Natively unfolded proteins.

[1]  H. Dyson,et al.  Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. , 1999, Journal of molecular biology.

[2]  C. Brown,et al.  Intrinsic protein disorder in complete genomes. , 2000, Genome informatics. Workshop on Genome Informatics.

[3]  V. Uversky,et al.  Why are “natively unfolded” proteins unstructured under physiologic conditions? , 2000, Proteins.

[4]  D. Eliezer,et al.  Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein* , 2001, The Journal of Biological Chemistry.

[5]  E L Sonnhammer,et al.  Integrated graphical analysis of protein sequence features predicted from sequence composition , 2001, Proteins.

[6]  P. Romero,et al.  Sequence complexity of disordered protein , 2001, Proteins.

[7]  K. Namba.  Roles of partly unfolded conformations in macromolecular self‐assembly , 2001, Genes to cells : devoted to molecular & cellular mechanisms.

[8]  K. Nakayama,et al.  Regulation of the cell cycle at the G1-S transition by proteolysis of cyclin E and p27Kip1. , 2001, Biochemical and biophysical research communications.

[9]  T. Südhof,et al.  The C2B domain of synaptotagmin I is a Ca2+-binding module. , 2001, Biochemistry.

[10]  J. Hoh,et al.  Predicting properties of intrinsically unstructured proteins. , 2001, Progress in biophysics and molecular biology.

[11]  H. Dyson,et al.  Coupling of folding and binding for unstructured proteins. , 2002, Current opinion in structural biology.

[12]  V. Uversky.  Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.

[13]  David G. Karlin,et al.  The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. , 2002, Virology.

[14]  K. Namba,et al.  Interactions between bacterial flagellar axial proteins in their monomeric state in solution. , 2002, Journal of molecular biology.

[15]  P. Tompa.  Intrinsically unstructured proteins. , 2002, Trends in biochemical sciences.

[16]  Vladimir N Uversky,et al.  What does it mean to be natively unfolded? , 2002, European journal of biochemistry.

[17]  Min Lu,et al.  An Alanine-Zipper Structure Determined by Long Range Intermolecular Interactions* , 2002, The Journal of Biological Chemistry.

[18]  L. Iakoucheva,et al.  Intrinsic disorder in cell-signaling and cancer-associated proteins. , 2002, Journal of molecular biology.

[19]  L. Serpell,et al.  Proteasomal degradation of tau protein , 2002, Journal of neurochemistry.

[20]  A. Nadra,et al.  High-risk (HPV16) human papillomavirus E7 oncoprotein is highly stable and extended, with conformational transitions that could explain its multiple cellular binding partners. , 2002, Biochemistry.

[21]  P. Tompa.  Intrinsically unstructured proteins evolve by repeat expansion , 2003, BioEssays : news and reviews in molecular, cellular and developmental biology.

[22]  Z. Gugolya,et al.  Interaction of the disordered terminal regions of flagellin upon flagellar filament formation , 2003, FEBS letters.

[23]  A Keith Dunker,et al.  Order, disorder, and flexibility: prediction from protein sequence. , 2003, Structure.

[24]  John Moult,et al.  Evaluation of disorder predictions in CASP5 , 2003, Proteins.

[25]  Zoran Obradovic,et al.  Prediction of Boundaries Between Intrinsically Ordered and Disordered Protein Regions , 2002, Pacific Symposium on Biocomputing.

[26]  E. Pérez-Payá,et al.  The Structural Plasticity of the C Terminus of p21Cip1 is a Determinant for Target Protein Recognition , 2003, Chembiochem : a European journal of chemical biology.

[27]  David T. Jones,et al.  Prediction of disordered regions in proteins from position specific score matrices , 2003, Proteins.

[28]  Ming-Ming Zhou,et al.  Coupling of folding and binding in the PTB domain of the signaling protein Shc. , 2003, Structure.

[29]  C. Cambillau,et al.  Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein* , 2003, Journal of Biological Chemistry.

[30]  K. Lechtreck,et al.  Centrin deficiency in Chlamydomonas causes defects in basal body replication, segregation and maturation , 2003, Journal of Cell Science.

[31]  Johannes Buchner,et al.  The N-terminal domain of p53 is natively unfolded. , 2003, Journal of molecular biology.

[32]  Sonia Longhi,et al.  The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein* , 2003, The Journal of Biological Chemistry.

[33]  R. Nussinov,et al.  Extended disordered proteins: targeting function with less scaffold. , 2003, Trends in biochemical sciences.

[34]  S. Vucetic,et al.  Flavors of protein disorder , 2003, Proteins.

[35]  T. Gibson,et al.  Protein disorder prediction: implications for structural proteomics. , 2003, Structure.

[36]  W. Jahnke,et al.  Thermodynamics of the Op18/Stathmin-Tubulin Interaction* , 2003, Journal of Biological Chemistry.

[37]  P. Tompa,et al.  Binding‐induced folding transitions in calpastatin subdomains A and C , 2003, Protein science : a publication of the Protein Society.

[38]  A. Haymet,et al.  'Antifreeze' glycoproteins from polar fish. , 2003, European journal of biochemistry.

[39]  Zoran Obradovic,et al.  Predicting intrinsic disorder from amino acid sequence , 2003, Proteins.

[40]  Sonia Longhi,et al.  Structural disorder and modular organization in Paramyxovirinae N and P. , 2003, The Journal of general virology.

[41]  Gregor Anderluh,et al.  A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template* , 2004, Journal of Biological Chemistry.

[42]  Bernard F. Buxton,et al.  The DISOPRED server for the prediction of protein disorder , 2004, Bioinform..

[43]  P. Radivojac,et al.  Protein flexibility and intrinsic disorder , 2004, Protein science : a publication of the Protein Society.

[44]  István Simon,et al.  Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. , 2004, Journal of molecular biology.

[45]  L. Serrano,et al.  A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. , 2004, Journal of molecular biology.

[46]  J. Wrana,et al.  Disorder in a Target for the Smad2 Mad Homology 2 Domain and Its Implications for Binding and Specificity* , 2004, Journal of Biological Chemistry.

[47]  Barbara J. B. Johnson,et al.  BBK32, a Fibronectin Binding MSCRAMM from Borrelia burgdorferi, Contains a Disordered Region That Undergoes a Conformational Change on Ligand Binding* , 2004, Journal of Biological Chemistry.

[48]  L. Young,et al.  TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. , 2004, Cancer research.

[49]  M. Garcia-Alai,et al.  The HPV16 E7 viral oncoprotein self-assembles into defined spherical oligomers. , 2004, Biochemistry.

[50]  Sonia Longhi,et al.  The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. , 2004, Virus research.

[51]  The arrestin‐bound conformation and dynamics of the phosphorylated carboxy‐terminal region of rhodopsin , 2004, FEBS letters.

[52]  Peter E Wright,et al.  Interaction of the TAZ1 Domain of the CREB-Binding Protein with the Activation Domain of CITED2 , 2004, Journal of Biological Chemistry.

[53]  J. S. Sodhi,et al.  Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. , 2004, Journal of molecular biology.

[54]  A Keith Dunker,et al.  Combining prediction, computation and experiment for the characterization of protein disorder. , 2004, Current opinion in structural biology.

[55]  L. Iakoucheva,et al.  The importance of intrinsic disorder for protein phosphorylation. , 2004, Nucleic acids research.

[56]  P. Hargrave,et al.  Conformational Changes in the Phosphorylated C-terminal Domain of Rhodopsin during Rhodopsin Arrestin Interactions* , 2004, Journal of Biological Chemistry.

[57]  H. Dyson,et al.  The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. , 2004, Biochemistry.

[58]  Leif Smith,et al.  IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. , 2004, Biochemistry.

[59]  Andrés Colubri,et al.  Prediction of Protein Structure by Simulating Coarse-grained Folding Pathways: A Preliminary Report , 2004, Journal of biomolecular structure & dynamics.

[60]  K. Namba,et al.  In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella. , 2004, Journal of molecular biology.

[61]  Peter Tompa,et al.  The role of structural disorder in the function of RNA and protein chaperones , 2004, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[62]  Zoran Obradovic,et al.  DisProt: a database of protein disorder , 2005, Bioinform..