메뉴 건너뛰기




Volumn 266, Issue 3, 1999, Pages 161-164

The developmental expression and activity of peptidylarginine deiminase in the mouse

Author keywords

Brain; Citrulline; Demyelination; Myelin; Myelin basic protein; Peptidylarginine deiminase

Indexed keywords

PROTEIN ARGININE DEIMINASE;

EID: 0033553648     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(99)00276-1     Document Type: Article
Times cited : (32)

References (17)
  • 1
    • 0032527897 scopus 로고    scopus 로고
    • The mechanism of demyelination in DM20 transgenic mice involves increased fatty acylation
    • Barrese N., Mak B., Fisher L., Moscarello M.A. The mechanism of demyelination in DM20 transgenic mice involves increased fatty acylation. J. Neurosci. Res. 53:1998;143-152.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 143-152
    • Barrese, N.1    Mak, B.2    Fisher, L.3    Moscarello, M.A.4
  • 2
    • 0021881685 scopus 로고
    • Characterization of myelin fractions from human brain white matter
    • Cruz T.F., Moscarello M.A. Characterization of myelin fractions from human brain white matter. J. Neurochem. 44:1985;1411-1418.
    • (1985) J. Neurochem. , vol.44 , pp. 1411-1418
    • Cruz, T.F.1    Moscarello, M.A.2
  • 3
    • 0025367237 scopus 로고
    • Myelin basic protein is affected by reduced synthesis of myelin proteolipid protein in the jimpy mouse
    • Fannon A., Moscarello M.A. Myelin basic protein is affected by reduced synthesis of myelin proteolipid protein in the jimpy mouse. Biochem. J. 268:1990;105-110.
    • (1990) Biochem. J. , vol.268 , pp. 105-110
    • Fannon, A.1    Moscarello, M.A.2
  • 4
    • 0028914527 scopus 로고
    • Studies of calcineurin-calmodulin interaction: Probing the role of arginine residues using peptidylarginine deimase
    • Imparl J.M., Senshu T., Graves D.J. Studies of calcineurin-calmodulin interaction: probing the role of arginine residues using peptidylarginine deimase. Arch. Biochem. Biophys. 318:1995;370-377.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 370-377
    • Imparl, J.M.1    Senshu, T.2    Graves, D.J.3
  • 5
    • 0024473081 scopus 로고
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J. Biol. Chem. 264:1989;18119-18127.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18119-18127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 6
    • 0021114827 scopus 로고
    • Purification and properties of a brain enzyme which deiminates proteins
    • Kubilus J., Baden H.P. Purification and properties of a brain enzyme which deiminates proteins. Biochim. Biophys. Acta. 745:1983;285-291.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 285-291
    • Kubilus, J.1    Baden, H.P.2
  • 7
    • 0013904886 scopus 로고
    • The isolation and characterization of an acid soluble protein from myelin
    • Lowden J.A., Morecki R., Moscarello M.A. The isolation and characterization of an acid soluble protein from myelin. Can. J. Biochem. 44:1965;1829.
    • (1965) Can. J. Biochem. , vol.44 , pp. 1829
    • Lowden, J.A.1    Morecki, R.2    Moscarello, M.A.3
  • 8
    • 0028903763 scopus 로고
    • Enzymatic deimination of glycogen phosphorylase and a peptide of the phosphorylation site: Identification of modification and roles in phosphorylation and activity
    • Luo S., Martin B.L., Senshu T., Graves D.J. Enzymatic deimination of glycogen phosphorylase and a peptide of the phosphorylation site: identification of modification and roles in phosphorylation and activity. Arch. Biochem. Biophys. 318:1995;362-369.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 362-369
    • Luo, S.1    Martin, B.L.2    Senshu, T.3    Graves, D.J.4
  • 10
    • 0030885947 scopus 로고    scopus 로고
    • Characterization of myelin basic protein charge microheterogeneity in developing mouse brain and in the transgenic shiverer mutant
    • Palma A.E., Owh P., Fredric C., Readhead C., Moscarello M.A. Characterization of myelin basic protein charge microheterogeneity in developing mouse brain and in the transgenic shiverer mutant. J. Neurochem. 69:1997;1753-1762.
    • (1997) J. Neurochem. , vol.69 , pp. 1753-1762
    • Palma, A.E.1    Owh, P.2    Fredric, C.3    Readhead, C.4    Moscarello, M.A.5
  • 11
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al.which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al.which is more generally applicable. Ann. Biochem. 83:1977;346-356.
    • (1977) Ann. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 12
    • 0032517246 scopus 로고    scopus 로고
    • A novel microtubule independent effect of paclitaxel: The inhibition of peptidylarginine deiminase from bovine brain
    • Pritzker L.B., Moscarello M.A. A novel microtubule independent effect of paclitaxel: the inhibition of peptidylarginine deiminase from bovine brain. Biochim. Biophys. Acta. 1388:1998;154-160.
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 154-160
    • Pritzker, L.B.1    Moscarello, M.A.2
  • 13
    • 0000358910 scopus 로고
    • Presence of citrulline residue derivation enzyme in the newborn rat epidermis
    • Sugawara K., Fuzisaki M. Presence of citrulline residue derivation enzyme in the newborn rat epidermis. Agr. Biol. Chem. 43:1979;2407-2408.
    • (1979) Agr. Biol. Chem. , vol.43 , pp. 2407-2408
    • Sugawara, K.1    Fuzisaki, M.2
  • 14
    • 0020106254 scopus 로고
    • Identification and properties of peptidylarginine deiminase from rabbit skeletal muscle
    • Sugawara K., Oikawa T., Ouchi J. Identification and properties of peptidylarginine deiminase from rabbit skeletal muscle. J. Biochem. 91:1982;1065-1071.
    • (1982) J. Biochem. , vol.91 , pp. 1065-1071
    • Sugawara, K.1    Oikawa, T.2    Ouchi, J.3
  • 15
    • 0030784777 scopus 로고    scopus 로고
    • The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases
    • Tarcsa E., Merekov L.N., Andreoli J., Idler W.W., Candi E., Chung S.I., Steinert P.M. The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases. J. Biol. Chem. 272:1997;27893-27901.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27893-27901
    • Tarcsa, E.1    Merekov, L.N.2    Andreoli, J.3    Idler, W.W.4    Candi, E.5    Chung, S.I.6    Steinert, P.M.7
  • 17
    • 0029927069 scopus 로고    scopus 로고
    • Acute multiple sclerosis (Marburg type) is associated with extensive modifications of myelin basic protein
    • Wood D.D., Bilbao J., O'Connors P., Moscarello M.A. Acute multiple sclerosis (Marburg type) is associated with extensive modifications of myelin basic protein. Ann. Neurol. 40:1996;18-24.
    • (1996) Ann. Neurol. , vol.40 , pp. 18-24
    • Wood, D.D.1    Bilbao, J.2    O'Connors, P.3    Moscarello, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.