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Volumn 12, Issue 1, 2011, Pages

Residue propensities, discrimination and binding site prediction of adenine and guanine phosphates

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE PHOSPHATE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; CYCLIC AMP; CYCLIC GMP; GUANINE PHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; PHOSPHATE; UNCLASSIFIED DRUG; ADENINE NUCLEOTIDE; GUANINE NUCLEOTIDE; PROTEIN;

EID: 79955829108     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-20     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 0346606671 scopus 로고
    • The Discovery of Adenosine Triphosphate and the Establishment of Its Structure
    • The Discovery of Adenosine Triphosphate and the Establishment of Its Structure. K Maruyama, Journal of the History of Biology 1991 24 145 154
    • (1991) Journal of the History of Biology , vol.24 , pp. 145-154
    • Maruyama, K.1
  • 3
    • 0003779650 scopus 로고    scopus 로고
    • The Cell - A Molecular Approach
    • Sinauer Associates, Inc
    • The Cell - A Molecular Approach. GM Cooper, Sunderland (MA) Sinauer Associates, Inc 2000
    • (2000) Sunderland (MA)
    • Cooper, G.M.1
  • 4
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate
    • DOI 10.1073/pnas.95.7.3661
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (,)methylenediphosphonate. T Muller-Reichert D Chretien F Severin AA Hyman, Proceedings National Academy Sciences 1998 95 3661 3666 10.1073/pnas.95.7.3661 (Pubitemid 28173184)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.7 , pp. 3661-3666
    • Muller-Reichert, T.1    Chretien, D.2    Severin, F.3    Hyman, A.A.4
  • 5
    • 0035504287 scopus 로고    scopus 로고
    • On the molecular discrimination between adenine and guanine by proteins
    • On the molecular discrimination between adenine and guanine by proteins. I Nobeli RA Laskowski WS Valdar JM Thornton, Nucleic Acids Research 2001 29 4294 4309 10.1093/nar/29.21.4294 11691917 (Pubitemid 33064770)
    • (2001) Nucleic Acids Research , vol.29 , Issue.21 , pp. 4294-4309
    • Nobeli, I.1    Laskowski, R.A.2    Valdar, W.S.J.3    Thornton, J.M.4
  • 6
    • 0031026288 scopus 로고    scopus 로고
    • Cell signalling through guanine-nucleotide-binding regulatory proteins (G proteins) and phospholipases
    • Cell signalling through guanine-nucleotide-binding regulatory proteins (G proteins) and phospholipases. JH Exton, Eur J Biochem 1997 243 10 20 10.1111/j.1432-1033.1997.t01-1-00010.x 9030716 (Pubitemid 27060379)
    • (1997) European Journal of Biochemistry , vol.243 , Issue.1-2 , pp. 10-20
    • Exton, J.H.1
  • 7
    • 0034682668 scopus 로고    scopus 로고
    • The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins
    • 10.1074/jbc.M001027200. 10843989
    • The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. B Zhang Y Zhang Z Wang Y Zheng, J Biol Chem 2000 275 25299 25307 10.1074/jbc.M001027200 10843989
    • (2000) J Biol Chem , vol.275 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 8
    • 0038377767 scopus 로고    scopus 로고
    • Adenosine signalling pathways in the pituitary gland: One ligand, multiple receptors
    • DOI 10.1677/joe.0.1770357
    • Adenosine signalling pathway in the pituitary gland: One ligand, multiple receptors. DA Rees MF Scanlon J Ham, J Endocrinol 2003 177 357 364 10.1677/joe.0.1770357 12773115 (Pubitemid 36722290)
    • (2003) Journal of Endocrinology , vol.177 , Issue.3 , pp. 357-364
    • Rees, D.A.1    Scanlon, M.F.2    Ham, J.3
  • 9
    • 16644366421 scopus 로고    scopus 로고
    • Evidence of a novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis
    • DOI 10.1105/tpc.104.023945
    • Evidence of a novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis. CR Jeter W Tang E Henaff T Butterfield SJ Roux, Plant Cell 2004 16 2652 2664 10.1105/tpc.104.023945 15367717 (Pubitemid 41071353)
    • (2004) Plant Cell , vol.16 , Issue.10 , pp. 2652-2664
    • Jeter, C.R.1    Tang, W.2    Henaff, E.3    Butterfield, T.4    Roux, S.J.5
  • 10
    • 24344496091 scopus 로고    scopus 로고
    • Effect of adenosine triphosphate on phosphate uptake in renal proximal tubule cells: Involvement of PKC and p38 MAPK
    • DOI 10.1002/jcp.20367
    • Effect of adenosine triphosphate on phosphate uptake in renal proximal tubule cells: Involvement of PKC and p38 MAPK. YJ Lee SH Park TO Jeung KW Kim JH Lee HJ Han, J Cell Physiol 2005 205 68 76 10.1002/jcp.20367 15880445 (Pubitemid 41262852)
    • (2005) Journal of Cellular Physiology , vol.205 , Issue.1 , pp. 68-76
    • Lee, Y.J.1    Park, S.H.2    Jeung, T.O.3    Kim, K.W.4    Lee, J.H.5    Han, H.J.6
  • 11
    • 64349107204 scopus 로고    scopus 로고
    • Adenine, a hairpin ribozyme cofactor - High-pressure and competition studies
    • 10.1111/j.1742-4658.2009.06983.x. 19476496
    • Adenine, a hairpin ribozyme cofactor - high-pressure and competition studies. M Ztouti H Kaddour F Miralles C Simian J Vergne G Hervé MC Maurel, FEBS J 2009 276 2574 2588 10.1111/j.1742-4658.2009.06983.x 19476496
    • (2009) FEBS J , vol.276 , pp. 2574-2588
    • Ztouti, M.1    Kaddour, H.2    Miralles, F.3    Simian, C.4    Vergne, J.5    Hervé, G.6    Maurel, M.C.7
  • 12
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied
    • Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied. J Weber S Wilke-Mounts RS Lee E Grell AE Senior, J Biol Chem 1993 268 27 20126 20133 8376371 (Pubitemid 23278911)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.27 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.-F.3    Grell, E.4    Senior, A.E.5
  • 13
    • 33646581731 scopus 로고    scopus 로고
    • Identification of phosphate binding residues of Escherichia coli ATP synthase
    • DOI 10.1007/s10863-005-9486-8
    • Identification of phosphate binding residues of Escherichia coli ATP synthase. Z Ahmad AE Senior, J Bioenerg Biomembr 2005 37 6 437 440 10.1007/s10863-005-9486-8 16691479 (Pubitemid 43725172)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.6 , pp. 437-440
    • Ahmad, Z.1    Senior, A.E.2
  • 14
    • 0034737965 scopus 로고    scopus 로고
    • ATP synthase: What we know about ATP hydrolysis and what we do not know about ATP synthesis
    • DOI 10.1016/S0005-2728(00)00082-7, PII S0005272800000827
    • ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. J Weber AE Senior, Biochim Biophys Acta 2000 1458 2-3 300 309 10.1016/S0005-2728(00)00082-7 10838046 (Pubitemid 30320713)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 300-309
    • Weber, J.1    Senior, A.E.2
  • 15
    • 0022480476 scopus 로고
    • Characterisation of phosphate binding to mitochondrial and bacterial membrane-bound ATP synthase by studies of inhibition with 4-chloro-7- nitrobenzofurazan
    • DOI 10.1016/0014-5793(86)81195-4
    • Characterisation of phosphate binding to mitochondrial and bacterial membrane-bound ATP synthase by studies of inhibition with 4-chloro-7- nitrobenzofurazan. JA Perez AJ Greenfield R Sutton SJ Ferguson, FEBS Lett 1986 198 1 113 118 10.1016/0014-5793(86)81195-4 2869972 (Pubitemid 16055179)
    • (1986) FEBS Letters , vol.198 , Issue.1 , pp. 113-118
    • Perez, J.A.1    Greenfield, A.J.2    Sutton, R.3    Ferguson, S.J.4
  • 16
    • 11844258832 scopus 로고    scopus 로고
    • Involvement of ATP synthase residues αArg-376, βArg-182, and βLys-155 in Pi binding
    • DOI 10.1016/j.febslet.2004.12.022, PII S0014579304015571
    • Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding. Z Ahmad AE Senior, FEBS Lett 2005 579 2 523 528 10.1016/j.febslet.2004.12.022 15642370 (Pubitemid 40092438)
    • (2005) FEBS Letters , vol.579 , Issue.2 , pp. 523-528
    • Ahmad, Z.1    Senior, A.E.2
  • 17
    • 3843104765 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1074/jbc.M404621200
    • Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase. Z Ahmad AE Senior, J Biol Chem 2004 279 30 31505 31513 10.1074/jbc.M404621200 15150266 (Pubitemid 39037819)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31505-31513
    • Ahmad, Z.1    Senior, A.E.2
  • 18
    • 8544243523 scopus 로고    scopus 로고
    • 1-ATPase
    • DOI 10.1074/jbc.M407608200
    • Role of betaAsn-243 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F(1)-ATPase. Z Ahmad AE Senior, J Biol Chem 2004 279 44 46057 46064 10.1074/jbc.M407608200 15322126 (Pubitemid 39491599)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 46057-46064
    • Ahmad, Z.1    Senior, A.E.2
  • 19
    • 23044512263 scopus 로고    scopus 로고
    • Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase
    • DOI 10.1074/jbc.M503955200
    • Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase. Z Ahmad AE Senior, J Biol Chem 2005 280 30 27981 27989 10.1074/jbc.M503955200 15939739 (Pubitemid 41076915)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27981-27989
    • Ahmad, Z.1    Senior, A.E.2
  • 20
    • 30644458567 scopus 로고    scopus 로고
    • Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride
    • DOI 10.1016/j.febslet.2005.12.057, PII S0014579305015401
    • Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride. Z Ahmad AE Senior, FEBS Lett 2006 580 2 517 520 10.1016/j.febslet.2005.12.057 16405964 (Pubitemid 43089681)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 517-520
    • Ahmad, Z.1    Senior, A.E.2
  • 21
    • 39749177088 scopus 로고    scopus 로고
    • Role of alphaPhe-291 residue in the phosphate-binding subdomain of catalytic sites of Escherichia coli ATP synthase
    • 10.1016/j.abb.2008.01.013. 18242162
    • Role of alphaPhe-291 residue in the phosphate-binding subdomain of catalytic sites of Escherichia coli ATP synthase. LE Brudecki JJ Grindstaff Z Ahmad, Arch Biochem Biophys 2008 471 2 168 175 10.1016/j.abb.2008.01.013 18242162
    • (2008) Arch Biochem Biophys , vol.471 , Issue.2 , pp. 168-175
    • Brudecki, L.E.1    Grindstaff, J.J.2    Ahmad, Z.3
  • 22
    • 67449106983 scopus 로고    scopus 로고
    • Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase
    • 10.1074/jbc.M809209200. 19240022
    • Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase. W Li LE Brudecki AE Senior Z Ahmad, J Biol Chem 2009 284 16 10747 10754 10.1074/jbc.M809209200 19240022
    • (2009) J Biol Chem , vol.284 , Issue.16 , pp. 10747-10754
    • Li, W.1    Brudecki, L.E.2    Senior, A.E.3    Ahmad, Z.4
  • 23
    • 0025048136 scopus 로고
    • The p-loop - A common motif in ATP- and GTP-binding proteins
    • 10.1016/0968-0004(90)90281-F. 2126155
    • The p-loop - a common motif in ATP- and GTP-binding proteins. M Saraste PR Sibbald A Wittinghofer, Trends Biochem Sci 1990 15 430 434 10.1016/0968-0004(90)90281-F 2126155
    • (1990) Trends Biochem Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 24
    • 0027293707 scopus 로고
    • Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli
    • DOI 10.1006/jmbi.1993.1459
    • Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli. KM Logan KL Knight, J Mol Biol 1993 232 1048 1059 10.1006/jmbi.1993.1459 8371266 (Pubitemid 23276420)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.4 , pp. 1048-1059
    • Logan, K.M.1    Knight, K.L.2
  • 25
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Active site comparisons highlight structural similarities between myosin and other p-loop proteins. CA Smith I Rayment, Biophys J 1996 70 1590 1602 10.1016/S0006-3495(96)79745-X 8785318 (Pubitemid 26103931)
    • (1996) Biophysical Journal , vol.70 , Issue.4 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 26
    • 0031709128 scopus 로고    scopus 로고
    • The central lysine in the P-loop motif of the Escherichia coli DnaA protein is essential for initiating DNA replication from the chromosomal origin, oriC, and the F factor origin, oriS, but is dispensable for initiation from the P1 plasmid origin, oriR
    • DOI 10.1006/plas.1998.1349
    • The central lysine in the p-loop motif of Escherichia coli DnaA protein is essential for initiating DNA replication from the chromosomal origin, oriC, and the F-factor origin, oriS, but is dispensable for initiation from the P1-plasmid origin, oriR. O Skovgaard K Oleson A Wright, Plasmid 1998 40 91 99 10.1006/plas.1998.1349 9735311 (Pubitemid 28409386)
    • (1998) Plasmid , vol.40 , Issue.2 , pp. 91-99
    • Skovgaard, O.1    Olesen, K.2    Wright, A.3
  • 27
    • 1542400269 scopus 로고    scopus 로고
    • Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information
    • DOI 10.1093/bioinformatics/btg432
    • Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information. S Ahmad MM Gromiha A Sarai, Bioinformatics 2004 20 4 477 486 10.1093/bioinformatics/btg432 14990443 (Pubitemid 38344327)
    • (2004) Bioinformatics , vol.20 , Issue.4 , pp. 477-486
    • Ahmad, S.1    Gromiha, M.M.2    Sarai, A.3
  • 28
    • 25444524842 scopus 로고    scopus 로고
    • PSSM-based prediction of DNA binding sites in proteins
    • 10.1186/1471-2105-6-33. 15720719
    • PSSM-based prediction of DNA binding sites in proteins. S Ahmad A Sarai, BMC Bioinformatics 2005 6 33 10.1186/1471-2105-6-33 15720719
    • (2005) BMC Bioinformatics , vol.6 , pp. 33
    • Ahmad, S.1    Sarai, A.2
  • 29
    • 33847317012 scopus 로고    scopus 로고
    • Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network
    • Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network. A Malik S Ahmad, BMC Struct Biol 2007 7 1
    • (2007) BMC Struct Biol , vol.7 , Issue.1
    • Malik, A.1    Ahmad, S.2
  • 30
    • 67649337519 scopus 로고    scopus 로고
    • Prediction of mono- and di-nucleotide-specific DNA-binding sites in proteins using neural networks
    • 10.1186/1472-6807-9-30. 19439068
    • Prediction of mono- and di-nucleotide-specific DNA-binding sites in proteins using neural networks. M Andrabi K Mizuguchi A Sarai S Ahmad, BMC Struct Biol 2009 9 30 10.1186/1472-6807-9-30 19439068
    • (2009) BMC Struct Biol , vol.9 , pp. 30
    • Andrabi, M.1    Mizuguchi, K.2    Sarai, A.3    Ahmad, S.4
  • 31
    • 31544440473 scopus 로고    scopus 로고
    • An empirical approach for detecting nucleotide-binding sites on proteins
    • DOI 10.1093/protein/gzj002
    • An empirical approach for detecting nucleotide-binding sites on proteins. M Saito M Go T Shirai, Protein Eng Des Sel 2006 19 67 75 16403825 (Pubitemid 43162258)
    • (2006) Protein Engineering, Design and Selection , vol.19 , Issue.2 , pp. 67-75
    • Saito, M.1    Go, M.2    Shirai, T.3
  • 32
    • 77950471248 scopus 로고    scopus 로고
    • Identification of ATP binding residues of a protein from its primary sequence
    • 10.1186/1471-2105-10-434. 20021687
    • Identification of ATP binding residues of a protein from its primary sequence. JS Chauhan NK Mishra GP Raghava, BMC Bioinformatics 2009 10 434 10.1186/1471-2105-10-434 20021687
    • (2009) BMC Bioinformatics , vol.10 , pp. 434
    • Chauhan, J.S.1    Mishra, N.K.2    Raghava, G.P.3
  • 33
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. SF Altschul TL Madden AA Schaffer JH Zhang Z Zhang W Miller DJ Lipman, Nucleic Acids Research 1997 25 3389 3402 10.1093/nar/25.17.3389 9254694 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 35
    • 0030859238 scopus 로고    scopus 로고
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase
    • DOI 10.1074/jbc.272.27.16946
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase. W Hemmer M McGlone I Tsigelny SS Taylor, J Biol Chem 1997 272 16946 16954 10.1074/jbc.272.27.16946 9202006 (Pubitemid 27289797)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.27 , pp. 16946-16954
    • Hemmer, W.1    McGlone, M.2    Tsigelny, I.3    Taylor, S.S.4
  • 36
    • 0035874464 scopus 로고    scopus 로고
    • Role of glycine-534 and glycine-1179 of human multidrug resistance protein (MDR1) in drug-mediated control of ATP hydrolysis
    • DOI 10.1042/0264-6021:3560071
    • Role of glycine-534 and glycine-1179 of human multidrug resistance protein (MDR1) in drug-mediated control of ATP hydrolysis. G Szakcs C Ozvegy E Bakos B Sarkadi A Vradi, Biochem J 2001 356 71 75 10.1042/0264-6021:3560071 11336637 (Pubitemid 34275707)
    • (2001) Biochemical Journal , vol.356 , Issue.1 , pp. 71-75
    • Szakacs, G.1    Ozvegy, C.2    Bakos, E.3    Sarkadi, B.4    Varadi, A.5
  • 37
    • 29144521525 scopus 로고    scopus 로고
    • 1 receptors: Mutagenesis indicates that the glycine at position 250 is important for channel function
    • DOI 10.1111/j.1471-4159.2005.03494.x
    • Contribution of conserved glycine residues to ATP action at human P2X1 receptors: mutagenesis indicates that the glycine at position 250 is important for channel function. HR Digby JA Roberts MJ Sutcliffe RJ Evans, J Neurochem 2005 95 1746 1754 10.1111/j.1471-4159.2005.03494.x 16236030 (Pubitemid 41804070)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1746-1754
    • Digby, H.R.1    Roberts, J.A.2    Sutcliffe, M.J.3    Evans, R.J.4
  • 38
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. NM Luscombe RA Laskowski JM Thornton, Nucleic Acids Research 2001 29 2860 2874 10.1093/nar/29.13.2860 11433033 (Pubitemid 32685051)
    • (2001) Nucleic Acids Research , vol.29 , Issue.13 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 39
    • 69749128313 scopus 로고    scopus 로고
    • Histidine affinity chromatography of homo-oligonucleotides. Role of multiple interactions on retention
    • 10.1002/bmc.1179. 19296518
    • Histidine affinity chromatography of homo-oligonucleotides. Role of multiple interactions on retention. A Sousa F Sousa DM Prazeres JA Queiroz, Biomed Chromatogr 2009 23 745 753 10.1002/bmc.1179 19296518
    • (2009) Biomed Chromatogr , vol.23 , pp. 745-753
    • Sousa, A.1    Sousa, F.2    Prazeres, D.M.3    Queiroz, J.A.4
  • 40
    • 0035800599 scopus 로고    scopus 로고
    • Structure-based analysis of protein-RNA interactions using the program ENTANGLE
    • DOI 10.1006/jmbi.2001.4857
    • Structure-based analysis of protein-RNA interactions using the program ENTANGLE. J Allers Y Shamoo, J Mol Biol 2001 311 75 86 10.1006/jmbi.2001.4857 11469858 (Pubitemid 32735315)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 75-86
    • Allers, J.1    Shamoo, Y.2
  • 41
    • 0037085010 scopus 로고    scopus 로고
    • 0-ATP synthase
    • DOI 10.1016/S0005-2728(02)00185-8, PII S0005272802001858
    • The molecular mechanism of ATP synthesis by F1F0-ATP synthase. AE Senior S Nadanaciva J Weber, Biochim Biophys Acta 2002 1553 3 188 211 10.1016/S0005-2728(02)00185-8 11997128 (Pubitemid 34460564)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1553 , Issue.3 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3


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