메뉴 건너뛰기




Volumn 150, Issue 2, 2006, Pages 256-267

Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan parasite proteomes

Author keywords

Apicomplexan parasites; Intrinsically unstructured proteins; Low complexity region; Plasmodium falciparum; Repeats

Indexed keywords

PARASITE ANTIBODY; PROTEOME; PROTOZOAL PROTEIN;

EID: 33750711671     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2006.08.011     Document Type: Article
Times cited : (104)

References (68)
  • 1
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite. Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., et al. Genome sequence of the human malaria parasite. Plasmodium falciparum. Nature 419 (2002) 498-511
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3
  • 3
    • 0035104190 scopus 로고    scopus 로고
    • Low-complexity regions in Plasmodium falciparum proteins
    • Pizzi E., and Frontali C. Low-complexity regions in Plasmodium falciparum proteins. Genome Res 11 (2001) 218-229
    • (2001) Genome Res , vol.11 , pp. 218-229
    • Pizzi, E.1    Frontali, C.2
  • 4
    • 0035101023 scopus 로고    scopus 로고
    • Function low-complexity regions in Plasmodium proteins: in search of a function
    • Brocchieri L. Function low-complexity regions in Plasmodium proteins: in search of a function. Genome Res 11 (2001) 195-197
    • (2001) Genome Res , vol.11 , pp. 195-197
    • Brocchieri, L.1
  • 5
    • 0033638015 scopus 로고    scopus 로고
    • CAST: an iterative algorithm for the complexity analysis of sequence tracts. Complexity analysis of sequence tracts
    • Promponas V.J., Enright A.J., Tsoka S., et al. CAST: an iterative algorithm for the complexity analysis of sequence tracts. Complexity analysis of sequence tracts. Bioinformatics 16 (2000) 915-922
    • (2000) Bioinformatics , vol.16 , pp. 915-922
    • Promponas, V.J.1    Enright, A.J.2    Tsoka, S.3
  • 6
    • 0001514262 scopus 로고
    • Statistics of local complexity in amino acid sequences and sequence databases
    • Wootton J.C., and Federhen S. Statistics of local complexity in amino acid sequences and sequence databases. Comput Chem 17 (1993) 149-163
    • (1993) Comput Chem , vol.17 , pp. 149-163
    • Wootton, J.C.1    Federhen, S.2
  • 7
    • 33745666810 scopus 로고    scopus 로고
    • Heterologous expression of proteins from Plasmodium falciparum: results from 1000 genes
    • Mehlin C., Boni E., Buckner F.S., et al. Heterologous expression of proteins from Plasmodium falciparum: results from 1000 genes. Mol Biochem Parasitol 148 (2006) 144-160
    • (2006) Mol Biochem Parasitol , vol.148 , pp. 144-160
    • Mehlin, C.1    Boni, E.2    Buckner, F.S.3
  • 9
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337 (2004) 635-645
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 10
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky V.N., Oldfield C.J., and Dunker A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18 (2005) 343-384
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 11
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 41 (2000) 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 12
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 27 (2002) 527-533
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 14
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6 (2005) 197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 15
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba K. Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells 6 (2001) 1-12
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 16
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P., Szasz C., and Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci 30 (2005) 484-489
    • (2005) Trends Biochem Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0036174712 scopus 로고    scopus 로고
    • Continuum secondary structure captures protein flexibility
    • Andersen C.A., Palmer A.G., Brunak S., and Rost B. Continuum secondary structure captures protein flexibility. Structure (Camb) 10 (2002) 175-184
    • (2002) Structure (Camb) , vol.10 , pp. 175-184
    • Andersen, C.A.1    Palmer, A.G.2    Brunak, S.3    Rost, B.4
  • 22
    • 0037015602 scopus 로고    scopus 로고
    • A proteomic view of the Plasmodium falciparum life cycle
    • Florens L., Washburn M.P., Raine J.D., et al. A proteomic view of the Plasmodium falciparum life cycle. Nature 419 (2002) 520-526
    • (2002) Nature , vol.419 , pp. 520-526
    • Florens, L.1    Washburn, M.P.2    Raine, J.D.3
  • 23
    • 0242362157 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins from position specific score matrices
    • Jones D.T., and Ward J.J. Prediction of disordered regions in proteins from position specific score matrices. Proteins 53 Suppl 6 (2003) 573-578
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 573-578
    • Jones, D.T.1    Ward, J.J.2
  • 24
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky J., Felder C.E., Zeev-Ben-Mordehai T., et al. FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21 (2005) 3435-3438
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3
  • 25
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z., Csizmok V., Tompa P., and Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347 (2005) 827-839
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 26
    • 24744453057 scopus 로고    scopus 로고
    • Striped sheets and protein contact prediction
    • MacCallum R.M. Striped sheets and protein contact prediction. Bioinformatics 20 Suppl 1 (2004) I224-I231
    • (2004) Bioinformatics , vol.20 , Issue.SUPPL. 1
    • MacCallum, R.M.1
  • 27
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J., and Rost B. NORSp: Predictions of long regions without regular secondary structure. Nucleic Acids Res 31 (2003) 3833-3835
    • (2003) Nucleic Acids Res , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 29
    • 0036968309 scopus 로고    scopus 로고
    • Loopy proteins appear conserved in evolution
    • Liu J., Tan H., and Rost B. Loopy proteins appear conserved in evolution. J Mol Biol 322 (2002) 53-64
    • (2002) J Mol Biol , vol.322 , pp. 53-64
    • Liu, J.1    Tan, H.2    Rost, B.3
  • 30
    • 4644370187 scopus 로고    scopus 로고
    • Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
    • Singh G.P., Chandra B.R., Bhattacharya A., Akhouri R.R., Singh S.K., and Sharma A. Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum. Mol Biochem Parasitol 137 (2004) 307-319
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 307-319
    • Singh, G.P.1    Chandra, B.R.2    Bhattacharya, A.3    Akhouri, R.R.4    Singh, S.K.5    Sharma, A.6
  • 31
    • 0034333196 scopus 로고    scopus 로고
    • Rapid automatic detection and alignment of repeats in protein sequences
    • Heger A., and Holm L. Rapid automatic detection and alignment of repeats in protein sequences. Proteins 41 (2000) 224-237
    • (2000) Proteins , vol.41 , pp. 224-237
    • Heger, A.1    Holm, L.2
  • 32
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P., and Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J 18 (2004) 1169-1175
    • (2004) FASEB J , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 33
    • 19944429644 scopus 로고    scopus 로고
    • A comprehensive survey of the Plasmodium life cycle by genomic, transcriptomic, and proteomic analyses
    • Hall N., Karras M., Raine J.D., et al. A comprehensive survey of the Plasmodium life cycle by genomic, transcriptomic, and proteomic analyses. Science 307 (2005) 82-86
    • (2005) Science , vol.307 , pp. 82-86
    • Hall, N.1    Karras, M.2    Raine, J.D.3
  • 34
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen M., Torkkila E., and Riikonen P. Accuracy of protein flexibility predictions. Proteins 19 (1994) 141-149
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 35
    • 0347364621 scopus 로고    scopus 로고
    • Protein flexibility and intrinsic disorder
    • Radivojac P., Obradovic Z., Smith D.K., et al. Protein flexibility and intrinsic disorder. Protein Sci 13 (2004) 71-80
    • (2004) Protein Sci , vol.13 , pp. 71-80
    • Radivojac, P.1    Obradovic, Z.2    Smith, D.K.3
  • 36
    • 1642588230 scopus 로고    scopus 로고
    • A large focus of naturally acquired Plasmodium knowlesi infections in human beings
    • Singh B., Kim Sung L., Matusop A., et al. A large focus of naturally acquired Plasmodium knowlesi infections in human beings. Lancet 363 (2004) 1017-1024
    • (2004) Lancet , vol.363 , pp. 1017-1024
    • Singh, B.1    Kim Sung, L.2    Matusop, A.3
  • 37
    • 33746295014 scopus 로고    scopus 로고
    • On the abundance, amino acid composition, and evolutionary dynamics of low-complexity regions in proteins
    • Depristo M.A., Zilversmit M.M., and Hartl D.L. On the abundance, amino acid composition, and evolutionary dynamics of low-complexity regions in proteins. Gene 378 (2006) 19-30
    • (2006) Gene , vol.378 , pp. 19-30
    • Depristo, M.A.1    Zilversmit, M.M.2    Hartl, D.L.3
  • 38
    • 12744257602 scopus 로고    scopus 로고
    • Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Tettelin H., Carucci D.J., et al. Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum. Science 282 (1998) 1126-1132
    • (1998) Science , vol.282 , pp. 1126-1132
    • Gardner, M.J.1    Tettelin, H.2    Carucci, D.J.3
  • 39
    • 0033527048 scopus 로고    scopus 로고
    • The complete nucleotide sequence of chromosome 3 of Plasmodium falciparum
    • Bowman S., Lawson D., Basham D., et al. The complete nucleotide sequence of chromosome 3 of Plasmodium falciparum. Nature 400 (1999) 506-507
    • (1999) Nature , vol.400 , pp. 506-507
    • Bowman, S.1    Lawson, D.2    Basham, D.3
  • 41
    • 33646559434 scopus 로고    scopus 로고
    • Plasmodium post-genomics: better the bug you know?
    • Kooij T.W., Janse C.J., and Waters A.P. Plasmodium post-genomics: better the bug you know?. Nat Rev Microbiol 4 (2006) 344-357
    • (2006) Nat Rev Microbiol , vol.4 , pp. 344-357
    • Kooij, T.W.1    Janse, C.J.2    Waters, A.P.3
  • 42
    • 8744234024 scopus 로고    scopus 로고
    • Global analysis of transcript and protein levels across the Plasmodium falciparum life cycle
    • Le Roch K.G., Johnson J.R., Florens L., et al. Global analysis of transcript and protein levels across the Plasmodium falciparum life cycle. Genome Res 14 (2004) 2308-2318
    • (2004) Genome Res , vol.14 , pp. 2308-2318
    • Le Roch, K.G.1    Johnson, J.R.2    Florens, L.3
  • 43
    • 10244221154 scopus 로고    scopus 로고
    • Comparative analysis of protein unfoldedness in human housekeeping and non-housekeeping proteins
    • Pandey N., Ganapathi M., Kumar K., Dasgupta D., Das Sutar S.K., and Dash D. Comparative analysis of protein unfoldedness in human housekeeping and non-housekeeping proteins. Bioinformatics 20 (2004) 2904-2910
    • (2004) Bioinformatics , vol.20 , pp. 2904-2910
    • Pandey, N.1    Ganapathi, M.2    Kumar, K.3    Dasgupta, D.4    Das Sutar, S.K.5    Dash, D.6
  • 44
    • 27444439702 scopus 로고    scopus 로고
    • Comparative genomics of malaria parasites
    • Hall N., and Carlton J. Comparative genomics of malaria parasites. Curr Opin Genet Dev 15 (2005) 609-613
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 609-613
    • Hall, N.1    Carlton, J.2
  • 45
    • 9444263051 scopus 로고    scopus 로고
    • The genome of model malaria parasites, and comparative genomics
    • Carlton J., Silva J., and Hall N. The genome of model malaria parasites, and comparative genomics. Curr Issues Mol Biol 7 (2005) 23-37
    • (2005) Curr Issues Mol Biol , vol.7 , pp. 23-37
    • Carlton, J.1    Silva, J.2    Hall, N.3
  • 46
    • 0038797827 scopus 로고    scopus 로고
    • Ten families of variant genes encoded in subtelomeric regions of multiple chromosomes of Plasmodium chabaudi, a malaria species that undergoes antigenic variation in the laboratory mouse
    • Fischer K., Chavchich M., Huestis R., Wilson D.W., Kemp D.J., and Saul A. Ten families of variant genes encoded in subtelomeric regions of multiple chromosomes of Plasmodium chabaudi, a malaria species that undergoes antigenic variation in the laboratory mouse. Mol Microbiol 48 (2003) 1209-1223
    • (2003) Mol Microbiol , vol.48 , pp. 1209-1223
    • Fischer, K.1    Chavchich, M.2    Huestis, R.3    Wilson, D.W.4    Kemp, D.J.5    Saul, A.6
  • 47
    • 27644474297 scopus 로고    scopus 로고
    • Unique insertions within Plasmodium falciparum subtilisin-like protease-1 are crucial for enzyme maturation and activity
    • Jean L., Withers-Martinez C., Hackett F., and Blackman M.J. Unique insertions within Plasmodium falciparum subtilisin-like protease-1 are crucial for enzyme maturation and activity. Mol Biochem Parasitol 144 (2005) 187-197
    • (2005) Mol Biochem Parasitol , vol.144 , pp. 187-197
    • Jean, L.1    Withers-Martinez, C.2    Hackett, F.3    Blackman, M.J.4
  • 48
    • 0037427472 scopus 로고    scopus 로고
    • Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development
    • Sarma G.N., Savvides S.N., Becker K., Schirmer M., Schirmer R.H., and Karplus P.A. Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development. J Mol Biol 328 (2003) 893-907
    • (2003) J Mol Biol , vol.328 , pp. 893-907
    • Sarma, G.N.1    Savvides, S.N.2    Becker, K.3    Schirmer, M.4    Schirmer, R.H.5    Karplus, P.A.6
  • 49
    • 0037373688 scopus 로고    scopus 로고
    • A unique insertion in Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: evolutionary and functional studies
    • Clarke J.L., Sodeinde O., and Mason P.J. A unique insertion in Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: evolutionary and functional studies. Mol Biochem Parasitol 127 (2003) 1-8
    • (2003) Mol Biochem Parasitol , vol.127 , pp. 1-8
    • Clarke, J.L.1    Sodeinde, O.2    Mason, P.J.3
  • 50
    • 20244389557 scopus 로고    scopus 로고
    • Crystal structure of the malaria vaccine candidate apical membrane antigen 1
    • Pizarro J.C., Normand B.V., Chesne-Seck M.L., et al. Crystal structure of the malaria vaccine candidate apical membrane antigen 1. Science 308 (2005) 408-411
    • (2005) Science , vol.308 , pp. 408-411
    • Pizarro, J.C.1    Normand, B.V.2    Chesne-Seck, M.L.3
  • 51
    • 20544463153 scopus 로고    scopus 로고
    • Structure and inter-domain interactions of domain II from the blood-stage malarial protein, apical membrane antigen 1
    • Feng Z.P., Keizer D.W., Stevenson R.A., et al. Structure and inter-domain interactions of domain II from the blood-stage malarial protein, apical membrane antigen 1. J Mol Biol 350 (2005) 641-656
    • (2005) J Mol Biol , vol.350 , pp. 641-656
    • Feng, Z.P.1    Keizer, D.W.2    Stevenson, R.A.3
  • 52
    • 0036389814 scopus 로고    scopus 로고
    • Structure of domain III of the blood-stage malaria vaccine candidate, Plasmodium falciparum apical membrane antigen 1 (AMA1)
    • Nair M., Hinds M.G., Coley A.M., et al. Structure of domain III of the blood-stage malaria vaccine candidate, Plasmodium falciparum apical membrane antigen 1 (AMA1). J Mol Biol 322 (2002) 741-753
    • (2002) J Mol Biol , vol.322 , pp. 741-753
    • Nair, M.1    Hinds, M.G.2    Coley, A.M.3
  • 53
    • 24644523245 scopus 로고    scopus 로고
    • Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket
    • Bai T., Becker M., Gupta A., et al. Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket. Proc Natl Acad Sci USA 102 (2005) 12736-12741
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12736-12741
    • Bai, T.1    Becker, M.2    Gupta, A.3
  • 54
    • 0033727467 scopus 로고    scopus 로고
    • Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family
    • Smith J.D., Subramanian G., Gamain B., Baruch D.I., and Miller L.H. Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family. Mol Biochem Parasitol 110 (2000) 293-310
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 293-310
    • Smith, J.D.1    Subramanian, G.2    Gamain, B.3    Baruch, D.I.4    Miller, L.H.5
  • 55
    • 0031467009 scopus 로고    scopus 로고
    • Conservation of structural motifs and antigenic diversity in the Plasmodium falciparum merozoite surface protein-3 (MSP-3)
    • McColl D.J., and Anders R.F. Conservation of structural motifs and antigenic diversity in the Plasmodium falciparum merozoite surface protein-3 (MSP-3). Mol Biochem Parasitol 90 (1997) 21-31
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 21-31
    • McColl, D.J.1    Anders, R.F.2
  • 56
    • 0028099611 scopus 로고
    • Molecular variation in a novel polymorphic antigen associated with Plasmodium falciparum merozoites
    • McColl D.J., Silva A., Foley M., et al. Molecular variation in a novel polymorphic antigen associated with Plasmodium falciparum merozoites. Mol Biochem Parasitol 68 (1994) 53-67
    • (1994) Mol Biochem Parasitol , vol.68 , pp. 53-67
    • McColl, D.J.1    Silva, A.2    Foley, M.3
  • 57
    • 0034064511 scopus 로고    scopus 로고
    • Conservation among HSP60 sequences in relation to structure, function, and evolution
    • Brocchieri L., and Karlin S. Conservation among HSP60 sequences in relation to structure, function, and evolution. Protein Sci 9 (2000) 476-486
    • (2000) Protein Sci , vol.9 , pp. 476-486
    • Brocchieri, L.1    Karlin, S.2
  • 58
    • 0026032311 scopus 로고
    • Structural diversity in the Plasmodium falciparum merozoite surface antigen 2
    • Smythe J.A., Coppel R.L., Day K.P., et al. Structural diversity in the Plasmodium falciparum merozoite surface antigen 2. Proc Natl Acad Sci USA 88 (1991) 1751-1755
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1751-1755
    • Smythe, J.A.1    Coppel, R.L.2    Day, K.P.3
  • 59
    • 0023395347 scopus 로고
    • Changes in repeat number, sequence, and reading frame in S-antigen genes of Plasmodium falciparum
    • Saint R.B., Coppel R.L., Cowman A.F., et al. Changes in repeat number, sequence, and reading frame in S-antigen genes of Plasmodium falciparum. Mol Cell Biol 7 (1987) 2968-2973
    • (1987) Mol Cell Biol , vol.7 , pp. 2968-2973
    • Saint, R.B.1    Coppel, R.L.2    Cowman, A.F.3
  • 60
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa P. Intrinsically unstructured proteins evolve by repeat expansion. Bioessays 25 (2003) 847-855
    • (2003) Bioessays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 62
    • 25144494777 scopus 로고    scopus 로고
    • Intragenic tandem repeats generate functional variability
    • Verstrepen K.J., Jansen A., Lewitter F., and Fink G.R. Intragenic tandem repeats generate functional variability. Nat Genet 37 (2005) 986-990
    • (2005) Nat Genet , vol.37 , pp. 986-990
    • Verstrepen, K.J.1    Jansen, A.2    Lewitter, F.3    Fink, G.R.4
  • 64
    • 28844483001 scopus 로고    scopus 로고
    • Duration of protection with RTS, S/AS02A malaria vaccine in prevention of Plasmodium falciparum disease in Mozambican children: single-blind extended follow-up of a randomised controlled trial
    • Alonso P.L., Sacarlal J., Aponte J.J., et al. Duration of protection with RTS, S/AS02A malaria vaccine in prevention of Plasmodium falciparum disease in Mozambican children: single-blind extended follow-up of a randomised controlled trial. Lancet 366 (2005) 2012-2018
    • (2005) Lancet , vol.366 , pp. 2012-2018
    • Alonso, P.L.1    Sacarlal, J.2    Aponte, J.J.3
  • 65
    • 0037086437 scopus 로고    scopus 로고
    • A recombinant blood-stage malaria vaccine reduces Plasmodium falciparum density and exerts selective pressure on parasite populations in a phase 1-2b trial in Papua New Guinea
    • Genton B., Betuela I., Felger I., et al. A recombinant blood-stage malaria vaccine reduces Plasmodium falciparum density and exerts selective pressure on parasite populations in a phase 1-2b trial in Papua New Guinea. J Infect Dis 185 (2002) 820-827
    • (2002) J Infect Dis , vol.185 , pp. 820-827
    • Genton, B.1    Betuela, I.2    Felger, I.3
  • 66
    • 0022996457 scopus 로고
    • Multiple cross-reactivities amongst antigens of Plasmodium falciparum impair the development of protective immunity against malaria
    • Anders R.F. Multiple cross-reactivities amongst antigens of Plasmodium falciparum impair the development of protective immunity against malaria. Parasite Immunol 8 (1986) 529-539
    • (1986) Parasite Immunol , vol.8 , pp. 529-539
    • Anders, R.F.1
  • 67
    • 0032374091 scopus 로고    scopus 로고
    • Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus
    • Penkett C.J., Redfield C., Jones J.A., et al. Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus. Biochemistry 37 (1998) 17054-17067
    • (1998) Biochemistry , vol.37 , pp. 17054-17067
    • Penkett, C.J.1    Redfield, C.2    Jones, J.A.3
  • 68
    • 4744357952 scopus 로고    scopus 로고
    • BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding
    • Kim J.H., Singvall J., Schwarz-Linek U., Johnson B.J., Potts J.R., and Hook M. BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J Biol Chem 279 (2004) 41706-41714
    • (2004) J Biol Chem , vol.279 , pp. 41706-41714
    • Kim, J.H.1    Singvall, J.2    Schwarz-Linek, U.3    Johnson, B.J.4    Potts, J.R.5    Hook, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.