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Volumn 30, Issue 2, 2012, Pages 137-149

Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life

Author keywords

Archaea; Bacteria; Eukaryotes; Evolution; Intrinsic disorder; Prokaryotes; Proteome complexity; Viruses

Indexed keywords

PROTEOME;

EID: 84859701551     PISSN: 07391102     EISSN: None     Source Type: Journal    
DOI: 10.1080/07391102.2012.675145     Document Type: Article
Times cited : (456)

References (84)
  • 1
    • 0030874420 scopus 로고    scopus 로고
    • Size and complexity among multicellular organisms
    • DOI 10.1006/bijl.1996.0108
    • Bell, G., & Mooers, A.O. (1997). Size and complexity among multicellular organisms. Biological Journal of the Linnean Society, 60, 345-363. (Pubitemid 27347373)
    • (1997) Biological Journal of the Linnean Society , vol.60 , Issue.3 , pp. 345-363
    • Bell, G.1    Mooers, A.O.2
  • 2
    • 79956190554 scopus 로고    scopus 로고
    • The diversity of physical forces and mechanisms in intermolecular interactions
    • Berezovsky, I.N. (2011). The diversity of physical forces and mechanisms in intermolecular interactions. Physical Biology, 8, 035002.
    • (2011) Physical Biology , vol.8 , pp. 035002
    • Berezovsky, I.N.1
  • 5
    • 77957766242 scopus 로고    scopus 로고
    • Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes
    • Burra, P.V., Kalmar, L., & Tompa, P. (2010). Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes. PLoS ONE, 5, e12069.
    • (2010) PLoS ONE , vol.5
    • Burra, P.V.1    Kalmar, L.2    Tompa, P.3
  • 6
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • DOI 10.1021/bi7012273
    • Cheng, Y., Oldfield, C.J., Meng, J., Romero, P., Uversky, V.N., & Dunker, A.K. (2007). Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry, 46, 13468-13477. (Pubitemid 350209945)
    • (2007) Biochemistry , vol.46 , Issue.47 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 8
    • 0035895513 scopus 로고    scopus 로고
    • Gene number. What if there are only 30,000 human genes?
    • Claverie, J.M. (2001). Gene number. What if there are only 30,000 human genes? Science, 291, 1255-1257.
    • (2001) Science , vol.291 , pp. 1255-1257
    • Claverie, J.M.1
  • 10
    • 49849097024 scopus 로고    scopus 로고
    • Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: The case of the notch ligand Delta-4
    • De Biasio, A., Guarnaccia, C., Popovic, M., Uversky, V.N., Pintar, A., & Pongor, S. (2008). Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: The case of the notch ligand Delta-4. Journal of Proteome Research, 7, 2496-2506.
    • (2008) Journal of Proteome Research , vol.7 , pp. 2496-2506
    • De Biasio, A.1    Guarnaccia, C.2    Popovic, M.3    Uversky, V.N.4    Pintar, A.5    Pongor, S.6
  • 12
    • 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, A.K., Cortese, M.S., Romero, P., Iakoucheva, L.M., &Uversky, V.N. (2005). Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS Journal, 272, 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
  • 16
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • DOI 10.1016/S0959-440X(02)00289-0
    • Dyson, H.J., & Wright, P.E. (2002). Coupling of folding and binding for unstructured proteins. Current Opinion in Structural Biology, 12, 54-60. (Pubitemid 34142721)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 17
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H.J., & Wright, P.E. (2005). Intrinsically unstructured proteins and their functions. Nature Reviews Molecular Cell Biology, 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
  • 18
    • 0032563113 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of halophilic proteins
    • DOI 10.1006/jmbi.1998.1904
    • Elcock, A.H., & McCammon, J.A. (1998). Electrostatic contributions to the stability of halophilic proteins. Journal of Molecular Biology, 280, 731-748. (Pubitemid 28336377)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.4 , pp. 731-748
    • Elcock, A.H.1    McCammon, J.A.2
  • 19
    • 33750711671 scopus 로고    scopus 로고
    • Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan parasite proteomes
    • DOI 10.1016/j.molbiopara.2006.08.011, PII S016668510600257X
    • Feng, Z.P., Zhang, X., Han, P., Arora, N., Anders, R.F., &Norton, R.S. (2006). Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan parasite proteomes. Molecular and Biochemical Parasitology, 150, 256-267. (Pubitemid 44696289)
    • (2006) Molecular and Biochemical Parasitology , vol.150 , Issue.2 , pp. 256-267
    • Feng, Z.-P.1    Zhang, X.2    Han, P.3    Arora, N.4    Anders, R.F.5    Norton, R.S.6
  • 20
    • 24744450331 scopus 로고    scopus 로고
    • The two ages of the RNA world, and the transition to the DNA world: A story of viruses and cells
    • Forterre, P. (2005). The two ages of the RNA world, and the transition to the DNA world: A story of viruses and cells. Biochimie, 87, 793-803.
    • (2005) Biochimie , vol.87 , pp. 793-803
    • Forterre, P.1
  • 21
    • 33645053240 scopus 로고    scopus 로고
    • The origin of viruses and their possible roles in major evolutionary transitions
    • Forterre, P. (2006). The origin of viruses and their possible roles in major evolutionary transitions. Virus Research, 117, 5-16.
    • (2006) Virus Research , vol.117 , pp. 5-16
    • Forterre, P.1
  • 22
    • 78751584657 scopus 로고    scopus 로고
    • A new fusion hypothesis for the origin of Eukarya: Better than previous ones, but probably also wrong
    • Forterre, P. (2011). A new fusion hypothesis for the origin of Eukarya: Better than previous ones, but probably also wrong. Research in Microbiology, 162, 77-91.
    • (2011) Research in Microbiology , vol.162 , pp. 77-91
    • Forterre, P.1
  • 23
    • 0037459217 scopus 로고    scopus 로고
    • Unique amino acid composition of proteins in halophilic bacteria
    • DOI 10.1016/S0022-2836(03)00150-5
    • Fukuchi, S., Yoshimune, K., Wakayama, M., Moriguchi, M., &Nishikawa, K. (2003). Unique amino acid composition of proteins in halophilic bacteria. Journal of Molecular Biology, 327, 347-357. (Pubitemid 36298706)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.2 , pp. 347-357
    • Fukuchi, S.1    Yoshimune, K.2    Wakayama, M.3    Moriguchi, M.4    Nishikawa, K.5
  • 24
    • 60849128834 scopus 로고    scopus 로고
    • Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome
    • Galea, C.A., High, A.A., Obenauer, J.C., Mishra, A., Park, C. G., Punta, M., ... Kriwacki, R.W. (2009). Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome. Journal of Proteome Research, 8, 211-226.
    • (2009) Journal of Proteome Research , vol.8 , pp. 211-226
    • Galea, C.A.1    High, A.A.2    Obenauer, J.C.3    Mishra, A.4    Park, C.G.5    Punta, M.6    Kriwacki, R.W.7
  • 27
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • REVIEWS1018
    • Gray, M.W., Burger, G., & Lang, B.F. (2001). The origin and early evolution of mitochondria. Genome Biology, 2, REVIEWS1018.
    • (2001) Genome Biology , vol.2
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 28
    • 2442606761 scopus 로고    scopus 로고
    • Macroevolution, hierarchy theory, and the C-value enigma
    • Gregory, T.R. (2004). Macroevolution, hierarchy theory, and the C-value enigma. Paleobiology, 30, 179-202.
    • (2004) Paleobiology , vol.30 , pp. 179-202
    • Gregory, T.R.1
  • 29
    • 0035992053 scopus 로고    scopus 로고
    • The g-value paradox
    • DOI 10.1046/j.1525-142X.2002.01069.x
    • Hahn, M.W., & Wray, G.A. (2002). The G-value paradox. Evolution & Development, 4, 73-75. (Pubitemid 34589446)
    • (2002) Evolution and Development , vol.4 , Issue.2 , pp. 73-75
    • Hahn, M.W.1    Wray, G.A.2
  • 31
    • 2942568227 scopus 로고    scopus 로고
    • A molecular timescale of eukaryote evolution and the rise of complex multicellular life
    • Hedges, S.B., Blair, J.E., Venturi, M.L., & Shoe, J.L. (2004). A molecular timescale of eukaryote evolution and the rise of complex multicellular life. BMC Evolutionary Biology, 4, 2.
    • (2004) BMC Evolutionary Biology , vol.4 , pp. 2
    • Hedges, S.B.1    Blair, J.E.2    Venturi, M.L.3    Shoe, J.L.4
  • 32
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic disorder in cell-signaling and cancer-associated proteins
    • DOI 10.1016/S0022-2836(02)00969-5
    • Iakoucheva, L.M., Brown, C.J., Lawson, J.D., Obradovic, Z., & Dunker, A.K. (2002). Intrinsic disorder in cell-signaling and cancer-associated proteins. Journal of Molecular Biology, 323, 573-584. (Pubitemid 35283681)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.3 , pp. 573-584
    • Iakoucheva, L.M.1    Brown, C.J.2    Lawson, J.D.3    Obradovic, Z.4    Dunker, A.K.5
  • 33
    • 30344451365 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP6
    • DOI 10.1002/prot.20734
    • Jin, Y., & Dunbrack, R.L.Jr. (2005). Assessment of disorder predictions in CASP6. Proteins, 61(Suppl. 7), 167-175. (Pubitemid 43069971)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.SUPPL. 7 , pp. 167-175
    • Jin, Y.1    Dunbrack, R.L.2
  • 35
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • Madern, D., Ebel, C., & Zaccai, G. (2000). Halophilic adaptation of enzymes. Extremophiles, 4, 91-98.
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 36
    • 33745617904 scopus 로고    scopus 로고
    • Intrinsically disordered C-terminal segments of voltage-activated potassium channels: A possible fishing rod-like mechanism for channel binding to scaffold proteins
    • DOI 10.1093/bioinformatics/btl137
    • Magidovich, E., Fleishman, S.J., & Yifrach, O. (2006). Intrinsically disordered C-terminal segments of voltage-activated potassium channels: A possible fishing rod-like mechanism for channel binding to scaffold proteins. Bioinformatics, 22, 1546-1550. (Pubitemid 43985286)
    • (2006) Bioinformatics , vol.22 , Issue.13 , pp. 1546-1550
    • Magidovich, E.1    Fleishman, S.J.2    Yifrach, O.3
  • 38
    • 0016830903 scopus 로고
    • Symbiotic theory of the origin of eukaryotic organelles; criteria for proof
    • Margulis, L. (1975). Symbiotic theory of the origin of eukaryotic organelles; criteria for proof. Symposia of the Society for Experimental Biology, 22, 21-38.
    • (1975) Symposia of the Society for Experimental Biology , vol.22 , pp. 21-38
    • Margulis, L.1
  • 39
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • DOI 10.1016/S0301-4622(00)00126-5, PII S0301462200001265
    • Mevarech, M., Frolow, F., & Gloss, L.M. (2000). Halophilic enzymes: Proteins with a grain of salt. Biophysical Chemistry, 86, 155-164. (Pubitemid 30665604)
    • (2000) Biophysical Chemistry , vol.86 , Issue.2-3 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 40
    • 34047113297 scopus 로고    scopus 로고
    • Intrinsically Disordered Regions of Human Plasma Membrane Proteins Preferentially Occur in the Cytoplasmic Segment
    • DOI 10.1016/j.jmb.2007.02.033, PII S0022283607002148
    • Minezaki, Y., Homma, K., & Nishikawa, K. (2007). Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment. Journal of Molecular Biology, 368, 902-913. (Pubitemid 46527614)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 902-913
    • Minezaki, Y.1    Homma, K.2    Nishikawa, K.3
  • 41
    • 76549240988 scopus 로고
    • The desoxyribonucleic acid content of animal cells and its evolutionary significance
    • Mirsky, A.E., & Ris, H. (1951). The desoxyribonucleic acid content of animal cells and its evolutionary significance. Journal of General Physiology, 34, 451-462.
    • (1951) Journal of General Physiology , vol.34 , pp. 451-462
    • Mirsky, A.E.1    Ris, H.2
  • 44
    • 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, W.J.Jr., Radivojac, P., Dunker, A.K., &Uversky, V.N. (2008). Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes. Molecular BioSystems, 4, 328-340. (Pubitemid 351422588)
    • (2008) Molecular BioSystems , vol.4 , Issue.4 , pp. 328-340
    • Mohan, A.1    Sullivan Jr., W.J.2    Radivojac, P.3    Dunker, A.K.4    Uversky, V.N.5
  • 46
    • 13644257647 scopus 로고    scopus 로고
    • Comparing and combining predictors of mostly disordered proteins
    • DOI 10.1021/bi047993o
    • Oldfield, C.J., Cheng, Y., Cortese, M.S., Brown, C.J., Uversky, V.N., & Dunker, A.K. (2005). Comparing and combining predictors of mostly disordered proteins. Biochemistry, 44, 1989-2000. (Pubitemid 40227474)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 1989-2000
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Brown, C.J.4    Uversky, V.N.5    Bunker, A.K.6
  • 47
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • DOI 10.1021/bi050736e
    • Oldfield, C.J., Cheng, Y., Cortese, M.S., Romero, P., Uversky, V.N., & Dunker, A.K. (2005). Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry, 44, 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
  • 48
    • 40849114643 scopus 로고    scopus 로고
    • The dynamic nature of eukaryotic genomes
    • DOI 10.1093/molbev/msn032
    • Parfrey, L.W., Lahr, D.J., & Katz, L.A. (2008). The dynamic nature of eukaryotic genomes. Molecular Biology and Evolution, 25, 787-794. (Pubitemid 351398334)
    • (2008) Molecular Biology and Evolution , vol.25 , Issue.4 , pp. 787-794
    • Parfrey, L.W.1    Lahr, D.J.G.2    Katz, L.A.3
  • 49
    • 47149088683 scopus 로고    scopus 로고
    • Molecular signature of hypersaline adaptation: Insights from genome and proteome composition of halophilic prokaryotes
    • Paul, S., Bag, S.K., Das, S., Harvill, E.T., & Dutta, C. (2008). Molecular signature of hypersaline adaptation: Insights from genome and proteome composition of halophilic prokaryotes. Genome Biology, 9, R70.
    • (2008) Genome Biology , vol.9
    • Paul, S.1    Bag, S.K.2    Das, S.3    Harvill, E.T.4    Dutta, C.5
  • 52
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe, D., & Petsko, G.A. (1986). Study of protein dynamics by X-ray diffraction. Methods in Enzymology, 131, 389-433. (Pubitemid 16002210)
    • (1986) Methods in Enzymology , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 54
    • 33746354305 scopus 로고    scopus 로고
    • Unraveling the nature of the segmentation clock: Intrinsic disorder of clock proteins and their interaction map
    • DOI 10.1016/j.compbiolchem.2006.04.005, PII S1476927106000302
    • Roy, S., Schnell, S., & Radivojac, P. (2006). Unraveling the nature of the segmentation clock: Intrinsic disorder of clock proteins and their interaction map. Computational Biology and Chemistry, 30, 241-248. (Pubitemid 44118829)
    • (2006) Computational Biology and Chemistry , vol.30 , Issue.4 , pp. 241-248
    • Roy, S.1    Schnell, S.2    Radivojac, P.3
  • 55
    • 33749402982 scopus 로고    scopus 로고
    • The cnidarian-bilaterian ancestor possessed at least 56 homeoboxes: Evidence from the starlet sea anemone, Nematostella vectensis
    • Ryan, J.F., Burton, P.M., Mazza, M.E., Kwong, G.K., Mullikin, J.C., & Finnerty, J.R. (2006). The cnidarian-bilaterian ancestor possessed at least 56 homeoboxes: Evidence from the starlet sea anemone, Nematostella vectensis. Genome Biology, 7, R64.
    • (2006) Genome Biology , vol.7
    • Ryan, J.F.1    Burton, P.M.2    Mazza, M.E.3    Kwong, G.K.4    Mullikin, J.C.5    Finnerty, J.R.6
  • 56
    • 82655175850 scopus 로고    scopus 로고
    • The relationship between proteome size, structural disorder and organism complexity
    • Schad, E., Tompa, P., & Hegyi, H. (2011). The relationship between proteome size, structural disorder and organism complexity. Genome Biology, 12, R120.
    • (2011) Genome Biology , vol.12
    • Schad, E.1    Tompa, P.2    Hegyi, H.3
  • 57
    • 84055213697 scopus 로고    scopus 로고
    • Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface
    • Siglioccolo, A., Paiardini, A., Piscitelli, M., & Pascarella, S. (2011). Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface. BMC Structural Biology, 11, 50.
    • (2011) BMC Structural Biology , vol.11 , pp. 50
    • Siglioccolo, A.1    Paiardini, A.2    Piscitelli, M.3    Pascarella, S.4
  • 59
    • 0000807693 scopus 로고
    • The desoxyribose nucleic acid content of animal nuclei
    • Swift, H.H. (1950). The desoxyribose nucleic acid content of animal nuclei. Physiological Zoology, 23, 169-198.
    • (1950) Physiological Zoology , vol.23 , pp. 169-198
    • Swift, H.H.1
  • 61
    • 0000822856 scopus 로고
    • The genetic organization of chromosomes
    • Thomas, C.A.Jr. (1971). The genetic organization of chromosomes. Annual Review of Genetics, 5, 237-256.
    • (1971) Annual Review of Genetics , vol.5 , pp. 237-256
    • Thomas Jr., C.A.1
  • 62
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002). Intrinsically unstructured proteins. Trends in Biochemical Sciences, 27, 527-533.
    • (2002) Trends in Biochemical Sciences , vol.27 , pp. 527-533
    • Tompa, P.1
  • 63
    • 33747191719 scopus 로고    scopus 로고
    • Prevalent structural disorder in E. coli and S. cerevisiae proteomes
    • DOI 10.1021/pr0600881
    • Tompa, P., Dosztanyi, Z., & Simon, I. (2006). Prevalent structural disorder in E. coli and S. cerevisiae proteomes. Journal of Proteome Research, 5, 1996-2000. (Pubitemid 44232712)
    • (2006) Journal of Proteome Research , vol.5 , Issue.8 , pp. 1996-2000
    • Tompa, P.1    Dosztanyi, Z.2    Simon, I.3
  • 65
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V.N., Gillespie, J.R., & Fink, A.L. (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
  • 66
    • 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, V.N., Oldfield, C.J., & Dunker, A.K. (2005). Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. Journal of Molecular Recognition, 18, 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
  • 68
    • 0033793144 scopus 로고    scopus 로고
    • Two genomic paths to the evolution of complexity in bodyplans
    • Valentine, J.W. (2000). Two genomic paths to the evolution of complexity in bodyplans. Paleobiology, 26, 513-519.
    • (2000) Paleobiology , vol.26 , pp. 513-519
    • Valentine, J.W.1
  • 69
    • 33646909100 scopus 로고    scopus 로고
    • Protein family expansions and biological complexity
    • Vogel, C., & Chothia, C. (2006). Protein family expansions and biological complexity. PLoS Computational Biology, 2, e48.
    • (2006) PLoS Computational Biology , vol.2
    • Vogel, C.1    Chothia, C.2
  • 70
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. (1989). Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature, 341, 456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 72
    • 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, L.M., Oldfield, C.J., Dunker, A.K., Obradovic, Z., & Uversky, V.N. (2007). Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. Journal of Proteome Research, 6, 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
  • 73
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., & von Heijne, G. (1998). Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Science, 7, 1029-1038. (Pubitemid 28216544)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 74
    • 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, J.J., Sodhi, J.S., McGuffin, L.J., Buxton, B.F., & Jones, D.T. (2004). Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. Journal of Molecular Biology, 337, 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
  • 75
    • 0036408309 scopus 로고    scopus 로고
    • The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases
    • DOI 10.1016/S0022-2836(02)00916-6
    • Wright, D.B., Banks, D.D., Lohman, J.R., Hilsenbeck, J.L., &Gloss, L.M. (2002). The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. Journal of Molecular Biology, 323, 327-344. (Pubitemid 35283695)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.2 , pp. 327-344
    • Wright, D.B.1    Banks, D.D.2    Lohman, J.R.3    Hilsenbeck, J.L.4    Gloss, L.M.5
  • 76
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • Wright, P.E., & Dyson, H.J. (1999). Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. Journal of Molecular Biology, 293, 321-331. (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 77
    • 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, L.M., Oldfield, C.J., Dunker, A.K., Uversky, V.N., & Obradovic, Z. (2007a). Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. Journal of Proteome Research, 6, 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
  • 78
    • 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, L.M., Oldfield, C.J., Dunker, A.K., Obradovic, Z., & Uversky, V.N. (2007b). Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. Journal of Proteome Research, 6, 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
  • 80
    • 72949087534 scopus 로고    scopus 로고
    • Analysis of structured and intrinsically disordered regions of transmembrane proteins
    • Xue, B., Li, L., Meroueh, S.O., Uversky, V.N., & Dunker, A. K. (2009). Analysis of structured and intrinsically disordered regions of transmembrane proteins. Molecular BioSystems, 5, 1688-1702.
    • (2009) Molecular BioSystems , vol.5 , pp. 1688-1702
    • Xue, B.1    Li, L.2    Meroueh, S.O.3    Uversky, V.N.4    Dunker, A.K.5
  • 81
    • 67349162535 scopus 로고    scopus 로고
    • CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions
    • Xue, B., Oldfield, C.J., Dunker, A.K., & Uversky, V.N. (2009). CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Letters, 583, 1469-1474.
    • (2009) FEBS Letters , vol.583 , pp. 1469-1474
    • Xue, B.1    Oldfield, C.J.2    Dunker, A.K.3    Uversky, V.N.4
  • 84
    • 0025143777 scopus 로고
    • Halophilic proteins and the influence of solvent on protein stabilization
    • Zaccai, G., & Eisenberg, H. (1990). Halophilic proteins and the influence of solvent on protein stabilization. Trends in Biochemical Sciences, 15, 333-337. (Pubitemid 20255490)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.9 , pp. 333-337
    • Zaccai, G.1    Eisenberg, H.2


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