| Year |
Citation |
Score |
| 2023 |
Gidden Z, Oi C, Johnston EJ, Konieczna Z, Bhaskar H, Mendive-Tapia L, de Moliner F, Rosser SJ, Mochrie SGJ, Vendrell M, Horrocks MH, Regan L. Imaging Proteins Sensitive to Direct Fusions Using Transient Peptide-Peptide Interactions. Nano Letters. PMID 37916770 DOI: 10.1021/acs.nanolett.3c03780 |
0.351 |
|
| 2023 |
Boni R, Regan L. Modulating the Viscoelastic Properties of Covalently Crosslinked Protein Hydrogels. Gels (Basel, Switzerland). 9. PMID 37367151 DOI: 10.3390/gels9060481 |
0.306 |
|
| 2023 |
Boni R, Blackburn EA, Kleinjan DJ, Jonaitis M, Hewitt-Harris F, Murdoch M, Rosser S, Hay DC, Regan L. Chemically cross-linked hydrogels from repetitive protein arrays. Journal of Structural Biology. 107981. PMID 37245604 DOI: 10.1016/j.jsb.2023.107981 |
0.335 |
|
| 2022 |
Grigas AT, Liu Z, Regan L, O'Hern CS. Core packing of well-defined X-ray and NMR structures is the same. Protein Science : a Publication of the Protein Society. 31: e4373. PMID 35900019 DOI: 10.1002/pro.4373 |
0.584 |
|
| 2020 |
Oi C, Mochrie SGJ, Horrocks MH, Regan L. PAINT using proteins: A new brush for super-resolution artists. Protein Science : a Publication of the Protein Society. PMID 32949055 DOI: 10.1002/Pro.3953 |
0.452 |
|
| 2020 |
Grigas AT, Mei Z, Treado JD, Levine ZA, Regan L, O'Hern CS. Using physical features of protein core packing to distinguish real proteins from decoys. Protein Science : a Publication of the Protein Society. PMID 32710566 DOI: 10.1002/Pro.3914 |
0.699 |
|
| 2020 |
Jasaitis L, Silver CD, Rawlings AE, Peters DT, Whelan F, Regan L, Pasquina-Lemonche L, Potts JR, Johnson SD, Staniland SS. Rational design and self-assembly of coiled-coil linked SasG protein fibrils. Acs Synthetic Biology. PMID 32551507 DOI: 10.1021/Acssynbio.0C00156 |
0.414 |
|
| 2020 |
Mei Z, Treado JD, Grigas AT, Levine ZA, Regan L, O'Hern CS. Analyses of protein cores reveal fundamental differences between solution and crystal structures. Proteins. PMID 32105366 DOI: 10.1002/Prot.25884 |
0.655 |
|
| 2020 |
Mei Z, Treado J, Regan LJ, Levine Z, O'Hern C. Understanding the Native Fluctuation of Protein Cores Biophysical Journal. 118: 23a. DOI: 10.1016/J.Bpj.2019.11.307 |
0.672 |
|
| 2019 |
Treado JD, Mei Z, Regan L, O'Hern CS. Void distributions reveal structural link between jammed packings and protein cores. Physical Review. E. 99: 022416. PMID 30934238 DOI: 10.1103/Physreve.99.022416 |
0.657 |
|
| 2018 |
Abascal NC, Regan L. The past, present and future of protein-based materials. Open Biology. 8. PMID 30381364 DOI: 10.1098/Rsob.180113 |
0.388 |
|
| 2018 |
Oi C, Treado JD, Levine ZA, Lim CS, Knecht KM, Xiong Y, O'Hern CS, Regan L. "A threonine zipper that mediates protein-protein interactions: Structure and prediction". Protein Science : a Publication of the Protein Society. PMID 30198622 DOI: 10.1002/Pro.3505 |
0.676 |
|
| 2018 |
Gaines JC, Acebes S, Virrueta A, Butler M, Regan L, O'Hern CS. Comparing side chain packing in soluble proteins, protein-protein interfaces, and transmembrane proteins. Proteins. PMID 29427530 DOI: 10.1002/Prot.25479 |
0.704 |
|
| 2017 |
Hinrichsen M, Lenz M, Edwards JM, Miller OK, Mochrie SGJ, Swain PS, Schwarz-Linek U, Regan L. A new method for post-translationally labeling proteins in live cells for fluorescence imaging and tracking. Protein Engineering, Design & Selection : Peds. PMID 29228311 DOI: 10.1093/Protein/Gzx059 |
0.44 |
|
| 2017 |
Gaines J, Clark A, Regan L, O'Hern C. Packing in protein cores. Journal of Physics. Condensed Matter : An Institute of Physics Journal. PMID 28557791 DOI: 10.1088/1361-648X/Aa75C2 |
0.71 |
|
| 2017 |
Gaines JC, Virrueta A, Buch DA, Fleishman SJ, O'Hern CS, Regan L. Collective repacking reveals that the structures of protein cores are uniquely specified by steric repulsive interactions. Protein Engineering, Design & Selection : Peds. 1-8. PMID 28201818 DOI: 10.1093/Protein/Gzx011 |
0.487 |
|
| 2016 |
Schloss AC, Liu W, Williams DM, Kaufman G, Hendrickson HP, Rudshteyn B, Fu L, Wang H, Batista VS, Osuji C, Yan ECY, Regan L. Fabrication of Modularly Functionalizable Microcapsules Using Protein-Based Technologies. Acs Biomaterials Science & Engineering. 2: 1856-1861. PMID 29805990 DOI: 10.1021/Acsbiomaterials.6B00447 |
0.404 |
|
| 2016 |
Chen J, Wang B, Regan L, Gerstein M. Intensification: A resource for amplifying population-genetic signals with protein repeats. Journal of Molecular Biology. PMID 27939289 DOI: 10.1016/J.Jmb.2016.12.003 |
0.741 |
|
| 2016 |
Schloss AC, Williams DM, Regan LJ. Protein-Based Hydrogels for Tissue Engineering. Advances in Experimental Medicine and Biology. 940: 167-177. PMID 27677513 DOI: 10.1007/978-3-319-39196-0_8 |
0.414 |
|
| 2016 |
Speltz EB, Sawyer N, Regan L. Combining Design and Selection to Create Novel Protein-Peptide Interactions. Methods in Enzymology. 580: 203-22. PMID 27586335 DOI: 10.1016/Bs.Mie.2016.05.008 |
0.472 |
|
| 2016 |
Caballero D, Virrueta A, O'Hern CS, Regan L. Steric interactions determine side-chain conformations in protein cores. Protein Engineering, Design & Selection : Peds. 29: 367-376. PMID 27416747 DOI: 10.1093/Protein/Gzw027 |
0.658 |
|
| 2016 |
Pratt S, Speltz E, Mochrie S, Regan L. Designed proteins as novel imaging reagents in living E. coli. Chembiochem : a European Journal of Chemical Biology. PMID 27304706 DOI: 10.1002/Cbic.201600252 |
0.424 |
|
| 2016 |
Noble DB, Mochrie SG, O'Hern CS, Pollard TD, Regan L. Promoting convergence: The integrated graduate program in physical and engineering biology at Yale University, a new model for graduate education. Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology. PMID 27292366 DOI: 10.1002/Bmb.20977 |
0.514 |
|
| 2016 |
Chen J, Rozowsky J, Galeev TR, Harmanci A, Kitchen R, Bedford J, Abyzov A, Kong Y, Regan L, Gerstein M. A uniform survey of allele-specific binding and expression over 1000-Genomes-Project individuals. Nature Communications. 7: 11101. PMID 27089393 DOI: 10.1038/Ncomms11101 |
0.67 |
|
| 2016 |
Gaines JC, Smith WW, Regan L, O'Hern CS. Random close packing in protein cores. Physical Review. E. 93: 032415. PMID 27078398 DOI: 10.1103/Physreve.93.032415 |
0.679 |
|
| 2016 |
Regan L, Hinrichsen MR, Oi C. Protein Engineering Strategies with Potential Applications for Altering Clinically Relevant Cellular Pathways at the Protein Level. Expert Review of Proteomics. PMID 27031866 DOI: 10.1586/14789450.2016.1172966 |
0.458 |
|
| 2016 |
Virrueta A, O'Hern CS, Regan L. Understanding the physical basis for the side chain conformational preferences of methionine. Proteins. PMID 26917446 DOI: 10.1002/Prot.25026 |
0.643 |
|
| 2015 |
Sethi A, Clarke D, Chen J, Kumar S, Galeev TR, Regan L, Gerstein M. Reads meet rotamers: structural biology in the age of deep sequencing. Current Opinion in Structural Biology. 35: 125-134. PMID 26658741 DOI: 10.1016/J.Sbi.2015.11.003 |
0.724 |
|
| 2015 |
Speltz EB, Brown RS, Hajare HS, Schlieker C, Regan L. A designed repeat protein as an affinity capture reagent. Biochemical Society Transactions. 43: 874-80. PMID 26517897 DOI: 10.1042/Bst20150091 |
0.496 |
|
| 2015 |
Cohen SS, Riven I, Cortajarena AL, De Rosa L, D'Andrea LD, Regan L, Haran G. Probing the Molecular Origin of Native-State Flexibility in Repeat Proteins. Journal of the American Chemical Society. 137: 10367-73. PMID 26207891 DOI: 10.1021/Jacs.5B06160 |
0.496 |
|
| 2015 |
Speltz EB, Nathan A, Regan L. Design of Protein-Peptide Interaction Modules for Assembling Supramolecular Structures in Vivo and in Vitro. Acs Chemical Biology. 10: 2108-15. PMID 26131725 DOI: 10.1021/Acschembio.5B00415 |
0.414 |
|
| 2015 |
Caballero D, Smith WW, O'Hern CS, Regan L. Equilibrium transitions between side chain conformations in leucine and isoleucine. Proteins. PMID 26018846 DOI: 10.1002/Prot.24837 |
0.623 |
|
| 2015 |
Regan L, Caballero D, Hinrichsen MR, Virrueta A, Williams DM, O'Hern CS. Protein Design: Past, Present and Future. Biopolymers. PMID 25784145 DOI: 10.1002/Bip.22639 |
0.672 |
|
| 2014 |
Sawyer N, Gassaway BM, Haimovich AD, Isaacs FJ, Rinehart J, Regan L. Designed phosphoprotein recognition in Escherichia coli. Acs Chemical Biology. 9: 2502-7. PMID 25272187 DOI: 10.1021/Cb500658W |
0.465 |
|
| 2014 |
Zhou AQ, O'Hern CS, Regan L. Predicting the side-chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models. Proteins. 82: 2574-84. PMID 24912976 DOI: 10.1002/Prot.24621 |
0.719 |
|
| 2014 |
Caballero D, Määttä J, Zhou AQ, Sammalkorpi M, O'Hern CS, Regan L. Intrinsic α-helical and β-sheet conformational preferences: a computational case study of alanine. Protein Science : a Publication of the Protein Society. 23: 970-80. PMID 24753338 DOI: 10.1002/Pro.2481 |
0.75 |
|
| 2014 |
Caballero D, Regan L, O'Hern CS. Correlations between Bond, Backbone, and Side Chain Dihedral Angles Enable Changes Among Different Dipeptide Configurations Biophysical Journal. 106: 52a-53a. DOI: 10.1016/J.Bpj.2013.11.372 |
0.666 |
|
| 2014 |
Zhou AQ, O'Hern CS, Regan L. Novel Computational Methods to Design Protein-Protein Interactions Biophysical Journal. 106: 654a-655a. DOI: 10.1016/J.Bpj.2013.11.3622 |
0.797 |
|
| 2014 |
Sawyer N, Williams DM, Regan L. Designing new proteins: Protein goldendoodles Biochemist. 36: 28-33. |
0.37 |
|
| 2013 |
Zhou AQ, Caballero D, O'Hern CS, Regan L. New insights into the interdependence between amino acid stereochemistry and protein structure. Biophysical Journal. 105: 2403-11. PMID 24268152 DOI: 10.1016/J.Bpj.2013.09.018 |
0.779 |
|
| 2013 |
Sawyer N, Speltz EB, Regan L. NextGen protein design. Biochemical Society Transactions. 41: 1131-6. PMID 24059497 DOI: 10.1042/Bst20130112 |
0.461 |
|
| 2013 |
Grove TZ, Regan L, Cortajarena AL. Nanostructured functional films from engineered repeat proteins. Journal of the Royal Society, Interface / the Royal Society. 10: 20130051. PMID 23594813 DOI: 10.1098/Rsif.2013.0051 |
0.366 |
|
| 2013 |
Speltz EB, Regan L. White and green screening with circular polymerase extension cloning for easy and reliable cloning. Protein Science : a Publication of the Protein Society. 22: 859-64. PMID 23592493 DOI: 10.1002/Pro.2268 |
0.352 |
|
| 2013 |
Sawyer N, Chen J, Regan L. All repeats are not equal: a module-based approach to guide repeat protein design. Journal of Molecular Biology. 425: 1826-38. PMID 23434848 DOI: 10.1016/J.Jmb.2013.02.013 |
0.74 |
|
| 2013 |
Chen J, Sawyer N, Regan L. Protein-protein interactions: general trends in the relationship between binding affinity and interfacial buried surface area. Protein Science : a Publication of the Protein Society. 22: 510-5. PMID 23389845 DOI: 10.1002/Pro.2230 |
0.694 |
|
| 2012 |
Grove TZ, Regan L. New materials from proteins and peptides. Current Opinion in Structural Biology. 22: 451-6. PMID 22832173 DOI: 10.1016/J.Sbi.2012.06.004 |
0.368 |
|
| 2012 |
Zhou AQ, O'Hern CS, Regan L. The power of hard-sphere models: explaining side-chain dihedral angle distributions of Thr and Val. Biophysical Journal. 102: 2345-52. PMID 22677388 DOI: 10.1016/J.Bpj.2012.01.061 |
0.751 |
|
| 2012 |
Liberles DA, Teichmann SA, Bahar I, Bastolla U, Bloom J, Bornberg-Bauer E, Colwell LJ, de Koning AP, Dokholyan NV, Echave J, Elofsson A, Gerloff DL, Goldstein RA, Grahnen JA, Holder MT, ... ... Regan L, et al. The interface of protein structure, protein biophysics, and molecular evolution. Protein Science : a Publication of the Protein Society. 21: 769-85. PMID 22528593 DOI: 10.1002/Pro.2071 |
0.531 |
|
| 2012 |
Grove TZ, Forster J, Pimienta G, Dufresne E, Regan L. A modular approach to the design of protein-based smart gels. Biopolymers. 97: 508-17. PMID 22328209 DOI: 10.1002/Bip.22033 |
0.375 |
|
| 2012 |
De Rosa L, Cortajarena AL, Romanelli A, Regan L, D'Andrea LD. Site-specific protein double labeling by expressed protein ligation: applications to repeat proteins. Organic & Biomolecular Chemistry. 10: 273-80. PMID 22072074 DOI: 10.1039/C1Ob06397A |
0.46 |
|
| 2012 |
Cortajarena AL, Regan L. The folding of repeat proteins Comprehensive Biophysics. 3: 267-289. DOI: 10.1016/B978-0-12-374920-8.00318-0 |
0.408 |
|
| 2011 |
Pimienta G, Herbert KM, Regan L. A compound that inhibits the HOP-Hsp90 complex formation and has unique killing effects in breast cancer cell lines. Molecular Pharmaceutics. 8: 2252-61. PMID 21882818 DOI: 10.1021/Mp200346Y |
0.324 |
|
| 2011 |
Zhou AQ, O'Hern CS, Regan L. Revisiting the Ramachandran plot from a new angle. Protein Science : a Publication of the Protein Society. 20: 1166-71. PMID 21538644 DOI: 10.1002/Pro.644 |
0.762 |
|
| 2011 |
Cortajarena AL, Mochrie SG, Regan L. Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble. Protein Science : a Publication of the Protein Society. 20: 1042-7. PMID 21495096 DOI: 10.1002/Pro.638 |
0.444 |
|
| 2011 |
Cortajarena AL, Regan L. Calorimetric study of a series of designed repeat proteins: modular structure and modular folding. Protein Science : a Publication of the Protein Society. 20: 336-40. PMID 21280125 DOI: 10.1002/Pro.564 |
0.53 |
|
| 2011 |
Zhou AQ, O'Hern CS, Regan L. Reply to: Comment on "Revisiting the Ramachandran plot from a new angle" Protein Science. 20: 1774. DOI: 10.1002/Pro.722 |
0.638 |
|
| 2010 |
Grove TZ, Osuji CO, Forster JD, Dufresne ER, Regan L. Stimuli-responsive smart gels realized via modular protein design. Journal of the American Chemical Society. 132: 14024-6. PMID 20860358 DOI: 10.1021/Ja106619W |
0.437 |
|
| 2010 |
Clarke J, Regan L. Protein engineering and design: from first principles to new technologies. Current Opinion in Structural Biology. 20: 480-1. PMID 20708403 DOI: 10.1016/J.Sbi.2010.07.001 |
0.369 |
|
| 2010 |
Kundrat L, Regan L. Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. Biochemistry. 49: 7428-38. PMID 20704274 DOI: 10.1021/Bi100386W |
0.807 |
|
| 2010 |
Ilagan RP, Rhoades E, Gruber DF, Kao HT, Pieribone VA, Regan L. A new bright green-emitting fluorescent protein--engineered monomeric and dimeric forms. The Febs Journal. 277: 1967-78. PMID 20345907 DOI: 10.1111/J.1742-4658.2010.07618.X |
0.453 |
|
| 2010 |
Grove TZ, Hands M, Regan L. Creating novel proteins by combining design and selection. Protein Engineering, Design & Selection : Peds. 23: 449-55. PMID 20304973 DOI: 10.1093/Protein/Gzq015 |
0.42 |
|
| 2010 |
Cortajarena AL, Wang J, Regan L. Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand. The Febs Journal. 277: 1058-66. PMID 20089039 DOI: 10.1111/J.1742-4658.2009.07549.X |
0.46 |
|
| 2010 |
Jackrel ME, Cortajarena AL, Liu TY, Regan L. Screening libraries to identify proteins with desired binding activities using a split-GFP reassembly assay. Acs Chemical Biology. 5: 553-62. PMID 20038141 DOI: 10.1021/Cb900272J |
0.793 |
|
| 2010 |
Cortajarena AL, Liu TY, Hochstrasser M, Regan L. Designed proteins to modulate cellular networks. Acs Chemical Biology. 5: 545-52. PMID 20020775 DOI: 10.1021/Cb9002464 |
0.692 |
|
| 2010 |
Kundrat L, Regan L. Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP. Journal of Molecular Biology. 395: 587-94. PMID 19913553 DOI: 10.1016/J.Jmb.2009.11.017 |
0.753 |
|
| 2010 |
Yi F, Doudevski I, Regan L. HOP is a monomer: investigation of the oligomeric state of the co-chaperone HOP. Protein Science : a Publication of the Protein Society. 19: 19-25. PMID 19866486 DOI: 10.1002/Pro.278 |
0.394 |
|
| 2010 |
Toofanny RD, Cortajarena AL, Regan L, Daggett V. Molecular Dynamics Simulations of Consensus Tetratricopeptide Repeat Proteins Biophysical Journal. 98: 636a-637a. DOI: 10.1016/J.Bpj.2009.12.3486 |
0.447 |
|
| 2010 |
Ilagan R, Kao H, Gruber D, Rhoades E, Regan L. Characterization of New and Improved Fluorescent Proteins and their Applications Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.3284 |
0.376 |
|
| 2010 |
Ledden B, Cortajarena AL, Regan L, Talaga D, Li J. Solid-State Nanopore Translocation of Idealized Helical Repeat Proteins Biophysical Journal. 98: 5-7. DOI: 10.1016/J.Bpj.2009.12.3253 |
0.385 |
|
| 2009 |
Kajander T, Sachs JN, Goldman A, Regan L. Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering. The Journal of Biological Chemistry. 284: 25364-74. PMID 19586912 DOI: 10.1074/Jbc.M109.033894 |
0.78 |
|
| 2009 |
Champion EA, Kundrat L, Regan L, Baserga SJ. A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics. Protein Engineering, Design & Selection : Peds. 22: 431-9. PMID 19515729 DOI: 10.1093/Protein/Gzp022 |
0.806 |
|
| 2009 |
Jackrel ME, Valverde R, Regan L. Redesign of a protein-peptide interaction: characterization and applications. Protein Science : a Publication of the Protein Society. 18: 762-74. PMID 19309728 DOI: 10.1002/Pro.75 |
0.8 |
|
| 2009 |
Yi F, Zhu P, Southall N, Inglese J, Austin CP, Zheng W, Regan L. An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction. Journal of Biomolecular Screening. 14: 273-81. PMID 19211782 DOI: 10.1177/1087057108330114 |
0.329 |
|
| 2008 |
Yi F, Regan L. A novel class of small molecule inhibitors of Hsp90. Acs Chemical Biology. 3: 645-54. PMID 18785742 DOI: 10.1021/Cb800162X |
0.385 |
|
| 2008 |
Champion EA, Lane BH, Jackrel ME, Regan L, Baserga SJ. A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21 is essential for efficient pre-rRNA processing. Molecular and Cellular Biology. 28: 6547-56. PMID 18725399 DOI: 10.1128/Mcb.00906-08 |
0.703 |
|
| 2008 |
Regan L, Woolfson DN. Protein folding and design: from simple models to complex systems. Current Opinion in Structural Biology. 18: 475-6. PMID 18644450 DOI: 10.1016/J.Sbi.2008.06.005 |
0.391 |
|
| 2008 |
Cortajarena AL, Lois G, Sherman E, O'Hern CS, Regan L, Haran G. Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state. Journal of Molecular Biology. 382: 203-12. PMID 18644382 DOI: 10.1016/J.Jmb.2008.07.005 |
0.655 |
|
| 2008 |
Grove TZ, Cortajarena AL, Regan L. Ligand binding by repeat proteins: natural and designed. Current Opinion in Structural Biology. 18: 507-15. PMID 18602006 DOI: 10.1016/J.Sbi.2008.05.008 |
0.482 |
|
| 2008 |
Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ. Comparison of the backbone dynamics of a natural and a consensus designed 3-TPR domain. Journal of Biomolecular Nmr. 41: 169-78. PMID 18566891 DOI: 10.1007/S10858-008-9250-6 |
0.436 |
|
| 2008 |
Cortajarena AL, Mochrie SG, Regan L. Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange. Journal of Molecular Biology. 379: 617-26. PMID 18462750 DOI: 10.1016/J.Jmb.2008.02.046 |
0.528 |
|
| 2008 |
Valverde R, Edwards L, Regan L. Structure and function of KH domains. The Febs Journal. 275: 2712-26. PMID 18422648 DOI: 10.1111/J.1742-4658.2008.06411.X |
0.658 |
|
| 2008 |
Cortajarena AL, Yi F, Regan L. Designed TPR modules as novel anticancer agents. Acs Chemical Biology. 3: 161-6. PMID 18355005 DOI: 10.1021/Cb700260Z |
0.412 |
|
| 2008 |
Dalal S, Canet D, Kaiser SE, Dobson CM, Regan L. Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins. Protein Engineering, Design & Selection : Peds. 21: 197-206. PMID 18299293 DOI: 10.1093/Protein/Gzm088 |
0.685 |
|
| 2008 |
van Nuland NA, Dobson CM, Regan L. Characterization of folding the four-helix bundle protein Rop by real-time NMR. Protein Engineering, Design & Selection : Peds. 21: 165-70. PMID 18299292 DOI: 10.1093/Protein/Gzm081 |
0.409 |
|
| 2007 |
Valverde R, Pozdnyakova I, Kajander T, Venkatraman J, Regan L. Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein. Structure (London, England : 1993). 15: 1090-8. PMID 17850748 DOI: 10.1016/J.Str.2007.06.022 |
0.746 |
|
| 2007 |
Kajander T, Cortajarena AL, Mochrie S, Regan L. Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins. Acta Crystallographica. Section D, Biological Crystallography. 63: 800-11. PMID 17582171 DOI: 10.1107/S0907444907024353 |
0.76 |
|
| 2006 |
Cheng CY, Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ. Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats. Biochemistry. 45: 12175-83. PMID 17002317 DOI: 10.1021/Bi060819A |
0.406 |
|
| 2006 |
Kajander T, Cortajarena AL, Regan L. Consensus design as a tool for engineering repeat proteins. Methods in Molecular Biology (Clifton, N.J.). 340: 151-70. PMID 16957336 DOI: 10.1385/1-59745-116-9:151 |
0.767 |
|
| 2006 |
Cortajarena AL, Regan L. Ligand binding by TPR domains. Protein Science : a Publication of the Protein Society. 15: 1193-8. PMID 16641492 DOI: 10.1110/Ps.062092506 |
0.386 |
|
| 2006 |
Magliery TJ, Regan L. Reassembled GFP: detecting protein-protein interactions and protein expression patterns. Methods of Biochemical Analysis. 47: 391-405. PMID 16342418 DOI: 10.1002/0471739499.Ch17 |
0.73 |
|
| 2005 |
Magliery TJ, Regan L. Sequence variation in ligand binding sites in proteins. Bmc Bioinformatics. 6: 240. PMID 16194281 DOI: 10.1186/1471-2105-6-240 |
0.722 |
|
| 2005 |
Wang J, Gülich S, Bradford C, Ramirez-Alvarado M, Regan L. A twisted four-sheeted model for an amyloid fibril. Structure (London, England : 1993). 13: 1279-88. PMID 16154085 DOI: 10.1016/J.Str.2005.06.010 |
0.313 |
|
| 2005 |
Main ER, Lowe AR, Mochrie SG, Jackson SE, Regan L. A recurring theme in protein engineering: the design, stability and folding of repeat proteins. Current Opinion in Structural Biology. 15: 464-71. PMID 16043339 DOI: 10.1016/J.Sbi.2005.07.003 |
0.537 |
|
| 2005 |
Kajander T, Cortajarena AL, Main ER, Mochrie SG, Regan L. A new folding paradigm for repeat proteins. Journal of the American Chemical Society. 127: 10188-90. PMID 16028928 DOI: 10.1021/Ja0524494 |
0.73 |
|
| 2005 |
Main ER, Stott K, Jackson SE, Regan L. Local and long-range stability in tandemly arrayed tetratricopeptide repeats. Proceedings of the National Academy of Sciences of the United States of America. 102: 5721-6. PMID 15824314 DOI: 10.1073/Pnas.0404530102 |
0.54 |
|
| 2005 |
Pozdnyakova I, Regan L. New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level. The Febs Journal. 272: 872-8. PMID 15670167 DOI: 10.1111/J.1742-4658.2004.04527.X |
0.383 |
|
| 2005 |
Wilson CG, Kajander T, Regan L. The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold. The Febs Journal. 272: 166-79. PMID 15634341 DOI: 10.1111/J.1432-1033.2004.04397.X |
0.754 |
|
| 2005 |
Magliery TJ, Wilson CG, Pan W, Mishler D, Ghosh I, Hamilton AD, Regan L. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. Journal of the American Chemical Society. 127: 146-57. PMID 15631464 DOI: 10.1021/Ja046699G |
0.802 |
|
| 2004 |
Wilson CG, Magliery TJ, Regan L. Detecting protein-protein interactions with GFP-fragment reassembly. Nature Methods. 1: 255-62. PMID 16145770 DOI: 10.1038/Nmeth1204-255 |
0.736 |
|
| 2004 |
Goehlert VA, Krupinska E, Regan L, Stone MJ. Analysis of side chain mobility among protein G B1 domain mutants with widely varying stabilities. Protein Science : a Publication of the Protein Society. 13: 3322-30. PMID 15537756 DOI: 10.1110/Ps.04926604 |
0.412 |
|
| 2004 |
Magliery TJ, Regan L. Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif. Journal of Molecular Biology. 343: 731-45. PMID 15465058 DOI: 10.1016/J.Jmb.2004.08.026 |
0.714 |
|
| 2004 |
Cortajarena AL, Kajander T, Pan W, Cocco MJ, Regan L. Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins. Protein Engineering, Design & Selection : Peds. 17: 399-409. PMID 15166314 DOI: 10.1093/Protein/Gzh047 |
0.75 |
|
| 2004 |
Magliery TJ, Regan L. Combinatorial approaches to protein stability and structure. European Journal of Biochemistry / Febs. 271: 1595-608. PMID 15096198 DOI: 10.1111/J.1432-1033.2004.04075.X |
0.74 |
|
| 2004 |
Magliery TJ, Regan L. Library approaches to biophysical problems. European Journal of Biochemistry / Febs. 271: 1593-4. PMID 15096197 DOI: 10.1111/J.1432-1033.2004.04092.X |
0.606 |
|
| 2004 |
Magliery TJ, Regan L. A cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics. Protein Engineering, Design & Selection : Peds. 17: 77-83. PMID 14985540 DOI: 10.1093/Protein/Gzh010 |
0.691 |
|
| 2003 |
D'Andrea LD, Regan L. TPR proteins: the versatile helix. Trends in Biochemical Sciences. 28: 655-62. PMID 14659697 DOI: 10.1016/J.Tibs.2003.10.007 |
0.484 |
|
| 2003 |
Mayer KL, Earley MR, Gupta S, Pichumani K, Regan L, Stone MJ. Covariation of backbone motion throughout a small protein domain. Nature Structural Biology. 10: 962-5. PMID 14528292 DOI: 10.1038/Nsb991 |
0.427 |
|
| 2003 |
Main ER, Jackson SE, Regan L. The folding and design of repeat proteins: reaching a consensus. Current Opinion in Structural Biology. 13: 482-9. PMID 12948778 DOI: 10.1016/S0959-440X(03)00105-2 |
0.536 |
|
| 2003 |
Main ER, Xiong Y, Cocco MJ, D'Andrea L, Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure (London, England : 1993). 11: 497-508. PMID 12737816 DOI: 10.1016/S0969-2126(03)00076-5 |
0.517 |
|
| 2003 |
Regan L. Molten globules move into action. Proceedings of the National Academy of Sciences of the United States of America. 100: 3553-4. PMID 12657734 DOI: 10.1073/Pnas.0830651100 |
0.449 |
|
| 2003 |
Ramírez-Alvarado M, Cocco MJ, Regan L. Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro. Protein Science : a Publication of the Protein Society. 12: 567-76. PMID 12592027 DOI: 10.1110/Ps.0227403 |
0.377 |
|
| 2002 |
Ramírez-Alvarado M, Regan L. Does the location of a mutation determine the ability to form amyloid fibrils? Journal of Molecular Biology. 323: 17-22. PMID 12368095 DOI: 10.1016/S0022-2836(02)00840-9 |
0.36 |
|
| 2001 |
Marino SF, Shechner D, Regan L. 'Morphs' (MRFs): metal-reversible folding domains for differential IgG binding. Chemistry & Biology. 8: 1221-9. PMID 11755400 DOI: 10.1016/S1074-5521(01)00088-6 |
0.726 |
|
| 2001 |
Bishop B, Koay DC, Sartorelli AC, Regan L. Reengineering granulocyte colony-stimulating factor for enhanced stability. The Journal of Biological Chemistry. 276: 33465-70. PMID 11406632 DOI: 10.1074/Jbc.M104494200 |
0.344 |
|
| 2001 |
Stone MJ, Gupta S, Snyder N, Regan L. Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants. Journal of the American Chemical Society. 123: 185-6. PMID 11273620 DOI: 10.1021/Ja003094L |
0.32 |
|
| 2000 |
Willis MA, Bishop B, Regan L, Brunger AT. Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Structure (London, England : 1993). 8: 1319-28. PMID 11188696 DOI: 10.1016/S0969-2126(00)00544-X |
0.675 |
|
| 2000 |
Dalal S, Regan L. Understanding the sequence determinants of conformational switching using protein design. Protein Science : a Publication of the Protein Society. 9: 1651-9. PMID 11045612 DOI: 10.1110/Ps.9.9.1651 |
0.69 |
|
| 2000 |
Balasubramanian S, Schneider T, Gerstein M, Regan L. Proteomics of Mycoplasma genitalium: identification and characterization of unannotated and atypical proteins in a small model genome. Nucleic Acids Research. 28: 3075-82. PMID 10931922 DOI: 10.1093/Nar/28.16.3075 |
0.607 |
|
| 2000 |
Ramirez-Alvarado M, Merkel JS, Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proceedings of the National Academy of Sciences of the United States of America. 97: 8979-84. PMID 10908649 DOI: 10.1073/Pnas.150091797 |
0.752 |
|
| 2000 |
Seewald MJ, Pichumani K, Stowell C, Tibbals BV, Regan L, Stone MJ. The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G. Protein Science : a Publication of the Protein Society. 9: 1177-93. PMID 10892810 DOI: 10.1110/Ps.9.6.1177 |
0.372 |
|
| 2000 |
Merkel JS, Regan L. Modulating protein folding rates in vivo and in vitro by side-chain interactions between the parallel beta strands of green fluorescent protein. The Journal of Biological Chemistry. 275: 29200-6. PMID 10844000 DOI: 10.1074/Jbc.M004734200 |
0.763 |
|
| 2000 |
Ghosh I, Hamilton AD, Regan L. Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein [12] Journal of the American Chemical Society. 122: 5658-5659. DOI: 10.1021/Ja994421W |
0.655 |
|
| 1999 |
Merkel JS, Sturtevant JM, Regan L. Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings. Structure (London, England : 1993). 7: 1333-43. PMID 10574793 DOI: 10.1016/S0969-2126(00)80023-4 |
0.696 |
|
| 1999 |
Marino SF, Regan L. Secondary ligands enhance affinity at a designed metal-binding site. Chemistry & Biology. 6: 649-55. PMID 10467132 DOI: 10.1016/S1074-5521(99)80116-1 |
0.743 |
|
| 1999 |
Ma Y, Cunningham ME, Wang X, Ghosh I, Regan L, Longley BJ. Inhibition of spontaneous receptor phosphorylation by residues in a putative alpha-helix in the KIT intracellular juxtamembrane region. The Journal of Biological Chemistry. 274: 13399-402. PMID 10224103 DOI: 10.1074/Jbc.274.19.13399 |
0.471 |
|
| 1999 |
Nagi AD, Anderson KS, Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein. Journal of Molecular Biology. 286: 257-65. PMID 9931264 DOI: 10.1006/Jmbi.1998.2474 |
0.453 |
|
| 1999 |
Prodromou C, Siligardi G, O'Brien R, Woolfson DN, Regan L, Panaretou B, Ladbury JE, Piper PW, Pearl LH. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. The Embo Journal. 18: 754-62. PMID 9927435 DOI: 10.1093/Emboj/18.3.754 |
0.401 |
|
| 1998 |
Merkel JS, Regan L. Aromatic rescue of glycine in beta sheets. Folding & Design. 3: 449-55. PMID 9889161 DOI: 10.1016/S1359-0278(98)00062-5 |
0.718 |
|
| 1998 |
Farinas E, Regan L. The de novo design of a rubredoxin-like Fe site. Protein Science : a Publication of the Protein Society. 7: 1939-46. PMID 9761474 DOI: 10.1002/Pro.5560070909 |
0.364 |
|
| 1998 |
Regan L. Proteins to order Structure. 6: 1-4. PMID 9493261 DOI: 10.1016/S0969-2126(98)00001-X |
0.436 |
|
| 1997 |
Dalal S, Balasubramanian S, Regan L. Transmuting alpha helices and beta sheets. Folding & Design. 2: R71-9. PMID 9377709 DOI: 10.1016/S1359-0278(97)00036-9 |
0.637 |
|
| 1997 |
Dalal S, Balasubramanian S, Regan L. Protein alchemy: changing beta-sheet into alpha-helix. Nature Structural Biology. 4: 548-52. PMID 9228947 DOI: 10.1038/Nsb0797-548 |
0.67 |
|
| 1997 |
Regan L. Helix is a helix is a helix Proceedings of the National Academy of Sciences of the United States of America. 94: 2796-2797. PMID 9096298 DOI: 10.1073/Pnas.94.7.2796 |
0.426 |
|
| 1997 |
Nagi AD, Regan L. An inverse correlation between loop length and stability in a four-helix-bundle protein Folding and Design. 2: 67-75. PMID 9080200 DOI: 10.1016/S1359-0278(97)00007-2 |
0.489 |
|
| 1996 |
Smith CK, Bu Z, Anderson KS, Sturtevant JM, Engelman DM, Regan L. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science : a Publication of the Protein Society. 5: 2009-19. PMID 8897601 DOI: 10.1002/Pro.5560051007 |
0.353 |
|
| 1996 |
Munson M, Balasubramanian S, Fleming KG, Nagi AD, O'Brien R, Sturtevant JM, Regan L. What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Science : a Publication of the Protein Society. 5: 1584-93. PMID 8844848 DOI: 10.1002/Pro.5560050813 |
0.751 |
|
| 1996 |
Predki PF, Agrawal V, Brünger AT, Regan L. Amino-acid substitutions in a surface turn modulate protein stability. Nature Structural Biology. 3: 54-8. PMID 8548455 DOI: 10.1038/Nsb0196-54 |
0.465 |
|
| 1996 |
Regan L. The design of proteins with novel structures and activities Acta Crystallographica Section a Foundations of Crystallography. 52: C212-C212. DOI: 10.1107/S0108767396090897 |
0.344 |
|
| 1995 |
Regan L, Rockwell A, Wasserman Z, DeGrado W. Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein. Protein Science : a Publication of the Protein Society. 3: 2419-27. PMID 7756995 DOI: 10.1002/Pro.5560031225 |
0.638 |
|
| 1995 |
Regan L. Protein design: novel metal-binding sites Trends in Biochemical Sciences. 20: 280-285. PMID 7667881 DOI: 10.1016/S0968-0004(00)89044-1 |
0.437 |
|
| 1995 |
Klemba M, Gardner KH, Marino S, Clarke ND, Regan L. Novel metal-binding proteins by design. Nature Structural Biology. 2: 368-73. PMID 7664093 DOI: 10.1038/Nsb0595-368 |
0.771 |
|
| 1995 |
Klemba M, Regan L. Characterization of Metal Binding by a Designed Protein: Single Ligand Substitutions at a Tetrahedral Cys2His2 Site Biochemistry. 34: 10094-10100. PMID 7632681 DOI: 10.1021/Bi00031A034 |
0.347 |
|
| 1995 |
Predki PF, Regan L. Redesigning the Topology of a Four-Helix-Bundle Protein: Monomeric Rop Biochemistry. 34: 9834-9839. PMID 7543279 DOI: 10.1021/Bi00031A003 |
0.551 |
|
| 1995 |
Predki PF, Nayak LM, Gottlieb MB, Regan L. Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell. 80: 41-50. PMID 7529141 DOI: 10.1016/0092-8674(95)90449-2 |
0.338 |
|
| 1995 |
Smith CK, Regan L. Guidelines for protein design: the energetics of beta sheet side chain interactions. Science (New York, N.Y.). 270: 980-2. PMID 7481801 DOI: 10.1126/Science.270.5238.980 |
0.404 |
|
| 1995 |
Smith CK, Munson M, Regan L. Studying α-helix and β-sheet formation in small proteins Techniques in Protein Chemistry. 6: 323-332. DOI: 10.1016/S1080-8914(06)80040-2 |
0.735 |
|
| 1994 |
Smith CK, Withka JM, Regan L. A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. Biochemistry. 33: 5510-7. PMID 8180173 DOI: 10.1021/Bi00184A020 |
0.484 |
|
| 1994 |
Munson M, Predki PF, Regan L. ColE1-compatible vectors for high-level expression of cloned DNAs from the T7 promoter. Gene. 144: 59-62. PMID 8026759 DOI: 10.1016/0378-1119(94)90203-8 |
0.651 |
|
| 1994 |
Regan L. Protein structure. Born to be beta. Current Biology : Cb. 4: 656-8. PMID 7953549 DOI: 10.1016/S0960-9822(00)00147-0 |
0.405 |
|
| 1994 |
Munson M, O'Brien R, Sturtevant JM, Regan L. Redesigning the hydrophobic core of a four-helix-bundle protein. Protein Science : a Publication of the Protein Society. 3: 2015-22. PMID 7535612 DOI: 10.1002/Pro.5560031114 |
0.73 |
|
| 1993 |
Regan L. The Design Of Metal-Binding Sites In Proteins Annual Review of Biophysics and Biomolecular Structure. 22: 257-281. PMID 8347991 DOI: 10.1146/Annurev.Bb.22.060193.001353 |
0.382 |
|
| 1991 |
Marqusee S, Regan L. Deconstructing protein structure. Current Biology : Cb. 1: 207-8. PMID 15336120 DOI: 10.1016/0960-9822(91)90057-4 |
0.519 |
|
| 1990 |
Regan L, Clarke ND. A tetrahedral Zinc(II)-binding site introduced into a designed protein Biochemistry. 29: 10878-10883. PMID 2271687 DOI: 10.1021/Bi00501A003 |
0.433 |
|
| 1988 |
Regan L, Buxbaum L, Hill K, Schimmel P. Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion. The Journal of Biological Chemistry. 263: 18598-600. PMID 3198590 |
0.448 |
|
| 1988 |
Frederick CA, Wang AH, Rich A, Regan L, Schimmel P. Crystallization of a small fragment of an aminoacyl tRNA synthetase. Journal of Molecular Biology. 203: 521-2. PMID 3058989 DOI: 10.1016/0022-2836(88)90019-8 |
0.47 |
|
| 1988 |
Regan L, DeGrado WF. Characterization of a helical protein designed from first principles. Science (New York, N.Y.). 241: 976-8. PMID 3043666 DOI: 10.1126/Science.3043666 |
0.642 |
|
| 1987 |
DeGrado WF, Regan L, Ho SP. The design of a four-helix bundle protein. Cold Spring Harbor Symposia On Quantitative Biology. 52: 521-6. PMID 3454275 DOI: 10.1101/Sqb.1987.052.01.059 |
0.637 |
|
| 1987 |
Regan L, Bowie J, Schimmel P. Polypeptide sequences essential for RNA recognition by an enzyme. Science (New York, N.Y.). 235: 1651-3. PMID 2435005 DOI: 10.1126/Science.2435005 |
0.554 |
|
| 1986 |
Regan L, Dignam JD, Schimmel P. A bacterial and silkworm aminoacyl-tRNA synthetase have a common epitope which maps to the catalytic domain of each. The Journal of Biological Chemistry. 261: 5241-4. PMID 2420799 |
0.422 |
|
| 1985 |
Jasin M, Regan L, Schimmel P. Two mutations in the dispensable part of alanine tRNA synthetase which affect the catalytic activity. The Journal of Biological Chemistry. 260: 2226-30. PMID 3882689 |
0.422 |
|
| 1984 |
Schimmel P, Jasin M, Regan L. Size polymorphism and the structure of aminoacyl-tRNA synthetases. Federation Proceedings. 43: 2987-90. PMID 6389183 |
0.428 |
|
| 1984 |
Jasin M, Regan L, Schimmel P. Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site. Cell. 36: 1089-95. PMID 6200234 DOI: 10.1016/0092-8674(84)90059-X |
0.64 |
|
| 1983 |
Jasin M, Regan L, Schimmel P. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase. Nature. 306: 441-7. PMID 6358898 DOI: 10.1038/306441A0 |
0.635 |
|
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