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Volumn 2, Issue 7, 2007, Pages 1006-1009

Importance of interaction between C1 domain and lipids in protein kinase Cα activation: Hydrophobic side chain direction in isobenzofuranone ligands controls enzyme activation level

Author keywords

Isobenzofuranone; Kinase modulators; Molecular modeling; Protein kinase C ; Structure activity relationships

Indexed keywords

FURAN DERIVATIVE; LIGAND; PROTEIN KINASE C ALPHA;

EID: 49649129954     PISSN: 18607179     EISSN: 18607187     Source Type: Journal    
DOI: 10.1002/cmdc.200700080     Document Type: Article
Times cited : (10)

References (29)
  • 8
    • 27744443750 scopus 로고    scopus 로고
    • and references therein. For a discussion of the activation mechanism of PKCα, see
    • For a discussion of the activation mechanism of PKCα, see: R. V. Stahelin, J. Wang, N. R. Blatner, J. D. Rafter, D. Murray, W. Cho, J. Biol. Chem. 2005, 280, 36452, and references therein.
    • (2005) J. Biol. Chem , vol.280 , pp. 36452
    • Stahelin, R.V.1    Wang, J.2    Blatner, N.R.3    Rafter, J.D.4    Murray, D.5    Cho, W.6
  • 9
    • 0344443708 scopus 로고    scopus 로고
    • The C1A and C1B domains of PKCα are proposed to have opposite affinities for DAG and phorbol ester; that is, phorbol ester has high affinity for the C1B domain of PKCα. See: a B. Ananthanarayanan, R. V. Stahelin, M. A. Digman, W. Cho, J. Biol. Chem. 2003, 278, 46886;
    • The C1A and C1B domains of PKCα are proposed to have opposite affinities for DAG and phorbol ester; that is, phorbol ester has high affinity for the C1B domain of PKCα. See: a) B. Ananthanarayanan, R. V. Stahelin, M. A. Digman, W. Cho, J. Biol. Chem. 2003, 278, 46886;
  • 10
    • 0034903846 scopus 로고    scopus 로고
    • M. Shindo, K. Irie, A. Nakahara, H. Ohigashi, H. Konishi, U. Kikkawa, H. Fukuda, P. A. Wender, Bioorg. Med. Chem. 2001, 9, 2073. Although it is possible that the C1A domain also contributes to phorbol ester binding, in this paper we focus on C1B domain to simplify the discussion. See, also reference [8g
    • b) M. Shindo, K. Irie, A. Nakahara, H. Ohigashi, H. Konishi, U. Kikkawa, H. Fukuda, P. A. Wender, Bioorg. Med. Chem. 2001, 9, 2073. Although it is possible that the C1A domain also contributes to phorbol ester binding, in this paper we focus on C1B domain to simplify the discussion. See, also reference [8g].
  • 16
    • 33646448125 scopus 로고    scopus 로고
    • and references therein;
    • b) P. A. Wender, V. A. Verma, Org. Lett. 2006, 8, 1893, and references therein;
    • (2006) Org. Lett , vol.8 , pp. 1893
    • Wender, P.A.1    Verma, V.A.2
  • 22
    • 0032554112 scopus 로고    scopus 로고
    • Phorbol ester derivatives having a hydrophilic side chain have been reported to act as inhibitors; a M. Sodeoka, M. A. Arai, K. Adachi, K. Uotsu, M. Shibasaki, J. Am. Chem. Soc. 1998, 120, 457;
    • Phorbol ester derivatives having a hydrophilic side chain have been reported to act as inhibitors; a) M. Sodeoka, M. A. Arai, K. Adachi, K. Uotsu, M. Shibasaki, J. Am. Chem. Soc. 1998, 120, 457;
  • 24
    • 0025784927 scopus 로고    scopus 로고
    • A few PKC inhibitors are reported to bind C1 domain; a R. F. Bruns, F. D. Miller, R. L. Merriman, J. J. Howbert, W. F. Heath, E. Kobayashi, I. Takahashi, T. Tamaoki, H. Nakano, Biochem. Biophys. Res. Commun. 1991, 176, 288;
    • A few PKC inhibitors are reported to bind C1 domain; a) R. F. Bruns, F. D. Miller, R. L. Merriman, J. J. Howbert, W. F. Heath, E. Kobayashi, I. Takahashi, T. Tamaoki, H. Nakano, Biochem. Biophys. Res. Commun. 1991, 176, 288;


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.