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Volumn 8, Issue 1, 2018, Pages

Erratum to: Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii (Scientific Reports, (2018), 8, 1, (6805), 10.1038/s41598-018-24772-7);Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii

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EID: 85046456536     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-018-31276-x     Document Type: Erratum
Times cited : (12)

References (83)
  • 1
    • 84878885712 scopus 로고    scopus 로고
    • What's in a name Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered
    • Dunker, A. K. et al. What's in a name Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered. Intrinsically Disordered Proteins 1, e24157 (2013).
    • (2013) Intrinsically Disordered Proteins , vol.1 , pp. e24157
    • Dunker, A.K.1
  • 2
    • 85016084753 scopus 로고    scopus 로고
    • Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs
    • Uversky, V. N. Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs. Intrinsically Disordered Proteins 2, 1-42 (2014).
    • (2014) Intrinsically Disordered Proteins , vol.2 , pp. 1-42
    • Uversky, V.N.1
  • 3
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E. & Dyson, H. J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293, 321-331 (1999).
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 4
    • 84903957091 scopus 로고    scopus 로고
    • Introducing protein intrinsic disorder
    • Habchi, J., Tompa, P., Longhi, S. & Uversky, V. N. Introducing protein intrinsic disorder. Chem Rev 114, 6561-6588 (2014).
    • (2014) Chem Rev , vol.114 , pp. 6561-6588
    • Habchi, J.1    Tompa, P.2    Longhi, S.3    Uversky, V.N.4
  • 5
    • 52249124593 scopus 로고    scopus 로고
    • TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder
    • Campen, A. et al. TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder. Protein Pept Lett 15, 956 (2008).
    • (2008) Protein Pept Lett , vol.15 , pp. 956
    • Campen, A.1
  • 6
    • 2342473198 scopus 로고    scopus 로고
    • The importance of intrinsic disorder for protein phosphorylation
    • Iakoucheva, L. M. et al. The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res 32, 1037-1049 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. 1037-1049
    • Iakoucheva, L.M.1
  • 7
    • 84905818711 scopus 로고    scopus 로고
    • The protein non-folding problem: Amino acid determinants of intrinsic order and disorder
    • Mauna Lani, Hawaii, USA, World Scientific publisher January
    • Mathura, V., et al, The protein non-folding problem: Amino acid determinants of intrinsic order and disorder. Paper presented at Pacific Symposium on Biocomputing: Disorder and flexibility in protein structure and function, Mauna Lani, Hawaii, USA, World Scientific publisher, 2001, January.
    • (2001) Pacific Symposium on Biocomputing: Disorder and Flexibility in Protein Structure and Function
    • Mathura, V.1
  • 8
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem Sci 27, 527-533 (2002).
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 9
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded
    • Uversky, V. N. What does it mean to be natively unfolded Eur J Biochem 269, 2-12 (2002).
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 10
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F. & Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337, 635-645 (2004).
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 11
    • 84892688932 scopus 로고    scopus 로고
    • Protein domain definition should allow for conditional disorder
    • Yegambaram, K., Bulloch, E. & Kingston, R. Protein domain definition should allow for conditional disorder. Protein Sci 22, 1502-1518 (2013).
    • (2013) Protein Sci , vol.22 , pp. 1502-1518
    • Yegambaram, K.1    Bulloch, E.2    Kingston, R.3
  • 12
    • 84898892010 scopus 로고    scopus 로고
    • Correlations between predicted protein disorder and post-translational modifications in plants
    • Kurotani, A. et al. Correlations between predicted protein disorder and post-translational modifications in plants. Bioinformatics 30, 1095-1103 (2014).
    • (2014) Bioinformatics , vol.30 , pp. 1095-1103
    • Kurotani, A.1
  • 13
    • 84902446848 scopus 로고    scopus 로고
    • Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function
    • Jakob, U., Kriwacki, R. & Uversky, V. N. Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function. Chem Rev 114, 6779-6805 (2014).
    • (2014) Chem Rev , vol.114 , pp. 6779-6805
    • Jakob, U.1    Kriwacki, R.2    Uversky, V.N.3
  • 14
    • 84907209314 scopus 로고    scopus 로고
    • The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane
    • Wang, H. et al. The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane. Mol Cell Proteomics 13, 2337-2353 (2014).
    • (2014) Mol Cell Proteomics , vol.13 , pp. 2337-2353
    • Wang, H.1
  • 15
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J. & Wright, P. E. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6, 197-208 (2005).
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 16
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky, V. N., Oldfield, C. J. & Dunker, A. K. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 37, 215-246 (2008).
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 17
    • 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, A. K. & Uversky, V. N. Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn 30, 137-149 (2012).
    • (2012) J Biomol Struct Dyn , vol.30 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 18
    • 82655175850 scopus 로고    scopus 로고
    • The relationship between proteome size, structural disorder and organism complexity
    • Schad, E., Tompa, P. & Hegyi, H. The relationship between proteome size, structural disorder and organism complexity. Genome Biol 12, 1-13 (2011).
    • (2011) Genome Biol , vol.12 , pp. 1-13
    • Schad, E.1    Tompa, P.2    Hegyi, H.3
  • 19
    • 84925227741 scopus 로고    scopus 로고
    • Exceptionally abundant exceptions: Comprehensive characterization of intrinsic disorder in all domains of life
    • Peng, Z. et al. Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. Cell Mol Life Sci 72, 137-151 (2015).
    • (2015) Cell Mol Life Sci , vol.72 , pp. 137-151
    • Peng, Z.1
  • 20
    • 84930625276 scopus 로고    scopus 로고
    • Plant development regulation: Overview and perspectives
    • Yruela, I. Plant development regulation: Overview and perspectives. J Plant Physiol 182, 62-78 (2015).
    • (2015) J Plant Physiol , vol.182 , pp. 62-78
    • Yruela, I.1
  • 21
    • 85026630385 scopus 로고    scopus 로고
    • Evidence for a strong correlation between transcription factor protein disorder and organismic complexity
    • Yruela, I., Oldfield, C. J., Niklas, K. J. & Dunker, A. K. Evidence for a strong correlation between transcription factor protein disorder and organismic complexity. Genome Biol Evol 9, 1248-1265 (2017).
    • (2017) Genome Biol Evol , vol.9 , pp. 1248-1265
    • Yruela, I.1    Oldfield, C.J.2    Niklas, K.J.3    Dunker, A.K.4
  • 22
    • 84930196016 scopus 로고    scopus 로고
    • Rethinking gene regulatory networks in light of alternative splicing, intrinsically disordered protein domains, and post-translational modifications
    • Niklas, K. J., Bondos, S. E., Dunker, A. K. & Newman, S. A. Rethinking gene regulatory networks in light of alternative splicing, intrinsically disordered protein domains, and post-translational modifications. Front Cell Dev Biol 3, 1-13 (2015).
    • (2015) Front Cell Dev Biol , vol.3 , pp. 1-13
    • Niklas, K.J.1    Bondos, S.E.2    Dunker, A.K.3    Newman, S.A.4
  • 23
  • 24
    • 85016112986 scopus 로고    scopus 로고
    • DisProt 7. 0: A major update of the database of disordered proteins
    • Piovesan, D. et al. DisProt 7. 0: A major update of the database of disordered proteins. Nucleic Acids Res 45, D219-D227 (2017).
    • (2017) Nucleic Acids Res , vol.45 , pp. D219-D227
    • Piovesan, D.1
  • 25
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The Database of Disordered Proteins
    • Sickmeier, M. et al. DisProt: The Database of Disordered Proteins. Nucleic Acids Res 35, D786-D793 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. D786-D793
    • Sickmeier, M.1
  • 26
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • Kovacs, D., Kalmar, E., Torok, Z. & Tompa, P. Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol 147, 381-390 (2008).
    • (2008) Plant Physiol , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 27
    • 77950597578 scopus 로고    scopus 로고
    • Intrinsically disordered chaperones in plants and animals
    • Tompa, P. & Kovacs, D. Intrinsically disordered chaperones in plants and animals. Biochem Cell Biol 88, 167-174 (2010).
    • (2010) Biochem Cell Biol , vol.88 , pp. 167-174
    • Tompa, P.1    Kovacs, D.2
  • 28
    • 84874524363 scopus 로고    scopus 로고
    • Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology
    • Sun, X., Rikkerink, E. H., Jones, W. T. & Uversky, V. N. Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology. Plant Cell 25, 38-55 (2013).
    • (2013) Plant Cell , vol.25 , pp. 38-55
    • Sun, X.1    Rikkerink, E.H.2    Jones, W.T.3    Uversky, V.N.4
  • 29
    • 80052622990 scopus 로고    scopus 로고
    • A functionally required unfoldome from the plant kingdom: Intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development
    • Sun, X. et al. A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development. Plant Mol Biol 77, 205-223 (2011).
    • (2011) Plant Mol Biol , vol.77 , pp. 205-223
    • Sun, X.1
  • 32
    • 84873590183 scopus 로고    scopus 로고
    • Genome-wide analysis of protein disorder in Arabidopsis thaliana: Implications for plant environmental adaptation
    • Pietrosemoli, N., García-Martín, J. A., Solano, R. & Pazos, F. Genome-wide analysis of protein disorder in Arabidopsis thaliana: implications for plant environmental adaptation. PloS one 8, e55524 (2013).
    • (2013) PloS One , vol.8 , pp. e55524
    • Pietrosemoli, N.1    García-Martín, J.A.2    Solano, R.3    Pazos, F.4
  • 33
    • 84975893918 scopus 로고    scopus 로고
    • A collection of intrinsic disorder characterizations from eukaryotic proteomes
    • Vincent, M. & Schnell, S. A collection of intrinsic disorder characterizations from eukaryotic proteomes. Sci Data 3, 1-9 (2016).
    • (2016) Sci Data , vol.3 , pp. 1-9
    • Vincent, M.1    Schnell, S.2
  • 34
    • 34247616119 scopus 로고    scopus 로고
    • Towards proteomic approaches for the identification of structural disorder
    • Csizmók, V., Dosztányi, Z., Simon, I. & Tompa, P. Towards proteomic approaches for the identification of structural disorder. Curr Protein Pept Sci 8, 173-179 (2007).
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 173-179
    • Csizmók, V.1    Dosztányi, Z.2    Simon, I.3    Tompa, P.4
  • 35
    • 26844566629 scopus 로고    scopus 로고
    • Uncovering the unfoldome: Enriching cell extracts for unstructured proteins by acid treatment
    • Cortese, M. S., Baird, J. P., Uversky, V. N. & Dunker, A. K. Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment. J Proteome Res 4, 1610-1618 (2005).
    • (2005) J Proteome Res , vol.4 , pp. 1610-1618
    • Cortese, M.S.1    Baird, J.P.2    Uversky, V.N.3    Dunker, A.K.4
  • 36
    • 33750097976 scopus 로고    scopus 로고
    • Proteomic studies of the intrinsically unstructured mammalian proteome
    • Galea, C. A. et al. Proteomic studies of the intrinsically unstructured mammalian proteome. J Proteome Res 5, 2839-2848 (2006).
    • (2006) J Proteome Res , vol.5 , pp. 2839-2848
    • Galea, C.A.1
  • 37
    • 33747886382 scopus 로고    scopus 로고
    • Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS
    • Irar, S., Oliveira, E. & Goday, A. Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS. Proteomics 6, 175-185 (2006).
    • (2006) Proteomics , vol.6 , pp. 175-185
    • Irar, S.1    Oliveira, E.2    Goday, A.3
  • 38
    • 0029616132 scopus 로고
    • Chlamydomonas reinhardtii as the photosynthetic yeast
    • Rochaix, J.-D. Chlamydomonas reinhardtii as the photosynthetic yeast. Annual Review of Genetics 29, 209-230 (1995).
    • (1995) Annual Review of Genetics , vol.29 , pp. 209-230
    • Rochaix, J.-D.1
  • 39
    • 84865813701 scopus 로고    scopus 로고
    • Regulation of glyceraldehyde-3-phosphate dehydrogenase in the eustigmatophyte Pseudocharaciopsis ovalis is intermediate between a chlorophyte and a diatom
    • Avilan, L. et al. Regulation of glyceraldehyde-3-phosphate dehydrogenase in the eustigmatophyte Pseudocharaciopsis ovalis is intermediate between a chlorophyte and a diatom. Eur J Phycol 47, 207-215 (2012).
    • (2012) Eur J Phycol , vol.47 , pp. 207-215
    • Avilan, L.1
  • 40
    • 0037826944 scopus 로고    scopus 로고
    • The small protein CP12: A protein linker for supramolecular complex assembly
    • Graciet, E. et al. The small protein CP12: A protein linker for supramolecular complex assembly. Biochem 42, 8163-8170 (2003).
    • (2003) Biochem , vol.42 , pp. 8163-8170
    • Graciet, E.1
  • 41
    • 84976645393 scopus 로고    scopus 로고
    • Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state
    • Launay, H. et al. Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state. Biochem Biophys Res Commun 477, 20-26 (2016).
    • (2016) Biochem Biophys Res Commun , vol.477 , pp. 20-26
    • Launay, H.1
  • 42
    • 84924039821 scopus 로고    scopus 로고
    • FRET analysis of CP12 structural interplay by GAPDH and PRK
    • Moparthi, S. B. et al. FRET analysis of CP12 structural interplay by GAPDH and PRK. Biochem Biophys Res Commun 458, 488-493 (2015).
    • (2015) Biochem Biophys Res Commun , vol.458 , pp. 488-493
    • Moparthi, S.B.1
  • 43
    • 84866673529 scopus 로고    scopus 로고
    • An intrinsically disordered protein, CP12: Jack of all trades and master of the Calvin cycle
    • Gontero, B. & Maberly, S. C. An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle. Biochem Soc Trans 40, 995-999 (2012).
    • (2012) Biochem Soc Trans , vol.40 , pp. 995-999
    • Gontero, B.1    Maberly, S.C.2
  • 44
    • 67649601197 scopus 로고    scopus 로고
    • CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase
    • Erales, J., Lignon, S. & Gontero, B. CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 284, 12735-12744 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 12735-12744
    • Erales, J.1    Lignon, S.2    Gontero, B.3
  • 45
    • 27944484845 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: A possible regulatory role within a PRK/GAPDH/CP12 complex
    • Delobel, A. et al. Mass spectrometric analysis of the interactions between CP12, a chloroplast protein, and metal ions: A possible regulatory role within a PRK/GAPDH/CP12 complex. Rapid Commun Mass Spectrom 19, 3379-3388 (2005).
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 3379-3388
    • Delobel, A.1
  • 46
    • 84969795490 scopus 로고    scopus 로고
    • A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle
    • Mackinder, L. C. et al. A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle. Proc Natl Acad Sci USA 113, 5958-5963 (2016).
    • (2016) Proc Natl Acad Sci USA , vol.113 , pp. 5958-5963
    • Mackinder, L.C.1
  • 47
    • 85020306216 scopus 로고    scopus 로고
    • Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions
    • Meng, F., Uversky, V. & Kurgan, L. Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions. Cell Mol Life Sci 74, 3069-3090 (2017).
    • (2017) Cell Mol Life Sci , vol.74 , pp. 3069-3090
    • Meng, F.1    Uversky, V.2    Kurgan, L.3
  • 48
    • 84964733917 scopus 로고    scopus 로고
    • Modulation of intrinsically disordered protein function by post-translational modifications
    • Bah, A. & Forman-Kay, J. D. Modulation of intrinsically disordered protein function by post-translational modifications. J Biol Chem 291, 6696-6705 (2016).
    • (2016) J Biol Chem , vol.291 , pp. 6696-6705
    • Bah, A.1    Forman-Kay, J.D.2
  • 49
    • 31544433157 scopus 로고    scopus 로고
    • Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins
    • Haynes, C. & Iakoucheva, L. M. Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res 34, 305-312 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 305-312
    • Haynes, C.1    Iakoucheva, L.M.2
  • 50
    • 0033564196 scopus 로고    scopus 로고
    • Developmental regulation of SR protein phosphorylation and activity
    • Sanford, J. R. & Bruzik, J. P. Developmental regulation of SR protein phosphorylation and activity. Genes Dev 13, 1513-1518 (1999).
    • (1999) Genes Dev , vol.13 , pp. 1513-1518
    • Sanford, J.R.1    Bruzik, J.P.2
  • 51
    • 85011866942 scopus 로고    scopus 로고
    • Probing the global kinome and phosphoproteome in Chlamydomonas reinhardtii via sequential enrichment and quantitative proteomics
    • Werth, E. G. et al. Probing the global kinome and phosphoproteome in Chlamydomonas reinhardtii via sequential enrichment and quantitative proteomics. Plant J 89, 416-426 (2017).
    • (2017) Plant J , vol.89 , pp. 416-426
    • Werth, E.G.1
  • 52
    • 84939817717 scopus 로고    scopus 로고
    • In silico analysis of correlations between protein disorder and post-translational modifications in algae
    • Kurotani, A. & Sakurai, T. In silico analysis of correlations between protein disorder and post-translational modifications in algae. Int J Mol Sci 16, 19812-19835 (2015).
    • (2015) Int J Mol Sci , vol.16 , pp. 19812-19835
    • Kurotani, A.1    Sakurai, T.2
  • 53
    • 84866117711 scopus 로고    scopus 로고
    • Protein disorder in plants: A view from the chloroplast
    • Yruela, I. & Contreras-Moreira, B. Protein disorder in plants: A view from the chloroplast. BMC Plant Biol 12, 165-176 (2012).
    • (2012) BMC Plant Biol , vol.12 , pp. 165-176
    • Yruela, I.1    Contreras-Moreira, B.2
  • 54
    • 0034069495 scopus 로고    scopus 로고
    • Gene Ontology: Tool for the unification of biology
    • Botstein, D. et al. Gene Ontology: Tool for the unification of biology. Nat Genet 25, 25-29 (2000).
    • (2000) Nat Genet , vol.25 , pp. 25-29
    • Botstein, D.1
  • 55
    • 84887347845 scopus 로고    scopus 로고
    • Genetic recombination is associated with intrinsic disorder in plant proteomes
    • Yruela, I. & Contreras-Moreira, B. Genetic recombination is associated with intrinsic disorder in plant proteomes. BMC genomics 14, 772-781 (2013).
    • (2013) BMC Genomics , vol.14 , pp. 772-781
    • Yruela, I.1    Contreras-Moreira, B.2
  • 56
    • 84870065644 scopus 로고    scopus 로고
    • Conditional disorder in chaperone action
    • Bardwell, J. C. & Jakob, U. Conditional disorder in chaperone action. Trends Biochem Sci 37, 517-525 (2012).
    • (2012) Trends Biochem Sci , vol.37 , pp. 517-525
    • Bardwell, J.C.1    Jakob, U.2
  • 57
    • 77951216943 scopus 로고    scopus 로고
    • Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone
    • Cremers, C. M., Reichmann, D., Hausmann, J., Ilbert, M. & Jakob, U. Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone. J Biol Chem 285, 11243-11251 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 11243-11251
    • Cremers, C.M.1    Reichmann, D.2    Hausmann, J.3    Ilbert, M.4    Jakob, U.5
  • 58
    • 34249866216 scopus 로고    scopus 로고
    • The redox-switch domain of Hsp33 functions as dual stress sensor
    • Ilbert, M. et al. The redox-switch domain of Hsp33 functions as dual stress sensor. Nat Struct Mol Biol 14, 556-563 (2007).
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 556-563
    • Ilbert, M.1
  • 59
    • 84863230577 scopus 로고    scopus 로고
    • Order out of disorder: Working cycle of an intrinsically unfolded chaperone
    • Reichmann, D. et al. Order out of disorder: working cycle of an intrinsically unfolded chaperone. Cell 148, 947-957 (2012).
    • (2012) Cell , vol.148 , pp. 947-957
    • Reichmann, D.1
  • 60
    • 84930038732 scopus 로고    scopus 로고
    • HSP33 in eukaryotes-an evolutionary tale of a chaperone adapted to photosynthetic organisms
    • Segal, N. A. & Shapira, M. HSP33 in eukaryotes-an evolutionary tale of a chaperone adapted to photosynthetic organisms. Plant J 82, 850-860 (2015).
    • (2015) Plant J , vol.82 , pp. 850-860
    • Segal, N.A.1    Shapira, M.2
  • 61
    • 84971241658 scopus 로고    scopus 로고
    • A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering
    • Borges, J. C., Seraphim, T. V., Dores-Silva, P. R. & Barbosa, L. R. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophys Rev 8, 107-120 (2016).
    • (2016) Biophys Rev , vol.8 , pp. 107-120
    • Borges, J.C.1    Seraphim, T.V.2    Dores-Silva, P.R.3    Barbosa, L.R.4
  • 62
    • 79957730170 scopus 로고    scopus 로고
    • Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
    • Genest, O., Hoskins, J. R., Camberg, J. L., Doyle, S. M. & Wickner, S. Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci USA 108, 8206-8211 (2011).
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 8206-8211
    • Genest, O.1    Hoskins, J.R.2    Camberg, J.L.3    Doyle, S.M.4    Wickner, S.5
  • 63
    • 84948397326 scopus 로고    scopus 로고
    • Hsp70 and Hsp90 of E. coli directly interact for collaboration in protein remodeling
    • Genest, O., Hoskins, J. R., Kravats, A. N., Doyle, S. M. & Wickner, S. Hsp70 and Hsp90 of E. coli directly interact for collaboration in protein remodeling. J Mol Biol 427, 3877-3889 (2015).
    • (2015) J Mol Biol , vol.427 , pp. 3877-3889
    • Genest, O.1    Hoskins, J.R.2    Kravats, A.N.3    Doyle, S.M.4    Wickner, S.5
  • 64
    • 11144271074 scopus 로고    scopus 로고
    • The translational apparatus of Chlamydomonas reinhardtii chloroplast
    • Beligni, M. V., Yamaguchi, K. & Mayfield, S. P. The translational apparatus of Chlamydomonas reinhardtii chloroplast. Photosynth Res 82, 315-325 (2004).
    • (2004) Photosynth Res , vol.82 , pp. 315-325
    • Beligni, M.V.1    Yamaguchi, K.2    Mayfield, S.P.3
  • 65
    • 3342917108 scopus 로고    scopus 로고
    • Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes
    • Christodoulou, J. et al. Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proc Natl Acad Sci USA 101, 10949-10954 (2004).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10949-10954
    • Christodoulou, J.1
  • 66
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • Hansen, J. C., Lu, X., Ross, E. D. & Woody, R. W. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 281, 1853-1856 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 67
    • 84976482604 scopus 로고    scopus 로고
    • Intrinsic protein disorder in histone lysine methylation
    • Lazar, T. et al. Intrinsic protein disorder in histone lysine methylation. Biol Direct 11, 30-39 (2016).
    • (2016) Biol Direct , vol.11 , pp. 30-39
    • Lazar, T.1
  • 68
    • 84862169121 scopus 로고    scopus 로고
    • More than just tails: Intrinsic disorder in histone proteins
    • Peng, Z., Mizianty, M. J., Xue, B., Kurgan, L. & Uversky, V. N. More than just tails: intrinsic disorder in histone proteins. Mol BioSyst 8, 1886-1901 (2012).
    • (2012) Mol BioSyst , vol.8 , pp. 1886-1901
    • Peng, Z.1    Mizianty, M.J.2    Xue, B.3    Kurgan, L.4    Uversky, V.N.5
  • 69
    • 84931568426 scopus 로고    scopus 로고
    • Phosphorylation regulates the disassembly of cilia
    • Liu, G. & Huang, K. Phosphorylation regulates the disassembly of cilia. Sci China Life Sci 58, 621-623 (2015).
    • (2015) Sci China Life Sci , vol.58 , pp. 621-623
    • Liu, G.1    Huang, K.2
  • 70
    • 79961240127 scopus 로고    scopus 로고
    • Protein phosphorylation is a key event of flagellar disassembly revealed by analysis of flagellar phosphoproteins during flagellar shortening in Chlamydomonas
    • Pan, J. et al. Protein phosphorylation is a key event of flagellar disassembly revealed by analysis of flagellar phosphoproteins during flagellar shortening in Chlamydomonas. J Proteome Res 10, 3830-3839 (2011).
    • (2011) J Proteome Res , vol.10 , pp. 3830-3839
    • Pan, J.1
  • 71
    • 84948783349 scopus 로고    scopus 로고
    • Unravelling the shape and structural assembly of the photosynthetic GAPDH-CP12-PRK complex from Arabidopsis thaliana by small-angle X-ray scattering analysis
    • Del Giudice, A. et al. Unravelling the shape and structural assembly of the photosynthetic GAPDH-CP12-PRK complex from Arabidopsis thaliana by small-angle X-ray scattering analysis. Acta Crystallogr D Biol Crystallogr 71, 2372-2385 (2015).
    • (2015) Acta Crystallogr D Biol Crystallogr , vol.71 , pp. 2372-2385
    • Del Giudice, A.1
  • 72
    • 84862274751 scopus 로고    scopus 로고
    • Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly
    • Fermani, S. et al. Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. J Biol Chem 287, 21372-21383 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 21372-21383
    • Fermani, S.1
  • 73
    • 77953712801 scopus 로고    scopus 로고
    • In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties
    • Marri, L. et al. In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties. J Plant Physiol 167, 939-950 (2010).
    • (2010) J Plant Physiol , vol.167 , pp. 939-950
    • Marri, L.1
  • 74
    • 84988037055 scopus 로고    scopus 로고
    • The intriguing CP12-like tail of adenylate kinase 3 from Chlamydomonas reinhardtii
    • Thieulin-Pardo, G. et al. The intriguing CP12-like tail of adenylate kinase 3 from Chlamydomonas reinhardtii. FEBS J 283, 3389-3407 (2016).
    • (2016) FEBS J , vol.283 , pp. 3389-3407
    • Thieulin-Pardo, G.1
  • 75
    • 0030964297 scopus 로고    scopus 로고
    • Memory and imprinting effects in multienzyme complexes
    • Avilan, L., Gontero, B., Lebreton, S. & Ricard, J. Memory and imprinting effects in multienzyme complexes. Eur J Biochem 246, 78-84 (1997).
    • (1997) Eur J Biochem , vol.246 , pp. 78-84
    • Avilan, L.1    Gontero, B.2    Lebreton, S.3    Ricard, J.4
  • 76
    • 70349434722 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a GDSL-motif carboxylester hydrolase from Carica papaya latex
    • Abdelkafi, S. et al. Identification and biochemical characterization of a GDSL-motif carboxylester hydrolase from Carica papaya latex. Biochim Biophys Acta Mol Cell Biol Lipids 1791, 1048-1056 (2009).
    • (2009) Biochim Biophys Acta Mol Cell Biol Lipids , vol.1791 , pp. 1048-1056
    • Abdelkafi, S.1
  • 77
    • 14544299774 scopus 로고    scopus 로고
    • Optimizing long intrinsic disorder predictors with protein evolutionary information
    • Peng, K. et al. Optimizing long intrinsic disorder predictors with protein evolutionary information. J Bioinform Comput Biol 03, 35-60 (2005).
    • (2005) J Bioinform Comput Biol , vol.3 , pp. 35-60
    • Peng, K.1
  • 78
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex©: A simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky, J. et al. FoldIndex©: A simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21, 3435-3438 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1
  • 79
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • Radivojac, P. et al. Intrinsic disorder and functional proteomics. Biophys J 92, 1439-1456 (2007).
    • (2007) Biophys J , vol.92 , pp. 1439-1456
    • Radivojac, P.1
  • 80
    • 84869020793 scopus 로고    scopus 로고
    • PredAlgo: A new subcellular localization prediction tool dedicated to green algae
    • Tardif, M. et al. PredAlgo: A new subcellular localization prediction tool dedicated to green algae. Mol Biol Evol 29, 3625-3639 (2012).
    • (2012) Mol Biol Evol , vol.29 , pp. 3625-3639
    • Tardif, M.1
  • 81
    • 35348896591 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals the evolution of key animal and plant functions
    • Merchant, S. S. et al. The Chlamydomonas genome reveals the evolution of key animal and plant functions. Sci 318, 245-250 (2007).
    • (2007) Sci , vol.318 , pp. 245-250
    • Merchant, S.S.1
  • 82
    • 34447539760 scopus 로고    scopus 로고
    • Composition Profiler: A tool for discovery and visualization of amino acid composition differences
    • Vacic, V., Uversky, V. N., Dunker, A. K. & Lonardi, S. Composition Profiler: A tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics 8, 1471-2105 (2007).
    • (2007) BMC Bioinformatics , vol.8 , pp. 1471-2105
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 83
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman, H. M. et al. The Protein Data Bank. Nucleic Acids Res 28, 235-242 (2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.