List of Publications

2014

Sawyer, N., Gassaway, B.M., Haimovich, A.D., Isaacs, F.J., Rinehart, J., and Regan, L.
Designed Phosphoprotein Recognition in Escherichia coli.
ACS Chemical Biology, 9(11): 2502-2507. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
Predicting the side-chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models.
Proteins, 82(10): 2574-2584. PDF

Caballero, D., Määttä, J., Zhou, A.Q., Sammalkorpi, M., O'Hern, C.S., and Regan, L.
Intrinsic alpha-helical and beta-sheet conformational preferences: A computational case study of alanine.
Protein Science, 23(7): 970-980. PDF

Schlingman, D.J., Mack, A.H., Kamenetska, M., Mochrie, S.G.J., and Regan, L.
Routes to DNA accessibility: alternative pathways for nucleosome unwinding.
Biophysical Journal, 107(2): 384-392. PDF

Zhao, Q., Saro, D., Sachpatzidis, A., Singh, T.R., Schlingman, D., Zheng, X.-F., Mack, A.,
Tsai, M.-S., Mochrie, S., Regan, L., Meetei, A.R., Sung, P., and Xiong, Y.
The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes.
Nature Communications, 5: 2987. PDF

2013

Zhou, A.Q., Caballero, D., O'Hern, C.S., and Regan, L.
New Insights into the Interdependence between Amino Acid Stereochemistry and Protein Structure.
Biophysical Journal, 105(10): 2403-2411. PDF

Mack, A.H*., Schlingman, D.J.*, Kamenetska, M., Collins, R., Mochrie, S.G.J., and Regan, L.
The molecular yo-yo method: Live jump detection improves throughput of single-molecule force spectroscopy for out-of-equilibrium transitions.
Review of Scientific Instruments, 84(8): 085119. PDF

Speltz, E. and Regan, L.
White and green screening with circular polymerase extension cloning for easy and reliable cloning.
Protein Science, 22(6): 859-864. PDF

Sawyer, N.*, Speltz, E.*, and Regan, L.
NextGen protein design.
Biochemical Society Transactions, 41(5): 1131-1136. PDF

Sawyer, N.*, Chen, J.*, and Regan, L.
All Repeats Are Not Equal: A Module-Based Approach to Guide Repeat Protein Design.
Journal of Molecular Biology, 425(10): 1826-1838. PDF

Chen, J., Sawyer, N., and Regan, L.
Protein-protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area.
Protein Science, 22(4): 510-151. PDF

Grove, T.Z., Regan, L., and Cortajarena, A.L.
Nanostructured functional films from engineered repeat proteins.
Journal of the Royal Society Interface, 10(83): 20130051. PDF

2012

Mack, A.H*., Schlingman, D.J.*, Ilagan, R.P., Mochrie, S.G.J., and Regan, L.
Kinetics and thermodynamics of phenotype: Unwinding and rewinding the nucleosome.
Journal of Molecular Biology, 423(5): 687-701. PDF

Mack, A.H., Schlingman, D.J., Regan, L., and Mochrie, S.G.J.
Practical Axial Optical Trapping.
Review of Scientific Instruments, 83(10): 103106. PDF

Grove, T.Z. and Regan, L.
New materials from proteins and peptides.
Current Opinion in Structural Biology, 22(4): 451-456. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val.
Biophysical Journal, 102(10): 2345-2352. PDF

Liberles, D.A., Teichmann, S.A., Bahar, I., Bastolla, U., Bloom, J.,
Bornberg-Bauer, E., Colwell, L.J., de Koning, A.P.J., Dokholyan, N.V., Echave, J. et al.
The interface of protein structure, protein biophysics, and molecular evolution.
Protein Science, 21(6): 769-785. PDF

Grove, T.Z., Forster, J., Pimienta, G., Dufresne, E., and Regan, L.
A modular approach to the design of protein-based smart gels.
Biopolymers, 97(7): 508-517. PDF

De Rosa, L., Cortajarena, A.L., Romanelli, A., Regan, L., and D'Andrea, L.D.
Site-specific protein double labeling by expressed protein ligation: applications to repeat proteins.
Organic & Biomolecular Chemistry, 10(2): 273-280. PDF

2011

Zhou, A.Q., O'Hern, C.S., and Regan, L.
Revisiting the Ramachandran plot from a new angle.
Protein Science, 20(7): 1166-1171. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
Reply to: Comment on "Revisiting the Ramachandran plot from a new angle".
Protein Science, 20(11): 1774-1774. PDF

Schlingman, D.J., Mack, A.H., Mochrie, S.G.J., and Regan, L.
A new method for the covalent attachment of DNA to a surface for single-molecule studies.
Colloids and Surfaces B-Biointerfaces, 83(1): 91-95. PDF

Pimienta, G., Herbert, K.M., and Regan, L.
A Compound That Inhibits the HOP-Hsp90 Complex Formation and Has Unique Killing Effects in Breast Cancer Cell Lines.
Molecular Pharmaceutics, 8(6): 2252-2261. PDF

Cortajarena, A.L. and Regan, L.
Calorimetric study of a series of designed repeat proteins: Modular structure and modular folding.
Protein Science, 20(2): 336-340. PDF

Cortajarena, A.L., Mochrie, S.G.J., and Regan, L.
Modulating repeat protein stability: The effect of individual helix stability on the collective behavior of the ensemble.
Protein Science, 20(6): 1042-1047. PDF

2010

Yi, F., Doudevski, I., and Regan, L.
HOP is a monomer: Investigation of the oligomeric state of the co-chaperone HOP.
Protein Science, 19(1): 19-25. PDF

Kundrat, L. and Regan, L.
Identification of Residues on Hsp70 and Hsp90 Ubiquitinated by the Cochaperone CHIP.
Journal of Molecular Biology, 395(3):587-594. PDF

Kundrat, L. and Regan, L.
Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP.
Biochemistry, 49(35): 7428-7438. PDF

Jackrel, M.E., Cortajarena, A.L., Liu, T.Y., and Regan, L.
Screening Libraries To Identify Proteins with Desired Binding Activities Using a Split-GFP Reassembly Assay.
ACS Chemical Biology, 5(6): 553-562. PDF

Ilagan, R.P., Rhoades, E., Gruber, D.F., Kao, H.-T., Pieribone, V.A., and Regan, L.
A new bright green-emitting fluorescent protein - engineered monomeric and dimeric forms.
FEBS Journal, 277(8): 1967-1978. PDF

Grove, T.Z., Osuji, C.O., Forster, J.D., Dufresne, E.R., and Regan, L.
Stimuli-Responsive Smart Gels Realized via Modular Protein Design.
Journal of the American Chemical Society, 132(40): 14024-14026. PDF

Grove, T.Z., Hands, M., and Regan, L.
Creating novel proteins by combining design and selection.
Protein Engineering Design & Selection , 23(6): 449-455. PDF

Cortajarena, A.L., Wang, J., and Regan, L.
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.
FEBS Journal, 277(4): 1058-1066. PDF

Cortajarena, A.L., Liu, T.Y., Hochstrasser, M., and Regan, L.
Designed Proteins To Modulate Cellular Networks.
ACS Chemical Biology, 5(6): 545-552. PDF

Clarke, J. and Regan, L.
Protein engineering and design: from first principles to new technologies.
Current Opinion in Structural Biology, 20(4): 480-481. PDF

2009

Kajander, T., Sachs, J.N., Goldman, A., and Regan, L.
Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90:
computational analysis and protein engineering.
Journal of Biological Chemistry, 284(37): 25364-25374. PDF

Champion, E.A., Kundrat, L., Regan, L., and Baserga, S.J.
A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics.
Protein Engineering Design & Selection, 22(7): 431-439. PDF

Jackrel, M.E., Valverde, R., and Regan, L.
Redesign of a protein-peptide interaction: characterization and applications.
Protein Science, 18(4): 762-774. PDF

Yi, F., Zhu, P., Southall, N., Inglese, J., Austin, C.P., Zheng, W., and Regan, L.
An AlphaScreen-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction.
Journal of Biomolecular Screening, 14(3): 273-281. PDF

2008

Yi, F. and Regan, L.
A novel class of small molecule inhibitors of Hsp90.
ACS Chemical Biology, 3(10): 645-654. PDF

Champion, E.A., Lane, B.H., Jackrel, M.E., Regan, L, and Baserga, S.J.
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(21): 6547-6556. PDF

Cortajarena, A.L., Lois, G., Sherman, E., O'Hern, C.S., Regan, L, and Haran, G.
Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state.
Journal of Molecular Biology, 382(1): 203-212. PDF

Grove, T.Z., Cortajarena, A.L., and Regan, L.
Ligand binding by repeat proteins: natural and designed.
Current Opinion in Structural Biology, 18(4): 507-515. PDF

Cortajarena, A.L., Mochrie, S.G., and Regan, L.
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange.
Journal of Molecular Biology, 379(3): 617-626. PDF

Valverde, R., Edwards, L., and Regan, L.
Structure and function of KH domains.
FEBS Journal, 275(11): 2712-2726. PDF

Cortajarena, A.L., Yi, F., and Regan, L.
Designed TPR modules as novel anticancer agents.
ACS Chemical Biology, 3(3): 161-166 . PDF

Dalal, S., Canet, D., Kaiser, S.E., Dobson, C.M., and Regan, L.
Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins.
Protein Engineering Design & Selection, 21(3): 197-206. PDF

van Nuland, N.A., Dobson, C.M., and Regan, L.
Characterization of folding the four-helix bundle protein Rop by real-time NMR.
Protein Engineering Design & Selection, 21(3): 165-70. PDF

2007

Valverde, R., Pozdnyakova, I., Kajander, T.,Venkatraman, J., and Regan, L.
Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein.
Structure, 15(9): 1090-1098. PDF

Kajander, T., Cortajarena, A.L., Mochrie S., and 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: 800-811. PDF

2006

Cheng, C.Y., Jarymowycz, V.A., Cortajarena, A.L., Regan, L., and Stone, M.J.
Repeat Motions and Backbone Flexibility in Designed Proteins with Different Numbers of Identical Consensus Tetratricopeptide Repeats.
Biochemistry, 45(39): 12175-12183. PDF

Kajander, T., Cortajarena, A.L., and Regan, L.
Consensus Design as a Tool for Engineering Repeat Proteins.
Methods in Molecular Biology, 340: 151-170. PDF

Cortajarena, A.L. and Regan, L.
Ligand binding by TPR domains.
Protein Science, 15(5): 1193-1198. PDF

Magliery T.J. and Regan, L.
Reassembled GFP: detecting protein-protein interactions and protein expression patterns.
Methods of Biochemical Analysis, 47: 391-405. PubMed

2005

Magliery, T.J. and Regan, L.
Sequence variation in ligand binding sites in proteins.
BMC Bioinformatics, 6: 240. PDF

Wang, J., Gulich, S., Bradford, C., Ramirez-Alvarado, M., and Regan, L.
A twisted four-sheeted model for an amyloid fibril.
Structure, 13(9): 1279-88. PDF

Main, E.R., Lowe, A.R., Mochrie, S.G., Jackson, S.E., and Regan, L.
A recurring theme in protein engineering: the design, stability and folding of repeat proteins.
Current Opinion in Structural Biology, 5(4): 464-71. PDF

Kajander, T., Cortajarena, A.L., Main, E.R., Mochrie, S.G., and Regan, L.
A new folding paradigm for repeat proteins.
Journal of the American Chemical Society, 127(29): 10188-90. PDFSupplementary Information

Main, E.R., Stott, K., Jackson, S.E., and Regan, L.
Local and long-range stability in tandemly arrayed tetratricopeptide repeats.
Proceedings of the National Academy of Sciences USA, 102(16): 5721-5726. PDF

Pozdnyakova, I. and Regan L.
New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level.
FEBS Journal, 272(3): 872-878. PDF

Wilson, C.G., Kajander, T., and Regan, L.
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
FEBS Journal, 272(1): 166-179. PDF

Magliery, T.J., Wilson, C.G.M., Pan, W., Mishler, D., Ghosh, I., Hamilton, A.D., and Regan L.
Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism.
Journal of the American Chemical Society, 127(1): 146-157. PDFSupplementary Information

2004

Wilson, C.G.M., Magliery, T.J., and Regan, L.
Detecting protein-protein interactions with GFP-fragment reassembly.
Nature Methods, 1(3): 255-262. PDFSupplementary FigureSupplementary Note

Magliery, T.J. and Regan, L.
Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif.
Journal of Molecular Biology, 343(3): 731-745. PDFSupplementary Information

Cortajarena, A.L., Kajander, T., Pan, W., Cocco, M., and Regan, L.
Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins.
Protein Engineering Design & Selection, 17(4): 399-409. PDF

Magliery, T.J. and Regan, L.
Library approaches to biophysical problems.
European Journal of Biochemistry, 271(9):1593-1594. PDF

Magliery, T.J. and Regan, L.
Combinatorial approaches to protein stability and structure.
European Journal of Biochemistry, 271(9): 1595-1608. PDF

Magliery, T.J. and 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, 17(1): 77-83. PDF

2003

D'Andrea, L.D. and Regan, L.
TPR proteins: the versatile helix.
Trends in Biochemical Sciences, 28(12): 655-662. PDF

Mayer, K.L., Earley, M.R., Gupta, S., Pichumani, K., Regan, L., and Stone, M.J.
Covariation in backbone motion throughout a small protein domain.
Nature Structural Biology, 10(11): 962-965. PDF

Main, E.R., Jackson, S.E., and Regan, L.
The folding and design of repeat proteins: reaching a consensus.
Current Opinion in Structural Biology, 13(4): 482-489. PDF

Regan, L. and Jackson, S.E.
Engineering and design. Protein design: theory and practice.
Current Opinion in Structural Biology, 13(4): 479-481. PDF

Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A.L., Carter, S.A.
A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.
Biophysical Journal, 85(2): 1135-1144. PDF

Main, E.R.G., Xiong, Y., Cocco, M.J., D'Andrea, L., and Regan, L.
Design of stable α-helical arrays from an idealized TPR motif.
Structure, 11(5): 497. PDF

Regan, L.
Molten globules move into action.
Proceedings of the National Academy of Sciences USA, 100(7): 3553-3554. PDF

Ramirez-Alvarado, M., Cocco, M.J., and Regan, L.
Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.
Protein Science, 12(3): 567-576. PDF

2002

Ramirez-Alvarado, M. and Regan, L.
Does the location of a mutation determine the ability to form amyloid fibrils?
Journal of Molecular Biology, 323(1): 17-22. PDF

2001

Marino, S.F., Shechner, D., and Regan, L.
'Morphs' (MRFs): metal-reversible folding domains for differential IgG binding.
Chemistry & Biology, 8(12): 1221-1229. PDF

Bishop, B., Koay, D.C., Sartorelli, A.C., and Regan, L.
Reengineering granulocyte colony-stimulating factor for enhanced stability.
Journal of Biological Chemistry, 276(36): 33465-33470. PDF

Stone, M.J., Gupta, S., Snyder, N., and 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(1): 185-186. PDF

Regan, L.
Engineering and design 2001: a design odyssey.
Current Opinion in Structural Biology, 11(4): 449. PDF

Regan, L.
Current genomic research: the proteins have it.
National Academy of Engineering: Sixth Annual Symposium on Frontiers of Engineering.
Washington, DC: National Academy Press. pp 54-61. PDF

2000

Willis, M.A., Bishop, B., Regan, L., and Brunger, A.T.
Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.
Structure, 8(12): 1319-1328. PDF

Ramirez-Alvarado, M., Merkel, J.S., and 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 USA, 97(16): 8979-8984. PDF

Merkel, J.S. and Regan, L.
Modulating protein folding rates in vivo and in vitro by side-chain interactions
between the parallel beta strands of green fluorescent protein.
Journal of Biological Chemistry, 275(38): 29200-29206. PDF

Dalal, S. and Regan, L.
Understanding the sequence determinants of conformational switching using protein design.
Protein Science, 9(9): 1651-1659. PDF

Seewald, M.J., Pichumani, K., Stowell, C., Tibbals, B.V., Regan, L., and Stone, M.J.
The role of backbone conformational heat capacity in protein stability:
temperature dependent dynamics of the B1 domain of Streptococcal protein G.
Protein Science, 9(6): 1177-1193. PDF

Balasubramanian, S., Schneider, T., Gerstein, M., and Regan, L.
Proteomics of Mycoplasma genitalium: identification and characterization
of unannotated and atypical proteins in a small model genome.
Nucleic Acids Research, 28(16): 3075-3082. PDF

Ghosh, I., Hamilton, A.D., and Regan, L.
Antiparallel leucine zipper-directed protein reassembly:
application to the green fluorscent protein.
Journal of the American Chemical Society, 122(23): 5658-5659. PDFSupporting Information

Lurio, L.B., Lumma, D., Sandy, A.R., Borthwick, M.A., Falus, P., Mochrie, S.G.J.,
Pelletier, J.-F., Sutton, M., Regan, L., Malik, A., Stephenson, G.B.
Absence of scaling for the intermediate scattering function of a hard-sphere suspension:
static and dynamic X-ray scattering from concentrated polystyrene latex spheres.
Physical Review Letters, 84(4): 785-788. PDF

1999

Regan, L.
Protein redesign.
Current Opinion in Structural Biology, 9(4): 494-499. PDF

Nagi, A.D., Anderson, K.S., and Regan, L.
Using loop length variants to dissect the folding pathway of a four-helix-bundle protein.
Journal of Molecular Biology, 286(1): 257-265. PDF

Merkel, J.S., Sturtevant, J.M., and Regan, L.
Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings.
Structure, 7(11): 1333-1343. PDF

Marino, S.F. and Regan, L.
Secondary ligands enhance affinity at a designed metal-binding site.
Chemistry & Biology, 6(9): 649-655. PDF

Prodromou, C., Siligardi, G., O'Brien, R., Woolfson, D.N., Regan, L.,
Panaretou, B., Ladbury, J.E., Piper, P.W., and Pearl, L.H.
Regulation of Hsp90 ATPase activity by tetratricopeptiderepeat(TPR)-domain co-chaperones.
EMBO Journal, 18(3): 754-762. PDF

Ma, Y., Cunningham, M.E., Wang, X., Ghosh, I., Regan, L., Longely, B.J.
Inhibition of spontaneous receptor phosphorylation by residues in a putatitve alpha-helix
in the KIT intracellular juxtamembrane region.
Journal of Biological Chemistry, 274(19): 13399-13402. PDF

1998

Regan, L. and Wells, J.
Engineering and design: recent adventures in molecular design.
Current Opinion in Structural Biology, 8(4): 441-442. PDF

Klemba, M.W., Munson, M., and Regan, L.
De novo design of protein structure and function.
Proteins: Analysis and Design. ed. Angeletti, R.H. Academic Press.

Regan, L.
Proteins to order?
Structure, 6(1): 1-4. PDF

Merkel, J.S. and Regan, L.
Aromatic rescue of glycine in beta sheets.
Folding & Design, 3(6): 449-455. PDF

Farinas, E. and Regan, L.
The de novo design of a rubredoxin-like Fe site.
Protein Science, 7(9): 1939-1946. PDF

1997

Smith, C.K. and Regan, L.
Construction and design of β-sheets.
Accounts of Chemical Research, 30(4): 153-161. PDF

Regan, L.
Engineering metal binding site in proteins.
Advances in Molecular and Cell Biology, 22: 51-80.
ed. Allewell, N. and Woodward, C. 22. Elsevier.

Regan, L.
Helix is a helix is a helix?
Proceedings of the National Academy of Sciences USA, 94(7): 2796-2797. PDF

Nagi, A.D. and Regan, L.
An inverse correlation between loop length and stability in a four-helix-bundle protein.
Folding & Design, 2(1): 67-75. PDF

Munson, M., Anderson, K.S., and Regan, L.
Speeding up protein folding: mutations that increase the rate at which Rop folds
and unfolds by over four orders of magnitude.
Folding & Design, 2(1): 77-87. PDF

Dalal, S., Balasubramanian, S., and Regan, L.
Transmuting alpha helices and beta sheets.
Folding & Design, 2(5): R71-R79. PDF

Dalal, S., Balasubramanian, S., and Regan, L.
Protein alchemy: changing β-sheet into α-helix.
Nature Structural Biology, 4(7): 548-552. PDF

1996

Smith, C.K., Bu, Z., Anderson, K.S., Sturtevant, J.M., Engelman, D.M., and Regan, L.
Surface point mutations that significantly alter the structure and stability of a protein's denatured state.
Protein Science, 5(10): 2009-2019. PDF

Predki, P.F., Agrawal, V., Brunger, A.T., and Regan, L.
Amino-acid substitutions in a surface turn modulate protein stability.
Nature Structural Biology, 3(1): 54-58. PDF

Munson, M., Balasubramanian, S., Fleming, K.G., Nagi, A.D., O'Brien, R., Sturtevant, J.M., and Regan, L.
What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties.
Protein Science, 5(8): 1584-1593. PDF

1995

Smith, C.K., Munson, M., and Regan, L.
Studying α-helix and β-sheet formation in small proteins.
Techniques in Protein Chemistry, 6: 323-332.

Smith, C.K. and Regan, L.
Guidelines for protein design: the energetics of β sheet side chain interactions.
Science, 270(5238): 980-982. PDF

Regan, L.
Protein design: novel metal-binding sites.
Trends in Biochemical Sciences, 20(7): 280-285. PDF

Predki, P.F. and Regan, L.
Redesigning the topology of a four-helix-bundle protein: monomeric Rop.
Biochemistry, 34(31): 9834-9839. PDF

Predki, P.F., Nayak, L.M., Gottlieb, M.B., and Regan, L.
Dissecting RNA-protein interactions: RNA-RNA recognition by Rop.
Cell, 80(1): 41-50. PDF

Klemba, M. and Regan, L.
Characterization of metal binding by a designed protein:
single ligand substitutions at a tetrahedral Cys2His2 site.
Biochemistry, 34(31): 10094-10100. PDF

Klemba, M., Gardner, K.H., Marino, S., Clarke, N.D., and Regan, L.
Novel metal-binding proteins by design.
Nature Structural Biology, 2(5): 368-373. PDF

1994

Smith, C.K., Withka, J.M., and Regan, L.
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
Biochemistry, 33(18): 5510-5517. PDF

Regan, L., Rockwell, A., Wasserman, Z., and DeGrado, W.
Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.
Protein Science, 3(12): 2419-2427. PDF

Regan, L.
Protein structure. Born to be beta.
Current Biology, 4(7): 656-658. PDF

Munson, M., Predki, P.F., and Regan, L.
ColE1-compatible vectors for high-level expression of cloned DNAs from the T7 promoter.
Gene, 144(1): 59-62. PDF

Munson, M., O'Brien, R., Sturtevant, J.M., and Regan, L.
Redesigning the hydrophobic core of a four-helix-bundle protein.
Protein Science, 3(11): 2015-2022. PDF

1993

Regan, L.
What determines where alpha-helices begin and end?
Proceedings of the National Academy of Sciences USA 90(23): 10907-10908. PDF

Regan, L.
The design of metal-binding sites in proteins.
Annual Review of Biophysics and Biomolecular Structure, 22: 257-287. PDF

1991

Marqusee, S. and Regan, L.
Deconstructing protein structure.
Current Biology, 1(4): 207-208. PDF

Regan, L.
Protein design.
Current Opinion in Biotechnology, 2(4): 544-550. PubMed

1990

Regan, L. and Clarke, N.
A tetrahedral Zn(II)-binding site introduced into a designed protein.
Biochemistry29(49): 10878-10883. PDF

Regan, L., Ho, S.P., Wasserman, Z., and Degrado, W.F.
Helical proteins: de novo design.
Protein Folding: Deciphering the Second Half of the Genetic Code.
ed. Gierasch, L.M. and King, J. Washington, D.C.: AAAS.

1988

Regan, L. and DeGrado, W.F.
Characterization of a helical protein designed from first principles.
Science, 241(4868): 976-978. PDF

Regan, L., Buxbaum, L., Hill, K., and Schimmel, P.
Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion.
Journal of Biological Chemistry, 263(35): 18598-18600. PDF

Frederick, C.A., Wang, A.H., Rich, A., Regan, L., and Schimmel, P.
Crystallization of a small fragment of an aminoacyl tRNA synthetase.
Journal of Molecular Biology, 203(2): 521-522. PDF

1987

Regan, L. and Schimmel, P.
Selection of aminoacyl tRNA synthetases with enhanced catalytic activity.
UCLA Symposia on Molecular & Cellular Biology, 69: 293.

Regan, L., Bowie, J., and Schimmel, P.
Polypeptide sequences essential for RNA recognition by an enzyme.
Science, 235(4796): 1651-1653. PDF

DeGrado, W.F., Regan, L., and Ho, S.P.
The design of a four-helix bundle protein.
Cold Spring Harbor Symposia on Quantitative Biology, 52: 521-526. PubMed

DeGrado, W.F., Ho, S., Wasserman, Z., and Regan, L.
1987. The design and characterization of four-helix-bundle proteins.
UCLA Symposiua on Molecular & Cellular Biology, 69: 429.

1986

Regan, L., Dignam, J.D., and Schimmel, P.
A bacterial and silkworm aminoacyl-tRNA synthetase have a common epitope
which maps to the catalytic domain of each.
Journal of Biological Chemistry, 261(12): 5241-5244. PDF

1985

Jasin, M., Regan, L., and Schimmel, P.
Two mutations in the dispensable part of alanine tRNA synthetase
which affect the catalytic activity.
Journal of Biological Chemistry, 260(4): 2226-2230. PDF

1984

Schimmel, P., Jasin, M., and Regan, L.
Size polymorphism and the structure of aminoacyl-tRNA synthetases.
Federation Proceedings, 43(15): 2987-2990. PubMed

Jasin, M., Regan, L., and Schimmel, P.
Dispensable pieces of an aminoacyl tRNA synthetase which activate the catalytic site.
Cell, 36(4): 1089-1095. PubMed

1983

Jasin, M., Regan, L., and Schimmel, P.
Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase.
Nature, 306(5942): 441-447. PubMed

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