메뉴 건너뛰기




Volumn 15, Issue 1, 2011, Pages 67-75

Trisulfides in proteins

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; CYSTEINE; HUMAN GROWTH HORMONE; IMMUNOGLOBULIN G2; INTERLEUKIN 6; SALCATONIN; SULFIDE; TRISULFIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79958219658     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2010.3677     Document Type: Article
Times cited : (50)

References (70)
  • 5
    • 20244390001 scopus 로고    scopus 로고
    • 2S induces a suspended animation-like state in mice
    • DOI 10.1126/science.1108581
    • Blackstone E, Morrison M, and Roth MB. H2S induces a suspended animation-like state in mice. Science 308: 518, 2005. (Pubitemid 40570576)
    • (2005) Science , vol.308 , Issue.5721 , pp. 518
    • Blackstone, E.1    Morrison, M.2    Roth, M.B.3
  • 6
    • 0016156485 scopus 로고
    • Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase
    • Branzoli U and Massey V. Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase. J Biol Chem 249: 4346-4349, 1974.
    • (1974) J Biol Chem , vol.249 , pp. 4346-4349
    • Branzoli, U.1    Massey, V.2
  • 8
    • 0018121854 scopus 로고
    • Sulfhydryl reactivity of human erythrocyte superoxide dismutase. On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin
    • Briggs RG and Fee JA. Sulfhydryl reactivity of human erythrocyte superoxide dismutase: On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin. Biochim Biophys Acta 537: 100-109, 1978. (Pubitemid 9060438)
    • (1978) Biochimica et Biophysica Acta , vol.537 , Issue.1 , pp. 100-109
    • Briggs, R.G.1    Fee, J.A.2
  • 10
    • 0029833152 scopus 로고    scopus 로고
    • Confirmation by mass spectrometry of a trisulfide variant in methionyl human growth hormone biosynthesized in Escherichia coli
    • Canova-Davis E, Baldonado IP, Chloupek RC, Ling VT, Gehant R, Olson K, and Gillece-Castro BL. Confirmation by mass spectrometry of a trisulfide variant in methionyl human growth hormone biosynthesized in Escherichia coli. Anal Chem 68: 4044-4051, 1996.
    • (1996) Anal Chem , vol.68 , pp. 4044-4051
    • Canova-Davis, E.1    Baldonado, I.P.2    Chloupek, R.C.3    Ling, V.T.4    Gehant, R.5    Olson, K.6    Gillece-Castro, B.L.7
  • 11
    • 0014691234 scopus 로고
    • Isolation of human hepatocuprein and cerebrocuprein. Their identity with erythrocuprein
    • Carrico RJ and Deutsch HF. Isolation of human hepatocuprein and cerebrocuprein. Their identity with erythrocuprein. J Biol Chem 244: 6087-6093, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6087-6093
    • Carrico, R.J.1    Deutsch, H.F.2
  • 13
    • 0030939626 scopus 로고    scopus 로고
    • Synthesis and pharmacology of novel analogues of oxytocin and deaminooxytocin: Directed methods for the construction of disulfide and trisulfide bridges in peptides
    • DOI 10.1021/jm9607156
    • Chen L, Zoulikova I, Slaninova J, and Barany G. Synthesis and pharmacology of novel analogues of oxytocin and deaminooxytocin: Directed methods for the construction of disulfide and trisulfide bridges in peptides. J Med Chem 40: 864-876, 1997. (Pubitemid 27131616)
    • (1997) Journal of Medicinal Chemistry , vol.40 , Issue.6 , pp. 864-876
    • Chen, L.1    Zoulikova, I.2    Slaninova, J.3    Barany, G.4
  • 14
    • 1942441011 scopus 로고    scopus 로고
    • Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties
    • DOI 10.1110/ps.03576904
    • De Beus MD, Chung J, and Colón W. Modification of cysteine 111 in Cu=Zn superoxide dismutase results in altered spectroscopic and biophysical properties. Protein Sci 13: 1347-1355, 2004. (Pubitemid 38526100)
    • (2004) Protein Science , vol.13 , Issue.5 , pp. 1347-1355
    • De Beus, M.D.1    Chung, J.2    Colon, W.3
  • 15
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, and Kossiakoff AA. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255: 306-312, 1992.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 16
    • 0032541713 scopus 로고    scopus 로고
    • Facile synthesis of cyclic peptides containing di-, tri-, tetra-, and pentasulfides
    • PII S0040403998014610
    • Erlanson DA and Wells JA. Facile synthesis of cyclic peptides containing di-, tri-, tetra-, and pentasulfides. Tetrahedron Lett 39: 6799-6802, 1998. (Pubitemid 28407358)
    • (1998) Tetrahedron Letters , vol.39 , Issue.38 , pp. 6799-6802
    • Erlanson, D.A.1    Wells, J.A.2
  • 17
    • 0028237753 scopus 로고
    • Free-radical repair by a novel perthiol: Reversible hydrogen transfer and perthiyl radical formation
    • Everett SA, Folkes LK, Wardman P, and Asmus K-D. Freeradical repair by a novel perthiol: Reversible hydrogen transfer and perthiyl radical formation. Free Radic Res 20: 387-400, 1994. (Pubitemid 24170148)
    • (1994) Free Radical Research , vol.20 , Issue.6 , pp. 387-400
    • Everett, S.A.1    Folkes, L.K.2    Wardman, P.3
  • 18
    • 0011783843 scopus 로고
    • The occurrence of bis-(2-amino-2- carboxyethyl) trisulphide in hydrolysates of wool and other proteins
    • Fletcher JC and Robson A. The occurrence of bis-(2-amino-2- carboxyethyl) trisulphide in hydrolysates of wool and other proteins. Biochem J 87: 553-559, 1963.
    • (1963) Biochem J , vol.87 , pp. 553-559
    • Fletcher, J.C.1    Robson, A.2
  • 19
    • 84961986802 scopus 로고    scopus 로고
    • On the origin of cytotoxicity of the natural product varacin. A novel example of a pentathiepin reaction that provides evidence for a triatomic sulfur intermediate
    • DOI 10.1021/ja016495p
    • Greer A. On the origin of cytotoxicity of the natural product varacin. A novel example of a pentathiepin reaction that provides evidence for a triatomic sulfur intermediate. J Am Chem Soc 123: 10379-10386, 2001. (Pubitemid 32979788)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.42 , pp. 10379-10386
    • Greer, A.1
  • 21
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations
    • Hansen RE and Winther JR. An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations. Anal Biochem 394: 147-158, 2009.
    • (2009) Anal Biochem , vol.394 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 23
    • 10544244908 scopus 로고
    • Enzymatic formation of polysulfides from mercaptopyruvate
    • Hylin JW and Wood JL. Enzymatic formation of polysulfides from mercaptopyruvate. J Biol Chem 234: 2141-2144, 1959.
    • (1959) J Biol Chem , vol.234 , pp. 2141-2144
    • Hylin, J.W.1    Wood, J.L.2
  • 24
    • 63049130448 scopus 로고    scopus 로고
    • Biological properties of garlic and garlic-derived organosulfur compounds
    • Iciek M, Kwiecien I, and Wlodek L. Biological properties of garlic and garlic-derived organosulfur compounds. Environ Mol Mutagen 50: 247-265, 2009.
    • (2009) Environ Mol Mutagen , vol.50 , pp. 247-265
    • Iciek, M.1    Kwiecien, I.2    Wlodek, L.3
  • 26
    • 33751439570 scopus 로고    scopus 로고
    • A scent of therapy: Pharmacological implications of natural products containing redox-active sulfur atoms
    • DOI 10.1039/b609523m
    • Jacob C. A scent of therapy: Pharmacological implications of natural products containing redox-active sulfur atoms. Nat Prod Rep 23: 851-863, 2006. (Pubitemid 44815547)
    • (2006) Natural Product Reports , vol.23 , Issue.6 , pp. 851-863
    • Jacob, C.1
  • 27
    • 45249120583 scopus 로고    scopus 로고
    • The chemistry behind redox regulation with a focus on sulphur redox systems
    • DOI 10.1111/j.1399-3054.2008.01080.x
    • Jacob C and Anwar A. The chemistry behind redox regulation with a focus on sulphur redox systems. Physiol Plant 133: 469-480, 2008. (Pubitemid 351841672)
    • (2008) Physiologia Plantarum , vol.133 , Issue.3 , pp. 469-480
    • Jacob, C.1    Anwar, A.2
  • 28
    • 56249132709 scopus 로고    scopus 로고
    • Perspective on recent developments on sulfur-containing agents and hydrogen sulfide signaling
    • Jacob C, Anwar A, and Burkholz T. Perspective on recent developments on sulfur-containing agents and hydrogen sulfide signaling. Planta Med 74: 1580-1592, 2008.
    • (2008) Planta Med , vol.74 , pp. 1580-1592
    • Jacob, C.1    Anwar, A.2    Burkholz, T.3
  • 29
    • 64549161166 scopus 로고    scopus 로고
    • Kinetic and thermodynamic aspects of cellular thiol-disulfide redox regulation
    • Jensen KS, Hansen RE, and Winther JR. Kinetic and thermodynamic aspects of cellular thiol-disulfide redox regulation. Antioxid Redox Signal 11: 1047-1058, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1047-1058
    • Jensen, K.S.1    Hansen, R.E.2    Winther, J.R.3
  • 30
  • 31
    • 3042651344 scopus 로고    scopus 로고
    • Endogenous production of hydrogen sulfide in mammals
    • Kamoun P. Endogenous production of hydrogen sulfide in mammals. Amino Acids 26: 243-254, 2004. (Pubitemid 38829787)
    • (2004) Amino Acids , vol.26 , Issue.3 , pp. 243-254
    • Kamoun, P.1
  • 32
    • 17644366461 scopus 로고    scopus 로고
    • Hydrogen sulfide as a biological mediator
    • DOI 10.1089/ars.2005.7.778
    • Kimura H. Hydrogen sulfide as a biological mediator. Antioxid Redox Signal 7: 778-780, 2005. (Pubitemid 40563218)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.5-6 , pp. 778-780
    • Kimura, H.1
  • 34
    • 49749158181 scopus 로고
    • Isolation and properties of a ßmercaptopyruvate- cleaving copper enzyme
    • Kun E and Fanshier DW. Isolation and properties of a ß mercaptopyruvate- cleaving copper enzyme. Biochim Biophys Acta 32: 338-348, 1959.
    • (1959) Biochim Biophys Acta , vol.32 , pp. 338-348
    • Kun, E.1    Fanshier, D.W.2
  • 35
    • 0028086255 scopus 로고
    • A convenient method for the synthesis of peptide trisulfides
    • DOI 10.1016/S0040-4039(00)73427-7
    • Lundin RHL, Norén BE, and Edlund PO. A convenient method for the synthesis of peptide trisulfides. Tetrahedron Lett 35: 6339-6342, 1994. (Pubitemid 24265056)
    • (1994) Tetrahedron Letters , vol.35 , Issue.34 , pp. 6339-6342
    • Lundin, R.H.L.1    Noren, B.E.2    Edlund, P.O.3
  • 36
    • 0014963075 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by cyanide
    • Massey V and Edmondson D. On the mechanism of inactivation of xanthine oxidase by cyanide. J Biol Chem 245: 6595-6598, 1970.
    • (1970) J Biol Chem , vol.245 , pp. 6595-6598
    • Massey, V.1    Edmondson, D.2
  • 37
    • 0015231837 scopus 로고
    • The presence of So- containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c
    • Massey V, Williams CH, and Palmer G. The presence of So- containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c. Biochem Biophys Res Commun 42: 730-738, 1971.
    • (1971) Biochem Biophys Res Commun , vol.42 , pp. 730-738
    • Massey, V.1    Williams, C.H.2    Palmer, G.3
  • 38
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6055, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 39
    • 0001189469 scopus 로고
    • The thermodynamics and kinetics of the hydrogen sulfide system in natural waters
    • Millero FJ. The thermodynamics and kinetics of the hydrogen sulfide system in natural waters. Mar Chem 18: 121-147, 1986.
    • (1986) Mar Chem , vol.18 , pp. 121-147
    • Millero, F.J.1
  • 44
    • 0028557060 scopus 로고
    • Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat
    • Ogasawara Y, Isoda S, and Tanabe S. Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat. Biol Pharm Bull 17: 1535-1542, 1994.
    • (1994) Biol Pharm Bull , vol.17 , pp. 1535-1542
    • Ogasawara, Y.1    Isoda, S.2    Tanabe, S.3
  • 45
    • 33751536134 scopus 로고    scopus 로고
    • Modification of Cysteine 111 in human Cu,Zn-superoxide dismutase
    • DOI 10.1016/j.freeradbiomed.2006.09.011, PII S0891584906005752
    • Okado-Matsumoto A, Guan Z, and Fridovich I. Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Free Radic Biol Med 41: 1837-1846, 2006. (Pubitemid 44839144)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.12 , pp. 1837-1846
    • Okado-Matsumoto, A.1    Guan, Z.2    Fridovich, I.3
  • 46
    • 0028364188 scopus 로고
    • Preparation of trisulfide derivatives of cystine and their formation as by-products during peptide synthesis
    • DOI 10.1016/S0040-4039(00)73228-X
    • Parmentier B, Moutiez M, Tartar A, and Sergheraert C. Preparation of trisulfide derivatives of cystine and their formation as by-products during peptide synthesis. Tetrahedron Lett 35: 3531-3534, 1994. (Pubitemid 24176473)
    • (1994) Tetrahedron Letters , vol.35 , Issue.21 , pp. 3531-3534
    • Parmentier, B.1    Moutiez, M.2    Tartar, A.3    Sergheraert, C.4
  • 47
    • 0026435063 scopus 로고
    • Hydrophobic interaction chromatography of recombinant human growth hormone, Genotropin
    • Pavlu B and Gellerfors P. Hydrophobic interaction chromatography of recombinant human growth hormone, Genotropin. Bioseparation 3: 257-265, 1993.
    • (1993) Bioseparation , vol.3 , pp. 257-265
    • Pavlu, B.1    Gellerfors, P.2
  • 48
    • 0015217023 scopus 로고
    • The oxygen sensitivity of spinach ferredoxin and other iron-sulfur proteins
    • Petering D, Fee JA, and Palmer G. The oxygen sensitivity of spinach ferredoxin and other iron-sulfur proteins. J Biol Chem 246: 643-653, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 643-653
    • Petering, D.1    Fee, J.A.2    Palmer, G.3
  • 49
    • 68049084746 scopus 로고    scopus 로고
    • Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody
    • Pristatsky P, Cohen SL, Krantz D, Acevedo J, Ionescu R, and Vlasak J. Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody. Anal Chem 81: 6148-6155, 2009.
    • (2009) Anal Chem , vol.81 , pp. 6148-6155
    • Pristatsky, P.1    Cohen, S.L.2    Krantz, D.3    Acevedo, J.4    Ionescu, R.5    Vlasak, J.6
  • 50
    • 0014402255 scopus 로고
    • Sulfur-containing amino acids II. Chromatography of disulfides and trisulfides with an automatic analyzer
    • Purdie JW, Gravelle RA, and Hanafi DE. Sulfur-containing amino acids II. Chromatography of disulfides and trisulfides with an automatic analyzer. J ChromatogrA 38: 346-350, 1968.
    • (1968) J ChromatogrA , vol.38 , pp. 346-350
    • Purdie, J.W.1    Gravelle, R.A.2    Hanafi, D.E.3
  • 51
    • 0010854216 scopus 로고
    • Reaction of cystine with sodium sulfide in sodium hydroxide solution
    • Rao GS and Gorin G. Reaction of cystine with sodium sulfide in sodium hydroxide solution. J Org Chem 24: 749-753, 1959.
    • (1959) J Org Chem , vol.24 , pp. 749-753
    • Rao, G.S.1    Gorin, G.2
  • 52
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • Riemer J, Bulleid N, and Herrmann JM. Disulfide formation in the ER and mitochondria: Two solutions to a common process. Science 324: 1284-1287, 2009.
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 53
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • DOI 10.1016/j.tibs.2006.12.005, PII S0968000406003331
    • Shaw BF and Valentine JS. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 32: 78-85, 2007. (Pubitemid 46199198)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.2 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 55
    • 70349687379 scopus 로고    scopus 로고
    • Dimethyl trisulfide as a characteristic odor associated with fungating cancer wounds
    • Shirasu M, Nagai S, Hayashi R, Ochiai A, and Touhara K. Dimethyl trisulfide as a characteristic odor associated with fungating cancer wounds. Biosci Biotechnol Biochem 73: 2117-2120, 2009.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 2117-2120
    • Shirasu, M.1    Nagai, S.2    Hayashi, R.3    Ochiai, A.4    Touhara, K.5
  • 57
    • 44849135016 scopus 로고    scopus 로고
    • Bioactive food components and cancer risk reduction
    • Stan SD, Kar S, Stoner GD, and Singh SV. Bioactive food components and cancer risk reduction. J Cell Biochem 104: 339-356, 2008.
    • (2008) J Cell Biochem , vol.104 , pp. 339-356
    • Stan, S.D.1    Kar, S.2    Stoner, G.D.3    Singh, S.V.4
  • 58
    • 0031009381 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of a C-terminal human growth hormone fragment and its the related trisulfide peptide
    • Strandberg E, Kö rdel J, Lundin R, Wehler T, and Widmalm G. Nuclear magnetic resonance studies of a C-terminal human growth hormone fragment and its the related trisulfide peptide. J Pept Res 49: 254-260, 1997. (Pubitemid 27280493)
    • (1997) Journal of Peptide Research , vol.49 , Issue.3 , pp. 254-260
    • Strandberg, E.1    Kordel, J.2    Lundin, R.3    Wehler, T.4    Widmalm, G.5
  • 60
    • 0028309526 scopus 로고
    • Pharmacological characterization of a biosynthetic trisulfide-containing hydrophobic derivative of human growth hormone: Comparison with standard 22 K growth hormone
    • Thomsen MK, Hansen BS, Nilsson P, Nowak J, Johansen PB, Thomsen PD, and Christiansen J. Pharmacological characterization of a biosynthetic trisulfide-containing hydrophobic derivative of human growth hormone:Comparisonwith standard 22 K growth hormone. Pharmacol Toxicol 74: 351-358, 1994. (Pubitemid 24180262)
    • (1994) Pharmacology and Toxicology , vol.74 , Issue.6 , pp. 351-358
    • Thomsen, M.K.1    Hansen, B.S.2    Nilsson, P.3    Nowak, J.4    Johansen, P.B.5    Thomsen, P.D.6    Christiansen, J.7
  • 64
    • 0025814867 scopus 로고
    • Biological sulfane sulfur
    • Westley AM and Westley J. Biological sulfane sulfur. Anal Biochem 195: 63-67, 1991.
    • (1991) Anal Biochem , vol.195 , pp. 63-67
    • Westley, A.M.1    Westley, J.2
  • 65
    • 47549089687 scopus 로고    scopus 로고
    • Reappraisal of H2S=sulfide concentration in vertebrate blood and its potential significance in ischemic preconditioning and vascular signaling
    • Whitfield NL, Kreimier EL, Verdial FC, Skovgaard N, and Olson KR. Reappraisal of H2S=sulfide concentration in vertebrate blood and its potential significance in ischemic preconditioning and vascular signaling. Am J Physiol Regul Integr Comp Physiol 294: R1930-R1937, 2008.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.294
    • Whitfield, N.L.1    Kreimier, E.L.2    Verdial, F.C.3    Skovgaard, N.4    Olson, K.R.5
  • 66
    • 0020490576 scopus 로고
    • Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide
    • Williamson G, Engel PC, Mizzer JP, Thorpe C, and Massey V. Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide. J Biol Chem257: 4314-4320, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 4314-4320
    • Williamson, G.1    Engel, P.C.2    Mizzer, J.P.3    Thorpe, C.4    Massey, V.5
  • 68
    • 0017302163 scopus 로고
    • Cyclic polysulfides from the red alga Chondria californica
    • Wratten SJ and Faulkner DJ. Cyclic polysulfides from the red alga Chondria californica. J Org Chem 41: 2465-2467, 1976.
    • (1976) J Org Chem , vol.41 , pp. 2465-2467
    • Wratten, S.J.1    Faulkner, D.J.2
  • 69
    • 76749156792 scopus 로고    scopus 로고
    • Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase
    • You Z, Cao X, Taylor AB, Hart PJ, and Levine RL. Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase. Biochemistry 49: 1191-1198, 2010.
    • (2010) Biochemistry , vol.49 , pp. 1191-1198
    • You, Z.1    Cao, X.2    Taylor, A.B.3    Hart, P.J.4    Levine, R.L.5
  • 70
    • 70350247861 scopus 로고    scopus 로고
    • Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques
    • Zhao Y and Jensen ON. Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques. Proteomics 9: 4632-4641, 2009.
    • (2009) Proteomics , vol.9 , pp. 4632-4641
    • Zhao, Y.1    Jensen, O.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.