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Volumn 32, Issue 5, 2006, Pages 369-374

Study on the hydrolysis mechanism of phosphodiesterase 4 using molecular dynamics simulations

Author keywords

cAMP; Hydration pattern; Hydrolysis mechanism; Molecular dynamics simulation; PDE4

Indexed keywords

COMPUTER SIMULATION; DRUG PRODUCTS; HYDRATION; HYDROGEN BONDS; HYDROLYSIS; MOLECULAR DYNAMICS;

EID: 33748534489     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020600717111     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 0028802726 scopus 로고
    • Cyclic nucleotide. phosphodiesterases; functional implications of multiple isoforms
    • J.A. Beavo. Cyclic nucleotide. phosphodiesterases; functional implications of multiple isoforms. Physiol, Rev., 75, 725 (1995).
    • (1995) Physiol, Rev. , vol.75 , pp. 725
    • Beavo, J.A.1
  • 2
    • 0033761535 scopus 로고    scopus 로고
    • Phosphodiesterases and cyclic nucleotide. signaling in endocrine cells
    • M. Conti. Phosphodiesterases and cyclic nucleotide. signaling in endocrine cells. Mol. Endocrinol., 14, 1317 (2002).
    • (2002) Mol. Endocrinol. , vol.14 , pp. 1317
    • Conti, M.1
  • 3
    • 0032605044 scopus 로고    scopus 로고
    • The molecular biology of cyclic nucleotide. phosphodiesterases
    • M. Conti, S.L. Jon. The molecular biology of cyclic nucleotide. phosphodiesterases. Prog. Nucleic Acid Res. Mol. Biol., 63, 1 (1999).
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.63 , pp. 1
    • Conti, M.1    Jon, S.L.2
  • 4
    • 0034009080 scopus 로고    scopus 로고
    • Regulation of cAMP and cGMP signaling; new phosphodiesterases and new functions
    • S.H. Soderling, J.A. Beavo. Regulation of cAMP and cGMP signaling; new phosphodiesterases and new functions. Curr. Opin. Cell. Biol., 12, 174 (2000).
    • (2000) Curr. Opin. Cell. Biol. , vol.12 , pp. 174
    • Soderling, S.H.1    Beavo, J.A.2
  • 8
    • 0036729478 scopus 로고    scopus 로고
    • Cyclic nucleotide. research still expanding after half a century
    • J.A. Beavo, L.L. Brunton. Cyclic nucleotide. research still expanding after half a century. Nat. Rev. Mol. Cell Biol., 3, 710 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 710
    • Beavo, J.A.1    Brunton, L.L.2
  • 10
    • 0027241030 scopus 로고
    • Novel phosphodiesterase inhibitors for the therapy of asthma
    • T.J. Torphy, G.P. Livi, S.B. Christensen. Novel phosphodiesterase inhibitors for the therapy of asthma. Drug News Perspect., 6, 537 (1993).
    • (1993) Drug News Perspect. , vol.6 , pp. 537
    • Torphy, T.J.1    Livi, G.P.2    Christensen, S.B.3
  • 11
    • 0001302572 scopus 로고
    • Phosphodiesterase inhibitors as antiasthmatic agents
    • Academic Press, New York
    • M.N. Palfreyman. Phosphodiesterase inhibitors as antiasthmatic agents. In Annual Reports in Medicinal Chemistry, Vol.29, p. 185, Academic Press, New York (1994).
    • (1994) Annual Reports in Medicinal Chemistry , vol.29 , pp. 185
    • Palfreyman, M.N.1
  • 13
    • 0030984966 scopus 로고    scopus 로고
    • Phosphodiesterase (PDE) 4 inhibitors; anti-inflammatory drugs of the future?
    • M.M. Teixeira, R.W. Gristwood, N. Cooper, P.O. Hallewell. Phosphodiesterase (PDE) 4 inhibitors; anti-inflammatory drugs of the future? TIPS, 18, 164 (1997).
    • (1997) TIPS , vol.18 , pp. 164
    • Teixeira, M.M.1    Gristwood, R.W.2    Cooper, N.3    Hallewell, P.O.4
  • 14
    • 0242401840 scopus 로고    scopus 로고
    • The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterases catalysts
    • Q. Huai, J. Colicelli, H. Ke. The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterases catalysts. Biochemistry, 42, 13220 (2003).
    • (2003) Biochemistry , vol.42 , pp. 13220
    • Huai, Q.1    Colicelli, J.2    Ke, H.3
  • 15
    • 1842581748 scopus 로고    scopus 로고
    • Crystal structure of phosphodiesterases 4 and 5 in complex with inhibitor IBMX suggest a conformation determinant of inhibitor selectivity
    • Q. Huai, Y. Liu, S.H. Francis, J.D. Corbin, H. Ke. Crystal structure of phosphodiesterases 4 and 5 in complex with inhibitor IBMX suggest a conformation determinant of inhibitor selectivity. J. Biol. Chem., 279, 13095 (2003).
    • (2003) J. Biol. Chem. , vol.279 , pp. 13095
    • Huai, Q.1    Liu, Y.2    Francis, S.H.3    Corbin, J.D.4    Ke, H.5
  • 16
    • 0038154006 scopus 로고    scopus 로고
    • Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity
    • Q. Huai. H. Wang, Y. Sun, H.Y. Kim, Y. Liu, H. Ke. Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity. Structure (Camb), 11, 865 (2003).
    • (2003) Structure (Camb) , vol.11 , pp. 865
    • Huai, Q.1    Wang, H.2    Sun, Y.3    Kim, H.Y.4    Liu, Y.5    Ke, H.6
  • 17
    • 3042795876 scopus 로고    scopus 로고
    • Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding
    • Q. Huai, H. Wang, W. Zhang, R.W. Colman, H. Robinson, H. Ke. Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding. Proc. Natl. Acad. Sci. USA, 101, 9624 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9624
    • Huai, Q.1    Wang, H.2    Zhang, W.3    Colman, R.W.4    Robinson, H.5    Ke, H.6
  • 18
    • 0037163858 scopus 로고    scopus 로고
    • Crystal structure of phosphodiesterase 4D and inhibitor complex
    • M.E. Lee, J. Markowitz, J.O. Lee, H. Lee. Crystal structure of phosphodiesterase 4D and inhibitor complex. FEBS Lett., 530, 53 (2002).
    • (2002) FEBS Lett. , vol.530 , pp. 53
    • Lee, M.E.1    Markowitz, J.2    Lee, J.O.3    Lee, H.4
  • 21
    • 1442323778 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of phosphodiesterase 4B complexed with amp 8-br-AMP, and rolipram
    • R.X. Xu, W.J. Rocque, M.H. Lambert, D.E. Vanderwall, M.A. Luther, R.T. Nolte. Crystal structure of the catalytic domain of phosphodiesterase 4B complexed with amp 8-br-AMP, and rolipram. J. Mol. Biol., 337, 355 (2004).
    • (2004) J. Mol. Biol. , vol.337 , pp. 355
    • Xu, R.X.1    Rocque, W.J.2    Lambert, M.H.3    Vanderwall, D.E.4    Luther, M.A.5    Nolte, R.T.6
  • 24
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, Y. Zhang, R.W. Pastor. Constant pressure molecular dynamics simulation: the Langevin piston method. J. Chem. Phys., 103, 4613 (1995).
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3
  • 26
    • 0030781893 scopus 로고    scopus 로고
    • Site-directed mutation study on hyper thermostability of rubredoxin from pyrococcus furiosus using molecular dynamics simulations in solution
    • D.H. Jung, N.S. Kang, M.S. Jhon. Site-directed mutation study on hyper thermostability of rubredoxin from pyrococcus furiosus using molecular dynamics simulations in solution. J. Phys. Chem., 101, 466 (1997).
    • (1997) J. Phys. Chem. , vol.101 , pp. 466
    • Jung, D.H.1    Kang, N.S.2    Jhon, M.S.3
  • 27
    • 0030981608 scopus 로고    scopus 로고
    • Role of conserved histidines in catalytic activity and inhibitor binding of human recombinant phosphodiesterase 4A
    • S. Jacobitz, M.D. Ryan, M.M. McLaughlin, G.P. Livi, W.E. Dewolf, T.J. Torphy. Role of conserved histidines in catalytic activity and inhibitor binding of human recombinant phosphodiesterase 4A. Mol. Pharmacol., 51, 999 (1997).
    • (1997) Mol. Pharmacol. , vol.51 , pp. 999
    • Jacobitz, S.1    Ryan, M.D.2    McLaughlin, M.M.3    Livi, G.P.4    Dewolf, W.E.5    Torphy, T.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.