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)

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  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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ValeLrie Belle, Sabrina Rouger, Stephanie Costanzo, Elodie Liquie`re, Janez Strancar, Bruno Guigliarelli, AndreL Fournel,and Sonia Longhi @

Mapping 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 VEL RONIQUE RECEVEUR-BREL CHOT, MICHAEL OGLESBEE, XINSHENG ZHANG, MATTHEW BUCCELLATO, HERVEL DARBON, BRUNO CANARD, STEL 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, ValeL rie Belle, Sabrina Rouger, SteLphanie Costanzo, Sandra Kure,AndreL Fournel, Sonia Longhi, Bruno Guigliarelli, and Janez Strancar

Conformational 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, VeLronique Receveur-BreLchot, David Karlin, Kenth Johansson, HerveL Darbon, David Bhella, Robert Yeo, SteLphanie 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 studies

Protein 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 Asturias

Mediator 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)