메뉴 건너뛰기




Volumn 393, Issue 1, 2009, Pages 41-47

Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry

Author keywords

Hierarchical phosphorylation; Interference of phosphorylation with proteolysis; Mass spectrometry; Mutually exclusive phosphorylation; PfCDPK1; PfGAP45; Phosphorylation

Indexed keywords

AFFINITY CHROMATOGRAPHY; DRUG PRODUCTS; ELECTROSPRAY IONIZATION; ENZYMES; GALLIUM COMPOUNDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEOLYSIS;

EID: 67651004664     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.06.022     Document Type: Article
Times cited : (23)

References (20)
  • 1
    • 20444407262 scopus 로고    scopus 로고
    • Dual phosphorylation of Mycoplasma pneumoniae HPr by enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr
    • Halbedel S., and Stulke J. Dual phosphorylation of Mycoplasma pneumoniae HPr by enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr. FEMS Microbiol. Lett. 247 (2005) 193-198
    • (2005) FEMS Microbiol. Lett. , vol.247 , pp. 193-198
    • Halbedel, S.1    Stulke, J.2
  • 5
    • 1842479262 scopus 로고    scopus 로고
    • In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner
    • Tang H.Y., and Speicher D.W. In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner. Biochemistry 43 (2004) 4251-4262
    • (2004) Biochemistry , vol.43 , pp. 4251-4262
    • Tang, H.Y.1    Speicher, D.W.2
  • 6
    • 0030595057 scopus 로고    scopus 로고
    • Stability characteristics of chemically-modified soluble trypsin
    • Murphy A., and Fagain C.O. Stability characteristics of chemically-modified soluble trypsin. J. Biotechnol. 49 (1996) 163-171
    • (1996) J. Biotechnol. , vol.49 , pp. 163-171
    • Murphy, A.1    Fagain, C.O.2
  • 7
    • 0034060128 scopus 로고    scopus 로고
    • Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion
    • Thiede B., Lamer S., Mattow J., Siejak F., Dimmler C., Rudel T., and Jungblut P.R. Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion. Rapid Commun. Mass Spectrom. 14 (2000) 496-502
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 496-502
    • Thiede, B.1    Lamer, S.2    Mattow, J.3    Siejak, F.4    Dimmler, C.5    Rudel, T.6    Jungblut, P.R.7
  • 8
    • 0035863653 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry
    • Schlosser A., Pipkorn R., Bossemeyer D., and Lehmann W.D. Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry. Anal. Chem. 73 (2001) 170-176
    • (2001) Anal. Chem. , vol.73 , pp. 170-176
    • Schlosser, A.1    Pipkorn, R.2    Bossemeyer, D.3    Lehmann, W.D.4
  • 9
    • 33645855615 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex
    • Jones M.L., Kitson E.L., and Rayner J.C. Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex. Mol. Biochem. Parasitol. 147 (2006) 74-84
    • (2006) Mol. Biochem. Parasitol. , vol.147 , pp. 74-84
    • Jones, M.L.1    Kitson, E.L.2    Rayner, J.C.3
  • 12
    • 0027416648 scopus 로고
    • Gene structure and expression of an unusual protein-kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF hand calcium binding proteins
    • Zhao Y., Kappes B., and Franklin R.M. Gene structure and expression of an unusual protein-kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF hand calcium binding proteins. J. Biol. Chem. 268 (1993) 4347-4354
    • (1993) J. Biol. Chem. , vol.268 , pp. 4347-4354
    • Zhao, Y.1    Kappes, B.2    Franklin, R.M.3
  • 13
    • 0028121976 scopus 로고
    • Plasmodium falciparum calcium-dependent protein-kinase phosphorylates proteins of the host erythrocytic membrane
    • Zhao Y., Franklin R.M., and Kappes B. Plasmodium falciparum calcium-dependent protein-kinase phosphorylates proteins of the host erythrocytic membrane. Mol. Biochem. Parasitol. 66 (1994) 329-343
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 329-343
    • Zhao, Y.1    Franklin, R.M.2    Kappes, B.3
  • 14
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., and Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1 (2006) 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 15
    • 23744460968 scopus 로고    scopus 로고
    • Specificity of immobilized metal affinity-based IMAC/C18 tip enrichment of phosphopeptides for protein phosphorylation analysis
    • Kokubu M., Ishihama Y., Sato T., Nagasu T., and Oda Y. Specificity of immobilized metal affinity-based IMAC/C18 tip enrichment of phosphopeptides for protein phosphorylation analysis. Anal. Chem. 77 (2005) 5144-5154
    • (2005) Anal. Chem. , vol.77 , pp. 5144-5154
    • Kokubu, M.1    Ishihama, Y.2    Sato, T.3    Nagasu, T.4    Oda, Y.5
  • 16
    • 60849090764 scopus 로고    scopus 로고
    • Citrate boosts the performance of phosphopeptide analysis by UPLC-ESI-MS/MS
    • Winter D., Seidler J., Ziv Y., Shiloh Y., and Lehmann W.D. Citrate boosts the performance of phosphopeptide analysis by UPLC-ESI-MS/MS. J. Proteome Res. 8 (2009) 418-424
    • (2009) J. Proteome Res. , vol.8 , pp. 418-424
    • Winter, D.1    Seidler, J.2    Ziv, Y.3    Shiloh, Y.4    Lehmann, W.D.5
  • 18
    • 21744457120 scopus 로고    scopus 로고
    • Plants, symbiosis, and parasites: a calcium signalling connection
    • Harper J.F., and Harmon A. Plants, symbiosis, and parasites: a calcium signalling connection. Nat. Rev. Mol. Cell Biol. 6 (2005) 555-566
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 555-566
    • Harper, J.F.1    Harmon, A.2
  • 19
    • 0345547409 scopus 로고    scopus 로고
    • Neutral loss of amino acid residues from protonated peptides in collision-induced dissociation generates N- or C-terminal sequence ladders
    • Salek M., and Lehmann W.D. Neutral loss of amino acid residues from protonated peptides in collision-induced dissociation generates N- or C-terminal sequence ladders. J. Mass Spectrom. 38 (2003) 1143-1149
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1143-1149
    • Salek, M.1    Lehmann, W.D.2
  • 20
    • 51649095905 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry
    • Xia Q.W., Cheng D.M., Duong D.M., Gearing M., Lah J.J., Levey A.I., and Peng J.M. Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry. J. Proteome Res. 7 (2008) 2845-2851
    • (2008) J. Proteome Res. , vol.7 , pp. 2845-2851
    • Xia, Q.W.1    Cheng, D.M.2    Duong, D.M.3    Gearing, M.4    Lah, J.J.5    Levey, A.I.6    Peng, J.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.