메뉴 건너뛰기




Volumn 107, Issue 12, 2010, Pages 5429-5434

Dual coding in alternative reading frames correlates with intrinsic protein disorder

Author keywords

Alternative splicing; Nonsense mediated decay; Unstructured protein

Indexed keywords

NUCLEOTIDE; RNA;

EID: 77950421789     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907841107     Document Type: Article
Times cited : (66)

References (61)
  • 1
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: New insights from global analyses
    • Blencowe BJ (2006) Alternative splicing: New insights from global analyses. Cell 126:37-47.
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 2
    • 38049061206 scopus 로고    scopus 로고
    • Alternative splicing: Current perspectives
    • Kim E, Goren A, Ast G (2008) Alternative splicing: Current perspectives. Bioessays 30:38-47.
    • (2008) Bioessays , vol.30 , pp. 38-47
    • Kim, E.1    Goren, A.2    Ast, G.3
  • 3
    • 0347623371 scopus 로고    scopus 로고
    • Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays
    • Johnson JM, et al. (2003) Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays. Science 302:2141-2144.
    • (2003) Science , vol.302 , pp. 2141-2144
    • Johnson, J.M.1
  • 4
    • 34848893914 scopus 로고    scopus 로고
    • Evolutionary impact of limited splicing fidelity in mammalian genes
    • DOI 10.1016/j.tig.2007.08.001, PII S016895250700265X
    • Zhang C, Krainer AR, Zhang MQ (2007) Evolutionary impact of limited splicing fidelity in mammalian genes. Trends Genet 23:484-488. (Pubitemid 47503443)
    • (2007) Trends in Genetics , vol.23 , Issue.10 , pp. 484-488
    • Zhang, C.1    Krainer, A.R.2    Zhang, M.Q.3
  • 5
    • 0037422575 scopus 로고    scopus 로고
    • Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans
    • Lewis BP, Green RE, Brenner SE (2003) Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans. Proc Natl Acad Sci USA 100:189-192.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 189-192
    • Lewis, B.P.1    Green, R.E.2    Brenner, S.E.3
  • 6
    • 48149095822 scopus 로고    scopus 로고
    • Alternative splicing resulting in nonsense-mediated mRNA decay: What is the meaning of nonsense?
    • McGlincy NJ, Smith CW (2008) Alternative splicing resulting in nonsense-mediated mRNA decay: What is the meaning of nonsense?. Trends Biochem Sci 33:385-393.
    • (2008) Trends Biochem Sci , vol.33 , pp. 385-393
    • McGlincy, N.J.1    Smith, C.W.2
  • 7
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: When nonsense affects RNA abundance
    • DOI 10.1016/S0968-0004(98)01208-0
    • Nagy E, Maquat LE (1998) A rule for termination-codon positionwithin intron-containing genes: when nonsense affects RNA abundance. Trends Biochem Sci 23:198-199. (Pubitemid 28302613)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.6 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 8
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in Paramyxovirinae N and P
    • DOI 10.1099/vir.0.19451-0
    • Karlin D, Ferron F, Canard B, Longhi S (2003) Structural disorder and modular organization in Paramyxovirinae N and P. J Gen Virol 84:3239-3252. (Pubitemid 37540753)
    • (2003) Journal of General Virology , vol.84 , Issue.12 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 9
    • 70349737853 scopus 로고    scopus 로고
    • Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation
    • Rancurel C, Khosravi M, Dunker AK, Romero PR, Karlin D (2009) Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation. J Virol 83:10719-10736.
    • (2009) J Virol , vol.83 , pp. 10719-10736
    • Rancurel, C.1    Khosravi, M.2    Dunker, A.K.3    Romero, P.R.4    Karlin, D.5
  • 10
    • 0034698122 scopus 로고    scopus 로고
    • Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death
    • Bingle CD, et al. (2000) Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J Biol Chem 275:22136-22146.
    • (2000) J Biol Chem , vol.275 , pp. 22136-22146
    • Bingle, C.D.1
  • 11
    • 0031446639 scopus 로고    scopus 로고
    • Inhibition of gonadotropin releasing hormone receptor signaling by expression of a splice variant of the human receptor
    • DOI 10.1210/me.11.9.1305
    • Grosse R, Schoneberg T, Schultz G, Gudermann T (1997) Inhibition of gonadotropin-releasing hormone receptor signaling by expression of a splice variant of the human receptor. Mol Endocrinol 11:1305-1318. (Pubitemid 28041337)
    • (1997) Molecular Endocrinology , vol.11 , Issue.9 , pp. 1305-1318
    • Grosse, R.1    Schoneberg, T.2    Schultz, G.3    Gudermann, T.4
  • 13
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • DOI 10.1016/S0092-8674(01)00611-0
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107:881-891. (Pubitemid 34084979)
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 14
    • 0035898609 scopus 로고    scopus 로고
    • Two overlapping reading frames in a single exon encode interacting proteins - A novel way of gene usage
    • DOI 10.1093/emboj/20.14.3849
    • Klemke M, Kehlenbach RH, Huttner WB (2001) Two overlapping reading frames in a single exon encode interacting proteins - A novel way of gene usage. EMBO J 20:3849-3860. (Pubitemid 32691796)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3849-3860
    • Klemke, M.1    Kehlenbach, R.H.2    Huttner, W.B.3
  • 15
    • 22144489899 scopus 로고    scopus 로고
    • INK4a/ARF: A multifunctional tumor suppressor locus
    • Sharpless NE (2005) INK4a/ARF: A multifunctional tumor suppressor locus. Mutat Res 576:22-38.
    • (2005) Mutat Res , vol.576 , pp. 22-38
    • Sharpless, N.E.1
  • 18
    • 32044464524 scopus 로고    scopus 로고
    • A genome-wide study of dual coding regions in human alternatively spliced genes
    • DOI 10.1111/j.1464-410X.2006.05874.x
    • Liang H, Landweber LF (2005) A genome-wide study of dual coding regions in human alternatively spliced genes. Genome Res 16:190-196. (Pubitemid 43200267)
    • (2006) Genome Research , vol.16 , Issue.2 , pp. 190-196
    • Liang, H.1    Landweber, L.F.2
  • 19
    • 42549161129 scopus 로고    scopus 로고
    • Bioinformatics prediction of overlapping frameshifted translation products in mammalian transcripts
    • Ribrioux S, Brungger A, Baumgarten B, Seuwen K, John MR (2008) Bioinformatics prediction of overlapping frameshifted translation products in mammalian transcripts. BMC Genomics 9:122.
    • (2008) BMC Genomics , vol.9 , pp. 122
    • Ribrioux, S.1    Brungger, A.2    Baumgarten, B.3    Seuwen, K.4    John, M.R.5
  • 20
    • 0346732315 scopus 로고    scopus 로고
    • Gene Fusion and Overlapping Reading Frames in the Mammalian Genes for 4E-BP3 and MASK
    • DOI 10.1074/jbc.M310761200
    • Poulin F, Brueschke A, Sonenberg N (2003) Gene fusion and overlapping reading frames in the mammalian genes for 4E-BP3 and MASK. J Biol Chem 278:52290-52297. (Pubitemid 38035817)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52290-52297
    • Poulin, F.1    Brueschke, A.2    Sonenberg, N.3
  • 21
    • 32644432826 scopus 로고    scopus 로고
    • PXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
    • DOI 10.1083/jcb.200508145
    • Yoshida H, Oku M, Suzuki M, Mori K (2006) pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J Cell Biol 172:565-575. (Pubitemid 43243877)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4
  • 22
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 23
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 24
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • Tompa P (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579:3346-3354. (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 25
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The database of disordered proteins
    • Sickmeier M, et al. (2007) DisProt: The database of disordered proteins. Nucleic Acids Res 35:D786-793.
    • (2007) Nucleic Acids Res , vol.35
    • Sickmeier, M.1
  • 26
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa P, Fuxreiter M (2008) Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33:2-8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 28
    • 33744814686 scopus 로고    scopus 로고
    • Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms
    • Romero PR, et al. (2006) Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms. Proc Natl Acad Sci USA 103:8390-8395.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8390-8395
    • Romero, P.R.1
  • 29
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • DOI 10.1016/j.tibs.2005.07.008, PII S0968000405002185
    • Tompa P, Szasz C, Buday L (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30:484-489. (Pubitemid 41206503)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.9 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 30
    • 52249124593 scopus 로고    scopus 로고
    • TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder
    • Campen A, et al. (2008) TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder. Protein Peptide Lett 15:956-963.
    • (2008) Protein Peptide Lett , vol.15 , pp. 956-963
    • Campen, A.1
  • 31
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • DOI 10.1093/bioinformatics/bti541
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) IUPred:Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21:3433-3434. (Pubitemid 41222453)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 32
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • DOI 10.1016/j.jmb.2005.01.071
    • Dosztányi Z, Csizmok V, Tompa P, Simon I (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and instrinsically unstructured proteins. J Mol Biol 347:827-839. (Pubitemid 40357923)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.4 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 33
  • 34
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 35
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson MP (1994) The structure and function of proline-rich regions in proteins. Biochem J 297:249-260. (Pubitemid 24026414)
    • (1994) Biochemical Journal , vol.297 , Issue.2 , pp. 249-260
    • Williamson, M.P.1
  • 36
    • 0029587551 scopus 로고
    • Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest
    • DOI 10.1016/0092-8674(95)90214-7
    • Quelle DE, Zindy F, Ashmun RA, Sherr CJ (1995) Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest. Cell 83:993-1000. (Pubitemid 26006540)
    • (1995) Cell , vol.83 , Issue.6 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 37
    • 0031991891 scopus 로고    scopus 로고
    • Tumor suppressor p16INK4A: Determination of solution structure and analyses of its interactionwith cyclin-dependent kinase 4
    • Byeon IJ, et al. (1998) Tumor suppressor p16INK4A: Determination of solution structure and analyses of its interactionwith cyclin-dependent kinase 4. Mol Cell 1:421-431.
    • (1998) Mol Cell , vol.1 , pp. 421-431
    • Byeon, I.J.1
  • 38
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown CJ, et al. (2002) Evolutionary rate heterogeneity in proteins with long disordered regions. J Mol Evol 55:104-110.
    • (2002) J Mol Evol , vol.55 , pp. 104-110
    • Brown, C.J.1
  • 39
    • 35248852356 scopus 로고    scopus 로고
    • Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation
    • DOI 10.1007/s00239-007-9011-2
    • Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ (2007) Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. J Mol Evol 65:277-288. (Pubitemid 47561689)
    • (2007) Journal of Molecular Evolution , vol.65 , Issue.3 , pp. 277-288
    • Daughdrill, G.W.1    Narayanaswami, P.2    Gilmore, S.H.3    Belczyk, A.4    Brown, C.J.5
  • 40
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady GE, Simon I (2001) The HMMTOP transmembrane topology prediction server. Bioinformatics 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 41
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J Mol Biol 305:567-580. (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 42
    • 0028949119 scopus 로고
    • In vitro characterization of the human recombinant soluble granulocyte-macrophage colony-stimulating factor receptor
    • Brown CB, Beaudry P, Laing TD, Shoemaker S, Kaushansky K (1995) In vitro characterization of the human recombinant soluble granulocyte-macrophage colony-stimulating factor receptor. Blood 85:1488-1495.
    • (1995) Blood , vol.85 , pp. 1488-1495
    • Brown, C.B.1    Beaudry, P.2    Laing, T.D.3    Shoemaker, S.4    Kaushansky, K.5
  • 46
    • 41149125082 scopus 로고    scopus 로고
    • Structural disorder serves as a weak signal for intracellular protein degradation
    • Tompa P, Prilusky J, Silman I, Sussman JL (2008) Structural disorder serves as a weak signal for intracellular protein degradation. Proteins 71:903-909.
    • (2008) Proteins , vol.71 , pp. 903-909
    • Tompa, P.1    Prilusky, J.2    Silman, I.3    Sussman, J.L.4
  • 47
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape
    • Dobson CM (2002) Getting out of shape. Nature 418:729-730.
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 48
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta 1698:131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 49
    • 4143133235 scopus 로고    scopus 로고
    • A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins
    • DOI 10.1016/j.jmb.2004.06.088, PII S0022283604007715
    • Linding R, Schymkowitz J, Rousseau F, Diella F, Serrano L (2004) A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. J Mol Biol 342:345-353. (Pubitemid 39094525)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.1 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 50
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • DOI 10.1038/sj.embor.7401034, PII 7401034
    • Monsellier E, Chiti F (2007) Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep 8:737-742. (Pubitemid 47202452)
    • (2007) EMBO Reports , vol.8 , Issue.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 51
    • 33846250450 scopus 로고    scopus 로고
    • Proline and Glycine Control Protein Self-Organization into Elastomeric or Amyloid Fibrils
    • DOI 10.1016/j.str.2006.09.008, PII S0969212606003947
    • Rauscher S, Baud S, Miao M, Keeley FW, Pomes R (2006) Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure 14:1667-1676. (Pubitemid 46107274)
    • (2006) Structure , vol.14 , Issue.11 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Miao, M.3    Keeley, F.4    Pomes, R.5
  • 52
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424:805-808. (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 53
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: Evolutionary interaction switches
    • DOI 10.1016/j.febslet.2005.04.005, PII S0014579305004618
    • Neduva V, Russell RB (2005) Linear motifs: Evolutionary interaction switches. FEBS Lett 579:3342-3345. (Pubitemid 40804684)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 54
    • 33846057724 scopus 로고    scopus 로고
    • NCBI reference sequences (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins
    • DOI 10.1093/nar/gkl842
    • Pruitt KD, Tatusova T, Maglott DR (2007) NCBI reference sequences (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res 35:D61-65. (Pubitemid 46056171)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL. 1
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 56
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • Dunker AK, et al. (2001) Intrinsically disordered protein. J Mol Graph Model 19:26-59.
    • (2001) J Mol Graph Model , vol.19 , pp. 26-59
    • Dunker, A.K.1
  • 57
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter M, Tompa P, Simon I (2007) Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23:950-956.
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 58
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 60
    • 66449084442 scopus 로고    scopus 로고
    • Infrastructure for the life sciences: Design and implementation of the UniProt website
    • Jain E, et al. (2009) Infrastructure for the life sciences: Design and implementation of the UniProt website. BMC Bioinformatics 10:136.
    • (2009) BMC Bioinformatics , vol.10 , pp. 136
    • Jain, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.