References on Intrinsically Disordered Proteins
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NMR analysis of IDPs
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H. Jane Dyson and Peter E. Wright Unfolded Proteins and Protein Folding Studied by NMR Chem. Rev. 104, 3607-3622 (2004) (PDF File) |
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H. Jane Dyson and Peter E. Wright INSIGHTS INTO PROTEIN FOLDING FROM NMR Annu. Rev. Phys. Chem. 47:369-395 (1996) (PDF File) |
IDPs in general
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Kenji Sugase, H. Jane Dyson & Peter E. Wright Mechanism of coupled folding and binding of an intrinsically disordered protein Nature 447: 1021-1025 (2007). (PDF File) |
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Peter E Wright and H Jane Dyson Linking folding and binding Curr. Opin. Struct. Biol. 19: 31-38 (2009) (PDF File) |
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Vladimir N. Uversky, A. Keith Dunker Review: Understanding protein non-folding Biochimica et Biophysica Acta 1804: 1231- 1264 (2010) (PDF File) |
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Peter Tompa Minireview: The interplay between structure and function in intrinsically unstructured proteins FEBS Letters 579: 3346-3354 (2005) (PDF File) |
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Vladimir N. Uversky, Anthony L. Fink Review: Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochimica et Biophysica Acta 1698: 131-153 (2004) (PDF File) |
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Gerard Kian-Meng Goh, A Keith Dunker and Vladimir N Uversky Protein intrinsic disorder and influenza virulence: the 1918 H1N1 and H5N1 viruses Virology Journal 2009, 6:69 (PDF File) |
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Unstructural biologycomingofage Peter Tompa CurrentOpinioninStructuralBiology 21:1–7(2011). (PDF File) |
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Dynamic protein–DNA recognition: beyond what can be seen Monika Fuxreiter, Istvan Simon and Sarah Bondos Trends in Biochemical Sciences xx (2011) 1–9. (PDF File) |
CREB-binding protein
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H. Jane Dyson and Peter E.Wright Inyrinsically unstructured proteins and their functions Nature Review Molecular Cell Biology 6: 197-208 (2005). (PDF File) |
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MeCP2
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Kristopher C. Hite, Valerie H. Adams, and Jefferey C. Hansen Recent advances in MeCP2 structure and function. Biochem. Cell Biol. 87: 219-227 (2009) (PDF File) |
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Valerie H. Adams, Steven J. McBryant, Paul A. Wade, Christopher L. Woodcock, and Jeffrey C. Hansen Intrinsic Disorder and Autonomous Domain Function in the Multifunctional Nuclear Protein, MeCP2 J. Biol. Chem. 282: 15057-15064 (2007). (PDF File) |
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Critical Review: Binding of the Rett Syndrome Protein, MeCP2, to Methylated and Unmethylated DNA and Chromatin Jeffrey C. Hansen, Rajarshi P. Ghosh and Christopher L. Woodcock IUBMB Life, 62(10): 732-738 (2010) (PDF File) |
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L1 retrotransposition in neurons is modulated by MeCP2 Alysson R. Muotri, Maria C. N. Marchetto, Nicole G. Coufal, Ruth Oefner, Gene Yeo, Kinichi Nakashima & Fred H. Gage Nature 468: 443-446 (2010). (PDF File) |
PQBP-1
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Masaki Takahashi, Mineyuki Mizuguchi, Hiroyuki Shinoda, Tomoyasu Aizawa, Makoto Demura, Hitoshi Okazawa, Keiichi Kawano Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain BBA - Proteins & Proteomics 1804(7) 1500-1507 (2010). (PDF File) |
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Masaki Takahashi, Mineyuki Mizuguchi, Hiroyuki Shinoda, Tomoyasu Aizawa, Makoto Demura, Hitoshi Okazawa, Keiichi Kawano Polyglutamine tract binding protein-1 is an intrinsically unstructured protein Biochimica et Biophysica Acta 1794 936-943 (2009). (PDF File) |
MeV (Virus) proteins
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Vale´rie Belle, Sabrina Rouger, Steｴphanie Costanzo, Elodie Liquie`re, Janez Strancar, Bruno Guigliarelli, Andre´ Fournel,and Sonia LonghiMapping a-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy Proteins (2008) (PDF File) |
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JEAN-MARIE BOURHIS,1 VE´ RONIQUE RECEVEUR-BRE´ CHOT, MICHAEL OGLESBEE, XINSHENG ZHANG, MATTHEW BUCCELLATO, HERVE´ DARBON, BRUNO CANARD, STE´ PHANIE FINET, and SONIA LONGHI The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded Protein Science (2005), 14:1975?1992 (PDF File) |
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Aleh Kavalenka, Iztok Urbancic, Vale´ rie Belle, Sabrina Rouger, Ste´phanie Costanzo, Sandra Kure,Andre´ Fournel, Sonia Longhi, Bruno Guigliarelli, and Janez StrancarConformational Analysis of the Partially Disordered Measles Virus NTAIL-XD Complex by SDSL EPR Spectroscopy Biophys. J. 98: 1055-1064 (2010) (PDF File) |
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Sonia Longhi, Ve´ronique Receveur-Bre´chot, David Karlin, Kenth Johansson, Herve´ Darbon, David Bhella, Robert Yeo, Ste´phanie Finet, and Bruno Canard The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein J. Biol. Chem. 278: 18638-18648 (2003) (PDF File). |
PTMA
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Vladimir N. Uversky, Joel R. Gillespie, Ian S. Millett, Anna V. Khodyakova, Anatoly M. Vasiliev, Tatyana V. Chernovskaya, Raisa N. Vasilenko, Galina D. Kozlovskaya, Dmitry A. Dolgikh, Anthony L. Fink, Sebastian Doniach, and Vyacheslav M. Abramov Natively Unfolded Human Prothymosin R Adopts Partially Folded Collapsed Conformation at Acidic pH Biochemistry 1999, 38, 15009-15016 (PDF File) |
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Shiluan Yi, Brian L. Boys, Anne Brickenden, Lars Konermann, and Wing-Yiu Choy Effects of Zinc Binding on the Structure and Dynamics of the Intrinsically Disordered Protein Prothymosin R: Evidence for Metalation as an Entropic Switch Biochemistry 46: 13120-13130 (2007) (PDF File) |
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Shiluan Yi, Anne Brickenden, Wing-Yiu Choy A new protocol for high-yield purification of recombinant human prothymosin a expressed in Escherichia coli for NMR studiesProtein Expression and Purification 57: 1-8 (2008) (PDF File) |
Mediator
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Gang Cai , Tsuyoshi Imasaki, Kentaro Yamada, Francesco Cardelli, Yuichiro Takagi & Francisco J AsturiasMediator Head module structure and functional interactions Nat. Struct. Biol. (2010) (PDF File) |
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FACT
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Yasuo Tsunaka, Junko Toga, Hiroto Yamaguchi, Shin-ichi Tate, Susumu Hirose, and Kosuke Morikawa Phosphorylated Intrinsically Disordered Region of FACT Masks Its Nucleosomal DNA Binding Elements J. Biol. Chem. 284(36): 24610-24621 (2009). (PDF File) |
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A. Miyagi, Y. Tsunaka, T. Uchihashi, K. Mayanagi, S. Hirose, K. Morikawa, and T. Ando Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy. Chem. Phys. Chem. 9(13):1859-1866 (2008). (PDF file) |
