메뉴 건너뛰기




Volumn 9, Issue , 2009, Pages

Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; A widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLYCOSIDASE; PROTEIN VPS10; SORTILIN; UNCLASSIFIED DRUG; VESICULAR TRANSPORT PROTEIN;

EID: 68149182718     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-9-46     Document Type: Article
Times cited : (32)

References (60)
  • 3
    • 0035106757 scopus 로고    scopus 로고
    • Sialidase-like asp-boxes: Sequence-similar structures within different protein folds
    • DOI 10.1110/ps.31901
    • Sialidase-like Asp-boxes: sequence-similar structures within different protein folds. RR Copley RB Russell CP Ponting, Protein Sci 2001 10 2 285 292 11266614 10.1110/ps.31901 (Pubitemid 32225648)
    • (2001) Protein Science , vol.10 , Issue.2 , pp. 285-292
    • Copley, R.R.1    Russell, R.B.2    Ponting, C.P.3
  • 4
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • DOI 10.1016/S0969-2126(00)00053-8
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. S Crennell E Garman G Laver E Vimr G Taylor, Structure 1994 2 6 535 544 10.1016/S0969-2126(00)00053-8 7922030 (Pubitemid 2100410)
    • (1994) Structure , vol.2 , Issue.6 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 5
    • 0029645872 scopus 로고
    • The three domains of a bacterial sialidase: A beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll
    • DOI 10.1016/S0969-2126(01)00255-6
    • The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. A Gaskell S Crennell G Taylor, Structure 1995 3 11 1197 1205 10.1016/S0969-2126(01)00255-6 8591030 (Pubitemid 3001427)
    • (1995) Structure , vol.3 , Issue.11 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.2    Taylor, G.3
  • 6
    • 44049099406 scopus 로고    scopus 로고
    • The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates
    • 18218621 10.1074/jbc.M710247200
    • The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates. SL Newstead JA Potter JC Wilson G Xu CH Chien AG Watts SG Withers GL Taylor, J Biol Chem 2008 283 14 9080 9088 18218621 10.1074/jbc.M710247200
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 9080-9088
    • Newstead, S.L.1    Potter, J.A.2    Wilson, J.C.3    Xu, G.4    Chien, C.H.5    Watts, A.G.6    Withers, S.G.7    Taylor, G.L.8
  • 7
    • 51149114195 scopus 로고    scopus 로고
    • Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA
    • 18765901 10.1107/S1744309108024044
    • Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA. G Xu X Li PW Andrew GL Taylor, Acta Crystallogr Sect F Struct Biol Cryst Commun 2008 64 Pt 9 772 775 18765901 10.1107/S1744309108024044
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , Issue.PART 9 , pp. 772-775
    • Xu, G.1    Li, X.2    Andrew, P.W.3    Taylor, G.L.4
  • 8
    • 84954358046 scopus 로고    scopus 로고
    • Crystal structure of the NanB sialidase from Streptococcus pneumoniae
    • 10.1016/j.jmb.2008.09.032 18835278
    • Crystal structure of the NanB sialidase from Streptococcus pneumoniae. G Xu JA Potter RJ Russell MR Oggioni PW Andrew GL Taylor, J Mol Biol 2008 384 2 436 449 10.1016/j.jmb.2008.09.032 18835278
    • (2008) J Mol Biol , vol.384 , Issue.2 , pp. 436-449
    • Xu, G.1    Potter, J.A.2    Russell, R.J.3    Oggioni, M.R.4    Andrew, P.W.5    Taylor, G.L.6
  • 9
    • 59649099923 scopus 로고    scopus 로고
    • Structural Studies on the Pseudomonas aeruginosa Sialidase-Like Enzyme PA2794 Suggest Substrate and Mechanistic Variations
    • 10.1016/j.jmb.2008.12.084 19166860
    • Structural Studies on the Pseudomonas aeruginosa Sialidase-Like Enzyme PA2794 Suggest Substrate and Mechanistic Variations. G Xu C Ryan MJ Kiefel JC Wilson GL Taylor, J Mol Biol 2009 386 3 828 40 10.1016/j.jmb.2008.12.084 19166860
    • (2009) J Mol Biol , vol.386 , Issue.3 , pp. 828-40
    • Xu, G.1    Ryan, C.2    Kiefel, M.J.3    Wilson, J.C.4    Taylor, G.L.5
  • 11
    • 0036809661 scopus 로고    scopus 로고
    • The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis
    • DOI 10.1016/S1097-2765(02)00680-9
    • The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. A Buschiazzo MF Amaya ML Cremona AC Frasch PM Alzari, Mol Cell 2002 10 4 757 768 10.1016/S1097-2765(02)00680-9 12419220 (Pubitemid 35339437)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 757-768
    • Buschiazzo, A.1    Amaya, M.F.2    Cremona, M.L.3    Frasch, A.C.4    Alzari, P.M.5
  • 12
    • 0032522642 scopus 로고    scopus 로고
    • The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2 - 3Gal specificity
    • 10.1016/S0969-2126(98)00053-7 9562562
    • The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2 - 3Gal specificity. Y Luo SC Li MY Chou YT Li M Luo, Structure 1998 6 4 521 530 10.1016/S0969-2126(98)00053-7 9562562
    • (1998) Structure , vol.6 , Issue.4 , pp. 521-530
    • Luo, Y.1    Li, S.C.2    Chou, M.Y.3    Li, Y.T.4    Luo, M.5
  • 13
    • 12844253114 scopus 로고    scopus 로고
    • Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition
    • 15501818
    • Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition. LM Chavas C Tringali P Fusi B Venerando G Tettamanti R Kato E Monti S Wakatsuki, J Biol Chem 2005 280 1 469 475 15501818
    • (2005) J Biol Chem , vol.280 , Issue.1 , pp. 469-475
    • Chavas, L.M.1    Tringali, C.2    Fusi, P.3    Venerando, B.4    Tettamanti, G.5    Kato, R.6    Monti, E.7    Wakatsuki, S.8
  • 15
    • 41149106300 scopus 로고    scopus 로고
    • Evolution of the beta-propeller fold
    • 10.1002/prot.21764 17979191
    • Evolution of the beta-propeller fold. I Chaudhuri J Soding AN Lupas, Proteins 2008 71 2 795 803 10.1002/prot.21764 17979191
    • (2008) Proteins , vol.71 , Issue.2 , pp. 795-803
    • Chaudhuri, I.1    Soding, J.2    Lupas, A.N.3
  • 16
    • 3142572747 scopus 로고    scopus 로고
    • Tandem repeat of a seven-bladed β-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase
    • DOI 10.1016/j.str.2004.04.020, PII S096921260400200X
    • Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase. K Yaoi H Kondo N Noro M Suzuki S Tsuda Y Mitsuishi, Structure 2004 12 7 1209 1217 10.1016/j.str.2004.04.020 15242597 (Pubitemid 38900763)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1209-1217
    • Yaoi, K.1    Kondo, H.2    Noro, N.3    Suzuki, M.4    Tsuda, S.5    Mitsuishi, Y.6
  • 18
    • 0038785977 scopus 로고    scopus 로고
    • Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
    • DOI 10.1046/j.1432-1327.1999.00176.x
    • Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. MU Jorgensen SD Emr JR Winther, Eur J Biochem 1999 260 2 461 469 10.1046/j.1432-1327.1999.00176.x 10095782 (Pubitemid 29122543)
    • (1999) European Journal of Biochemistry , vol.260 , Issue.2 , pp. 461-469
    • Jorgensen, M.U.1    Emr, S.D.2    Winther, J.R.3
  • 20
    • 33747626961 scopus 로고    scopus 로고
    • Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography
    • DOI 10.1038/sj.emboj.7601240, PII 7601240
    • Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography. T Nogi N Yasui M Hattori K Iwasaki J Takagi, EMBO J 2006 25 15 3675 3683 16858396 10.1038/sj.emboj.7601240 (Pubitemid 44264877)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3675-3683
    • Nogi, T.1    Yasui, N.2    Hattori, M.3    Iwasaki, K.4    Takagi, J.5
  • 21
    • 0032568859 scopus 로고    scopus 로고
    • Detection of protein three-dimensional side-chain patterns: New examples of convergent evolution
    • DOI 10.1006/jmbi.1998.1844
    • Detection of protein three-dimensional side-chain patterns: new examples of convergent evolution. RB Russell, J Mol Biol 1998 279 5 1211 1227 10.1006/jmbi.1998.1844 9642096 (Pubitemid 28302396)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.5 , pp. 1211-1227
    • Russell, R.B.1
  • 22
    • 0030249583 scopus 로고    scopus 로고
    • Site-directed mutations of the catalytic and conserved amino acids of the neuraminidase gene, nanH, of Clostridium perfringens ATCC 10543
    • DOI 10.1016/0141-0229(95)00245-6
    • Site-directed mutations of the catalytic and conserved amino acids of the neuraminidase gene, nanH, of Clostridium perfringens ATCC 10543. CH Chien YJ Shann SY Sheu, Enzyme Microb Technol 1996 19 4 267 276 10.1016/0141-0229(95) 00245-6 8987487 (Pubitemid 26293739)
    • (1996) Enzyme and Microbial Technology , vol.19 , Issue.4 , pp. 267-276
    • Chien, C.-H.1    Shann, Y.-J.2    Sheu, S.-Y.3
  • 23
    • 0034993094 scopus 로고    scopus 로고
    • Protein folds propelled by diversity
    • DOI 10.1016/S0079-6107(01)00007-4, PII S0079610701000074
    • Protein folds propelled by diversity. M Paoli, Prog Biophys Mol Biol 2001 76 1-2 103 130 10.1016/S0079-6107(01)00007-4 11389935 (Pubitemid 32523899)
    • (2001) Progress in Biophysics and Molecular Biology , vol.76 , Issue.1-2 , pp. 103-130
    • Paoli, M.1
  • 24
    • 0026619682 scopus 로고
    • Bacterial sialidases-roles in pathogenicity and nutrition
    • 10.1093/glycob/2.6.509 1472757
    • Bacterial sialidases-roles in pathogenicity and nutrition. T Corfield, Glycobiology 1992 2 6 509 521 10.1093/glycob/2.6.509 1472757
    • (1992) Glycobiology , vol.2 , Issue.6 , pp. 509-521
    • Corfield, T.1
  • 25
    • 0029781171 scopus 로고    scopus 로고
    • Invasive phenotype of Trypanosoma cruzi restricted to a population expressing trans-sialidase
    • 8751943
    • Invasive phenotype of Trypanosoma cruzi restricted to a population expressing trans-sialidase. ME Pereira K Zhang Y Gong EM Herrera M Ming, Infect Immun 1996 64 9 3884 3892 8751943
    • (1996) Infect Immun , vol.64 , Issue.9 , pp. 3884-3892
    • Pereira, M.E.1    Zhang, K.2    Gong, Y.3    Herrera, E.M.4    Ming, M.5
  • 28
    • 40849088147 scopus 로고    scopus 로고
    • Roles of plasma membrane-associated sialidase NEU3 in human cancers
    • 18023981
    • Roles of plasma membrane-associated sialidase NEU3 in human cancers. T Miyagi T Wada K Yamaguchi, Biochim Biophys Acta 2008 1780 3 532 537 18023981
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.3 , pp. 532-537
    • Miyagi, T.1    Wada, T.2    Yamaguchi, K.3
  • 29
    • 0001437175 scopus 로고    scopus 로고
    • Disorders of Glycoprotein Degradation: -Mannosidosis, -Mannosidosis, Fucosidosis, and Sialidosis
    • New York: McGraw-Hill Beaudet AL, Sly SD, Valle D
    • Disorders of Glycoprotein Degradation: -Mannosidosis, -Mannosidosis, Fucosidosis, and Sialidosis. GH Thomas, The metabolic and molecular bases of inherited disease New York: McGraw-Hill, Beaudet AL, Sly SD, Valle D, 2001 3507 3534
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3507-3534
    • Thomas, G.H.1
  • 30
    • 56549111118 scopus 로고    scopus 로고
    • VPS10P-domain receptors - Regulators of neuronal viability and function
    • 10.1038/nrn2516 19002190
    • VPS10P-domain receptors - regulators of neuronal viability and function. TE Willnow CM Petersen A Nykjaer, Nat Rev Neurosci 2008 9 12 899 909 10.1038/nrn2516 19002190
    • (2008) Nat Rev Neurosci , vol.9 , Issue.12 , pp. 899-909
    • Willnow, T.E.1    Petersen, C.M.2    Nykjaer, A.3
  • 31
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • DOI 10.1016/0022-2836(89)90583-4
    • Conformation of beta-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. BL Sibanda TL Blundell JM Thornton, J Mol Biol 1989 206 4 759 777 10.1016/0022-2836(89)90583-4 2500530 (Pubitemid 19137429)
    • (1989) Journal of Molecular Biology , vol.206 , Issue.4 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 32
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • 7756980 10.1002/pro.5560031206
    • A revised set of potentials for beta-turn formation in proteins. EG Hutchinson JM Thornton, Protein Sci 1994 3 12 2207 2216 7756980 10.1002/pro.5560031206
    • (1994) Protein Sci , vol.3 , Issue.12 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 33
    • 33746614112 scopus 로고    scopus 로고
    • Crystal structure of a type III pantothenate kinase: Insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria
    • DOI 10.1128/JB.00469-06
    • Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria. K Yang Y Eyobo LA Brand D Martynowski D Tomchick E Strauss H Zhang, J Bacteriol 2006 188 15 5532 5540 16855243 10.1128/JB.00469-06 (Pubitemid 44157310)
    • (2006) Journal of Bacteriology , vol.188 , Issue.15 , pp. 5532-5540
    • Yang, K.1    Eyobo, Y.2    Brand, L.A.3    Martynowski, D.4    Tomchick, D.5    Strauss, E.6    Zhang, H.7
  • 34
    • 0000232426 scopus 로고
    • Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7 A resolution
    • 10.1107/S0907444992007261 15299531
    • Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7 A resolution. J Sevcik CP Hill Z Dauter KS Wilson, Acta Crystallogr D Biol Crystallogr 1993 49 Pt 2 257 271 10.1107/S0907444992007261 15299531
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , Issue.PART 2 , pp. 257-271
    • Sevcik, J.1    Hill, C.P.2    Dauter, Z.3    Wilson, K.S.4
  • 35
    • 0030935726 scopus 로고    scopus 로고
    • RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations
    • 10.1093/protein/10.3.273 9153077
    • RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations. AL Okorokov KI Panov WA Offen VG Mukhortov AA Antson MY Karpeisky AJ Wilkinson GG Dodson, Protein Eng 1997 10 3 273 278 10.1093/protein/10.3.273 9153077
    • (1997) Protein Eng , vol.10 , Issue.3 , pp. 273-278
    • Okorokov, A.L.1    Panov, K.I.2    Offen, W.A.3    Mukhortov, V.G.4    Antson, A.A.5    Karpeisky, M.Y.6    Wilkinson, A.J.7    Dodson, G.G.8
  • 38
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • 15214846
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition. AB Boraston DN Bolam HJ Gilbert GJ Davies, Biochem J 2004 382 Pt 3 769 781 15214846
    • (2004) Biochem J , vol.382 , Issue.PART 3 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 39
    • 0033794678 scopus 로고    scopus 로고
    • Stereochemical metrics of lectin-carbohydrate interactions: Comparison with protein-protein interfaces
    • 10.1093/glycob/10.10.993 11030745
    • Stereochemical metrics of lectin-carbohydrate interactions: comparison with protein-protein interfaces. E Garcia-Hernandez RA Zubillaga A Rodriguez-Romero A Hernandez-Arana, Glycobiology 2000 10 10 993 1000 10.1093/glycob/10.10.993 11030745
    • (2000) Glycobiology , vol.10 , Issue.10 , pp. 993-1000
    • Garcia-Hernandez, E.1    Zubillaga, R.A.2    Rodriguez-Romero, A.3    Hernandez-Arana, A.4
  • 40
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • 10.1146/annurev.bi.65.070196.002301 8811186
    • Structural basis of lectin-carbohydrate recognition. WI Weis K Drickamer, Annu Rev Biochem 1996 65 441 473 10.1146/annurev.bi.65.070196.002301 8811186
    • (1996) Annu Rev Biochem , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 43
    • 0242558716 scopus 로고    scopus 로고
    • Beta propellers: Structural rigidity and functional diversity
    • 10.1016/S0959-440X(99)00035-4 10607670
    • Beta propellers: structural rigidity and functional diversity. V Fulop DT Jones, Curr Opin Struct Biol 1999 9 6 715 721 10.1016/S0959-440X(99)00035-4 10607670
    • (1999) Curr Opin Struct Biol , vol.9 , Issue.6 , pp. 715-721
    • Fulop, V.1    Jones, D.T.2
  • 44
    • 0032475963 scopus 로고    scopus 로고
    • Supersites within superfolds. Binding site similarity in the absence of homology
    • DOI 10.1006/jmbi.1998.2043
    • Supersites within superfolds. Binding site similarity in the absence of homology. RB Russell PD Sasieni MJ Sternberg, J Mol Biol 1998 282 4 903 918 10.1006/jmbi.1998.2043 9743635 (Pubitemid 28442355)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.4 , pp. 903-918
    • Russell, R.B.1    Sasieni, P.D.2    Sternberg, M.J.E.3
  • 45
    • 3142595278 scopus 로고    scopus 로고
    • Crystal structure of the HGF β-chain in complex with the Sema domain of the Met receptor
    • DOI 10.1038/sj.emboj.7600243
    • Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor. J Stamos RA Lazarus X Yao D Kirchhofer C Wiesmann, EMBO J 2004 23 12 2325 2335 15167892 10.1038/sj.emboj.7600243 (Pubitemid 38954840)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2325-2335
    • Stamos, J.1    Lazarus, R.A.2    Yao, X.3    Kirchhofer, D.4    Wiesmann, C.5
  • 46
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
    • DOI 10.1038/13294
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. M Paoli BF Anderson HM Baker WT Morgan A Smith EN Baker, Nat Struct Biol 1999 6 10 926 931 10.1038/13294 10504726 (Pubitemid 29463305)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 47
    • 0033522446 scopus 로고    scopus 로고
    • Tachylectin-2: Crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
    • DOI 10.1093/emboj/18.9.2313
    • Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. HG Beisel S Kawabata S Iwanaga R Huber W Bode, EMBO J 1999 18 9 2313 2322 10228146 10.1093/emboj/18.9.2313 (Pubitemid 29213265)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2313-2322
    • Beisel, H.-G.1    Kawabata, S.-I.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 48
    • 0026671355 scopus 로고
    • Structural principles for the propeller assembly of beta-sheets: The preference for seven-fold symmetry
    • 10.1002/prot.340140206 1409568
    • Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. AG Murzin, Proteins 1992 14 2 191 201 10.1002/prot.340140206 1409568
    • (1992) Proteins , vol.14 , Issue.2 , pp. 191-201
    • Murzin, A.G.1
  • 49
    • 37849008677 scopus 로고    scopus 로고
    • RCC1-like repeat proteins: A pangenomic, structurally diverse new superfamily of beta-propeller domains
    • 10.1002/prot.21521 17680689
    • RCC1-like repeat proteins: a pangenomic, structurally diverse new superfamily of beta-propeller domains. TJ Stevens M Paoli, Proteins 2008 70 2 378 387 10.1002/prot.21521 17680689
    • (2008) Proteins , vol.70 , Issue.2 , pp. 378-387
    • Stevens, T.J.1    Paoli, M.2
  • 50
    • 33746536641 scopus 로고    scopus 로고
    • Engineering of β-propeller protein scaffolds by multiple gene duplication and fusion of an idealized WD repeat
    • DOI 10.1016/j.bioeng.2006.02.002, PII S1389034406000219
    • Engineering of beta-propeller protein scaffolds by multiple gene duplication and fusion of an idealized WD repeat. M Nikkhah Z Jawad-Alami M Demydchuk D Ribbons M Paoli, Biomol Eng 2006 23 4 185 194 10.1016/j.bioeng.2006. 02.002 16651025 (Pubitemid 44142330)
    • (2006) Biomolecular Engineering , vol.23 , Issue.4 , pp. 185-194
    • Nikkhah, M.1    Jawad-Alami, Z.2    Demydchuk, M.3    Ribbons, D.4    Paoli, M.5
  • 51
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • Cambridge: Royal Society of Chemistry Gilbert HJ, Davies GJ, Henrissat B, Svensson B
    • Carbohydrate-active enzymes: an integrated database approach. PM Coutinho B Henrissat, Recent advances in Carbohydrate Bioenginerring Cambridge: Royal Society of Chemistry, Gilbert HJ, Davies GJ, Henrissat B, Svensson B, 1999 3 12
    • (1999) Recent Advances in Carbohydrate Bioenginerring , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 54
  • 55
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • DOI 10.1006/jmbi.1998.2393
    • Recognition of spatial motifs in protein structures. GJ Kleywegt, J Mol Biol 1999 285 4 1887 1897 10.1006/jmbi.1998.2393 9917419 (Pubitemid 29060478)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 58
    • 58149187898 scopus 로고    scopus 로고
    • PDBsum new things
    • 18996896 10.1093/nar/gkn860
    • PDBsum new things. RA Laskowski, Nucleic Acids Res 2009 37 Database D355 9 18996896 10.1093/nar/gkn860
    • (2009) Nucleic Acids Res , pp. 355-9
    • Laskowski, R.A.1
  • 60
    • 1342288004 scopus 로고    scopus 로고
    • The Jalview Java alignment editor
    • DOI 10.1093/bioinformatics/btg430
    • The Jalview Java alignment editor. M Clamp J Cuff SM Searle GJ Barton, Bioinformatics 2004 20 3 426 427 10.1093/bioinformatics/btg430 14960472 (Pubitemid 38262778)
    • (2004) Bioinformatics , vol.20 , Issue.3 , pp. 426-427
    • Clamp, M.1    Cuff, J.2    Searle, S.M.3    Barton, G.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.