메뉴 건너뛰기




Volumn 14, Issue 1, 2013, Pages

Prediction of vitamin interacting residues in a vitamin binding protein using evolutionary information

Author keywords

PSSM; Pyridoxal 5 phosphate; SVM; Vitamin interacting residue; VitaPred

Indexed keywords

PSSM; PYRIDOXAL 5 PHOSPHATES; SVM; VITAMIN-INTERACTING RESIDUE; VITAPRED;

EID: 84873390712     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-14-44     Document Type: Article
Times cited : (22)

References (66)
  • 2
    • 34848842809 scopus 로고    scopus 로고
    • Editorial: vitamins and cofactors - chemistry, biochemistry and biology
    • Leeper FJ, Smith AG. Editorial: vitamins and cofactors - chemistry, biochemistry and biology. Nat Prod Rep 2007, 24(5):923-926.
    • (2007) Nat Prod Rep , vol.24 , Issue.5 , pp. 923-926
    • Leeper, F.J.1    Smith, A.G.2
  • 3
    • 68049087737 scopus 로고    scopus 로고
    • Vitamins and cofactors: highlights of ESBOC 2009
    • McDonald E. Vitamins and cofactors: highlights of ESBOC 2009. Nat Chem Biol 2009, 5(8):530-533.
    • (2009) Nat Chem Biol , vol.5 , Issue.8 , pp. 530-533
    • McDonald, E.1
  • 5
    • 38549122739 scopus 로고    scopus 로고
    • Unexpected actions of vitamin D: new perspectives on the regulation of innate and adaptive immunity
    • Adams JS, Hewison M. Unexpected actions of vitamin D: new perspectives on the regulation of innate and adaptive immunity. Nat Clin Pract Endocrinol Metab 2008, 4:80-90.
    • (2008) Nat Clin Pract Endocrinol Metab , vol.4 , pp. 80-90
    • Adams, J.S.1    Hewison, M.2
  • 7
    • 0004024282 scopus 로고    scopus 로고
    • Cambridge, U.K.: Cambridge University Press, ISBN 978-0-521-80388-5
    • Bender DA. Nutritional biochemistry of the vitamins 2003, Cambridge, U.K.: Cambridge University Press, ISBN 978-0-521-80388-5.
    • (2003) Nutritional biochemistry of the vitamins
    • Bender, D.A.1
  • 9
    • 78349231316 scopus 로고    scopus 로고
    • Vitamin B6 biosynthesis is essential for survival and virulence of Mycobacterium tuberculosis
    • Dick T, Manjunatha U, Kappes B, Gengenbacher M. Vitamin B6 biosynthesis is essential for survival and virulence of Mycobacterium tuberculosis. Mol Microbiol 2010, 78(4):980-988.
    • (2010) Mol Microbiol , vol.78 , Issue.4 , pp. 980-988
    • Dick, T.1    Manjunatha, U.2    Kappes, B.3    Gengenbacher, M.4
  • 10
    • 84859464651 scopus 로고    scopus 로고
    • The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference
    • Knöckel J, Müller IB, Butzloff S, Bergmann B, Walter RD, Wrenger C. The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference. Biochem J 2012, 443(2):397-405.
    • (2012) Biochem J , vol.443 , Issue.2 , pp. 397-405
    • Knöckel, J.1    Müller, I.B.2    Butzloff, S.3    Bergmann, B.4    Walter, R.D.5    Wrenger, C.6
  • 11
    • 84881156988 scopus 로고    scopus 로고
    • Poisoning pyridoxal 5-phosphate-dependent enzymes: a new strategy to target the malaria parasite Plasmodium falciparum
    • Müller IB, Wu F, Bergmann B, Knöckel J, Walter RD, Gehring H, Wrenger C. Poisoning pyridoxal 5-phosphate-dependent enzymes: a new strategy to target the malaria parasite Plasmodium falciparum. PLoS One 2009, 4(2):e4406.
    • (2009) PLoS One , vol.4 , Issue.2
    • Müller, I.B.1    Wu, F.2    Bergmann, B.3    Knöckel, J.4    Walter, R.D.5    Gehring, H.6    Wrenger, C.7
  • 12
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann PP, Pegg AE. Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Ther 1992, 54(2):195-215.
    • (1992) Pharmacol Ther , vol.54 , Issue.2 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 13
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy
    • Renwick SB, Snell K, Baumann U. The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure 1998, 6(9):1105-1116.
    • (1998) Structure , vol.6 , Issue.9 , pp. 1105-1116
    • Renwick, S.B.1    Snell, K.2    Baumann, U.3
  • 14
    • 0029455991 scopus 로고
    • Ornithine decarboxylase as a target for chemoprevention
    • Pegg AE, Shantz LM, Coleman CS. Ornithine decarboxylase as a target for chemoprevention. J Cell Biochem 1995, 22(Suppl):132-138.
    • (1995) J Cell Biochem , vol.22 , Issue.SUPPL , pp. 132-138
    • Pegg, A.E.1    Shantz, L.M.2    Coleman, C.S.3
  • 15
    • 0034826435 scopus 로고    scopus 로고
    • Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties
    • Bertoldi M, Castellani S, Bori Voltattorni C. Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties. Eur J Biochem 2001, 268(10):2975-2981.
    • (2001) Eur J Biochem , vol.268 , Issue.10 , pp. 2975-2981
    • Bertoldi, M.1    Castellani, S.2    Bori Voltattorni, C.3
  • 17
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein
    • Meier M, Janosik M, Kery V, Kraus JP, Burkhard P. Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J 2001, 20(15):3910-3916.
    • (2001) EMBO J , vol.20 , Issue.15 , pp. 3910-3916
    • Meier, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 18
    • 0032573591 scopus 로고    scopus 로고
    • The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme
    • Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J Mol Biol 1998, 284(2):401-419.
    • (1998) J Mol Biol , vol.284 , Issue.2 , pp. 401-419
    • Alexeev, D.1    Alexeeva, M.2    Baxter, R.L.3    Campopiano, D.J.4    Webster, S.P.5    Sawyer, L.6
  • 19
    • 0034416476 scopus 로고    scopus 로고
    • Structural Arrangement for Functional Requirements of Brain Recombinant 4-Aminobutyrate Aminotransferase
    • Sung BK, Kim YT. Structural Arrangement for Functional Requirements of Brain Recombinant 4-Aminobutyrate Aminotransferase. J Biochem Mol Biol 2000, 33(1):43-48.
    • (2000) J Biochem Mol Biol , vol.33 , Issue.1 , pp. 43-48
    • Sung, B.K.1    Kim, Y.T.2
  • 20
    • 3342978121 scopus 로고    scopus 로고
    • Molecular characterization of bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium falciparum
    • Kasekarn W, Sirawaraporn R, Chahomchuen T, Cowman AF, Sirawaraporn W. Molecular characterization of bifunctional hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium falciparum. Mol Biochem Parasitol 2004, 137(1):43-53.
    • (2004) Mol Biochem Parasitol , vol.137 , Issue.1 , pp. 43-53
    • Kasekarn, W.1    Sirawaraporn, R.2    Chahomchuen, T.3    Cowman, A.F.4    Sirawaraporn, W.5
  • 21
    • 34547100037 scopus 로고    scopus 로고
    • Synthesis of p-aminophenyl aryl H-phosphinic acids and esters via cross-coupling reactions: elaboration to phosphinic acid pseudopeptide analogues of pteroyl glutamic acid and related antifolates
    • Yang Y, Coward JK. Synthesis of p-aminophenyl aryl H-phosphinic acids and esters via cross-coupling reactions: elaboration to phosphinic acid pseudopeptide analogues of pteroyl glutamic acid and related antifolates. J Org Chem 2007, 72(15):5748-5758.
    • (2007) J Org Chem , vol.72 , Issue.15 , pp. 5748-5758
    • Yang, Y.1    Coward, J.K.2
  • 22
    • 79952467900 scopus 로고    scopus 로고
    • Thiamin (vitamin B1) biosynthesis and regulation: a rich source of antimicrobial drug targets?
    • Du Q, Wang H, Xie J. Thiamin (vitamin B1) biosynthesis and regulation: a rich source of antimicrobial drug targets?. Int J Biol Sci 2011, 7(1):41-52.
    • (2011) Int J Biol Sci , vol.7 , Issue.1 , pp. 41-52
    • Du, Q.1    Wang, H.2    Xie, J.3
  • 23
    • 12344312032 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast
    • Foth BJ, Stimmler LM, Handman E, Crabb BS, Hodder AN, McFadden GI. The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Mol Microbiol 2005, 55(1):39-53.
    • (2005) Mol Microbiol , vol.55 , Issue.1 , pp. 39-53
    • Foth, B.J.1    Stimmler, L.M.2    Handman, E.3    Crabb, B.S.4    Hodder, A.N.5    McFadden, G.I.6
  • 24
    • 12344298301 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases
    • McMillan PJ, Stimmler LM, Foth BJ, McFadden GI, Müller S. The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol 2005, 55(1):27-38.
    • (2005) Mol Microbiol , vol.55 , Issue.1 , pp. 27-38
    • McMillan, P.J.1    Stimmler, L.M.2    Foth, B.J.3    McFadden, G.I.4    Müller, S.5
  • 25
    • 0028220681 scopus 로고
    • Modification of aminoacyl-tRNA synthetases with pyridoxal-5'-phosphate. Identification of the labeled amino acid residues
    • Kalogerakos T, Hountondji C, Berne PF, Dukta S, Blanquet S. Modification of aminoacyl-tRNA synthetases with pyridoxal-5'-phosphate. Identification of the labeled amino acid residues. Biochimie 1994, 76(1):33-44.
    • (1994) Biochimie , vol.76 , Issue.1 , pp. 33-44
    • Kalogerakos, T.1    Hountondji, C.2    Berne, P.F.3    Dukta, S.4    Blanquet, S.5
  • 26
    • 17644389617 scopus 로고    scopus 로고
    • Support vector machine-based method for subcellular localization of human proteins using amino acid compositions, their order, and similarity search
    • Garg A, Bhasin M, Raghava GPS. Support vector machine-based method for subcellular localization of human proteins using amino acid compositions, their order, and similarity search. J Biol Chem 2005, 280:14427-14432.
    • (2005) J Biol Chem , vol.280 , pp. 14427-14432
    • Garg, A.1    Bhasin, M.2    Raghava, G.P.S.3
  • 27
    • 38649127567 scopus 로고    scopus 로고
    • Identification of DNA-binding proteins using support vector machines and evolutionary profiles
    • Kumar M, Gromiha MM, Raghava GPS. Identification of DNA-binding proteins using support vector machines and evolutionary profiles. BMC Bioinformatics 2007, 8:463.
    • (2007) BMC Bioinformatics , vol.8 , pp. 463
    • Kumar, M.1    Gromiha, M.M.2    Raghava, G.P.S.3
  • 28
    • 0036007085 scopus 로고    scopus 로고
    • Prediction of protein structural classes by support vector machines
    • Cai YD, Liu XJ, Xu XB, Chou KC. Prediction of protein structural classes by support vector machines. Comput Chem 2002, 26:293-296.
    • (2002) Comput Chem , vol.26 , pp. 293-296
    • Cai, Y.D.1    Liu, X.J.2    Xu, X.B.3    Chou, K.C.4
  • 29
    • 1542400269 scopus 로고    scopus 로고
    • Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information
    • Ahmad S, Gromiha MM, Sarai A. Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information. Bioinformatics 2004, 20:477-486.
    • (2004) Bioinformatics , vol.20 , pp. 477-486
    • Ahmad, S.1    Gromiha, M.M.2    Sarai, A.3
  • 30
    • 33746526551 scopus 로고    scopus 로고
    • Prediction of RNA binding sites in proteins from amino acid sequence
    • Terribilini M, Lee JH, Yan C, Jernigan RL, Honavar V, Dobbs D. Prediction of RNA binding sites in proteins from amino acid sequence. RNA 2006, 12:1450-1462.
    • (2006) RNA , vol.12 , pp. 1450-1462
    • Terribilini, M.1    Lee, J.H.2    Yan, C.3    Jernigan, R.L.4    Honavar, V.5    Dobbs, D.6
  • 31
    • 37249047085 scopus 로고    scopus 로고
    • A Weighted profile based method for protein-RNA interacting residue prediction
    • Jeong E, Miyano S. A Weighted profile based method for protein-RNA interacting residue prediction. Lecture notes in computer science 2006, 3939:123-139.
    • (2006) Lecture notes in computer science , vol.3939 , pp. 123-139
    • Jeong, E.1    Miyano, S.2
  • 32
    • 0034057552 scopus 로고    scopus 로고
    • Analysis and prediction of carbohydrate binding sites
    • Taroni C, Jones S, Thornton JM. Analysis and prediction of carbohydrate binding sites. Protein Eng 2000, 13(2):89-98.
    • (2000) Protein Eng , vol.13 , Issue.2 , pp. 89-98
    • Taroni, C.1    Jones, S.2    Thornton, J.M.3
  • 33
    • 70349307195 scopus 로고    scopus 로고
    • Prediction of protein-glucose binding sites using support vector machines
    • Nassif H, Al-Ali H, Khuri S, Keirouz W. Prediction of protein-glucose binding sites using support vector machines. Proteins 2009, 77(1):121-132.
    • (2009) Proteins , vol.77 , Issue.1 , pp. 121-132
    • Nassif, H.1    Al-Ali, H.2    Khuri, S.3    Keirouz, W.4
  • 34
    • 77449099952 scopus 로고    scopus 로고
    • Prediction of lipid-interacting amino acid residues from sequence features
    • Wang L, Irausquin SJ, Yang JY. Prediction of lipid-interacting amino acid residues from sequence features. Int J Comput Biol Drug Des 2008, 1(1):14-25.
    • (2008) Int J Comput Biol Drug Des , vol.1 , Issue.1 , pp. 14-25
    • Wang, L.1    Irausquin, S.J.2    Yang, J.Y.3
  • 35
    • 77956263332 scopus 로고    scopus 로고
    • Prediction of lipid-binding sites based on support vector machine and position specific scoring matrix
    • Xiong W, Guo Y, Li M. Prediction of lipid-binding sites based on support vector machine and position specific scoring matrix. Protein J 2010, 29(6):427-431.
    • (2010) Protein J , vol.29 , Issue.6 , pp. 427-431
    • Xiong, W.1    Guo, Y.2    Li, M.3
  • 37
    • 67650539034 scopus 로고    scopus 로고
    • Prediction of DNA-binding residues from protein sequence information using random forests
    • Wang L, Yang MQ, Yang JY. Prediction of DNA-binding residues from protein sequence information using random forests. BMC Genomics 2009, 10(Suppl 1):S1.
    • (2009) BMC Genomics , vol.10 , Issue.SUPPL. 1
    • Wang, L.1    Yang, M.Q.2    Yang, J.Y.3
  • 38
    • 77953886400 scopus 로고    scopus 로고
    • BindN + for accurate prediction of DNA and RNA-binding residues from protein sequence features
    • Wang L, Huang C, Yang MQ, Yang JY. BindN + for accurate prediction of DNA and RNA-binding residues from protein sequence features. BMC Syst Biol 2010, 4(Suppl 1):S3.
    • (2010) BMC Syst Biol , vol.4 , Issue.SUPPL. 1
    • Wang, L.1    Huang, C.2    Yang, M.Q.3    Yang, J.Y.4
  • 39
    • 84856577919 scopus 로고    scopus 로고
    • Prediction and analysis of nucleotide-binding residues using sequence and sequence-derived structural descriptors
    • Chen K, Mizianty MJ, Kurgan L. Prediction and analysis of nucleotide-binding residues using sequence and sequence-derived structural descriptors. Bioinformatics 2012, 28(3):331-341.
    • (2012) Bioinformatics , vol.28 , Issue.3 , pp. 331-341
    • Chen, K.1    Mizianty, M.J.2    Kurgan, L.3
  • 41
    • 77950471248 scopus 로고    scopus 로고
    • Identification of ATP binding residues of a protein from its primary sequence
    • Chauhan JS, Mishra NK, Raghava GPS. Identification of ATP binding residues of a protein from its primary sequence. BMC Bioinformatics 2009, 10:434.
    • (2009) BMC Bioinformatics , vol.10 , pp. 434
    • Chauhan, J.S.1    Mishra, N.K.2    Raghava, G.P.S.3
  • 42
    • 84861592844 scopus 로고    scopus 로고
    • Predicting protein-ATP binding sites from primary sequence through fusing bi-profile sampling of multi-view features
    • Zhang YN, Yu DJ, Li SS, Fan YX, Huang Y, Shen HB. Predicting protein-ATP binding sites from primary sequence through fusing bi-profile sampling of multi-view features. BMC Bioinformatics 2012, 13:118.
    • (2012) BMC Bioinformatics , vol.13 , pp. 118
    • Zhang, Y.N.1    Yu, D.J.2    Li, S.S.3    Fan, Y.X.4    Huang, Y.5    Shen, H.B.6
  • 43
    • 77952971734 scopus 로고    scopus 로고
    • Prediction of GTP interacting residues, dipeptides and tripeptides in a protein from its evolutionary information
    • Chauhan JS, Mishra NK, Raghava GPS. Prediction of GTP interacting residues, dipeptides and tripeptides in a protein from its evolutionary information. BMC Bioinformatics 2010, 11:301.
    • (2010) BMC Bioinformatics , vol.11 , pp. 301
    • Chauhan, J.S.1    Mishra, N.K.2    Raghava, G.P.S.3
  • 44
    • 77950423114 scopus 로고    scopus 로고
    • Identification of NAD interacting residues in proteins
    • Ansari HR, Raghava GPS. Identification of NAD interacting residues in proteins. BMC Bioinformatics 2010, 11:160.
    • (2010) BMC Bioinformatics , vol.11 , pp. 160
    • Ansari, H.R.1    Raghava, G.P.S.2
  • 45
    • 75149173507 scopus 로고    scopus 로고
    • Prediction of FAD interacting residues in a protein from its primary sequence using evolutionary information
    • Mishra NK, Raghava GPS. Prediction of FAD interacting residues in a protein from its primary sequence using evolutionary information. BMC Bioinformatics 2010, 11:S48.
    • (2010) BMC Bioinformatics , vol.11
    • Mishra, N.K.1    Raghava, G.P.S.2
  • 46
    • 80052721796 scopus 로고    scopus 로고
    • Identification of Mannose Interacting Residues using Local Composition
    • Agarwal S, Mishra NK, Singh H, Raghava GPS. Identification of Mannose Interacting Residues using Local Composition. PLoS One 2011, 6(9):e24039.
    • (2011) PLoS One , vol.6 , Issue.9
    • Agarwal, S.1    Mishra, N.K.2    Singh, H.3    Raghava, G.P.S.4
  • 47
    • 75149160598 scopus 로고    scopus 로고
    • SvmPRAT: SVM-based protein residue annotation toolkit
    • Rangwala H, Kauffman C, Karypis G. svmPRAT: SVM-based protein residue annotation toolkit. BMC Bioinformatics 2009, 10:439.
    • (2009) BMC Bioinformatics , vol.10 , pp. 439
    • Rangwala, H.1    Kauffman, C.2    Karypis, G.3
  • 48
    • 61449091497 scopus 로고    scopus 로고
    • Prediction of protein-protein binding site by using core interface residue and support vector machine
    • Li N, Sun Z, Jiang F. Prediction of protein-protein binding site by using core interface residue and support vector machine. BMC Bioinformatics 2008, 9:553.
    • (2008) BMC Bioinformatics , vol.9 , pp. 553
    • Li, N.1    Sun, Z.2    Jiang, F.3
  • 49
    • 36949013631 scopus 로고    scopus 로고
    • Support Vector Machine-based classification of protein folds using the structural properties of amino acid residues and amino acid residue pairs
    • Shamim MT, Anwaruddin M, Nagarajaram HA. Support Vector Machine-based classification of protein folds using the structural properties of amino acid residues and amino acid residue pairs. Bioinformatics 2007, 23(24):3320-3327.
    • (2007) Bioinformatics , vol.23 , Issue.24 , pp. 3320-3327
    • Shamim, M.T.1    Anwaruddin, M.2    Nagarajaram, H.A.3
  • 50
    • 33746634756 scopus 로고    scopus 로고
    • An approach of encoding for prediction of splice sites using SVM
    • Huang J, Li T, Chen K, Wu J. An approach of encoding for prediction of splice sites using SVM. Biochimie 2006, 88(7):923-929.
    • (2006) Biochimie , vol.88 , Issue.7 , pp. 923-929
    • Huang, J.1    Li, T.2    Chen, K.3    Wu, J.4
  • 51
    • 26444473604 scopus 로고    scopus 로고
    • Real value prediction of solvent accessibility in proteins using multiple sequence alignment and secondary structure
    • Garg A, Kaur H, Raghava GPS. Real value prediction of solvent accessibility in proteins using multiple sequence alignment and secondary structure. Proteins 2005, 61:318-324.
    • (2005) Proteins , vol.61 , pp. 318-324
    • Garg, A.1    Kaur, H.2    Raghava, G.P.S.3
  • 56
    • 0032594959 scopus 로고    scopus 로고
    • An overview of statistical learning theory
    • Vapnik VN. An overview of statistical learning theory. IEEE Trans Neural Netw 1999, 10:988-999.
    • (1999) IEEE Trans Neural Netw , vol.10 , pp. 988-999
    • Vapnik, V.N.1
  • 57
    • 0002714543 scopus 로고    scopus 로고
    • Making large-scale SVM learning particles
    • Cambridge, MA: MIT Press, Scholkopf B, Berges C, Smola A
    • Joachims T. Making large-scale SVM learning particles. Advances in kernel methods support vector learning 1999, 42-56. Cambridge, MA: MIT Press, Scholkopf B, Berges C, Smola A.
    • (1999) Advances in kernel methods support vector learning , pp. 42-56
    • Joachims, T.1
  • 58
    • 37249058502 scopus 로고    scopus 로고
    • Support vector machine-based method for predicting subcellular localization of mycobacterial proteins using evolutionary information and motifs
    • Rashid M, Saha S, Raghava GPS. Support vector machine-based method for predicting subcellular localization of mycobacterial proteins using evolutionary information and motifs. BMC Bioinformatics 2007, 8:337.
    • (2007) BMC Bioinformatics , vol.8 , pp. 337
    • Rashid, M.1    Saha, S.2    Raghava, G.P.S.3
  • 60
    • 34548606295 scopus 로고    scopus 로고
    • Recent progresses in protein subcellular location prediction
    • Chou KC, Shen HB. Recent progresses in protein subcellular location prediction. Anal Biochem 2007, 370:1-16.
    • (2007) Anal Biochem , vol.370 , pp. 1-16
    • Chou, K.C.1    Shen, H.B.2
  • 61
    • 23144467078 scopus 로고    scopus 로고
    • GPCRsclass: A web tool for classification of amine type of G-protein coupled Receptors
    • Bhasin M, Raghava GPS. GPCRsclass: A web tool for classification of amine type of G-protein coupled Receptors. Nucleic Acids Res 2005, 33:W143-W147.
    • (2005) Nucleic Acids Res , vol.33
    • Bhasin, M.1    Raghava, G.P.S.2
  • 62
    • 23144436397 scopus 로고    scopus 로고
    • BhairPred: A webserver for Prediction of Beta-hairpins in proteins from Multiple Alignment Information Using ANN and SVM Techniques
    • Kumar M, Bhasin M, Natt NK, Raghava GPS. BhairPred: A webserver for Prediction of Beta-hairpins in proteins from Multiple Alignment Information Using ANN and SVM Techniques. Nucleic Acids Res 2005, 33:W154-W159.
    • (2005) Nucleic Acids Res , vol.33
    • Kumar, M.1    Bhasin, M.2    Natt, N.K.3    Raghava, G.P.S.4
  • 63
    • 0033931867 scopus 로고    scopus 로고
    • Assessing the accuracy of prediction algorithms for classification: an overview
    • Baldi P, Brunak S, Chauvin Y, Andersen CA, Nielsen H. Assessing the accuracy of prediction algorithms for classification: an overview. Bioinformatics 2000, 16:412-424.
    • (2000) Bioinformatics , vol.16 , pp. 412-424
    • Baldi, P.1    Brunak, S.2    Chauvin, Y.3    Andersen, C.A.4    Nielsen, H.5
  • 64
    • 33745622868 scopus 로고    scopus 로고
    • Two Sample Logo: A Graphical Representation of the Differences between Two Sets of Sequence Alignments
    • Vacic V, Iakoucheva LM, Radivojac P. Two Sample Logo: A Graphical Representation of the Differences between Two Sets of Sequence Alignments. Bioinformatics 2006, 22(12):1536-1537.
    • (2006) Bioinformatics , vol.22 , Issue.12 , pp. 1536-1537
    • Vacic, V.1    Iakoucheva, L.M.2    Radivojac, P.3
  • 65
    • 0037372098 scopus 로고    scopus 로고
    • Prediction of β-turns in proteins from multiple alignment using neural network
    • Kaur H, Raghava GPS. Prediction of β-turns in proteins from multiple alignment using neural network. Protein Sci 2003, 12:627-634.
    • (2003) Protein Sci , vol.12 , pp. 627-634
    • Kaur, H.1    Raghava, G.P.S.2
  • 66
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani R, Peracchi A. A genomic overview of pyridoxal-phosphate-dependent enzymes. EMBO Rep 2003, 4(9):850-854.
    • (2003) EMBO Rep , vol.4 , Issue.9 , pp. 850-854
    • Percudani, R.1    Peracchi, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.