메뉴 건너뛰기




Volumn 405, Issue 29, 2013, Pages 9321-9331

Specific biotinylation and sensitive enrichment of citrullinated peptides

Author keywords

Biotinylation; Chemical modification; Mass spectrometry; Peptide enrichment; Protein citrullination; Rheumatoid arthritis

Indexed keywords

BIOTINYLATIONS; FLIGHT MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION; MYELIN BASIC PROTEIN; POST-TRANSLATIONAL MODIFICATIONS; RHEUMATOID ARTHRITIS; SELECTIVE ENRICHMENT; SENSITIVE TECHNIQUES;

EID: 84890047183     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-013-7376-1     Document Type: Article
Times cited : (24)

References (27)
  • 2
    • 0029824853 scopus 로고    scopus 로고
    • Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • 10.1074/jbc.271.48.30709 1:CAS:528:DyaK28XntlaksLk%3D
    • Tarcsa E, Marekov LN, Mei G, Melino G, Lee SC, Steinert PM (1996) Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 271(48):30709-30716
    • (1996) J Biol Chem , vol.271 , Issue.48 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, L.N.2    Mei, G.3    Melino, G.4    Lee, S.C.5    Steinert, P.M.6
  • 3
    • 33745331328 scopus 로고    scopus 로고
    • Citrullination: A posttranslational modification in health and disease
    • 10.1016/j.biocel.2006.03.008
    • Gyorgy B, Toth E, Tarcsa E, Falus A, Buzas EI (2006) Citrullination: a posttranslational modification in health and disease. Int J Biochem Cell Biol 38(10):1662-1677
    • (2006) Int J Biochem Cell Biol , vol.38 , Issue.10 , pp. 1662-1677
    • Gyorgy, B.1    Toth, E.2    Tarcsa, E.3    Falus, A.4    Buzas, E.I.5
  • 4
    • 84867985009 scopus 로고    scopus 로고
    • Citrullination under physiological and pathological conditions
    • 10.1016/j.jbspin.2012.01.008 1:CAS:528:DC%2BC38XhsFyjsr3P
    • Baka Z, Gyorgy B, Geher P, Buzas EI, Falus A, Nagy G (2012) Citrullination under physiological and pathological conditions. Joint Bone Spine 79(5):431-436
    • (2012) Joint Bone Spine , vol.79 , Issue.5 , pp. 431-436
    • Baka, Z.1    Gyorgy, B.2    Geher, P.3    Buzas, E.I.4    Falus, A.5    Nagy, G.6
  • 5
    • 73249145617 scopus 로고    scopus 로고
    • Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis
    • 10.1111/j.0105-2896.2009.00850.x 1:CAS:528:DC%2BC3cXjslartbc%3D
    • Wegner N, Lundberg K, Kinloch A, Fisher B, Malmstrom V, Feldmann M, Venables PJ (2010) Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis. Immunol Rev 233(1):34-54
    • (2010) Immunol Rev , vol.233 , Issue.1 , pp. 34-54
    • Wegner, N.1    Lundberg, K.2    Kinloch, A.3    Fisher, B.4    Malmstrom, V.5    Feldmann, M.6    Venables, P.J.7
  • 6
    • 17044409168 scopus 로고    scopus 로고
    • Fibrin deimination in synovial tissue is not specific for rheumatoid arthritis but commonly occurs during synovitides
    • 1:CAS:528:DC%2BD2MXivFKhsrY%3D
    • Chapuy-Regaud S, Sebbag M, Baeten D, Clavel C, Foulquier C, De KF, Serre G (2005) Fibrin deimination in synovial tissue is not specific for rheumatoid arthritis but commonly occurs during synovitides. J Immunol 174(8):5057-5064
    • (2005) J Immunol , vol.174 , Issue.8 , pp. 5057-5064
    • Chapuy-Regaud, S.1    Sebbag, M.2    Baeten, D.3    Clavel, C.4    Foulquier, C.5    De, K.F.6    Serre, G.7
  • 7
    • 0028342830 scopus 로고
    • Myelin in multiple sclerosis is developmentally immature
    • 10.1172/JCI117300 1:CAS:528:DyaK2cXltlWmtLg%3D
    • Moscarello MA, Wood DD, Ackerley C, Boulias C (1994) Myelin in multiple sclerosis is developmentally immature. J Clin Invest 94(1):146-154
    • (1994) J Clin Invest , vol.94 , Issue.1 , pp. 146-154
    • Moscarello, M.A.1    Wood, D.D.2    Ackerley, C.3    Boulias, C.4
  • 8
    • 20244368810 scopus 로고    scopus 로고
    • Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease
    • 10.1002/jnr.20431 1:CAS:528:DC%2BD2MXjtlSmsrk%3D
    • Ishigami A, Ohsawa T, Hiratsuka M, Taguchi H, Kobayashi S, Saito Y, Murayama S, Asaga H, Toda T, Kimura N, Maruyama N (2005) Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. J Neurosci Res 80(1):120-128
    • (2005) J Neurosci Res , vol.80 , Issue.1 , pp. 120-128
    • Ishigami, A.1    Ohsawa, T.2    Hiratsuka, M.3    Taguchi, H.4    Kobayashi, S.5    Saito, Y.6    Murayama, S.7    Asaga, H.8    Toda, T.9    Kimura, N.10    Maruyama, N.11
  • 9
    • 79959508911 scopus 로고    scopus 로고
    • PADI4 and tumourigenesis
    • 10.1186/1475-2867-10-7
    • Chang X, Fang K (2010) PADI4 and tumourigenesis. Cancer Cell Int 10:7
    • (2010) Cancer Cell Int , vol.10 , pp. 7
    • Chang, X.1    Fang, K.2
  • 10
    • 0031974911 scopus 로고    scopus 로고
    • Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies
    • 10.1172/JCI1316 1:CAS:528:DyaK1cXjtFSjsg%3D%3D
    • Schellekens GA, de Jong BA, van den Hoogen FH, van de Putte LB, van Venrooij WJ (1998) Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies. J Clin Invest 101(1):273-281
    • (1998) J Clin Invest , vol.101 , Issue.1 , pp. 273-281
    • Schellekens, G.A.1    De Jong, B.A.2    Van Den Hoogen, F.H.3    Van De Putte, L.B.4    Van Venrooij, W.J.5
  • 11
    • 0034091322 scopus 로고    scopus 로고
    • The diagnostic properties of rheumatoid arthritis antibodies recognizing a cyclic citrullinated peptide
    • 10.1002/1529-0131(200001)43:1<155: AID-ANR20>3.0.CO;2-3 1:CAS:528:DC%2BD3cXns1ygtg%3D%3D
    • Schellekens GA, Visser H, de Jong BA, van den Hoogen FH, Hazes JM, Breedveld FC, van Venrooij WJ (2000) The diagnostic properties of rheumatoid arthritis antibodies recognizing a cyclic citrullinated peptide. Arthritis Rheum 43(1):155-163
    • (2000) Arthritis Rheum , vol.43 , Issue.1 , pp. 155-163
    • Schellekens, G.A.1    Visser, H.2    De Jong, B.A.3    Van Den Hoogen, F.H.4    Hazes, J.M.5    Breedveld, F.C.6    Van Venrooij, W.J.7
  • 12
    • 84860349570 scopus 로고    scopus 로고
    • In vivo relevance of citrullinated proteins and the challenges in their detection
    • De Ceuleneer M, Van Steendam K, Dhaenens M, Deforce D (2012) In vivo relevance of citrullinated proteins and the challenges in their detection. Proteomics 12(6):752-760
    • (2012) Proteomics , vol.12 , Issue.6 , pp. 752-760
    • De Ceuleneer, M.1    Van Steendam, K.2    Dhaenens, M.3    Deforce, D.4
  • 13
    • 0026764429 scopus 로고
    • Detection of citrulline residues in deiminated proteins on polyvinylidene difluoride membrane
    • 10.1016/0003-2697(92)90047-B 1:CAS:528:DyaK38XksVers7o%3D
    • Senshu T, Sato T, Inoue T, Akiyama K, Asaga H (1992) Detection of citrulline residues in deiminated proteins on polyvinylidene difluoride membrane. Anal Biochem 203(1):94-100
    • (1992) Anal Biochem , vol.203 , Issue.1 , pp. 94-100
    • Senshu, T.1    Sato, T.2    Inoue, T.3    Akiyama, K.4    Asaga, H.5
  • 14
    • 33646053191 scopus 로고    scopus 로고
    • Specific modification of peptide-bound citrulline residues
    • 10.1016/j.ab.2006.02.007 1:CAS:528:DC%2BD28XjvFSiu7w%3D
    • Holm A, Rise F, Sessler N, Sollid LM, Undheim K, Fleckenstein B (2006) Specific modification of peptide-bound citrulline residues. Anal Biochem 352(1):68-76
    • (2006) Anal Biochem , vol.352 , Issue.1 , pp. 68-76
    • Holm, A.1    Rise, F.2    Sessler, N.3    Sollid, L.M.4    Undheim, K.5    Fleckenstein, B.6
  • 16
  • 17
    • 69249152923 scopus 로고    scopus 로고
    • Targeted analysis of protein citrullination using chemical modification and tandem mass spectrometry
    • 10.1002/rcm.4185 1:CAS:528:DC%2BD1MXpsl2jsro%3D
    • Stensland M, Holm A, Kiehne A, Fleckenstein B (2009) Targeted analysis of protein citrullination using chemical modification and tandem mass spectrometry. Rapid Commun Mass Spectrom 23(17):2754-2762
    • (2009) Rapid Commun Mass Spectrom , vol.23 , Issue.17 , pp. 2754-2762
    • Stensland, M.1    Holm, A.2    Kiehne, A.3    Fleckenstein, B.4
  • 18
    • 79956303758 scopus 로고    scopus 로고
    • Modification of citrulline residues with 2,3-butanedione facilitates their detection by liquid chromatography/mass spectrometry
    • 10.1002/rcm.5015
    • De Ceuleneer M, De Wit V, Van Steendam K, Van Nieuwerburgh F, Tilleman K, Deforce D (2011) Modification of citrulline residues with 2,3-butanedione facilitates their detection by liquid chromatography/mass spectrometry. Rapid Commun Mass Spectrom 25(11):1536-1542
    • (2011) Rapid Commun Mass Spectrom , vol.25 , Issue.11 , pp. 1536-1542
    • De Ceuleneer, M.1    De Wit, V.2    Van Steendam, K.3    Van Nieuwerburgh, F.4    Tilleman, K.5    Deforce, D.6
  • 19
    • 62149126994 scopus 로고    scopus 로고
    • Neutral loss of isocyanic acid in peptide CID spectra: A novel diagnostic marker for mass spectrometric identification of protein citrullination
    • 10.1016/j.jasms.2008.12.012
    • Hao G, Wang D, Gu J, Shen Q, Gross SS, Wang Y (2008) Neutral loss of isocyanic acid in peptide CID spectra: a novel diagnostic marker for mass spectrometric identification of protein citrullination. J Am Soc Mass Spectrom 20(4):723-727
    • (2008) J Am Soc Mass Spectrom , vol.20 , Issue.4 , pp. 723-727
    • Hao, G.1    Wang, D.2    Gu, J.3    Shen, Q.4    Gross, S.S.5    Wang, Y.6
  • 20
    • 84867544956 scopus 로고    scopus 로고
    • Seeing citrulline: Development of a phenylglyoxal-based probe to visualize protein citrullination
    • 10.1021/ja308871v 1:CAS:528:DC%2BC38XhsVGqtbzJ
    • Bicker KL, Subramanian V, Chumanevich AA, Hofseth LJ, Thompson PR (2012) Seeing citrulline: development of a phenylglyoxal-based probe to visualize protein citrullination. J Am Chem Soc 134(41):17015-17018
    • (2012) J Am Chem Soc , vol.134 , Issue.41 , pp. 17015-17018
    • Bicker, K.L.1    Subramanian, V.2    Chumanevich, A.A.3    Hofseth, L.J.4    Thompson, P.R.5
  • 21
    • 84875958816 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization-time of flight mass spectrometry identification of peptide citrullination site using Br signature
    • 10.1016/j.ab.2013.03.003 1:CAS:528:DC%2BC3sXlvVWnsrs%3D
    • Choi M, Song JS, Kim HJ, Cha S, Lee EY (2013) Matrix-assisted laser desorption ionization-time of flight mass spectrometry identification of peptide citrullination site using Br signature. Anal Biochem 437(1):62-67
    • (2013) Anal Biochem , vol.437 , Issue.1 , pp. 62-67
    • Choi, M.1    Song, J.S.2    Kim, H.J.3    Cha, S.4    Lee, E.Y.5
  • 22
    • 77953361021 scopus 로고    scopus 로고
    • A technique for the specific enrichment of citrulline-containing peptides
    • 10.1016/j.ab.2010.04.012 1:CAS:528:DC%2BC3cXmvVWhsLc%3D
    • Tutturen AE, Holm A, Jorgensen M, Stadtmuller P, Rise F, Fleckenstein B (2010) A technique for the specific enrichment of citrulline-containing peptides. Anal Biochem 403(1-2):43-51
    • (2010) Anal Biochem , vol.403 , Issue.1-2 , pp. 43-51
    • Tutturen, A.E.1    Holm, A.2    Jorgensen, M.3    Stadtmuller, P.4    Rise, F.5    Fleckenstein, B.6
  • 23
    • 0018039687 scopus 로고
    • A new RNA-RNA crosslinking reagent and its application to ribosomal 5S RNA
    • 10.1093/nar/5.11.4065 1:CAS:528:DyaE1MXltFSmtg%3D%3D
    • Wagner R, Garrett RA (1978) A new RNA-RNA crosslinking reagent and its application to ribosomal 5S RNA. Nucleic Acids Res 5(11):4065-4075
    • (1978) Nucleic Acids Res , vol.5 , Issue.11 , pp. 4065-4075
    • Wagner, R.1    Garrett, R.A.2
  • 24
    • 3042662113 scopus 로고    scopus 로고
    • In silico proteome analysis to facilitate proteomics experiments using mass spectrometry
    • 10.1186/1477-5956-1-5
    • Cagney G, Amiri S, Premawaradena T, Lindo M, Emili A (2003) In silico proteome analysis to facilitate proteomics experiments using mass spectrometry. Proteome Sci 1(1):5-19
    • (2003) Proteome Sci , vol.1 , Issue.1 , pp. 5-19
    • Cagney, G.1    Amiri, S.2    Premawaradena, T.3    Lindo, M.4    Emili, A.5
  • 25
    • 59949090515 scopus 로고    scopus 로고
    • Primary sequence, together with other factors, influence peptide deimination by peptidylarginine deiminase-4
    • 10.1515/BC.2009.019 1:CAS:528:DC%2BD1MXhvVajsrs%3D
    • Stensland ME, Pollmann S, Molberg O, Sollid LM, Fleckenstein B (2009) Primary sequence, together with other factors, influence peptide deimination by peptidylarginine deiminase-4. Biol Chem 390(2):99-107
    • (2009) Biol Chem , vol.390 , Issue.2 , pp. 99-107
    • Stensland, M.E.1    Pollmann, S.2    Molberg, O.3    Sollid, L.M.4    Fleckenstein, B.5
  • 26
    • 33845921213 scopus 로고    scopus 로고
    • Site-selective modifications of arginine residues in human hemoglobin induced by methylglyoxal
    • 10.1021/bi061410o 1:CAS:528:DC%2BD28XhtlChurrF
    • Gao Y, Wang Y (2006) Site-selective modifications of arginine residues in human hemoglobin induced by methylglyoxal. Biochemistry 45(51):15654-15660
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15654-15660
    • Gao, Y.1    Wang, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.