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Volumn 6, Issue 5, 1997, Pages 1110-1113

Identification and structural influence of a differentially modified N- terminal methionine in human S100b

Author keywords

calcium binding protein; mass spectrometry; N terminal formylation; protein heterogeneity; S100 protein

Indexed keywords

CALCIUM BINDING PROTEIN; PROTEIN S 100;

EID: 0030895690     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060518     Document Type: Article
Times cited : (20)

References (20)
  • 1
    • 0014413570 scopus 로고
    • On the release of the formyl group from nascent protein
    • Adams JM. 1968. On the release of the formyl group from nascent protein J Mol Biol 33:571-589.
    • (1968) J Mol Biol , vol.33 , pp. 571-589
    • Adams, J.M.1
  • 3
    • 0000808942 scopus 로고
    • The folding, stability and dynamics of T4 lysozyme: A perspective using nuclear magnetic resonance
    • Clore GM, Gronenborn AM, eds. London: McMillan Press
    • Anderson DE, Lu J, McIntosh L, Dahlquist FW. 1993. The folding, stability and dynamics of T4 lysozyme: A perspective using nuclear magnetic resonance. In: Clore GM, Gronenborn AM, eds. NMR of proteins. London: McMillan Press, pp 258-304.
    • (1993) NMR of Proteins , pp. 258-304
    • Anderson, D.E.1    Lu, J.2    McIntosh, L.3    Dahlquist, F.W.4
  • 4
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • Arfin SM, Bradshaw RA. 1989. Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry 27:7979-7984.
    • (1989) Biochemistry , vol.27 , pp. 7979-7984
    • Arfin, S.M.1    Bradshaw, R.A.2
  • 5
    • 0023135722 scopus 로고
    • Processing of the initiator methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S. 1987. Processing of the initiator methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure. J Bacteriol 169:751-757.
    • (1987) J Bacteriol , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 6
    • 0027953502 scopus 로고
    • Analysis of protein modifications: Recent advances in detection, characterization and mapping
    • Bradshaw RA, Stewart AE. 1994. Analysis of protein modifications: Recent advances in detection, characterization and mapping Curr Opin Biotech 5:85-93.
    • (1994) Curr Opin Biotech , vol.5 , pp. 85-93
    • Bradshaw, R.A.1    Stewart, A.E.2
  • 9
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gagne SM, Tsuda S, Li MX, Chandra M, Smillie LB, Sykes BD. 1994. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci 3:1961-1974.
    • (1994) Protein Sci , vol.3 , pp. 1961-1974
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 10
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sites than insights
    • Heizmann CW, Hunziker W. 1991. Intracellular calcium-binding proteins: More sites than insights. Trends Biochem Sci 16:98-103.
    • (1991) Trends Biochem Sci , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 11
    • 0027244568 scopus 로고
    • Analytical and micropreparative peptide mapping by high performance liquid chromatography/electrospray mass spectrometry of proteins purified by gel electrophoresis
    • Hess D, Covey TC, Winz R, Brownsey RW, Aebersold R. 1993. Analytical and micropreparative peptide mapping by high performance liquid chromatography/electrospray mass spectrometry of proteins purified by gel electrophoresis. Protein Sci 2:1342-1351.
    • (1993) Protein Sci , vol.2 , pp. 1342-1351
    • Hess, D.1    Covey, T.C.2    Winz, R.3    Brownsey, R.W.4    Aebersold, R.5
  • 12
    • 0002692362 scopus 로고
    • The S-100 protein family: A biochemical and functional overview
    • Heizmann CW, ed. Novel calcium-binding proteins. Berlin: Springer-Verlag
    • Hilt DC, Kligman D. 1991. The S-100 protein family: A biochemical and functional overview. In: Heizmann CW, ed. Novel calcium-binding proteins. Fundamentals and clinical implications. Berlin: Springer-Verlag. pp 65-103.
    • (1991) Fundamentals and Clinical Implications , pp. 65-103
    • Hilt, D.C.1    Kligman, D.2
  • 13
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel H, Schmitter JM, Dessen P, Fayat G, Blanquet S. 1989. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc Natl Acad Sci USA 86:8247-8251.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8247-8251
    • Hirel, H.1    Schmitter, J.M.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 14
    • 0028951155 scopus 로고
    • Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein
    • Kilby PM, Van Eldik LJ, Roberts GCK. 1995 Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein FEBS Lett 363:90-96.
    • (1995) FEBS Lett , vol.363 , pp. 90-96
    • Kilby, P.M.1    Van Eldik, L.J.2    Roberts, G.C.K.3
  • 15
    • 0030587521 scopus 로고    scopus 로고
    • The solution structure of the bovine S100b dimer in the calcium-free state
    • Kilby PM, Van Eldik LJ, Roberts GCK. 1996. The solution structure of the bovine S100b dimer in the calcium-free state. Structure 4:1041-1052.
    • (1996) Structure , vol.4 , pp. 1041-1052
    • Kilby, P.M.1    Van Eldik, L.J.2    Roberts, G.C.K.3
  • 17
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme in eubacterial translation
    • Mazel D, Pochel S, Marliere P. 1994. Genetic characterization of polypeptide deformylase, a distinctive enzyme in eubacterial translation. EMBO J 13:914-923.
    • (1994) EMBO J , vol.13 , pp. 914-923
    • Mazel, D.1    Pochel, S.2    Marliere, P.3
  • 18
    • 0025076172 scopus 로고
    • The fats of life: Importance and function of protein acylation
    • McIlhinney RAJ. 1990. The fats of life: Importance and function of protein acylation. Trends Biochem Sci 15:387-391.
    • (1990) Trends Biochem Sci , vol.15 , pp. 387-391
    • McIlhinney, R.A.J.1
  • 20
    • 0030016315 scopus 로고    scopus 로고
    • Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface
    • Smith SP, Barber KR, Dunn SD, Shaw GS. 1996. Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface. Biochemistry 35:8805-8814.
    • (1996) Biochemistry , vol.35 , pp. 8805-8814
    • Smith, S.P.1    Barber, K.R.2    Dunn, S.D.3    Shaw, G.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.