메뉴 건너뛰기




Volumn 2, Issue 4, 2005, Pages 319-324

Perspectives in proteomics: Structural folds of a predicted and an experimentally determined cation channel

Author keywords

ATP activated purinergic receptor; Cation channel; KcsA protein; P2x receptor; Proteomics; Structural bioinformatics

Indexed keywords

STREPTOMYCES LIVIDANS;

EID: 31144438893     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016405775201775     Document Type: Review
Times cited : (3)

References (36)
  • 1
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Auth, D. M., Cortes, Cuello, L. G. and Perozo, E. (2001). Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117: 165-80.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Auth, D.M.1    Cortes2    Cuello, L.G.3    Perozo, E.4
  • 2
    • 0029916915 scopus 로고    scopus 로고
    • The PROSITE database
    • Bairoch, A. (1996). The PROSITE database. Nucleic Acid Res. 24: 189-96.
    • (1996) Nucleic Acid Res. , vol.24 , pp. 189-196
    • Bairoch, A.1
  • 3
    • 0037079576 scopus 로고    scopus 로고
    • The elastic net algorithm and protein structure prediction
    • Ball, K. D., Erman, B. and Dill, K. A. (2002). The elastic net algorithm and protein structure prediction. J. Comput. Chem. 23: 77-83.
    • (2002) J. Comput. Chem. , vol.23 , pp. 77-83
    • Ball, K.D.1    Erman, B.2    Dill, K.A.3
  • 4
    • 3042806532 scopus 로고    scopus 로고
    • Introduction: P2 receptors
    • Burnstock, G. (2004). Introduction: P2 receptors. Curr. Top. Med. Chem. 4: 793-803.
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 793-803
    • Burnstock, G.1
  • 6
    • 0036891697 scopus 로고    scopus 로고
    • Long membrane helices and short loops predicted less accurately
    • Chen, C. P. and Rost, B. (2002a). Long membrane helices and short loops predicted less accurately. Protein Sci. 11: 2766-73.
    • (2002) Protein Sci. , vol.11 , pp. 2766-2773
    • Chen, C.P.1    Rost, B.2
  • 7
    • 0001911218 scopus 로고    scopus 로고
    • State-of-the-art in membrane protein predictions
    • Chen, C. P. and Rost, B. (2002b). State-of-the-art in membrane protein predictions. Appl. Bioinformatics 1: 21-35.
    • (2002) Appl. Bioinformatics , vol.1 , pp. 21-35
    • Chen, C.P.1    Rost, B.2
  • 8
    • 0036893269 scopus 로고    scopus 로고
    • Transmembrane helix predictions revisited
    • Chen, C. P., Kernytsky, A. and Rost, B. (2002). Transmembrane helix predictions revisited. Protein Sci. 11: 2774-91.
    • (2002) Protein Sci. , vol.11 , pp. 2774-2791
    • Chen, C.P.1    Kernytsky, A.2    Rost, B.3
  • 9
    • 0037095757 scopus 로고    scopus 로고
    • Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor
    • Clyne, J. D., Wang, L.-F. and Hume, R. I. (2002). Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor. J. Neurosci. 22: 3873-80.
    • (2002) J. Neurosci. , vol.22 , pp. 3873-3880
    • Clyne, J.D.1    Wang, L.-F.2    Hume, R.I.3
  • 11
    • 0036154216 scopus 로고    scopus 로고
    • Conserved cysteine residues in the extracellular loop of the human P2X1 receptor form disulfide bonds and are involved in receptor trafficking to the cell surface
    • Ennion S. J. and Evans, R. J. (2002). Conserved cysteine residues in the extracellular loop of the human P2X1 receptor form disulfide bonds and are involved in receptor trafficking to the cell surface. Mol. Pharmacol. 61: 303-11.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 303-311
    • Ennion, S.J.1    Evans, R.J.2
  • 13
    • 0033566578 scopus 로고    scopus 로고
    • The role of evolutionary information in predicting the disulfide-bonding state of cysteines in proteins
    • Fariselli, P., Riccobelli, P. and Casadio, R. (1999). The role of evolutionary information in predicting the disulfide-bonding state of cysteines in proteins. Proteins 36: 340-6.
    • (1999) Proteins , vol.36 , pp. 340-346
    • Fariselli, P.1    Riccobelli, P.2    Casadio, R.3
  • 14
    • 0031668776 scopus 로고    scopus 로고
    • ATP binding site of P2X channel proteins: Structural similarities with class II aminoacyl-tRNA synthetases
    • Freist, W., Verhey, J. F., Stuhmer, W. and Gaus, D. H. (1998). ATP binding site of P2X channel proteins: structural similarities with class II aminoacyl-tRNA synthetases. FEBS Lett. 434: 61-5.
    • (1998) FEBS Lett. , vol.434 , pp. 61-65
    • Freist, W.1    Verhey, J.F.2    Stuhmer, W.3    Gaus, D.H.4
  • 15
    • 0038386050 scopus 로고    scopus 로고
    • 3-D Jury: A simple approach to improve protein structure predictions
    • Ginalski, E., Elofsson, A., Fischer, D. and Rychlewski, L. (2003). 3-D Jury: a simple approach to improve protein structure predictions. Bioinformatics 19:1015-8.
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, E.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 16
    • 0037307081 scopus 로고    scopus 로고
    • Molecular modeling of ion channels: Structural predictions
    • Giorgetti, A. and Carloni, P. (2003). Molecular modeling of ion channels: structural predictions. Curr. Opin. Chem. Biol. 7: 150-6.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 150-156
    • Giorgetti, A.1    Carloni, P.2
  • 17
    • 0037012653 scopus 로고    scopus 로고
    • P2X4 receptor is a glycosylated cardiac receptor mediating a positive inotropic response to ATP
    • Hu, B., Senkler, C., Yang, A., Soto, F. and Liang, B. T. (2002). P2X4 receptor is a glycosylated cardiac receptor mediating a positive inotropic response to ATP. J. Biol. Chem. 277: 15752-7.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15752-15757
    • Hu, B.1    Senkler, C.2    Yang, A.3    Soto, F.4    Liang, B.T.5
  • 18
    • 0346727217 scopus 로고    scopus 로고
    • Molecular physiology of P2 receptors in the central nervous system
    • Illes, P. and Ribeiro, J. (2004). Molecular physiology of P2 receptors in the central nervous system. Eur. J. Pharmacol. 483: 5-17.
    • (2004) Eur. J. Pharmacol. , vol.483 , pp. 5-17
    • Illes, P.1    Ribeiro, J.2
  • 19
    • 0035287474 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors and ATP signalling at synapses
    • Khakh, B. S. (2001). Molecular physiology of P2X receptors and ATP signalling at synapses. Nat. Rev. Neurosci. 2: 165-74.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 165-174
    • Khakh, B.S.1
  • 20
    • 0035890154 scopus 로고    scopus 로고
    • Proteomic and functional evidence for a P2X7 receptor signalling complex
    • Kim, M., Jiang, L.-H., Wilson, H. L., North, R. A. and Surprenant, A. (2001). Proteomic and functional evidence for a P2X7 receptor signalling complex. EMBO J. 20: 6347-58.
    • (2001) EMBO J. , vol.20 , pp. 6347-6358
    • Kim, M.1    Jiang, L.-H.2    Wilson, H.L.3    North, R.A.4    Surprenant, A.5
  • 21
    • 0030589514 scopus 로고    scopus 로고
    • Phi-Psi-chology: Ramachandran Revisited
    • Kleywegt, G. J. and Jones, T. A. (1996) Phi-Psi-chology: Ramachandran Revisited. Structure 4:1395-400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 22
    • 18744396365 scopus 로고    scopus 로고
    • P2X and P2Y receptors as possible targets of therapeutic manipulations in CNS illness
    • Köles, L., Fürst, S. and Illes, P. (2005). P2X and P2Y receptors as possible targets of therapeutic manipulations in CNS illness. Drug News Perspect. 18: 1-17.
    • (2005) Drug News Perspect. , vol.18 , pp. 1-17
    • Köles, L.1    Fürst, S.2    Illes, P.3
  • 26
    • 10644241979 scopus 로고    scopus 로고
    • Bridging the gap between structural bioinformatics and receptor research: The membrane-embedded, ligand-gated, P2X glycoprotein receptor
    • Mager, P. P., Weber, A. and Illes, P. (2004). Bridging the gap between structural bioinformatics and receptor research: the membrane-embedded, ligand-gated, P2X glycoprotein receptor. Curr. Topics Med. Chem.4: 1657-705.
    • (2004) Curr. Topics Med. Chem. , vol.4 , pp. 1657-1705
    • Mager, P.P.1    Weber, A.2    Illes, P.3
  • 27
    • 31144465703 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship analysis of the cation permeability of the P2X2 channel
    • Mager, P. P., Weber, A. and Illes, P. (2005a). Quantitative structure-activity relationship analysis of the cation permeability of the P2X2 channel. Med. Chem. 1: 109-15.
    • (2005) Med. Chem. , vol.1 , pp. 109-115
    • Mager, P.P.1    Weber, A.2    Illes, P.3
  • 28
    • 31144448632 scopus 로고    scopus 로고
    • The monomers of the P2X1 receptor model and KcsA protein share a similar structural fold
    • Mager, P. P., Weber, A., Sanchez, L., Wirkner, K. and Illes, P. (2005b). The monomers of the P2X1 receptor model and KcsA protein share a similar structural fold. Protein Pept. Lett. 13(1): 77-81.
    • (2005) Protein Pept. Lett. , vol.13 , Issue.1 , pp. 77-81
    • Mager, P.P.1    Weber, A.2    Sanchez, L.3    Wirkner, K.4    Illes, P.5
  • 29
    • 0033755889 scopus 로고    scopus 로고
    • Neuronal P2X receptors: Localisation and functional properties
    • Norenberg, W. and Illes, P. (2000). Neuronal P2X receptors: localisation and functional properties. Naunyn Schmiedebergs Arch. Pharmacol. 362: 324-39.
    • (2000) Naunyn Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 324-339
    • Norenberg, W.1    Illes, P.2
  • 30
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R. A. (2002). Molecular physiology of P2X receptors. Physiol. Rev. 82: 1013-67.
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 32
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profile
    • Pollastri, G., Przybylski, D., Rost, B. and Baldi, P. (2002). Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profile. Proteins 47: 228-35.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 33
    • 0035782925 scopus 로고    scopus 로고
    • Protein secondary structure prediction continues to rise
    • Rost, B. (2001). Protein secondary structure prediction continues to rise. J. Struct. Biol. 134: 204-18.
    • (2001) J. Struct. Biol. , vol.134 , pp. 204-218
    • Rost, B.1
  • 34
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B. and Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 35
    • 0028841033 scopus 로고
    • A prokyryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf, H., Schmidt, O., Kuemmerlen, R., Hinnah, S., Mueller, D., Betzler, M., Steinkamp, T. and Wagner, R. (1995). A prokyryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14: 5170-8.
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kuemmerlen, R.3    Hinnah, S.4    Mueller, D.5    Betzler, M.6    Steinkamp, T.7    Wagner, R.8
  • 36
    • 15744376891 scopus 로고    scopus 로고
    • Molecular determinants of the agonist binding domain of a P2X receptor channel
    • Yan, Z., Liang, Z., Tomic, M., Obasil, T. and Stojilkovic, S. S. (2005). Molecular determinants of the agonist binding domain of a P2X receptor channel. Mol. Pharmacol. 67: 1078-88.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1078-1088
    • Yan, Z.1    Liang, Z.2    Tomic, M.3    Obasil, T.4    Stojilkovic, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.