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Volumn 71, Issue 8, 2014, Pages 1477-1504

A creature with a hundred waggly tails: Intrinsically disordered proteins in the ribosome

Author keywords

Intrinsically disordered protein; Moonlighting protein; Protein protein interaction; Protein RNA interaction; Ribosomal proteins

Indexed keywords

HYBRID PROTEIN; INTRINSICALLY DISORDERED PROTEIN; RIBOSOME PROTEIN;

EID: 84897112748     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1446-6     Document Type: Article
Times cited : (115)

References (140)
  • 2
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • Uversky VN, Dunker AK (2010) Understanding protein non-folding. Biochim Biophys Acta 1804(6):1231-1264
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.6 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 3
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337(3):635-645 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 4
    • 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(3):415-427
    • (2000) Proteins , vol.41 , Issue.3 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 5
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life
    • Xue B, Dunker AK, Uversky VN (2012) Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 30(2):137-149
    • (2012) J Biomol Struct Dyn , vol.30 , Issue.2 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 7
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293(2):321-331 (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 9
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27(10):527-533
    • (2002) Trends Biochem Sci , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 11
    • 77949328500 scopus 로고    scopus 로고
    • The mysterious unfoldome: Structureless, underappreciated, yet vital part of any given proteome
    • Uversky VN (2010) The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome. J Biomed Biotechnol 2010:568068
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 568068
    • Uversky, V.N.1
  • 13
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets: The roles of intrinsic disorder in protein interaction networks
    • DOI 10.1111/j.1742-4658.2005.04948.x
    • Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN (2005) Flexible nets: the roles of intrinsic disorder in protein interaction networks. FEBS J 272(20):5129-5148 (Pubitemid 41503146)
    • (2005) FEBS Journal , vol.272 , Issue.20 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 14
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • DOI 10.1002/jmr.747
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18(5):343-384 (Pubitemid 41341287)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.5 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 16
    • 34249282661 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions
    • DOI 10.1021/pr060393m
    • Vucetic S, Xie H, Iakoucheva LM, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN (2007) Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. J Proteome Res 6(5):1899-1916 (Pubitemid 46814513)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1899-1916
    • Vucetic, S.1    Xie, H.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 17
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • DOI 10.1021/pr060392u
    • Xie H, Vucetic S, Iakoucheva LM, Oldfield CJ, Dunker AK, Uversky VN, Obradovic Z (2007) Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J Proteome Res 6(5):1882-1898 (Pubitemid 46814512)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Uversky, V.N.6    Obradovic, Z.7
  • 18
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • DOI 10.1021/pr060394e
    • Xie H, Vucetic S, Iakoucheva LM, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN (2007) Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J Proteome Res 6(5):1917-1932 (Pubitemid 46814514)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 22
    • 33744829805 scopus 로고    scopus 로고
    • Human Transcription Factors Contain a High Fraction of Intrinsically Disordered Regions Essential for Transcriptional Regulation
    • DOI 10.1016/j.jmb.2006.04.016, PII S0022283606004669
    • Minezaki Y, Homma K, Kinjo AR, Nishikawa K (2006) Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation. J Mol Biol 359(4):1137-1149 (Pubitemid 43831930)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.4 , pp. 1137-1149
    • Minezaki, Y.1    Homma, K.2    Kinjo, A.R.3    Nishikawa, K.4
  • 24
    • 79952182929 scopus 로고    scopus 로고
    • An intrinsically disordered C terminus allows the la protein to assist the biogenesis of diverse noncoding RNA precursors
    • Kucera NJ, Hodsdon ME, Wolin SL (2011) An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors. Proc Natl Acad Sci USA 108(4):1308-1313
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.4 , pp. 1308-1313
    • Kucera, N.J.1    Hodsdon, M.E.2    Wolin, S.L.3
  • 25
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • DOI 10.1096/fj.04-1584rev
    • Tompa P, Csermely P (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J 18(11):1169-1175 (Pubitemid 39006878)
    • (2004) FASEB Journal , vol.18 , Issue.11 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 26
    • 39449097872 scopus 로고    scopus 로고
    • RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae
    • DOI 10.1093/nar/gkm1051
    • Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL (2008) RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. Nucleic Acids Res 36(3):712-725 (Pubitemid 351267229)
    • (2008) Nucleic Acids Research , vol.36 , Issue.3 , pp. 712-725
    • Ivanyi-Nagy, R.1    Lavergne, J.-P.2    Gabus, C.3    Ficheux, D.4    Darlix, J.-L.5
  • 27
    • 31044439245 scopus 로고    scopus 로고
    • The bunyavirus nucleocapsid protein is an RNA chaperone: Possible roles in viral RNA panhandle formation and genome replication
    • DOI 10.1261/rna.2101906
    • Mir MA, Panganiban AT (2006) The bunyavirus nucleocapsid protein is an RNA chaperone: possible roles in viral RNA panhandle formation and genome replication. RNA 12(2):272-282 (Pubitemid 43121932)
    • (2006) RNA , vol.12 , Issue.2 , pp. 272-282
    • Ayoub, M.M.1    Panganiban, A.T.2
  • 28
    • 33745257290 scopus 로고    scopus 로고
    • Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein
    • DOI 10.1128/JVI.00147-06
    • Mir MA, Panganiban AT (2006) Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein. J Virol 80(13):6276-6285 (Pubitemid 43927430)
    • (2006) Journal of Virology , vol.80 , Issue.13 , pp. 6276-6285
    • Mir, M.A.1    Panganiban, A.T.2
  • 29
    • 38349088979 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA
    • Murray CL, Marcotrigiano J, Rice CM (2008) Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. J Virol 82(3):1294-1304
    • (2008) J Virol , vol.82 , Issue.3 , pp. 1294-1304
    • Murray, C.L.1    Marcotrigiano, J.2    Rice, C.M.3
  • 30
    • 31544433157 scopus 로고    scopus 로고
    • Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins
    • DOI 10.1093/nar/gkj424
    • Haynes C, Iakoucheva LM (2006) Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res 34(1):305-312 (Pubitemid 43160053)
    • (2006) Nucleic Acids Research , vol.34 , Issue.1 , pp. 305-312
    • Haynes, C.1    Iakoucheva, L.M.2
  • 31
    • 77958071499 scopus 로고    scopus 로고
    • Intrinsic disorder and function of the HIV-1 Tat protein
    • Shojania S, O'Neil JD (2011) Intrinsic disorder and function of the HIV-1 Tat protein. Protein Pept Lett 17(8):999-1011
    • (2011) Protein Pept Lett , vol.17 , Issue.8 , pp. 999-1011
    • Shojania, S.1    O'Neil, J.D.2
  • 32
    • 84860843718 scopus 로고    scopus 로고
    • Protein intrinsic disorder as a flexible armor and a weapon of HIV-1
    • Xue B, Mizianty MJ, Kurgan L, Uversky VN (2012) Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cell Mol Life Sci 69(8):1211-1259
    • (2012) Cell Mol Life Sci , vol.69 , Issue.8 , pp. 1211-1259
    • Xue, B.1    Mizianty, M.J.2    Kurgan, L.3    Uversky, V.N.4
  • 34
    • 3242685090 scopus 로고    scopus 로고
    • The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure
    • DOI 10.1021/bi036314r
    • Thapar R, Mueller GA, Marzluff WF (2004) The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. Biochemistry 43(29):9390-9400 (Pubitemid 38955472)
    • (2004) Biochemistry , vol.43 , Issue.29 , pp. 9390-9400
    • Thapar, R.1    Mueller, G.A.2    Marzluff, W.F.3
  • 36
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing TM, Ramakrishnan V (2009) What recent ribosome structures have revealed about the mechanism of translation. Nature 461(7268):1234-1242
    • (2009) Nature , vol.461 , Issue.7268 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 37
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11(2):113-127
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.2 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 38
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136(4):731-745
    • (2009) Cell , vol.136 , Issue.4 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 39
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA-ribosome and subunit-subunit interactions
    • DOI 10.1016/S0092-8674(01)00539-6
    • Spahn CM, Beckmann R, Eswar N, Penczek PA, Sali A, Blobel G, Frank J (2001) Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA-ribosome and subunit-subunit interactions. Cell 107(3):373-386 (Pubitemid 33049980)
    • (2001) Cell , vol.107 , Issue.3 , pp. 373-386
    • Spahn, C.M.T.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 40
    • 81555219350 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6
    • Klinge S, Voigts-Hoffmann F, Leibundgut M, Arpagaus S, Ban N (2011) Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6. Science 334(6058):941-948
    • (2011) Science , vol.334 , Issue.6058 , pp. 941-948
    • Klinge, S.1    Voigts-Hoffmann, F.2    Leibundgut, M.3    Arpagaus, S.4    Ban, N.5
  • 41
    • 0037115872 scopus 로고    scopus 로고
    • Comparative analysis of ribosomal proteins in complete genomes: An example of reductive evolution at the domain scale
    • DOI 10.1093/nar/gkf693
    • Lecompte O, Ripp R, Thierry JC, Moras D, Poch O (2002) Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res 30(24):5382-5390 (Pubitemid 36113915)
    • (2002) Nucleic Acids Research , vol.30 , Issue.24 , pp. 5382-5390
    • Lecompte, O.1    Ripp, R.2    Thierry, J.-C.3    Moras, D.4    Poch, O.5
  • 42
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli
    • Zengel JM, Lindahl L (1994) Diverse mechanisms for regulating ribosomal protein synthesis in Escherichia coli. Prog Nucleic Acid Res Mol Biol 47:331-370
    • (1994) Prog Nucleic Acid Res Mol Biol , vol.47 , pp. 331-370
    • Zengel, J.M.1    Lindahl, L.2
  • 43
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • DOI 10.1126/science.289.5481.905
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289(5481):905-920 (Pubitemid 30659939)
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 46
    • 0035977093 scopus 로고    scopus 로고
    • High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
    • DOI 10.1016/S0092-8674(01)00546-3
    • Harms J, Schluenzen F, Zarivach R, Bashan A, Gat S, Agmon I, Bartels H, Franceschi F, Yonath A (2001) High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. Cell 107(5):679-688 (Pubitemid 34014868)
    • (2001) Cell , vol.107 , Issue.5 , pp. 679-688
    • Harms, J.1    Schluenzen, F.2    Zarivach, R.3    Bashan, A.4    Gat, S.5    Agmon, I.6    Bartels, H.7    Franceschi, F.8    Yonath, A.9
  • 49
    • 63549150458 scopus 로고    scopus 로고
    • The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly
    • Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M (2009) The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. Int J Mol Sci 10(3):817-834
    • (2009) Int J Mol Sci , vol.10 , Issue.3 , pp. 817-834
    • Timsit, Y.1    Acosta, Z.2    Allemand, F.3    Chiaruttini, C.4    Springer, M.5
  • 50
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem A, Jenner L, Yusupova G, Yusupov M (2011) Crystal structure of the eukaryotic ribosome. Science 330(6008):1203-1209
    • (2011) Science , vol.330 , Issue.6008 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 51
    • 0021009482 scopus 로고
    • Structure and role of eubacterial ribosomal proteins
    • Garrett RA (1983) Structure and role of eubacterial ribosomal proteins. Horiz Biochem Biophys 7:101-138
    • (1983) Horiz Biochem Biophys , vol.7 , pp. 101-138
    • Garrett, R.A.1
  • 52
    • 0036303417 scopus 로고    scopus 로고
    • Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16 S RNA
    • DOI 10.1006/jmbi.2001.5359
    • Brodersen DE, Clemons WM Jr, Carter AP, Wimberly BT, Ramakrishnan V (2002) Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA. J Mol Biol 316(3):725-768 (Pubitemid 34729252)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.3 , pp. 725-768
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Wimberly, B.T.4    Ramakrishnan, V.5
  • 53
    • 2942615089 scopus 로고    scopus 로고
    • The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit
    • DOI 10.1016/j.jmb.2004.03.076, PII S0022283604003845
    • Klein DJ, Moore PB, Steitz TA (2004) The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J Mol Biol 340(1):141-177 (Pubitemid 38739442)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.1 , pp. 141-177
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 54
    • 0347125312 scopus 로고    scopus 로고
    • RPG: The Ribosomal Protein Gene database
    • Nakao A, Yoshihama M, Kenmochi N (2004) RPG: the Ribosomal Protein Gene database. Nucleic Acids Res 32(Database issue):D168-D170 (Pubitemid 38081631)
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATABASE ISS.
    • Nakao, A.1    Yoshihama, M.2    Kenmochi, N.3
  • 55
    • 77956502766 scopus 로고    scopus 로고
    • Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources
    • Mizianty MJ, Stach W, Chen K, Kedarisetti KD, Disfani FM, Kurgan L (2010) Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources. Bioinformatics 26(18):i489-i496
    • (2010) Bioinformatics , vol.26 , Issue.18
    • Mizianty, M.J.1    Stach, W.2    Chen, K.3    Kedarisetti, K.D.4    Disfani, F.M.5    Kurgan, L.6
  • 56
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium
    • UniProt Consortium (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res 40(Database issue):D71-D75
    • (2012) Nucleic Acids Res , vol.40 , Issue.DATABASE ISSUE
  • 58
    • 84986483798 scopus 로고
    • The double cubic lattice method - efficient approaches to numerical-integration of surface-area and volume and to dot surface contouring of molecular assemblies
    • Eisenhaber F, Lijnzaad P, Argos P, Sander C, Scharf M (1995) The double cubic lattice method - efficient approaches to numerical-integration of surface-area and volume and to dot surface contouring of molecular assemblies. J Comput Chem 16(3):273-284
    • (1995) J Comput Chem , vol.16 , Issue.3 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Argos, P.3    Sander, C.4    Scharf, M.5
  • 59
    • 0033665510 scopus 로고    scopus 로고
    • BALL - rapid software prototyping in computational molecular biology. Biochemicals algorithms library
    • Kohlbacher O, Lenhof HP (2000) BALL - rapid software prototyping in computational molecular biology. Biochemicals algorithms library. Bioinformatics 16(9):815-824
    • (2000) Bioinformatics , vol.16 , Issue.9 , pp. 815-824
    • Kohlbacher, O.1    Lenhof, H.P.2
  • 60
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • DOI 10.1016/j.jmb.2004.07.002, PII S0022283604008010
    • Gunasekaran K, Tsai CJ, Nussinov R (2004) Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J Mol Biol 341(5):1327-1341 (Pubitemid 39092318)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.-J.2    Nussinov, R.3
  • 62
    • 34447539760 scopus 로고    scopus 로고
    • Composition profiler: A tool for discovery and visualization of amino acid composition differences
    • Vacic V, Uversky VN, Dunker AK, Lonardi S (2007) Composition profiler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinforma 8:211
    • (2007) BMC Bioinforma , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 65
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • DOI 10.1093/nar/gkg519
    • Linding R, Russell RB, Neduva V, Gibson TJ (2003) Glob-Plot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 31(13):3701-3708 (Pubitemid 37442227)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 66
    • 84862499641 scopus 로고    scopus 로고
    • Prediction of protein domain with mRMR feature selection and analysis
    • Li BQ, Hu LL, Chen L, Feng KY, Cai YD, Chou KC (2012) Prediction of protein domain with mRMR feature selection and analysis. PLoS One 7(6):e39308
    • (2012) PLoS One , vol.7 , Issue.6
    • Li, B.Q.1    Hu, L.L.2    Chen, L.3    Feng, K.Y.4    Cai, Y.D.5    Chou, K.C.6
  • 68
    • 84857129811 scopus 로고    scopus 로고
    • Comprehensive comparative assessment of in-silico predictors of disordered regions
    • Peng ZL, Kurgan L (2012) Comprehensive comparative assessment of in-silico predictors of disordered regions. Curr Protein Pept Sci 13:6-18
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 6-18
    • Peng, Z.L.1    Kurgan, L.2
  • 69
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK, Uversky VN (2009) Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays 31(3):328-335
    • (2009) Bioessays , vol.31 , Issue.3 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 70
    • 74249104442 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP8
    • Noivirt-Brik O, Prilusky J, Sussman JL (2009) Assessment of disorder predictions in CASP8. Proteins 77(Suppl 9):210-216
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 210-216
    • Noivirt-Brik, O.1    Prilusky, J.2    Sussman, J.L.3
  • 72
  • 73
    • 67349162535 scopus 로고    scopus 로고
    • CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions
    • Xue B, Oldfield CJ, Dunker AK, Uversky VN (2009) CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Lett 583(9):1469-1474
    • (2009) FEBS Lett , vol.583 , Issue.9 , pp. 1469-1474
    • Xue, B.1    Oldfield, C.J.2    Dunker, A.K.3    Uversky, V.N.4
  • 74
    • 41049091705 scopus 로고    scopus 로고
    • Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes
    • DOI 10.1039/b719168e
    • Mohan A, Sullivan WJ Jr, Radivojac P, Dunker AK, Uversky VN (2008) Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes. Mol Biosyst 4(4):328-340 (Pubitemid 351422588)
    • (2008) Molecular BioSystems , vol.4 , Issue.4 , pp. 328-340
    • Mohan, A.1    Sullivan, J.W.J.2    Radivojac, P.3    Dunker, A.K.4    Uversky, V.N.5
  • 76
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith TF, Waterman MS (1981) Identification of common molecular subsequences. J Mol Biol 147(1):195-197
    • (1981) J Mol Biol , vol.147 , Issue.1 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 77
    • 84863518014 scopus 로고    scopus 로고
    • MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins
    • Disfani FM, Hsu W-L, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L (2012) MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics 28(12):i75-83
    • (2012) Bioinformatics , vol.28 , Issue.12
    • Disfani, F.M.1    Hsu, W.-L.2    Mizianty, M.J.3    Oldfield, C.J.4    Xue, B.5    Dunker, A.K.6    Uversky, V.N.7    Kurgan, L.8
  • 78
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • DOI 10.1021/bi050736e
    • Oldfield CJ, Cheng Y, Cortese MS, Romero P, Uversky VN, Dunker AK (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44(37):12454-12470 (Pubitemid 41324337)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 81
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292(2):195-202
    • (1999) J Mol Biol , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 82
    • 33748505263 scopus 로고    scopus 로고
    • Incorporating background frequency improves entropy-based residue conservation measures
    • Wang K, Samudrala R (2006) Incorporating background frequency improves entropy-based residue conservation measures. BMC Bioinforma 7:385
    • (2006) BMC Bioinforma , vol.7 , pp. 385
    • Wang, K.1    Samudrala, R.2
  • 84
    • 0036495004 scopus 로고    scopus 로고
    • Getting the most from PSI-BLAST
    • DOI 10.1016/S0968-0004(01)02039-4, PII S0968000401020394
    • Jones DT, Swindells MB (2002) Getting the most from PSI-BLAST. Trends Biochem Sci 27(3):161-164 (Pubitemid 34219327)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 161-164
    • Jones, D.T.1    Swindells, M.B.2
  • 85
    • 84862169121 scopus 로고    scopus 로고
    • More than just tails: Intrinsic disorder in histone proteins
    • Peng Z, Mizianty MJ, Xue B, Kurgan L, Uversky VN (2012) More than just tails: intrinsic disorder in histone proteins. Mol Biosyst 8(7):1886-1901
    • (2012) Mol Biosyst , vol.8 , Issue.7 , pp. 1886-1901
    • Peng, Z.1    Mizianty, M.J.2    Xue, B.3    Kurgan, L.4    Uversky, V.N.5
  • 86
    • 84856577919 scopus 로고    scopus 로고
    • Prediction and analysis of nucleotide-binding residues using sequence and sequence-derived structural descriptors
    • Chen K, Mizianty MJ, Kurgan L (2012) Prediction and analysis of nucleotide-binding residues using sequence and sequence-derived structural descriptors. Bioinformatics 28(3):331-341
    • (2012) Bioinformatics , vol.28 , Issue.3 , pp. 331-341
    • Chen, K.1    Mizianty, M.J.2    Kurgan, L.3
  • 87
    • 77954686958 scopus 로고    scopus 로고
    • A comparative study of conservation and variation scores
    • Johansson F, Toh H (2010) A comparative study of conservation and variation scores. BMC Bioinforma 11(1):388
    • (2010) BMC Bioinforma , vol.11 , Issue.1 , pp. 388
    • Johansson, F.1    Toh, H.2
  • 88
    • 0026941784 scopus 로고
    • Folding and assembly of oligomeric proteins in Escherichia coli
    • Teschke CM, King J (1992) Folding and assembly of oligomeric proteins in Escherichia coli. Curr Opin Biotechnol 3(5):468-473
    • (1992) Curr Opin Biotechnol , vol.3 , Issue.5 , pp. 468-473
    • Teschke, C.M.1    King, J.2
  • 89
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • Xu D, Tsai CJ, Nussinov R (1998) Mechanism and evolution of protein dimerization. Protein Sci 7(3):533-544 (Pubitemid 28130874)
    • (1998) Protein Science , vol.7 , Issue.3 , pp. 533-544
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 90
    • 4444351205 scopus 로고    scopus 로고
    • Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression
    • DOI 10.1128/MCB.24.18.8276-8287.2004
    • Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ (2004) Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol 24(18):8276-8287 (Pubitemid 39167475)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.18 , pp. 8276-8287
    • Gerbasi, V.R.1    Weaver, C.M.2    Hill, S.3    Friedman, D.B.4    Link, A.J.5
  • 91
    • 0017681674 scopus 로고
    • Physical studies on the conformation of ribosomal protein S4 from Escherichia coli
    • DOI 10.1111/j.1432-1033.1977.tb11724.x
    • Morrison CA, Garrett RA, Bradbury EM (1977) Physical studies on the conformation of ribosomal protein S4 from Escherichia coli. Eur J Biochem 78(1):153-159 (Pubitemid 8164732)
    • (1977) European Journal of Biochemistry , vol.78 , Issue.1 , pp. 153-159
    • Morrison, C.A.1    Garrett, R.A.2    Bradbury, E.M.3
  • 93
    • 0021104739 scopus 로고
    • 500-MHz 1H-NMR studies of ribosomal proteins isolated from 70-S ribosomes of Escherichia coli
    • van de Ven FJ, de Bruin SH, Hilbers CW (1983) 500-MHz 1H-NMR studies of ribosomal proteins isolated from 70-S ribosomes of Escherichia coli. Eur J Biochem 134(3):429-438
    • (1983) Eur J Biochem , vol.134 , Issue.3 , pp. 429-438
    • Van De Ven, F.J.1    De Bruin, S.H.2    Hilbers, C.W.3
  • 94
    • 0034619497 scopus 로고    scopus 로고
    • Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy
    • Sayers EW, Gerstner RB, Draper DE, Torchia DA (2000) Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy. Biochemistry 39(44):13602-13613
    • (2000) Biochemistry , vol.39 , Issue.44 , pp. 13602-13613
    • Sayers, E.W.1    Gerstner, R.B.2    Draper, D.E.3    Torchia, D.A.4
  • 95
    • 0036565779 scopus 로고    scopus 로고
    • The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold
    • DOI 10.1042/0264-6021:3630553
    • Woestenenk EA, Gongadze GM, Shcherbakov DV, Rak AV, Garber MB, Hard T, Berglund H (2002) The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold. Biochem J 363(Pt 3):553-561 (Pubitemid 34526376)
    • (2002) Biochemical Journal , vol.363 , Issue.3 , pp. 553-561
    • Woestenenk, E.A.1    Gongadze, G.M.2    Shcherbakov, D.V.3    Rak, A.V.4    Garber, M.B.5    Hard, T.6    Berglund, H.7
  • 97
    • 0038663211 scopus 로고    scopus 로고
    • NMR structure of the ribosomal protein L23 from Thermus thermophilus
    • DOI 10.1023/A:1023502307069
    • Ohman A, Rak A, Dontsova M, Garber MB, Hard T (2003) NMR structure of the ribosomal protein L23 from Thermus thermophilus. J Biomol NMR 26(2):131-137 (Pubitemid 36609045)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.2 , pp. 131-137
    • Ohman, A.1    Rak, A.2    Dontsova, M.3    Garber, M.B.4    Hard, T.5
  • 100
    • 1542501914 scopus 로고    scopus 로고
    • The solution structure of ribosomal protein L18 from Bacillus stearothermophilus
    • DOI 10.1016/j.jmb.2003.11.018, PII S0022283603014153
    • Turner CF, Moore PB (2004) The solution structure of ribosomal protein L18 from Bacillus stearothermophilus. J Mol Biol 335(3):679-684 (Pubitemid 38352811)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 679-684
    • Turner, C.F.1    Moore, P.B.2
  • 103
    • 67649185437 scopus 로고    scopus 로고
    • Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricus
    • Edmondson SP, Turri J, Smith K, Clark A, Shriver JW (2009) Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricus. Biochemistry 48(24):5553-5562
    • (2009) Biochemistry , vol.48 , Issue.24 , pp. 5553-5562
    • Edmondson, S.P.1    Turri, J.2    Smith, K.3    Clark, A.4    Shriver, J.W.5
  • 104
    • 39549101754 scopus 로고    scopus 로고
    • Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus
    • DOI 10.1110/ps.073273008
    • Wu B, Lukin J, Yee A, Lemak A, Semesi A, Ramelot TA, Kennedy MA, Arrowsmith CH (2008) Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus. Protein Sci 17(3):589-596 (Pubitemid 351281561)
    • (2008) Protein Science , vol.17 , Issue.3 , pp. 589-596
    • Wu, B.1    Lukin, J.2    Yee, A.3    Lemak, A.4    Semesi, A.5    Ramelot, T.A.6    Kennedy, M.A.7    Arrowsmith, C.H.8
  • 105
    • 80855132587 scopus 로고    scopus 로고
    • Evaluation of residue-residue contact predictions in CASP9
    • Monastyrskyy B, Fidelis K, Tramontano A, Kryshtafovych A (2011) Evaluation of residue-residue contact predictions in CASP9. Proteins 79(Suppl 10):119-125
    • (2011) Proteins , vol.79 , Issue.SUPPL. 10 , pp. 119-125
    • Monastyrskyy, B.1    Fidelis, K.2    Tramontano, A.3    Kryshtafovych, A.4
  • 108
    • 9344260242 scopus 로고    scopus 로고
    • RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli
    • DOI 10.1261/rna.7121704
    • Semrad K, Green R, Schroeder R (2004) RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli. RNA 10(12):1855-1860 (Pubitemid 39557823)
    • (2004) RNA , vol.10 , Issue.12 , pp. 1855-1860
    • Semrad, K.1    Green, R.2    Schroeder, R.3
  • 110
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky VN (2011) Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem Soc Rev 40(3):1623-1634
    • (2011) Chem Soc Rev , vol.40 , Issue.3 , pp. 1623-1634
    • Uversky, V.N.1
  • 111
    • 0025912715 scopus 로고
    • The assembly of prokaryotic ribosomes
    • Nierhaus KH (1991) The assembly of prokaryotic ribosomes. Biochimie 73(6):739-755
    • (1991) Biochimie , vol.73 , Issue.6 , pp. 739-755
    • Nierhaus, K.H.1
  • 112
    • 0018129317 scopus 로고
    • Mutational alterations in 50 proteins of the Escherichia coli ribosome
    • Dabbs ER (1978) Mutational alterations in 50 proteins of the Escherichia coli ribosome. Mol Gen Genet 165(1):73-78
    • (1978) Mol Gen Genet , vol.165 , Issue.1 , pp. 73-78
    • Dabbs, E.R.1
  • 113
    • 0004637907 scopus 로고
    • Mutant studies on the prokaryotic ribosome
    • Hardesty B, Kramer G (eds) Springer, New York
    • Dabbs ER (1986) Mutant studies on the prokaryotic ribosome. In: Hardesty B, Kramer G (eds) Structure, function and genetics of ribosomes. Springer, New York, pp 733-748
    • (1986) Structure, Function and Genetics of Ribosomes , pp. 733-748
    • Dabbs, E.R.1
  • 114
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A, Nakamura H (2006) Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett 580(8):2041-2045
    • (2006) FEBS Lett , vol.580 , Issue.8 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 115
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman D, Light S, Bjorklund AK, Elofsson A (2006) What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? Genome Biol 7(6):R45
    • (2006) Genome Biol , vol.7 , Issue.6
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 117
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • DOI 10.1021/pr060171o
    • Dosztanyi Z, Chen J, Dunker AK, Simon I, Tompa P (2006) Disorder and sequence repeats in hub proteins and their implications for network evolution. J Proteome Res 5(11):2985-2995 (Pubitemid 44749217)
    • (2006) Journal of Proteome Research , vol.5 , Issue.11 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 118
    • 33847081239 scopus 로고    scopus 로고
    • Role of intrinsic disorder in transient interactions of hub proteins
    • Singh GP, Ganapathi M, Dash D (2007) Role of intrinsic disorder in transient interactions of hub proteins. Proteins 66(4):761-765
    • (2007) Proteins , vol.66 , Issue.4 , pp. 761-765
    • Singh, G.P.1    Ganapathi, M.2    Dash, D.3
  • 119
    • 34447558571 scopus 로고    scopus 로고
    • Intrinsic disorder in yeast transcriptional regulatory network
    • DOI 10.1002/prot.21497
    • Singh GP, Dash D (2007) Intrinsic disorder in yeast transcriptional regulatory network. Proteins 68(3):602-605 (Pubitemid 47068300)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.3 , pp. 602-605
    • Singh, G.P.1    Dash, D.2
  • 120
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Wool IG (1996) Extraribosomal functions of ribosomal proteins. Trends Biochem Sci 21(5):164-165
    • (1996) Trends Biochem Sci , vol.21 , Issue.5 , pp. 164-165
    • Wool, I.G.1
  • 121
    • 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(9):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
  • 122
    • 57749097722 scopus 로고    scopus 로고
    • Transcription by moonlight: Structural basis of an extraribosomal activity of ribosomal protein S10
    • Weisberg RA (2008) Transcription by moonlight: structural basis of an extraribosomal activity of ribosomal protein S10. Mol Cell 32(6):747-748
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 747-748
    • Weisberg, R.A.1
  • 123
    • 58249107143 scopus 로고    scopus 로고
    • Emerging functions of ribosomal proteins in gene-specific transcription and translation
    • Lindstrom MS (2009) Emerging functions of ribosomal proteins in gene-specific transcription and translation. Biochem Biophys Res Commun 379(2):167-170
    • (2009) Biochem Biophys Res Commun , vol.379 , Issue.2 , pp. 167-170
    • Lindstrom, M.S.1
  • 124
    • 63649157049 scopus 로고    scopus 로고
    • How common are extraribosomal functions of ribosomal proteins?
    • Warner JR, McIntosh KB (2009) How common are extraribosomal functions of ribosomal proteins? Mol Cell 34(1):3-11
    • (2009) Mol Cell , vol.34 , Issue.1 , pp. 3-11
    • Warner, J.R.1    McIntosh, K.B.2
  • 126
    • 0023414494 scopus 로고
    • Autogenous control of the S10 ribosomal protein operon of Escherichia coli: Genetic dissection of transcriptional and posttranscriptional regulation
    • Freedman LP, Zengel JM, Archer RH, Lindahl L (1987) Autogenous control of the S10 ribosomal protein operon of Escherichia coli: genetic dissection of transcriptional and posttranscriptional regulation. Proc Natl Acad Sci USA 84(18):6516-6520
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.18 , pp. 6516-6520
    • Freedman, L.P.1    Zengel, J.M.2    Archer, R.H.3    Lindahl, L.4
  • 127
    • 0025375756 scopus 로고
    • Escherichia coli ribosomal protein L4 stimulates transcription termination at a specific site in the leader of the S10 operon independent of L4-mediated inhibition of translation
    • DOI 10.1016/S0022-2836(05)80122-6
    • Zengel JM, Lindahl L (1990) Escherichia coli ribosomal protein L4 stimulates transcription termination at a specific site in the leader of the S10 operon independent of L4-mediated inhibition of translation. J Mol Biol 213(1):67-78 (Pubitemid 20171098)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.1 , pp. 67-78
    • Zengel, J.M.1    Lindahl, L.2
  • 128
    • 0025269449 scopus 로고
    • Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader
    • Zengel JM, Lindahl L (1990) Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader. Proc Natl Acad Sci USA 87(7):2675-2679
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.7 , pp. 2675-2679
    • Zengel, J.M.1    Lindahl, L.2
  • 129
    • 0029845147 scopus 로고    scopus 로고
    • Ribosomal protein L4 from Escherichia coli utilizes nonidentical determinants for its structural and regulatory functions
    • Li X, Lindahl L, Zengel JM (1996) Ribosomal protein L4 from Escherichia coli utilizes nonidentical determinants for its structural and regulatory functions. RNA 2(1):24-37 (Pubitemid 26371309)
    • (1996) RNA , vol.2 , Issue.1 , pp. 24-37
    • Li, X.1    Lindahl, L.2    Zengel, J.M.3
  • 130
    • 0025827734 scopus 로고
    • Structural basis for the regulation of splicing of a yeast messenger RNA
    • Eng FJ, Warner JR (1991) Structural basis for the regulation of splicing of a yeast messenger RNA. Cell 65(5):797-804 (Pubitemid 121001311)
    • (1991) Cell , vol.65 , Issue.5 , pp. 797-804
    • Eng, F.J.1    Warner, J.R.2
  • 131
    • 0032939495 scopus 로고    scopus 로고
    • Ribosomal protein S14 of Saccharomyces cerevisiae regulates its expression by binding to RPS14B pre-mRNA and to 18S rRNA
    • Fewell SW, Woolford JL Jr (1999) Ribosomal protein S14 of Saccharomyces cerevisiae regulates its expression by binding to RPS14B pre-mRNA and to 18S rRNA. Mol Cell Biol 19(1):826-834 (Pubitemid 29018483)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 826-834
    • Fewell, S.W.1    Woolford Jr., J.L.2
  • 132
    • 0025770052 scopus 로고
    • The ribosomal protein L2 in S.cerevisiae controls the level of accumulation of its own mRNA
    • Presutti C, Ciafre SA, Bozzoni I (1991) The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA. EMBO J 10(8):2215-2221 (Pubitemid 21905694)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 2215-2221
    • Presutti, C.1    Ciafre, S.-A.2    Bozzoni, I.3
  • 133
    • 36148994348 scopus 로고    scopus 로고
    • Human ribosomal protein S13 regulates expression of its own gene at the splicing step by a feedback mechanism
    • DOI 10.1093/nar/gkm701
    • Malygin A, Parakhnevitch NM, Ivanov AV, Eperon IC, Karpova GG (2007) Human ribosomal protein S13 regulates expression of its own gene at the splicing step by a feedback mechanism. Nucleic Acids Res 35(19):6414-6423 (Pubitemid 350111611)
    • (2007) Nucleic Acids Research , vol.35 , Issue.19 , pp. 6414-6423
    • Malygin, A.A.1    Parakhnevitch, N.M.2    Ivanov, A.V.3    Eperon, I.C.4    Karpova, G.G.5
  • 135
    • 0033856880 scopus 로고    scopus 로고
    • Unproductively spliced ribosomal protein mRNAs are natural targets of mRNA surveillance in C. Elegans
    • Mitrovich QM, Anderson P (2000) Unproductively spliced ribosomal protein mRNAs are natural targets of mRNA surveillance in C. elegans. Genes Dev 14(17):2173-2184
    • (2000) Genes Dev , vol.14 , Issue.17 , pp. 2173-2184
    • Mitrovich, Q.M.1    Anderson, P.2
  • 136
    • 36849148382 scopus 로고
    • Origin of life: The RNA world
    • Gilbert W (1986) Origin of life: the RNA world. Nature 319(6055):618
    • (1986) Nature , vol.319 , Issue.6055 , pp. 618
    • Gilbert, W.1
  • 139
    • 0032479475 scopus 로고    scopus 로고
    • Origins of globular structure in proteins
    • DOI 10.1016/S0014-5793(98)00674-7, PII S0014579398006747
    • Doi N, Yanagawa H (1998) Origins of globular structure in proteins. FEBS Lett 430(3):150-153 (Pubitemid 28337902)
    • (1998) FEBS Letters , vol.430 , Issue.3 , pp. 150-153
    • Doi, N.1    Yanagawa, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.