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Volumn 8, Issue , 2008, Pages

Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYTOPLASM PROTEIN; DISULFIDE; CYSTINE; PROTEIN; SOLVENT;

EID: 58649113381     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-8-55     Document Type: Article
Times cited : (40)

References (100)
  • 1
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • 7020376
    • The anatomy and taxonomy of protein structure. JS Richardson, Adv Protein Chem 1981 34 167 339 7020376
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 2
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • 7338898
    • Disulphide bridges in globular proteins. JM Thornton, J Mol Biol 1981 151 2 261 287 7338898
    • (1981) J Mol Biol , vol.151 , Issue.2 , pp. 261-287
    • Thornton, J.M.1
  • 4
    • 2542586190 scopus 로고    scopus 로고
    • Prediction of the bonding states of cysteines using the support vector machines based on multiple feature vectors and cysteine state sequences
    • 15146500
    • Prediction of the bonding states of cysteines using the support vector machines based on multiple feature vectors and cysteine state sequences. YC Chen YS Lin CJ Lin JK Hwang, Proteins 2004 55 4 1036 1042 15146500
    • (2004) Proteins , vol.55 , Issue.4 , pp. 1036-1042
    • Chen, Y.C.1    Lin, Y.S.2    Lin, C.J.3    Hwang, J.K.4
  • 5
    • 0033566578 scopus 로고    scopus 로고
    • Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins
    • 10409827
    • Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins. P Fariselli P Riccobelli R Casadio, Proteins 1999 36 3 340 346 10409827
    • (1999) Proteins , vol.36 , Issue.3 , pp. 340-346
    • Fariselli, P.1    Riccobelli, P.2    Casadio, R.3
  • 6
    • 0026579140 scopus 로고
    • Different sequence environments of cysteines and half cystines in proteins. Application to predict disulfide forming residues
    • 1633841
    • Different sequence environments of cysteines and half cystines in proteins. Application to predict disulfide forming residues. A Fiser M Cserzo E Tudos I Simon, FEBS Lett 1992 302 2 117 120 1633841
    • (1992) FEBS Lett , vol.302 , Issue.2 , pp. 117-120
    • Fiser, A.1    Cserzo, M.2    Tudos, E.3    Simon, I.4
  • 7
    • 0034039497 scopus 로고    scopus 로고
    • Predicting the oxidation state of cysteines by multiple sequence alignment
    • 10869018
    • Predicting the oxidation state of cysteines by multiple sequence alignment. A Fiser I Simon, Bioinformatics 2000 16 3 251 256 10869018
    • (2000) Bioinformatics , vol.16 , Issue.3 , pp. 251-256
    • Fiser, A.1    Simon, I.2
  • 8
    • 0036285587 scopus 로고    scopus 로고
    • Predicting redox state of cysteines in proteins
    • 12078485
    • Predicting redox state of cysteines in proteins. A Fiser I Simon, Methods Enzymol 2002 353 10 21 12078485
    • (2002) Methods Enzymol , vol.353 , pp. 10-21
    • Fiser, A.1    Simon, I.2
  • 10
    • 2942624211 scopus 로고    scopus 로고
    • Prediction of disulfide-bonded cysteines in proteomes with a hidden neural network
    • 15174135
    • Prediction of disulfide-bonded cysteines in proteomes with a hidden neural network. PL Martelli P Fariselli R Casadio, Proteomics 2004 4 6 1665 1671 15174135
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1665-1671
    • Martelli, P.L.1    Fariselli, P.2    Casadio, R.3
  • 11
    • 0036937367 scopus 로고    scopus 로고
    • Prediction of the disulfide bonding state of cysteines in proteins with hidden neural networks
    • 12601133
    • Prediction of the disulfide bonding state of cysteines in proteins with hidden neural networks. PL Martelli P Fariselli L Malaguti R Casadio, Protein Eng 2002 15 12 951 953 12601133
    • (2002) Protein Eng , vol.15 , Issue.12 , pp. 951-953
    • Martelli, P.L.1    Fariselli, P.2    Malaguti, L.3    Casadio, R.4
  • 12
    • 0036839271 scopus 로고    scopus 로고
    • Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy
    • 12381855
    • Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy. PL Martelli P Fariselli L Malaguti R Casadio, Protein Sci 2002 11 11 2735 2739 12381855
    • (2002) Protein Sci , vol.11 , Issue.11 , pp. 2735-2739
    • Martelli, P.L.1    Fariselli, P.2    Malaguti, L.3    Casadio, R.4
  • 13
    • 0037083493 scopus 로고    scopus 로고
    • Predicting the disulfide bonding state of cysteines using protein descriptors
    • 11835499
    • Predicting the disulfide bonding state of cysteines using protein descriptors. MH Mucchielli-Giorgi S Hazout P Tuffery, Proteins 2002 46 3 243 249 11835499
    • (2002) Proteins , vol.46 , Issue.3 , pp. 243-249
    • Mucchielli-Giorgi, M.H.1    Hazout, S.2    Tuffery, P.3
  • 14
    • 0025118064 scopus 로고
    • Prediction of the disulfide-bonding state of cysteine in proteins
    • 2217140
    • Prediction of the disulfide-bonding state of cysteine in proteins. SM Muskal SR Holbrook SH Kim, Protein Eng 1990 3 8 667 672 2217140
    • (1990) Protein Eng , vol.3 , Issue.8 , pp. 667-672
    • Muskal, S.M.1    Holbrook, S.R.2    Kim, S.H.3
  • 15
    • 4143139761 scopus 로고    scopus 로고
    • Learning to discriminate between ligand-bound and disulfide-bound cysteines
    • 15166311
    • Learning to discriminate between ligand-bound and disulfide-bound cysteines. A Passerini P Frasconi, Protein Eng Des Sel 2004 17 4 367 373 15166311
    • (2004) Protein Eng des Sel , vol.17 , Issue.4 , pp. 367-373
    • Passerini, A.1    Frasconi, P.2
  • 16
    • 1942456707 scopus 로고    scopus 로고
    • Prediction of the disulfide-bonding state of cysteines in proteins based on dipeptide composition
    • 15110765
    • Prediction of the disulfide-bonding state of cysteines in proteins based on dipeptide composition. JN Song ML Wang WJ Li WB Xu, Biochem Biophys Res Commun 2004 318 1 142 147 15110765
    • (2004) Biochem Biophys Res Commun , vol.318 , Issue.1 , pp. 142-147
    • Song, J.N.1    Wang, M.L.2    Li, W.J.3    Xu, W.B.4
  • 17
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 11101221
    • 13C NMR chemical shifts can predict disulfide bond formation. D Sharma K Rajarathnam, J Biomol NMR 2000 18 2 165 171 11101221
    • (2000) J Biomol NMR , vol.18 , Issue.2 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 18
    • 0034781580 scopus 로고    scopus 로고
    • Prediction of disulfide connectivity in proteins
    • 11673241
    • Prediction of disulfide connectivity in proteins. P Fariselli R Casadio, Bioinformatics 2001 17 10 957 964 11673241
    • (2001) Bioinformatics , vol.17 , Issue.10 , pp. 957-964
    • Fariselli, P.1    Casadio, R.2
  • 19
    • 19544393195 scopus 로고    scopus 로고
    • Disulfide connectivity prediction using secondary structure information and diresidue frequencies
    • 15741247
    • Disulfide connectivity prediction using secondary structure information and diresidue frequencies. F Ferre P Clote, Bioinformatics 2005 21 10 2336 2346 15741247
    • (2005) Bioinformatics , vol.21 , Issue.10 , pp. 2336-2346
    • Ferre, F.1    Clote, P.2
  • 20
    • 23144437891 scopus 로고    scopus 로고
    • DiANNA: A web server for disulfide connectivity prediction
    • 15980459
    • DiANNA: a web server for disulfide connectivity prediction. F Ferre P Clote, Nucleic Acids Res 2005 33 Web Server W230 232 15980459
    • (2005) Nucleic Acids Res , Issue.33 WEB SERVER , pp. 230-232
    • Ferre, F.1    Clote, P.2
  • 21
    • 28944438120 scopus 로고    scopus 로고
    • Improving disulfide connectivity prediction with sequential distance between oxidized cysteines
    • 16223789
    • Improving disulfide connectivity prediction with sequential distance between oxidized cysteines. CH Tsai BJ Chen CH Chan HL Liu CY Kao, Bioinformatics 2005 21 24 4416 4419 16223789
    • (2005) Bioinformatics , vol.21 , Issue.24 , pp. 4416-4419
    • Tsai, C.H.1    Chen, B.J.2    Chan, C.H.3    Liu, H.L.4    Kao, C.Y.5
  • 23
    • 1842455284 scopus 로고    scopus 로고
    • Disulfide connectivity prediction using recursive neural networks and evolutionary information
    • 15033872
    • Disulfide connectivity prediction using recursive neural networks and evolutionary information. A Vullo P Frasconi, Bioinformatics 2004 20 5 653 659 15033872
    • (2004) Bioinformatics , vol.20 , Issue.5 , pp. 653-659
    • Vullo, A.1    Frasconi, P.2
  • 24
    • 17444411155 scopus 로고    scopus 로고
    • Cysteine separations profiles on protein sequences infer disulfide connectivity
    • 15585533
    • Cysteine separations profiles on protein sequences infer disulfide connectivity. E Zhao HL Liu CH Tsai HK Tsai CH Chan CY Kao, Bioinformatics 2005 21 8 1415 1420 15585533
    • (2005) Bioinformatics , vol.21 , Issue.8 , pp. 1415-1420
    • Zhao, E.1    Liu, H.L.2    Tsai, C.H.3    Tsai, H.K.4    Chan, C.H.5    Kao, C.Y.6
  • 25
    • 0024046835 scopus 로고
    • Model building of disulfide bonds in proteins with known three-dimensional structure
    • 3244694
    • Model building of disulfide bonds in proteins with known three-dimensional structure. B Hazes BW Dijkstra, Protein Eng 1988 2 2 119 125 3244694
    • (1988) Protein Eng , vol.2 , Issue.2 , pp. 119-125
    • Hazes, B.1    Dijkstra, B.W.2
  • 26
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • 2594728
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. R Sowdhamini N Srinivasan B Shoichet D Santi C Ramakrishnan P Balaram, Protein Eng 1989 3 2 95 103 2594728
    • (1989) Protein Eng , vol.3 , Issue.2 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.4    Ramakrishnan, C.5    Balaram, P.6
  • 28
    • 0041819762 scopus 로고    scopus 로고
    • Relationship between protein structures and disulfide-bonding patterns
    • 12945044
    • Relationship between protein structures and disulfide-bonding patterns. CC Chuang CY Chen JM Yang PC Lyu JK Hwang, Proteins 2003 53 1 1 5 12945044
    • (2003) Proteins , vol.53 , Issue.1 , pp. 1-5
    • Chuang, C.C.1    Chen, C.Y.2    Yang, J.M.3    Lyu, P.C.4    Hwang, J.K.5
  • 30
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: Simulations and bioninformatics analysis
    • 10891282
    • What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis. VI Abkevich EI Shakhnovich, J Mol Biol 2000 300 4 975 985 10891282
    • (2000) J Mol Biol , vol.300 , Issue.4 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 31
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • 15642731
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. M Berkmen D Boyd J Beckwith, J Biol Chem 2005 280 12 11387 11394 15642731
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 32
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • 8251931
    • Disulfide bonds and the stability of globular proteins. SF Betz, Protein Sci 1993 2 10 1551 1558 8251931
    • (1993) Protein Sci , vol.2 , Issue.10 , pp. 1551-1558
    • Betz, S.F.1
  • 33
    • 0034491013 scopus 로고    scopus 로고
    • The effects of disulfide bonds on the denatured state of barnase
    • 11206061
    • The effects of disulfide bonds on the denatured state of barnase. J Clarke AM Hounslow CJ Bond AR Fersht V Daggett, Protein Sci 2000 9 12 2394 2404 11206061
    • (2000) Protein Sci , vol.9 , Issue.12 , pp. 2394-2404
    • Clarke, J.1    Hounslow, A.M.2    Bond, C.J.3    Fersht, A.R.4    Daggett, V.5
  • 34
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineered disulfide bond
    • 2916125
    • Control of enzyme activity by an engineered disulfide bond. M Matsumura BW Matthews, Science 1989 243 4892 792 794 2916125
    • (1989) Science , vol.243 , Issue.4892 , pp. 792-794
    • Matsumura, M.1    Matthews, B.W.2
  • 35
    • 0026319603 scopus 로고
    • Stabilization of functional proteins by introduction of multiple disulfide bonds
    • 1784181
    • Stabilization of functional proteins by introduction of multiple disulfide bonds. M Matsumura BW Matthews, Methods Enzymol 1991 202 336 356 1784181
    • (1991) Methods Enzymol , vol.202 , pp. 336-356
    • Matsumura, M.1    Matthews, B.W.2
  • 36
    • 0034886351 scopus 로고    scopus 로고
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
    • 11525170
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. O Mayans J Wuerges S Canela M Gautel M Wilmanns, Structure 2001 9 4 331 340 11525170
    • (2001) Structure , vol.9 , Issue.4 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 38
    • 0035822622 scopus 로고    scopus 로고
    • Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins
    • 11478871
    • Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. E Welker WJ Wedemeyer M Narayan HA Scheraga, Biochemistry 2001 40 31 9059 9064 11478871
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9059-9064
    • Welker, E.1    Wedemeyer, W.J.2    Narayan, M.3    Scheraga, H.A.4
  • 39
    • 0032477917 scopus 로고    scopus 로고
    • Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation
    • 9477955
    • Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation. E Drakopoulou J Vizzavona J Neyton V Aniort F Bouet H Virelizier A Menez C Vita, Biochemistry 1998 37 5 1292 1301 9477955
    • (1998) Biochemistry , vol.37 , Issue.5 , pp. 1292-1301
    • Drakopoulou, E.1    Vizzavona, J.2    Neyton, J.3    Aniort, V.4    Bouet, F.5    Virelizier, H.6    Menez, A.7    Vita, C.8
  • 40
    • 0024084164 scopus 로고
    • Coordinated amino acid changes in homologous protein families
    • 3237684
    • Coordinated amino acid changes in homologous protein families. D Altschuh T Vernet P Berti D Moras K Nagai, Protein Eng 1988 2 3 193 199 3237684
    • (1988) Protein Eng , vol.2 , Issue.3 , pp. 193-199
    • Altschuh, D.1    Vernet, T.2    Berti, P.3    Moras, D.4    Nagai, K.5
  • 41
    • 0028826172 scopus 로고
    • Paired natural cysteine mutation mapping: Aid to constraining models of protein tertiary structure
    • 8563638
    • Paired natural cysteine mutation mapping: Aid to constraining models of protein tertiary structure. R Kreisberg V Buchner D Arad, Protein Sci 1995 4 11 2405 2410 8563638
    • (1995) Protein Sci , vol.4 , Issue.11 , pp. 2405-2410
    • Kreisberg, R.1    Buchner, V.2    Arad, D.3
  • 42
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • 7723011
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures. AG Murzin SE Brenner T Hubbard C Chothia, J Mol Biol 1995 247 4 536 540 7723011
    • (1995) J Mol Biol , vol.247 , Issue.4 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 43
    • 0028128093 scopus 로고
    • Response of dynamic structure to removal of a disulfide bond: Normal mode refinement of C77A/C95A mutant of human lysozyme
    • 8142902
    • Response of dynamic structure to removal of a disulfide bond: normal mode refinement of C77A/C95A mutant of human lysozyme. A Kidera K Inaka M Matsushima N Go, Protein Sci 1994 3 1 92 102 8142902
    • (1994) Protein Sci , vol.3 , Issue.1 , pp. 92-102
    • Kidera, A.1    Inaka, K.2    Matsushima, M.3    Go, N.4
  • 44
    • 0029820584 scopus 로고    scopus 로고
    • Engineered disulfide bonds in staphylococcal nuclease: Effects on the stability and conformation of the folded protein
    • 8756688
    • Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. AP Hinck DM Truckses JL Markley, Biochemistry 1996 35 32 10328 10338 8756688
    • (1996) Biochemistry , vol.35 , Issue.32 , pp. 10328-10338
    • Hinck, A.P.1    Truckses, D.M.2    Markley, J.L.3
  • 45
    • 0023956149 scopus 로고
    • Disulphide bonds and protein stability
    • 3282505
    • Disulphide bonds and protein stability. TE Creighton, Bioessays 1988 8 2 57 63 3282505
    • (1988) Bioessays , vol.8 , Issue.2 , pp. 57-63
    • Creighton, T.E.1
  • 46
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • 3986190
    • Theory for the folding and stability of globular proteins. KA Dill, Biochemistry 1985 24 6 1501 1509 3986190
    • (1985) Biochemistry , vol.24 , Issue.6 , pp. 1501-1509
    • Dill, K.A.1
  • 47
    • 0019489088 scopus 로고
    • Folding of protein fragments
    • 6266231
    • Folding of protein fragments. DB Wetlaufer, Adv Protein Chem 1981 34 61 92 6266231
    • (1981) Adv Protein Chem , vol.34 , pp. 61-92
    • Wetlaufer, D.B.1
  • 48
    • 0024379820 scopus 로고
    • The de novo design of protein structures
    • 2672455
    • The de novo design of protein structures. JS Richardson DC Richardson, Trends Biochem Sci 1989 14 7 304 309 2672455
    • (1989) Trends Biochem Sci , vol.14 , Issue.7 , pp. 304-309
    • Richardson, J.S.1    Richardson, D.C.2
  • 49
    • 0030573025 scopus 로고    scopus 로고
    • The Disulphide [beta]-Cross: From Cystine Geometry and Clustering to Classification of Small Disulphide-rich Protein Folds
    • 8969308
    • The Disulphide [beta]-Cross: From Cystine Geometry and Clustering to Classification of Small Disulphide-rich Protein Folds. PM Harrison MJE Sternberg, Journal of Molecular Biology 1996 264 3 603 623 8969308
    • (1996) Journal of Molecular Biology , vol.264 , Issue.3 , pp. 603-623
    • Harrison, P.M.1    Sternberg, M.J.E.2
  • 50
    • 0034677208 scopus 로고    scopus 로고
    • New structural motifs on the chymotrypsin fold and their potential roles in complement factor B
    • 10637221
    • New structural motifs on the chymotrypsin fold and their potential roles in complement factor B. H Jing Y Xu M Carson D Moore KJ Macon JE Volanakis SV Narayana, Embo J 2000 19 2 164 173 10637221
    • (2000) Embo J , vol.19 , Issue.2 , pp. 164-173
    • Jing, H.1    Xu, Y.2    Carson, M.3    Moore, D.4    MacOn, K.J.5    Volanakis, J.E.6    Narayana, S.V.7
  • 51
    • 0034723145 scopus 로고    scopus 로고
    • Human plasminogen catalytic domain undergoes an unusual conformational change upon activation
    • 10656799
    • Human plasminogen catalytic domain undergoes an unusual conformational change upon activation. X Wang S Terzyan J Tang JA Loy X Lin XC Zhang, J Mol Biol 2000 295 4 903 914 10656799
    • (2000) J Mol Biol , vol.295 , Issue.4 , pp. 903-914
    • Wang, X.1    Terzyan, S.2    Tang, J.3    Loy, J.A.4    Lin, X.5    Zhang, X.C.6
  • 52
    • 0032530323 scopus 로고    scopus 로고
    • The crystal structure of the novel snake venom plasminogen activator TSV-PA: A prototype structure for snake venom serine proteinases
    • 9753698
    • The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases. MA Parry U Jacob R Huber A Wisner C Bon W Bode, Structure 1998 6 9 1195 1206 9753698
    • (1998) Structure , vol.6 , Issue.9 , pp. 1195-1206
    • Parry, M.A.1    Jacob, U.2    Huber, R.3    Wisner, A.4    Bon, C.5    Bode, W.6
  • 53
    • 0035826861 scopus 로고    scopus 로고
    • Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins
    • 11331761
    • Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins. JC Lougheed JM Holton T Alber JF Bazan TM Handel, Proc Natl Acad Sci USA 2001 98 10 5515 5520 11331761
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.10 , pp. 5515-5520
    • Lougheed, J.C.1    Holton, J.M.2    Alber, T.3    Bazan, J.F.4    Handel, T.M.5
  • 54
    • 0025836761 scopus 로고
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm
    • 1938970
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. AI Derman J Beckwith, Journal of bacteriology 1991 173 23 7719 7722 1938970
    • (1991) Journal of Bacteriology , vol.173 , Issue.23 , pp. 7719-7722
    • Derman, A.I.1    Beckwith, J.2
  • 56
    • 0030941829 scopus 로고    scopus 로고
    • The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coli Cytoplasm
    • 9188456
    • The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coli Cytoplasm. WA Prinz F Aslund A Holmgren J Beckwith, J Biol Chem 1997 272 25 15661 15667 9188456
    • (1997) J Biol Chem , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 57
  • 58
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone Activity with a Redox Switch
    • 10025400
    • Chaperone Activity with a Redox Switch. U Jakob W Muse M Eser JCA Bardwell, Cell 1999 96 3 341 352 10025400
    • (1999) Cell , vol.96 , Issue.3 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 59
    • 0034636987 scopus 로고    scopus 로고
    • The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
    • 10926519
    • The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. EA Toth C Worby JE Dixon ER Goedken S Marqusee TO Yeates, Journal of Molecular Biology 2000 301 2 433 450 10926519
    • (2000) Journal of Molecular Biology , vol.301 , Issue.2 , pp. 433-450
    • Toth, E.A.1    Worby, C.2    Dixon, J.E.3    Goedken, E.R.4    Marqusee, S.5    Yeates, T.O.6
  • 61
  • 62
    • 0347989249 scopus 로고    scopus 로고
    • Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. a structural and mechanistic comparison between the recombinant human and the purified porcine enzyme
    • 14719797
    • Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme. J Bar A Weber T Hoffmann J Stork M Wermann L Wagner S Aust B Gerhartz HU Demuth, Biol Chem 2003 384 12 1553 1563 14719797
    • (2003) Biol Chem , vol.384 , Issue.12 , pp. 1553-1563
    • Bar, J.1    Weber, A.2    Hoffmann, T.3    Stork, J.4    Wermann, M.5    Wagner, L.6    Aust, S.7    Gerhartz, B.8    Demuth, H.U.9
  • 64
    • 0032578420 scopus 로고    scopus 로고
    • Thermophilic xylanase from Thermomyces lanuginosus: High-resolution X-ray structure and modeling studies
    • 9753433
    • Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies. K Gruber G Klintschar M Hayn A Schlacher W Steiner C Kratky, Biochemistry 1998 37 39 13475 13485 9753433
    • (1998) Biochemistry , vol.37 , Issue.39 , pp. 13475-13485
    • Gruber, K.1    Klintschar, G.2    Hayn, M.3    Schlacher, A.4    Steiner, W.5    Kratky, C.6
  • 66
    • 0035937258 scopus 로고    scopus 로고
    • An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase
    • 11254389
    • An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase. DH Anderson G Harth MA Horwitz D Eisenberg, J Mol Biol 2001 307 2 671 681 11254389
    • (2001) J Mol Biol , vol.307 , Issue.2 , pp. 671-681
    • Anderson, D.H.1    Harth, G.2    Horwitz, M.A.3    Eisenberg, D.4
  • 67
    • 0030000290 scopus 로고    scopus 로고
    • Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1
    • 8676383
    • Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1. Z Xia W Dai Y Zhang SA White GD Boyd FS Mathews, J Mol Biol 1996 259 3 480 501 8676383
    • (1996) J Mol Biol , vol.259 , Issue.3 , pp. 480-501
    • Xia, Z.1    Dai, W.2    Zhang, Y.3    White, S.A.4    Boyd, G.D.5    Mathews, F.S.6
  • 68
    • 0033544694 scopus 로고    scopus 로고
    • Calcium-mediated thermostability in the subtilisin superfamily: The crystal structure of Bacillus Ak.1 protease at 1.8 a resolution
    • 10588904
    • Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution. CA Smith HS Toogood HM Baker RM Daniel EN Baker, J Mol Biol 1999 294 4 1027 1040 10588904
    • (1999) J Mol Biol , vol.294 , Issue.4 , pp. 1027-1040
    • Smith, C.A.1    Toogood, H.S.2    Baker, H.M.3    Daniel, R.M.4    Baker, E.N.5
  • 69
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus
    • 9784374
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus. W Gong X Zhu S Liu M Teng L Niu, J Mol Biol 1998 283 3 657 668 9784374
    • (1998) J Mol Biol , vol.283 , Issue.3 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 70
    • 0346493041 scopus 로고    scopus 로고
    • A Novel Database of Disulfide Patterns and its Application to the Discovery of Distantly Related Homologs
    • 14698301
    • A Novel Database of Disulfide Patterns and its Application to the Discovery of Distantly Related Homologs. HWT van Vlijmen A Gupta LS Narasimhan J Singh, Journal of Molecular Biology 2004 335 4 1083 1092 14698301
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 1083-1092
    • Van Vlijmen, H.W.T.1    Gupta, A.2    Narasimhan, L.S.3    Singh, J.4
  • 71
    • 0033777743 scopus 로고    scopus 로고
    • Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer
    • 11106161
    • Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer. T Xiao DL DeCamp SR Spran, Protein Sci 2000 9 10 1889 1897 11106161
    • (2000) Protein Sci , vol.9 , Issue.10 , pp. 1889-1897
    • Xiao, T.1    Decamp, D.L.2    Spran, S.R.3
  • 72
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • 11439028
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. L Serre K Pereira de Jesus C Zelwer N Bureaud F Schoentgen H Benedetti, J Mol Biol 2001 310 3 617 634 11439028
    • (2001) J Mol Biol , vol.310 , Issue.3 , pp. 617-634
    • Serre, L.1    Pereira De Jesus, K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Benedetti, H.6
  • 73
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • 11188691
    • A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. CL Colbert MM Couture LD Eltis JT Bolin, Structure 2000 8 12 1267 1278 11188691
    • (2000) Structure , vol.8 , Issue.12 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.2    Eltis, L.D.3    Bolin, J.T.4
  • 74
    • 1842339881 scopus 로고    scopus 로고
    • Interresidue interactions in protein classes
    • 9094738
    • Interresidue interactions in protein classes. Z Gugolya Z Dosztanyi I Simon, Proteins 1997 27 3 360 366 9094738
    • (1997) Proteins , vol.27 , Issue.3 , pp. 360-366
    • Gugolya, Z.1    Dosztanyi, Z.2    Simon, I.3
  • 75
    • 0031551577 scopus 로고    scopus 로고
    • Stabilization centers in proteins: Identification, characterization and predictions
    • 9325115
    • Stabilization centers in proteins: identification, characterization and predictions. Z Dosztanyi A Fiser I Simon, J Mol Biol 1997 272 4 597 612 9325115
    • (1997) J Mol Biol , vol.272 , Issue.4 , pp. 597-612
    • Dosztanyi, Z.1    Fiser, A.2    Simon, I.3
  • 76
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • 934293
    • Structural patterns in globular proteins. M Levitt C Chothia, Nature 1976 261 5561 552 558 934293
    • (1976) Nature , vol.261 , Issue.5561 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 77
    • 13944284540 scopus 로고    scopus 로고
    • Native and modeled disulfide bonds in proteins: Knowledge-based approaches toward structure prediction of disulfide-rich polypeptides
    • 15645448
    • Native and modeled disulfide bonds in proteins: knowledge-based approaches toward structure prediction of disulfide-rich polypeptides. RR Thangudu A Vinayagam G Pugalenthi A Manonmani B Offmann R Sowdhamini, Proteins 2005 58 4 866 879 15645448
    • (2005) Proteins , vol.58 , Issue.4 , pp. 866-879
    • Thangudu, R.R.1    Vinayagam, A.2    Pugalenthi, G.3    Manonmani, A.4    Offmann, B.5    Sowdhamini, R.6
  • 78
    • 0037880487 scopus 로고    scopus 로고
    • MODIP revisited: Re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins
    • 12702798
    • MODIP revisited: re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins. VS Dani C Ramakrishnan R Varadarajan, Protein Eng 2003 16 3 187 193 12702798
    • (2003) Protein Eng , vol.16 , Issue.3 , pp. 187-193
    • Dani, V.S.1    Ramakrishnan, C.2    Varadarajan, R.3
  • 79
    • 27544439433 scopus 로고    scopus 로고
    • Evolutionary plasticity of protein families: Coupling between sequence and structure variation
    • 16184609
    • Evolutionary plasticity of protein families: coupling between sequence and structure variation. AR Panchenko YI Wolf LA Panchenko T Madej, Proteins 2005 61 3 535 544 16184609
    • (2005) Proteins , vol.61 , Issue.3 , pp. 535-544
    • Panchenko, A.R.1    Wolf, Y.I.2    Panchenko, L.A.3    Madej, T.4
  • 80
    • 0034677669 scopus 로고    scopus 로고
    • Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores
    • 10704319
    • Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores. CA Wilson J Kreychman M Gerstein, J Mol Biol 2000 297 1 233 249 10704319
    • (2000) J Mol Biol , vol.297 , Issue.1 , pp. 233-249
    • Wilson, C.A.1    Kreychman, J.2    Gerstein, M.3
  • 81
    • 14744305761 scopus 로고    scopus 로고
    • Using a library of structural templates to recognise catalytic sites and explore their evolution in homologous families
    • 15755451
    • Using a library of structural templates to recognise catalytic sites and explore their evolution in homologous families. JW Torrance GJ Bartlett CT Porter JM Thornton, J Mol Biol 2005 347 3 565 581 15755451
    • (2005) J Mol Biol , vol.347 , Issue.3 , pp. 565-581
    • Torrance, J.W.1    Bartlett, G.J.2    Porter, C.T.3    Thornton, J.M.4
  • 82
    • 0027934188 scopus 로고
    • Intra-A chain disulfide bond (A6-11) of insulin is essential for displaying its activity
    • 7804129
    • Intra-A chain disulfide bond (A6-11) of insulin is essential for displaying its activity. Y Dai JG Tang, Biochem Mol Biol Int 1994 33 6 1049 1053 7804129
    • (1994) Biochem Mol Biol Int , vol.33 , Issue.6 , pp. 1049-1053
    • Dai, Y.1    Tang, J.G.2
  • 83
    • 0025292406 scopus 로고
    • Structural effects induced by removal of a disulfide-bridge: The X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 a
    • 1699222
    • Structural effects induced by removal of a disulfide-bridge: the X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A. C Eigenbrot M Randal AA Kossiakoff, Protein Eng 1990 3 7 591 598 1699222
    • (1990) Protein Eng , vol.3 , Issue.7 , pp. 591-598
    • Eigenbrot, C.1    Randal, M.2    Kossiakoff, A.A.3
  • 84
    • 0036187342 scopus 로고    scopus 로고
    • Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor
    • 11842239
    • Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor. T Li H Yamane T Arakawa LO Narhi J Philo, Protein Eng 2002 15 1 59 64 11842239
    • (2002) Protein Eng , vol.15 , Issue.1 , pp. 59-64
    • Li, T.1    Yamane, H.2    Arakawa, T.3    Narhi, L.O.4    Philo, J.5
  • 85
    • 0022003075 scopus 로고
    • The genealogy of some recently evolved vertebrate proteins
    • The genealogy of some recently evolved vertebrate proteins. RF Doolittle, Trends in Biochemical Sciences 1985 10 6 233 237
    • (1985) Trends in Biochemical Sciences , vol.10 , Issue.6 , pp. 233-237
    • Doolittle, R.F.1
  • 86
    • 0037162464 scopus 로고    scopus 로고
    • Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds
    • 12107280
    • Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds. P Mallick DR Boutz D Eisenberg TO Yeates, Proc Natl Acad Sci USA 2002 99 15 9679 9684 12107280
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.15 , pp. 9679-9684
    • Mallick, P.1    Boutz, D.R.2    Eisenberg, D.3    Yeates, T.O.4
  • 87
    • 38049059360 scopus 로고    scopus 로고
    • Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea"
    • 17508126
    • Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea". R Ladenstein B Ren, Extremophiles 2008 12 1 29 38 17508126
    • (2008) Extremophiles , vol.12 , Issue.1 , pp. 29-38
    • Ladenstein, R.1    Ren, B.2
  • 88
    • 0028239038 scopus 로고
    • Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies
    • 8145256
    • Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies. H Nakashima K Nishikawa, J Mol Biol 1994 238 1 54 61 8145256
    • (1994) J Mol Biol , vol.238 , Issue.1 , pp. 54-61
    • Nakashima, H.1    Nishikawa, K.2
  • 89
    • 0020817034 scopus 로고
    • Classification of proteins into groups based on amino acid composition and other characters. II. Grouping into four types
    • 6643433
    • Classification of proteins into groups based on amino acid composition and other characters. II. Grouping into four types. K Nishikawa Y Kubota T Ooi, Journal of biochemistry 1983 94 3 997 1007 6643433
    • (1983) Journal of Biochemistry , vol.94 , Issue.3 , pp. 997-1007
    • Nishikawa, K.1    Kubota, Y.2    Ooi, T.3
  • 90
    • 33947434131 scopus 로고    scopus 로고
    • Analycys: A database for conservation and conformation of disulphide bonds in homologous protein domains
    • 17285632
    • Analycys: a database for conservation and conformation of disulphide bonds in homologous protein domains. RR Thangudu P Sharma N Srinivasan B Offmann, Proteins 2007 67 2 255 261 17285632
    • (2007) Proteins , vol.67 , Issue.2 , pp. 255-261
    • Thangudu, R.R.1    Sharma, P.2    Srinivasan, N.3    Offmann, B.4
  • 92
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • 10891285
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. O Emanuelsson H Nielsen S Brunak G von Heijne, J Mol Biol 2000 300 4 1005 1016 10891285
    • (2000) J Mol Biol , vol.300 , Issue.4 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 93
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • 10087920
    • PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. K Nakai P Horton, Trends Biochem Sci 1999 24 1 34 36 10087920
    • (1999) Trends Biochem Sci , vol.24 , Issue.1 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 94
    • 0034843744 scopus 로고    scopus 로고
    • Support vector machine approach for protein subcellular localization prediction
    • 11524373
    • Support vector machine approach for protein subcellular localization prediction. S Hua Z Sun, Bioinformatics 2001 17 8 721 728 11524373
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 721-728
    • Hua, S.1    Sun, Z.2
  • 95
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • 1409577
    • Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. RB Russell GJ Barton, Proteins 1992 14 2 309 323 1409577
    • (1992) Proteins , vol.14 , Issue.2 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 96
    • 0011016770 scopus 로고
    • A method to determine heavy-atom positions for virus structures
    • A method to determine heavy-atom positions for virus structures. P Argos MG Rossmann, Acta Crystallographica 1976 B32 2975 2979
    • (1976) Acta Crystallographica , vol.32 , pp. 2975-2979
    • Argos, P.1    Rossmann, M.G.2
  • 97
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • 6667333
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. W Kabsch C Sander, Biopolymers 1983 22 12 2577 2637 6667333
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 98
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • 5551392
    • The interpretation of protein structures: estimation of static accessibility. B Lee FM Richards, J Mol Biol 1971 55 3 379 400 5551392
    • (1971) J Mol Biol , vol.55 , Issue.3 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 100
    • 0037316590 scopus 로고    scopus 로고
    • DPX: For the analysis of the protein core
    • 12538266
    • DPX: for the analysis of the protein core. A Pintar O Carugo S Pongor, Bioinformatics 2003 19 2 313 314 12538266
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 313-314
    • Pintar, A.1    Carugo, O.2    Pongor, S.3


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