CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins
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Rohit V Pappu | Alex S Holehouse | R. Pappu | A. Holehouse | Rahul K Das | James N Ahad | Mary O G Richardson | Rahul K. Das | Mary O. G. Richardson | J. N. Ahad | M. Richardson
[1] Martin Blackledge,et al. NMR characterization of long-range order in intrinsically disordered proteins. , 2010, Journal of the American Chemical Society.
[2] R. Pappu,et al. Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling , 2016, Proceedings of the National Academy of Sciences.
[3] A. Dobrynin,et al. Flory Theory of a Polyampholyte Chain , 1995 .
[4] Zsuzsanna Dosztányi,et al. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content , 2005, Bioinform..
[5] R. Pappu,et al. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues , 2013, Proceedings of the National Academy of Sciences.
[6] Abraham Lempel,et al. On the Complexity of Finite Sequences , 1976, IEEE Trans. Inf. Theory.
[7] Robert B Best,et al. Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations. , 2015, The journal of physical chemistry. B.
[8] Christopher J. Oldfield,et al. Classification of Intrinsically Disordered Regions and Proteins , 2014, Chemical reviews.
[9] David R. Liu,et al. Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein. , 2016, Molecular cell.
[10] L. Malinovska,et al. Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation , 2015, Proceedings of the National Academy of Sciences.
[11] V. Uversky. Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.
[12] R. Pappu,et al. Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. , 2016, Journal of the American Chemical Society.
[13] Gad M. Landau,et al. Sequence complexity profiles of prokaryotic genomic sequences: A fast algorithm for calculating linguistic complexity , 2002, Bioinform..
[14] Erinna F. Lee,et al. Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. , 2008, Journal of molecular biology.
[15] María Martín,et al. UniProt: A hub for protein information , 2015 .
[16] The Uniprot Consortium,et al. UniProt: a hub for protein information , 2014, Nucleic Acids Res..
[17] R. Levy,et al. Simplified amino acid alphabets for protein fold recognition and implications for folding. , 2000, Protein engineering.
[18] J. Marsh,et al. Sequence determinants of compaction in intrinsically disordered proteins. , 2010, Biophysical journal.
[19] S. Schnell,et al. A collection of intrinsic disorder characterizations from eukaryotic proteomes , 2016, Scientific Data.
[20] P. Romero,et al. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions. , 2006, Journal of Proteome Research.
[21] Christopher J. Oldfield,et al. Intrinsically disordered proteins in human diseases: introducing the D2 concept. , 2008, Annual review of biophysics.
[22] R. Pappu,et al. Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck , 2015, Proceedings of the National Academy of Sciences.
[23] Silvio C. E. Tosatto,et al. Large‐scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe , 2016, Protein science : a publication of the Protein Society.
[24] L. Reymond,et al. Charge interactions can dominate the dimensions of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.
[25] C. Dieterich,et al. Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells. , 2014, Nature chemical biology.
[26] John C. Wootton,et al. Statistics of Local Complexity in Amino Acid Sequences and Sequence Databases , 1993, Comput. Chem..
[27] Rohit V Pappu,et al. Relating sequence encoded information to form and function of intrinsically disordered proteins. , 2015, Current opinion in structural biology.
[28] Cara T. Pager,et al. Host‐guest scale of left‐handed polyproline II helix formation , 2003, Proteins.
[29] Zhengshuang Shi,et al. Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[30] Caitlin L. Chicoine,et al. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.
[31] Maria E. Tomasso,et al. Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities , 2016, PLoS Comput. Biol..
[32] R. Crowther,et al. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans , 1996, Nature.
[33] Zoran Obradovic,et al. DisProt: the Database of Disordered Proteins , 2006, Nucleic Acids Res..
[34] Ronald D. Vale,et al. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin , 1996, Nature.
[35] Jane Clarke,et al. Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not ‘Diffusion-Limited’ , 2013, Journal of the American Chemical Society.
[36] P. Tompa,et al. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. , 2012, Biochemical Society transactions.
[37] R. Pappu,et al. A quantitative measure for protein conformational heterogeneity. , 2013, The Journal of chemical physics.
[38] P. Tompa,et al. Structural Disorder in Eukaryotes , 2012, PloS one.
[39] Jane Clarke,et al. GADIS: Algorithm for designing sequences to achieve target secondary structure profiles of intrinsically disordered proteins. , 2016, Protein engineering, design & selection : PEDS.
[40] Silvio C. E. Tosatto,et al. MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins , 2014, Nucleic Acids Res..
[41] Diana M. Mitrea,et al. Phase separation in biology; functional organization of a higher order , 2016, Cell Communication and Signaling.
[42] V. Hilser,et al. Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites , 2013, Protein science : a publication of the Protein Society.
[43] S. Alberti. Phase separation in biology , 2017, Current Biology.
[44] H. Dyson,et al. Intrinsically disordered proteins in cellular signalling and regulation , 2014, Nature Reviews Molecular Cell Biology.
[45] P. Tompa,et al. Reduction in Structural Disorder and Functional Complexity in the Thermal Adaptation of Prokaryotes , 2010, PloS one.
[46] Marco Y. Hein,et al. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation , 2015, Cell.
[47] Lucy J. Colwell,et al. A core subunit of Polycomb repressive complex 1 is broadly conserved in function but not primary sequence , 2012, Proceedings of the National Academy of Sciences.
[48] Timothy D. Craggs,et al. Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles , 2015, Molecular cell.