h-fluoren-9-ylmethyl ester: A convenient transient-biotinylation reagent for use in affinity chromatography. Tetrahedron Lett. 36 (1995) 9097-9100
    • (1995) Tetrahedron Lett. , vol.36 , pp. 9097-9100
    • Kazmierski, W.M.1    McDermed, J.2
  • 24
    • 0023055743 scopus 로고
    • Preparation of protein conjugates via intermolecular hydrazone linkage
    • King T.P., Zhao S.W., and Lam T. Preparation of protein conjugates via intermolecular hydrazone linkage. Biochemistry 25 (1986) 5774-5779
    • (1986) Biochemistry , vol.25 , pp. 5774-5779
    • King, T.P.1    Zhao, S.W.2    Lam, T.3
  • 25
    • 0010998813 scopus 로고
    • Two-step affinity chromatography. Model systems and an example using biotin-avidin binding and a fluoridolyzable linker
    • Lin W.-C., and Morton T.H. Two-step affinity chromatography. Model systems and an example using biotin-avidin binding and a fluoridolyzable linker. J. Org. Chem. 56 (1991) 6850-6856
    • (1991) J. Org. Chem. , vol.56 , pp. 6850-6856
    • Lin, W.-C.1    Morton, T.H.2
  • 26
    • 36749047362 scopus 로고    scopus 로고
    • Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation
    • MacKinnon A.L., Garrison J.L., Hegde R.S., and Taunton J. Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. J. Am. Chem. Soc. 129 (2007) 14560-14561
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14560-14561
    • MacKinnon, A.L.1    Garrison, J.L.2    Hegde, R.S.3    Taunton, J.4
  • 27
    • 0037508878 scopus 로고    scopus 로고
    • Affinity thermoprecipitation and recovery of biotinylated biomolecules via a mutant streptavidin-smart polymer conjugate
    • Malmstadt N., Hyre D.E., Ding Z., Hoffman A.S., and Stayton P.S. Affinity thermoprecipitation and recovery of biotinylated biomolecules via a mutant streptavidin-smart polymer conjugate. Bioconjug. Chem. 14 (2003) 575-580
    • (2003) Bioconjug. Chem. , vol.14 , pp. 575-580
    • Malmstadt, N.1    Hyre, D.E.2    Ding, Z.3    Hoffman, A.S.4    Stayton, P.S.5
  • 28
    • 0025025824 scopus 로고
    • Affinity chromatography purification of angiotensin II receptor using photoactivable biotinylated probes
    • Marie J., Seyer R., Lombard C., Desarnaud F., Aumelas A., Jard S., and Bonnafous J.C. Affinity chromatography purification of angiotensin II receptor using photoactivable biotinylated probes. Biochemistry 29 (1990) 8943-8950
    • (1990) Biochemistry , vol.29 , pp. 8943-8950
    • Marie, J.1    Seyer, R.2    Lombard, C.3    Desarnaud, F.4    Aumelas, A.5    Jard, S.6    Bonnafous, J.C.7
  • 29
    • 0029996541 scopus 로고    scopus 로고
    • Reversibility of biotin-binding by selective modification of tyrosine in avidin
    • Morag E., Bayer E.A., and Wilchek M. Reversibility of biotin-binding by selective modification of tyrosine in avidin. Biochem. J. 316 (1996) 193-199
    • (1996) Biochem. J. , vol.316 , pp. 193-199
    • Morag, E.1    Bayer, E.A.2    Wilchek, M.3
  • 30
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev V.V., Green L.G., Fokin V.V., and Sharpless K.B. A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 41 (2002) 2596-2599
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 32
    • 67651109475 scopus 로고    scopus 로고
    • Affinity chromatography
    • Dingermann T. (Ed), Wiley-VCH Verlag GmbH, Weinheim, Germany
    • Scriba G.K.E. Affinity chromatography. In: Dingermann T. (Ed). Molecular Biology in Medicinal Chemistry (2004), Wiley-VCH Verlag GmbH, Weinheim, Germany 211-241
    • (2004) Molecular Biology in Medicinal Chemistry , pp. 211-241
    • Scriba, G.K.E.1
  • 33
    • 0003610959 scopus 로고
    • A chemically cleavable biotinylated nucleotide: usefulness in the recovery of protein-DNA complexes from avidin affinity columns
    • Shimkus M., Levy J., and Herman T. A chemically cleavable biotinylated nucleotide: usefulness in the recovery of protein-DNA complexes from avidin affinity columns. Proc. Natl. Acad. Sci. USA 82 (1985) 2593-2597
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2593-2597
    • Shimkus, M.1    Levy, J.2    Herman, T.3
  • 35
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers A.E., Adam G.C., and Cravatt B.F. Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125 (2003) 4686-4687
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 36
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers A.E., and Cravatt B.F. Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11 (2004) 535-546
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 37
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • Speers A.E., and Cravatt B.F. A tandem orthogonal proteolysis strategy for high-content chemical proteomics. J. Am. Chem. Soc. 127 (2005) 10018-10019
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 38
    • 31544446908 scopus 로고    scopus 로고
    • Carbohydrate and protein immobilization onto solid surfaces by sequential Diels-Alder and azide-alkyne cycloadditions
    • Sun X.-L., Stabler C.L., Cazalis C.S., and Chaikof E.L. Carbohydrate and protein immobilization onto solid surfaces by sequential Diels-Alder and azide-alkyne cycloadditions. Bioconjug. Chem. 17 (2006) 52-57
    • (2006) Bioconjug. Chem. , vol.17 , pp. 52-57
    • Sun, X.-L.1    Stabler, C.L.2    Cazalis, C.S.3    Chaikof, E.L.4
  • 39
    • 33646838202 scopus 로고    scopus 로고
    • NMR study of conformation and isomerization of aryl- and heteroarylaldehyde 4-tert-butylphenoxyacetylhydrazones
    • Syakaev V.V., Podyachev S.N., Buzykin B.I., Latypov S.K., Habicher W.D., and Konovalov A.I. NMR study of conformation and isomerization of aryl- and heteroarylaldehyde 4-tert-butylphenoxyacetylhydrazones. J. Mol. Struct. 788 (2006) 55-62
    • (2006) J. Mol. Struct. , vol.788 , pp. 55-62
    • Syakaev, V.V.1    Podyachev, S.N.2    Buzykin, B.I.3    Latypov, S.K.4    Habicher, W.D.5    Konovalov, A.I.6
  • 40
    • 0028263246 scopus 로고
    • Photocleavable biotinylated ligands for affinity chromatography
    • Thiele C., and Fahrenholz F. Photocleavable biotinylated ligands for affinity chromatography. Anal. Biochem. 218 (1994) 330-337
    • (1994) Anal. Biochem. , vol.218 , pp. 330-337
    • Thiele, C.1    Fahrenholz, F.2
  • 41
    • 0027121247 scopus 로고
    • Solid-phase method for the purification of DNA sequencing reactions
    • Tong X., and Smith L.M. Solid-phase method for the purification of DNA sequencing reactions. Anal. Chem. 64 (1992) 2672-2677
    • (1992) Anal. Chem. , vol.64 , pp. 2672-2677
    • Tong, X.1    Smith, L.M.2
  • 42
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides
    • Tornoe C.W., Christensen C., and Meldal M. Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 67 (2002) 3057-3064
    • (2002) J. Org. Chem. , vol.67 , pp. 3057-3064
    • Tornoe, C.W.1    Christensen, C.2    Meldal, M.3
  • 44
    • 34247273992 scopus 로고    scopus 로고
    • A mild chemically cleavable linker system for functional proteomic applications
    • Verhelst S.H.L., Fonovic M., and Bogyo M. A mild chemically cleavable linker system for functional proteomic applications. Angew. Chem. Int. Ed. Engl. 46 (2007) 1284-1286
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 1284-1286
    • Verhelst, S.H.L.1    Fonovic, M.2    Bogyo, M.3
  • 45
    • 33745726644 scopus 로고    scopus 로고
    • Chemical genetics
    • Walsh D.P., and Chang Y.T. Chemical genetics. Chem. Rev. 106 (2006) 2476-2530
    • (2006) Chem. Rev. , vol.106 , pp. 2476-2530
    • Walsh, D.P.1    Chang, Y.T.2
  • 46
    • 18744366642 scopus 로고    scopus 로고
    • Reaction of aldehydes and pyrazolones in the presence of sodium dodecyl sulfate in aqueous media
    • Wang W., Wang S.X., Qin X.Y., and Li J.T. Reaction of aldehydes and pyrazolones in the presence of sodium dodecyl sulfate in aqueous media. Synth. Commun. 35 (2005) 1263-1269
    • (2005) Synth. Commun. , vol.35 , pp. 1263-1269
    • Wang, W.1    Wang, S.X.2    Qin, X.Y.3    Li, J.T.4
  • 47
    • 45549108466 scopus 로고    scopus 로고
    • Disparate proteome reactivity profiles of carbon electrophiles
    • Weerapana E., Simon G.M., and Cravatt B.F. Disparate proteome reactivity profiles of carbon electrophiles. Nat. Chem. Biol. 4 (2008) 405-407
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 405-407
    • Weerapana, E.1    Simon, G.M.2    Cravatt, B.F.3
  • 48
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • Wilchek M., and Bayer E. Introduction to avidin-biotin technology. Methods Enzymol. 184 (1990) 14-45
    • (1990) Methods Enzymol. , vol.184 , pp. 14-45
    • Wilchek, M.1    Bayer, E.2
  • 49
    • 20744437590 scopus 로고    scopus 로고
    • Engineering soluble monomeric streptavidin with reversible biotin binding capability
    • Wu S.C., and Wong S.L. Engineering soluble monomeric streptavidin with reversible biotin binding capability. J. Biol. Chem. 280 (2005) 23225-23231
    • (2005) J. Biol. Chem. , vol.280 , pp. 23225-23231
    • Wu, S.C.1    Wong, S.L.2
  • 50
    • 0022559094 scopus 로고
    • Use of avidin-iminobiotin complexes for purifying plasma membrane proteins
    • Zeheb R., and Orr G.A. Use of avidin-iminobiotin complexes for purifying plasma membrane proteins. Methods Enzymol. 122 (1986) 87-94
    • (1986) Methods Enzymol. , vol.122 , pp. 87-94
    • Zeheb, R.1    Orr, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.