Aksel, 2009, Chapter 4 analysis of repeat-protein folding using nearest-neighbor statistical mechanical models, Methods Enzymol., 455, 95, 10.1016/S0076-6879(08)04204-3
Aksel, 2014, Direct observation of parallel folding pathways revealed using a symmetric repeat protein system, Biophys. J., 107, 220, 10.1016/j.bpj.2014.04.058
Babu, 2016, The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease, Biochem. Soc. Trans., 44, 1185, 10.1042/BST20160172
Binz, 2003, Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins, J. Mol. Biol., 332, 489, 10.1016/S0022-2836(03)00896-9
Boersma, 2011, DARPins and other repeat protein scaffolds: advances in engineering and applications, Curr. Opin. Biotechnol., 22, 849, 10.1016/j.copbio.2011.06.004
Chan, 1989, Intrachain loops in polymers: effects of excluded volume, J. Chem. Phys., 90, 492, 10.1063/1.456500
Christendat, 2000, Structural proteomics of an archaeon, Nat. Struct. Biol., 7, 903, 10.1038/82823
Cortajarena, 2008, Designed TPR modules as novel anticancer agents, ACS Chem. Biol., 3, 161, 10.1021/cb700260z
Das, 2013, Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues, Proc. Natl. Acad. Sci. U.S.A., 110, 13392, 10.1073/pnas.1304749110
Das, 2015, Relating sequence encoded information to form and function of intrinsically disordered proteins, Curr. Opin. Struct. Biol., 32, 102, 10.1016/j.sbi.2015.03.008
Davis, 1999, New fusion protein systems designed to give soluble expression in Escherichia coli, Biotechnol. Bioeng., 65, 382, 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I
Dyson, 2016, Making sense of intrinsically disordered proteins, Biophys. J., 110, 1013, 10.1016/j.bpj.2016.01.030
Dyson, 2005, Intrinsically unstructured proteins and their functions, Nat. Rev. Mol. Cell Biol., 6, 197, 10.1038/nrm1589
Gasteiger, 2005, Protein identification and analysis tools on the ExPASy server, 571
Gibbs, 2017, Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain, Nat. Commun., 8, 1, 10.1038/ncomms15233
Golovanov, 2004, A simple method for improving protein solubility and long-term stability, J. Am. Chem. Soc., 126, 8933, 10.1021/ja049297h
Gronenborn, 2009, Protein acrobatics in pairs - dimerization via domain swapping, Curr. Opin. Struct. Biol., 19, 39, 10.1016/j.sbi.2008.12.002
Guettler, 2011, Structural basis and sequence rules for substrate recognition by Tankyrase explain the basis for cherubism disease, Cell, 147, 1340, 10.1016/j.cell.2011.10.046
Ha, 2015, Engineered domain swapping as an on/off switch for protein function, Chem. Biol., 22, 1384, 10.1016/j.chembiol.2015.09.007
Haikarainen, 2014, Tankyrases: structure, function and therapeutic implications in cancer, Curr. Pharmaceut. Des., 20, 6472, 10.2174/1381612820666140630101525
Harmon, 2017, Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins, Elife, 6, 1, 10.7554/eLife.30294
Holehouse, 2017, CIDER: resources to analyze sequence-ensemble relationships of intrinsically disordered proteins, Biophys. J., 112, 16, 10.1016/j.bpj.2016.11.3200
Jacobson, 1950, Intramolecular reaction in polycondensations. I. The theory of linear systems, J. Chem. Phys., 18, 1600, 10.1063/1.1747547
Kajander, 2005, A new folding paradigm for repeat proteins, J. Am. Chem. Soc., 127, 10188, 10.1021/ja0524494
Kajander, 2006, Consensus design as a tool for engineering repeat proteins, Methods Mol. Biol., 340, 151
Kajander, 2007, Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins, Acta Crystallogr. Sect. D Biol. Crystallogr., 63, 800, 10.1107/S0907444907024353
Kobe, 2000, When protein folding is simplified to protein coiling: the continuum of solenoid protein structures, Trends Biochem. Sci., 25, 509, 10.1016/S0968-0004(00)01667-4
Kundu, 2004, Molecular mechanism of domain swapping in proteins: an analysis of slower motions, Biophys. J., 86, 3846, 10.1529/biophysj.103.034736
Ladurner, 1997, Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates, J. Mol. Biol., 273, 330, 10.1006/jmbi.1997.1304
Lafita, 2019, Tandem domain swapping: determinants of multidomain protein misfolding, Curr. Opin. Struct. Biol., 58, 97, 10.1016/j.sbi.2019.05.012
Löw, 2008, Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein, Proc. Natl. Acad. Sci. U.S.A., 105, 3779, 10.1073/pnas.0710657105
Madden, 2019, Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold, Protein Sci., 28, 738, 10.1002/pro.3586
Main, 2003, The folding and design of repeat proteins: reaching a consensus, Curr. Opin. Struct. Biol., 13, 482, 10.1016/S0959-440X(03)00105-2
Main, 2003, Design of stable α-helical arrays from an idealized TPR motif, Structure, 11, 497, 10.1016/S0969-2126(03)00076-5
Mao, 2010, Net charge per residue modulates conformational ensembles of intrinsically disordered proteins, Proc. Natl. Acad. Sci. U.S.A., 107, 8183, 10.1073/pnas.0911107107
Marsh, 2010, Sequence determinants of compaction in intrinsically disordered proteins, Biophys. J., 98, 2383, 10.1016/j.bpj.2010.02.006
Martin, 2016, Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation, J. Am. Chem. Soc., 138, 15323, 10.1021/jacs.6b10272
Millership, 2016, Ising model reprogramming of a repeat protein's equilibrium unfolding pathway, J. Mol. Biol., 428, 1804, 10.1016/j.jmb.2016.02.022
Müller-Späth, 2010, Charge interactions can dominate the dimensions of intrinsically disordered proteins, Proc. Natl. Acad. Sci. U.S.A., 107, 14609, 10.1073/pnas.1001743107
Nagi, 1997, An inverse correlation between loop length and stability in a four-helix-bundle protein, Folding Des., 2, 67, 10.1016/S1359-0278(97)00007-2
Nandwani, 2019, A five-residue motif for the design of domain swapping in proteins, Nat. Commun., 10, 10.1038/s41467-019-08295-x
Pellegrini, 1999, A fast algorithm for genome-wide analysis of proteins with repeated sequences, Proteins Struct. Funct. Genet., 35, 440, 10.1002/(SICI)1097-0134(19990601)35:4<440::AID-PROT7>3.0.CO;2-Y
Perez-Riba, 2017, A method for rapid high-throughput biophysical analysis of proteins, Sci. Rep., 7, 9071, 10.1038/s41598-017-08664-w
Perez-Riba, 2018, Context-dependent energetics of loop extensions in a family of tandem-repeat proteins, Biophys. J., 114, 2552, 10.1016/j.bpj.2018.03.038
Perez-Riba, 2019, Decoupling a tandem-repeat protein: impact of multiple loop insertions on a modular scaffold, Sci. Rep., 9, 1, 10.1038/s41598-019-49905-4
Phillips, 2012, Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors, Protein Sci., 21, 327, 10.1002/pro.2018
Phillips, 2012, Fibrous nanostructures from the self-assembly of designed repeat protein modules, Angew. Chem. Int. Ed., 51, 13132, 10.1002/anie.201203795
Portz, 2017, Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain, Nat. Commun., 8, 1, 10.1038/ncomms15231
Riback, 2017, Stress-triggered phase separation is an adaptive, evolutionarily tuned response, Cell, 168, 1028, 10.1016/j.cell.2017.02.027
Rousseau, 2013, Implications of 3D domain swapping for protein folding, misfolding and function, Adv. Exp. Med. Biol., 747, 137, 10.1007/978-1-4614-3229-6_9
Schlunegger, 1997, Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly, Adv. Protein Chem., 50, 61, 10.1016/S0065-3233(08)60319-8
Sherry, 2017, Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor, Proc. Natl. Acad. Sci. U.S.A., 114, E9243, 10.1073/pnas.1706083114
Sickmeier, 2007, DisProt: the database of disordered proteins, Nucleic Acids Res., 35, D786, 10.1093/nar/gkl893
Śledź, 2011, From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1, Angew. Chem., Int. Ed. Engl., 50, 4003, 10.1002/anie.201008019
Smialowski, 2007, Protein solubility: sequence based prediction and experimental verification, Bioinformatics, 23, 2536, 10.1093/bioinformatics/btl623
Tang, 1999, Stability and folding of the tumour suppressor protein p16, J. Mol. Biol., 285, 1869, 10.1006/jmbi.1998.2420
Tompa, 2014, A Million peptide motifs for the molecular biologist, Mol. Cell., 55, 161, 10.1016/j.molcel.2014.05.032
Van Roey, 2014, Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation, Chem. Rev., 114, 6733, 10.1021/cr400585q
Viguera, 1997, Loop length, intramolecular diffusion and protein folding, Nat. Struct. Biol., 4, 939, 10.1038/nsb1197-939
Waterhouse, 2018, SWISS-MODEL: Homology modelling of protein structures and complexes, Nucleic Acids Res., 46, W296, 10.1093/nar/gky427
Wilkinson, 1991, Predicting the solubility of recombinant proteins in Escherichia coli, Nat. Biotechnol., 9, 443, 10.1038/nbt0591-443