A Buried Polar Interaction Imparts Structural Uniqueness in a Designed Heterodimeric Coiled Coil

Some Factors in the Interpretation of Protein Denaturation

Kauzmann, W. (1959) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,880 · see citing works

Predicting coiled coils from protein sequences.

Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953 · see citing works

Dominant forces in protein folding

Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,824 · see citing works

Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *

Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438 · see citing works

[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

Pace, C. N. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,267 · see citing works

Protein denaturation. C. Theoretical models for the mechanism of denaturation.

Tanford, C. (1970) · PubMed · Cited by 1,546 · see citing works

A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants

Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · see citing works

X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil

O’Shea, E. K., Klemm, J. D., Kim, P. S., & Alber, T. (1991) · Science · doi:10.1126/science.1948029 · Cited by 1,442 · see citing works

The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

Kuwajima, K. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340060202 · Cited by 1,440 · see citing works

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Englander, S. W., & Kallenbach, N. R. (1983) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005217 · Cited by 1,359 · see citing works

Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe

Semisotnov, G. V., Родионова, Н. А., RAZGULYAEV, O. I., Uversky, V. N., Gripas’, A. F., & Gilmanshin, R. (1991) · Biopolymers · doi:10.1002/bip.360310111 · Cited by 1,270 · see citing works

The nature of the accessible and buried surfaces in proteins

Chothia, C. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90191-1 · Cited by 1,165 · see citing works

Ion-pairs in proteins

Barlow, D. J., & Thornton, J. M. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80079-5 · Cited by 712 · see citing works

Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure

McLachlan, A., & Stewart, M. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80119-7 · Cited by 664 · see citing works

Do salt bridges stabilize proteins? A continuum electrostatic analysis

Hendsch, Z. S., & Tidor, B. (1994) · Protein Science · doi:10.1002/pro.5560030206 · Cited by 638 · see citing works

[3] The preparation of guanidine hydrochloride

Nozaki, Y. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(72)26005-0 · Cited by 540 · see citing works

Crystal structure of an isoleucine-zipper trimer

Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472 · see citing works

Peptide ‘Velcro’: Design of a heterodimeric coiled coil

O’Shea, E. K., Lumb, K. J., & Kim, P. S. (1993) · Current Biology · doi:10.1016/0960-9822(93)90063-t · Cited by 437 · see citing works

Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

O'Shea, E. K., Rutkowski, R., & Kim, P. S. (1992) · Cell · doi:10.1016/0092-8674(92)90145-3 · Cited by 422 · see citing works

Conformational states in .beta.-lactamase: molten-globule states at acidic and alkaline pH with high salt

Goto, Y., & Fink, A. L. (1989) · Biochemistry · doi:10.1021/bi00429a004 · Cited by 408 · see citing works

Are buried salt bridges important for protein stability and conformational specificity?

Waldburger, C. D., Schildbach, J. F., & Sauer, R. T. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0295-122 · Cited by 324 · see citing works

Protein stability parameters measured by hydrogen exchange

Bai, Y., Milne, J. S., Mayne, L. C., & Englander, S. W. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340200103 · Cited by 305 · see citing works

Crystal Structure of a Synthetic Triple-Stranded α-Helical Bundle

Lovejoy, B., Choe, S., Cascio, D., McRorie, D. K., DeGrado, W. F., & Eisenberg, D. S. (1993) · Science · doi:10.1126/science.8446897 · Cited by 288 · see citing works

Metal Ion-Dependent Modulation of the Dynamics of a Designed Protein

Handel, T. M., Williams, S. A., & DeGrado, W. F. (1993) · Science · doi:10.1126/science.8346440 · Cited by 253 · see citing works

Tropomyosin: Amino Acid Sequence and Coiled-Coil StructurePreprint

Hodges, R. S., Sodek, J., Smillie, L. B., & Jurasek, L. (1973) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1973.037.01.040 · Cited by 196 · see citing works

The Role of Interhelical Ionic Interactions in Controlling Protein Folding and Stability

Zhou, N., Kay, C. M., & Hodges, R. S. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1250 · Cited by 194 · see citing works

Coiled-coils in α-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins

Parry, D. A. D. (1982) · Bioscience Reports · doi:10.1007/bf01122170 · Cited by 190 · see citing works

Packing and hydrophobicity effects on protein folding and stability: Effects of β ‐branched amino acids, valine and isoleucine, on the formation and stability of two‐stranded α ‐helical coiled coils/leucine zippers

Zhu, B., Zhou, M. E., Kay, C. M., & Hodges, R. S. (1993) · Protein Science · doi:10.1002/pro.5560020310 · Cited by 187 · see citing works

Guanidinium Chloride Induction of Partial Unfolding in Amide Proton Exchange in RNase A

Mayo, S. L., & Baldwin, R. L. (1993) · Science · doi:10.1126/science.8235609 · Cited by 181 · see citing works

Structural features in the heptad substructure and longer range repeats of two-stranded α-fibrous proteins

Conway, J. F., & Parry, D. A. D. (1990) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(90)90023-4 · Cited by 167 · see citing works

Controlled formation of model homo- and heterodimer coiled coil polypeptides

Graddis, T. J., Myszka, D. G., & Chaiken, I. M. (1993) · Biochemistry · doi:10.1021/bi00210a015 · Cited by 153 · see citing works

α-Helical Coiled Coils: More Facts and Better Predictions

Cohen, C., & Parry, D. A. D. (1994) · Science · doi:10.1126/science.8290957 · Cited by 153 · see citing works

A general method for facilitating heterodimeric pairing between two proteins: application to expression of alpha and beta T-cell receptor extracellular segments.

Chang, H. C., Bao, Z., Yao, Y., Tse, A. G. D., Goyarts, E. C., Madsen, M., Kawasaki, E. S., Brauer, P. P., Sacchettini, J. C., & Nathenson, S. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.24.11408 · Cited by 148 · see citing works

De novo protein design: from molten globules to native-like states

Betz, S. F., Raleigh, D. P., & DeGrado, W. F. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90090-8 · Cited by 146 · see citing works

On the environment of ionizable groups in globular proteins

Rashin, A. A., & Honig, B. H. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90394-2 · Cited by 146 · see citing works

Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper.

Lumb, K., & Kim, P. S. (1995) · Science · doi:10.1126/science.7716550 · Cited by 145 · see citing works

Betadoublet: de novo design, synthesis, and characterization of a beta-sandwich protein.

Quinn, T. P., Tweedy, N. B., Williams, R. W., Richardson, J. S., & Richardson, D. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.8747 · Cited by 142 · see citing works

Redesigning the hydrophobic core of a four‐helix‐bundle protein

Munson, M., Regan, L., O’Brien, R., & Sturtevant, J. M. (1994) · Protein Science · doi:10.1002/pro.5560031114 · Cited by 124 · see citing works

Crystal Structure of α 1 : Implications for Protein Design

Hill, C. P., Anderson, D. H., Wesson, L., DeGrado, W. F., & Eisenberg, D. S. (1990) · Science · doi:10.1126/science.2382133 · Cited by 122 · see citing works

Protein Folding: Solid evidence for molten globules

Dobson, C. M. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00141-x · Cited by 117 · see citing works

Subdomain Folding of the Coiled Coil Leucine Zipper from the bZIP Transcriptional Activator GCN4

Lumb, K. J., Carr, C. M., & Kim, P. S. (1994) · Biochemistry · doi:10.1021/bi00189a042 · Cited by 112 · see citing works

[22] Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange

Röder, H. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)76024-9 · Cited by 105 · see citing works

A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state

Raleigh, D. P., & DeGrado, W. F. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00051a061 · Cited by 79 · see citing works

Hydrogen exchange in unligated and ligated staphylococcal nuclease

Loh, S. N., Prehoda, K. E., Wang, J., & Markley, J. L. (1993) · Biochemistry · doi:10.1021/bi00092a011 · Cited by 76 · see citing works

De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates.

Fezoui, Y., Weaver, D. L., & Osterhout, J. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.9.3675 · Cited by 72 · see citing works

Design of two-stranded and three-stranded coiled-coil peptides

Betz, S., Fairman, R., O'Neil, K., Lear, J., & DeGrado, W. F. (1995) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1995.0048 · Cited by 66 · see citing works

De novo protein design: what are we learning?

DeGrado, W. F., Raleigh, D. P., & Handel, T. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90095-b · Cited by 58 · see citing works

Synthesis and properties of the peptide corresponding to the mutant form of the leucine zipper of the transcriptional activator GCN4 from yeast

Potekhin, S. A., Medvedkin, V. N., KASHPAROV, I. A., & Venyaminov, S. Y. (1994) · Protein Engineering Design and Selection · doi:10.1093/protein/7.9.1097 · Cited by 48 · see citing works

The Basic-Region Leucine-Zipper Family of DNA Binding Proteins

Hu, J. C., & Sauer, R. T. (1992) · Nucleic acids and molecular biology · doi:10.1007/978-3-642-77356-3_5 · Cited by 43 · see citing works

Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to GCN4 leucine zipper.

John, M., Briand, J., Schnarr, M., & Granger‐Schnarr, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34000-0 · Cited by 38 · see citing works

Characteristics of a de novo designed protein

Tanaka, T., Kimura, H., Hayashi, M., Fujiyoshi, Y., Fukuhara, K.-I., & Nakamura, H. (1994) · Protein Science · doi:10.1002/pro.5560030306 · Cited by 30 · see citing works

Cooperative deformation of a de novo designed protein

Tanaka, T., Kuroda, Y., Kimura, H., Kidokoro, S., & Nakamura, H. (1994) · Protein Engineering Design and Selection · doi:10.1093/protein/7.8.969 · Cited by 29 · see citing works

Mutational analysis of protein stability

Sauer, R. T., & Lim, W. A. (1992) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(92)90175-7 · Cited by 21 · see citing works

Reversible Hydrogels from Self-Assembling Artificial Proteins

Petka, W. A., Harden, J. L., McGrath, K. P., Wirtz, D., & Tirrell, D. A. (1998) · Science · doi:10.1126/science.281.5375.389 · Cited by 1,075 · see citing works

Adaptable Hydrogel Networks with Reversible Linkages for Tissue Engineering

Wang, H., & Heilshorn, S. C. (2015) · Advanced Materials · doi:10.1002/adma.201501558 · Cited by 723 · see citing works

Foldamers with Heterogeneous Backbones

Horne, W. S., & Gellman, S. H. (2008) · Accounts of Chemical Research · doi:10.1021/ar800009n · Cited by 689 · see citing works

The Design of Coiled-Coil Structures and Assemblies

Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585 · see citing works

THE TWO-COMPONENT SIGNALING PATHWAY OF BACTERIAL CHEMOTAXIS: A Molecular View of Signal Transduction by Receptors, Kinases, and Adaptation Enzymes

Falke, J. J., Bass, R. B., Butler, S. L., Chervitz, S. A., & Danielson, M. A. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.457 · Cited by 534 · see citing works

Atomic structure of a thermostable subdomain of HIV-1 gp41

Tan, K., Liu, J.-H., Wang, J., Shen, S. S., & Lu, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12303 · Cited by 532 · see citing works

An Orientation-dependent Hydrogen Bonding Potential Improves Prediction of Specificity and Structure for Proteins and Protein–Protein Complexes

Kortemme, T., Morozov, A. V., & Baker, D. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00021-4 · Cited by 516 · see citing works

Peptidic foldamers: ramping up diversity

Martinek, T. A., & Fülöp, F. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15097a · Cited by 483 · see citing works

Context-dependent secondary structure formation of a designed protein sequence

Minor, D. L., & Kim, P. S. (1996) · Nature · doi:10.1038/380730a0 · Cited by 393 · see citing works

Crystal Structure of the Ebola Virus Membrane Fusion Subunit, GP2, from the Envelope Glycoprotein Ectodomain

Weissenhorn, W., Carfı́, A., Lee, K.-H., Skehel, J. J., & Wiley, D. C. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80159-8 · Cited by 390 · see citing works

SOCKET: a program for identifying and analysing coiled-coil motifs within protein structures11Edited by J. Thornton

Walshaw, J., & Woolfson, D. N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4545 · Cited by 357 · see citing works

Protein oligomerization: How and why

Ali, M. H., & Imperiali, B. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.05.037 · Cited by 349 · see citing works

Retrovirus envelope domain at 1.7 Å resolution

Fass, D., Harrison, S. C., & Kim, P. S. (1996) · Nature Structural Biology · doi:10.1038/nsb0596-465 · Cited by 312 · see citing works

De novo design of protein homo-oligomers with modular hydrogen-bond network–mediated specificity

Boyken, S. E., Chen, Z., Groves, B., Langan, R. A., Oberdorfer, G., Ford, A., Gilmore, J. M., Xu, C., DiMaio, F., Pereira, J. H., et al. (2016) · Science · doi:10.1126/science.aad8865 · Cited by 298 · see citing works

Structure-derived potentials and protein simulations

Jernigan, R. L., & Bahar, İ. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80075-3 · Cited by 275 · see citing works

NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly

Baek, K., Krist, D. T., Prabu, J. R., Hill, S., Klügel, M., Neumaier, L.-M., von Gronau, S., Kleiger, G., & Schulman, B. A. (2020) · Nature · doi:10.1038/s41586-020-2000-y · Cited by 270 · see citing works

A Basis Set of <i>de Novo</i> Coiled-Coil Peptide Oligomers for Rational Protein Design and Synthetic Biology

Fletcher, J. M., Boyle, A. L., Bruning, M., Bartlett, G. J., Vincent, T. L., Zaccai, N. R., Armstrong, C. T., Bromley, E. H. C., Booth, P. J., Brady, R. L., et al. (2012) · ACS Synthetic Biology · doi:10.1021/sb300028q · Cited by 262 · see citing works

Engineering the morphology of a self-assembling protein fibre

Ryadnov, M. G., & Woolfson, D. N. (2003) · Nature Materials · doi:10.1038/nmat885 · Cited by 255 · see citing works

Mei-S332, a drosophila protein required for sister-chromatid cohesion, can localize to meiotic centromere regions

Kerrebrock, A. W., Moore, D., Wu, J. S., & Orr‐Weaver, T. L. (1995) · Cell · doi:10.1016/0092-8674(95)90166-3 · Cited by 250 · see citing works

The K domain mediates heterodimerization of the Arabidopsis floral organ identity proteins, APETALA3 and PISTILLATA

Yang, Y., Fanning, L. R., & Jack, T. P. (2003) · The Plant Journal · doi:10.1046/j.0960-7412.2003.01473.x · Cited by 249 · see citing works

Effects of side-chain characteristics on stability and oligomerization state of a de Novo -designed model coiled-coil: 20 amino acid substitutions in position “d” 1 1Edited by P. E. Wright

Tripet, B., Wagschal, K. C., Lavigne, P., Mant, C. T., & Hodges, R. S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3866 · Cited by 241 · see citing works

Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain

Tao, Y. J., Strelkov, S. V., Mesyanzhinov, V. V., & Rossmann, M. G. (1997) · Structure · doi:10.1016/s0969-2126(97)00233-5 · Cited by 224 · see citing works

Peptide and Protein Building Blocks for Synthetic Biology: From Programming Biomolecules to Self-Organized Biomolecular Systems

Bromley, E. H. C., Channon, K., Moutevelis, E., & Woolfson, D. N. (2008) · ACS Chemical Biology · doi:10.1021/cb700249v · Cited by 216 · see citing works

Buried polar residues and structural specificity in the GCN4 leucine zipper

Gonzalez, L. C., Woolfson, D. N., & Alber, T. (1996) · Nature Structural Biology · doi:10.1038/nsb1296-1011 · Cited by 215 · see citing works

Automated protein crystal structure determination using elves

Holton, J. M., & Alber, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306241101 · Cited by 208 · see citing works

Multifunctional Materials through Modular Protein Engineering

DiMarco, R. L., & Heilshorn, S. C. (2012) · Advanced Materials · doi:10.1002/adma.201200051 · Cited by 207 · see citing works

Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation correct?

Skolnick, J., Godzik, A., Jaroszewski, L., & Koliński, A. (1997) · Protein Science · doi:10.1002/pro.5560060317 · Cited by 201 · see citing works

Aromatic interactions in peptides: Impact on structure and function

Waters, M. L. (2004) · Biopolymers · doi:10.1002/bip.20144 · Cited by 186 · see citing works

Energy Functions for Protein Design: Adjustment with Protein–Protein Complex Affinities, Models for the Unfolded State, and Negative Design of Solubility and Specificity

Pokala, N., & Handel, T. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.019 · Cited by 184 · see citing works

Design of three-dimensional domain-swapped dimers and fibrous oligomers

Ogihara, N. L., Ghirlanda, G., Bryson, J. W., Gingery, M., DeGrado, W. F., & Eisenberg, D. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1404 · Cited by 183 · see citing works

Programmable design of orthogonal protein heterodimers

Chen, Z., Boyken, S. E., Jia, M., Büsch, F., Flores‐Solis, D., Bick, M. J., Lu, P., VanAernum, Z. L., Sahasrabuddhe, A., Langan, R. A., et al. (2018) · Nature · doi:10.1038/s41586-018-0802-y · Cited by 171 · see citing works

The role of position a in determining the stability and oligomerization state of α‐helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins

Wagschal, K. C., Tripet, B., Mant, C. T., Hodges, R. S., & Lavigne, P. (1999) · Protein Science · doi:10.1110/ps.8.11.2312 · Cited by 169 · see citing works

A Buried Polar Interaction Can Direct the Relative Orientation of Helices in a Coiled Coil

Oakley, M. G., & Kim, P. S. (1998) · Biochemistry · doi:10.1021/bi981269m · Cited by 168 · see citing works

An in vivo library-versus-library selection of optimized protein–protein interactions

Pelletier, J. N., Arndt, K. M., Plückthun, A., & Michnick, S. W. (1999) · Nature Biotechnology · doi:10.1038/10897 · Cited by 166 · see citing works

Sequence space, folding and protein design

Cordes, M. H. J., Davidson, A. R., & Sauer, R. T. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80088-1 · Cited by 154 · see citing works

Cooperatively folded proteins in random sequence libraries

Davidson, A. R., Lumb, K. J., & Sauer, R. T. (1995) · Nature Structural Biology · doi:10.1038/nsb1095-856 · Cited by 152 · see citing works

Structure-Function Relationships in a Type I Antifreeze Polypeptide

Zhang, W., & Laursen, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34806 · Cited by 150 · see citing works

The coiled-coil domain of Stat3 is essential for its SH2 domain-mediated receptor binding and subsequent activation induced by epidermal growth factor and interleukin-6

Zhang, T., Kee, W. H., Seow, K. T., Fung, W., & Cao, X. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7132-7139.2000 · Cited by 150 · see citing works

Sophistication of foldamer form and function in vitro and in vivo

Bautista, A. D., Craig, C. J., Harker, E. A., & Schepartz, A. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.09.009 · Cited by 149 · see citing works

Transmembrane Structure of an Inwardly Rectifying Potassium Channel

Minor, D. L., Masseling, S., Jan, Y. N., & Jan, L. Y. (1999) · Cell · doi:10.1016/s0092-8674(00)80597-8 · Cited by 148 · see citing works

Aromatic–aromatic interactions in and around α-helices

Bhattacharyya, R., Samanta, U., & Chakrabarti, P. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.2.91 · Cited by 146 · see citing works

The crystal structure of the designed trimeric coiled coil coil‐VaLd: Implications for engineering crystals and supramolecular assemblies

Ogihara, N. L., Weiss, M. S., Eisenberg, D. S., & DeGrado, W. F. (1997) · Protein Science · doi:10.1002/pro.5560060109 · Cited by 144 · see citing works

New currency for old rope: from coiled-coil assemblies to α-helical barrels

Woolfson, D. N., Bartlett, G. J., Bruning, M., & Thomson, A. R. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.03.002 · Cited by 138 · see citing works

Programmable protein circuit design

Chen, Z., & Elowitz, M. B. (2021) · Cell · doi:10.1016/j.cell.2021.03.007 · Cited by 137 · see citing works

From coiled coils to small globular proteins: Design of a native‐like three‐helix bundle

Bryson, J. W., Desjarlais, J. R., Handel, T. M., & DeGrado, W. F. (1998) · Protein Science · doi:10.1002/pro.5560070617 · Cited by 134 · see citing works

The Curious Case of Arenavirus Entry, and Its Inhibition

Nunberg, J. H., & York, J. (2012) · Viruses · doi:10.3390/v4010083 · Cited by 132 · see citing works

Genetically engineered polymers: status and prospects for controlled release

Haider, M. A., Megeed, Z., & Ghandehari, H. (2004) · Journal of Controlled Release · doi:10.1016/j.jconrel.2003.11.011 · Cited by 132 · see citing works

Electrostatics in computational protein design

Vizcarra, C. L., & Mayo, S. L. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.10.014 · Cited by 123 · see citing works

Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding

Hendsch, Z. S., & Tidor, B. (1999) · Protein Science · doi:10.1110/ps.8.7.1381 · Cited by 123 · see citing works

Tanford–Kirkwood electrostatics for protein modeling

Havranek, J. J., & Harbury, P. B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11145 · Cited by 120 · see citing works

The Crystal Structure of the SIV gp41 Ectodomain at 1.47 Å Resolution

Yang, Z., Mueser, T. C., Kaufman, J. D., Stahl, S. J., Wingfield, P. T., & Hyde, C. C. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4116 · Cited by 120 · see citing works

Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

Javanbakht, H., Yuan, W., Yeung, D. F., Song, B., Diaz‐Griffero, F., Li, Y., Li, X., Stremlau, M. H., & Sodroski, J. (2006) · Virology · doi:10.1016/j.virol.2006.05.017 · Cited by 119 · see citing works

A specific hydrophobic core in the α-lactalbumin molten globule

Wu, L. C., & Kim, P. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1825 · Cited by 116 · see citing works

Self-Assembling Peptide-Polymer Hydrogels Designed From the Coiled Coil Region of Fibrin

Jing, P., Rudra, J. S., Herr, A. B., & Collier, J. H. (2008) · Biomacromolecules · doi:10.1021/bm800459v · Cited by 112 · see citing works

Predicting specificity in bZIP coiled-coil protein interactions

Fong, J. H., Keating, A. E., & Singh, M. (2004) · Genome biology · doi:10.1186/gb-2004-5-2-r11 · Cited by 111 · see citing works

Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper

Lavigne, P., Crump, M. P., Gagné, S. M., Hodges, R. S., Kay, C. M., & Sykes, B. D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1914 · Cited by 109 · see citing works

De novo design of α-helical coiled coils and bundles: models for the development of protein-design principles

Kohn, W. D. (1998) · Trends in biotechnology · doi:10.1016/s0167-7799(98)01212-8 · Cited by 108 · see citing works

Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils

Woolfson, D. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104579 · Cited by 106 · see citing works

The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H+ channel Hv1

Fujiwara, Y., Kurokawa, T., Takeshita, K., Kobayashi, M. S., Okochi, Y., Nakagawa, A., & Okamura, Y. (2012) · Nature Communications · doi:10.1038/ncomms1823 · Cited by 105 · see citing works

A heterodimeric coiled-coil peptide pair selected in vivo from a designed library- versus -library ensemble 1 1Edited by A. R. Fersht

Arndt, K. M., Pelletier, J. N., Müller, K. M., Alber, T., Michnick, S. W., & Plückthun, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3352 · Cited by 104 · see citing works

Molecular Architecture of the Transport Channel of the Nuclear Pore Complex

Solmaz, S. R., Chauhan, R., Blobel, G., & Melčák, I. (2011) · Cell · doi:10.1016/j.cell.2011.09.034 · Cited by 102 · see citing works

Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues

Eckert, D. M., Malashkevich, V. N., & Kim, P. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2214 · Cited by 101 · see citing works

High Resolution NMR Solution Structure of the Leucine Zipper Domain of the c-Jun Homodimer

Junius, F. K., O’Donoghue, S. I., Nilges, M., Weiss, A. S., & King, G. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13663 · Cited by 97 · see citing works

Engineering Increased Stability into Self‐Assembled Protein Fibers

Smith, A. M., Banwell, E. F., Edwards, W. R., Pandya, M. J., & Woolfson, D. N. (2006) · Advanced Functional Materials · doi:10.1002/adfm.200500568 · Cited by 96 · see citing works

De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints

Smock, R. G., Yadid, I., Dym, O., Clarke, J., & Tawfik, D. S. (2016) · Cell · doi:10.1016/j.cell.2015.12.024 · Cited by 95 · see citing works

Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in α-helical coiled-coils

Kohn, W. D., Kay, C. M., & Hodges, R. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2125 · Cited by 95 · see citing works

Toward β-Amino Acid Proteins: Design, Synthesis, and Characterization of a Fifteen Kilodalton β-Peptide Tetramer

Petersson, E. J., & Schepartz, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja077245x · Cited by 92 · see citing works

Buried asparagines determine the dimerization specificities of leucine zipper mutants

Zeng, X., Herndon, A., & Hu, J. C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3673 · Cited by 92 · see citing works

Crystal structure of tetranectin, a trimeric plasminogen‐binding protein with an α‐helical coiled coil

Nielsen, B. B., Kastrup, J. S., Rasmussen, H. B., Holtet, T. L., Graversen, J. H., Etzerodt, M., Thøgersen, H. C., & Larsen, I. K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00664-9 · Cited by 90 · see citing works

Surface salt bridges stabilize the GCN4 leucine zipper

Spek, E. J., Bui, A. H., Lu, M., & Kallenbach, N. R. (1998) · Protein Science · doi:10.1002/pro.5560071121 · Cited by 90 · see citing works

Effects of salt bridges on protein structure and design

Sindelar, C. V., Hendsch, Z. S., & Tidor, B. (1998) · Protein Science · doi:10.1002/pro.5560070906 · Cited by 89 · see citing works

Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism

Gonzalez, L. C., Brown, R. A., Richardson, D., & Alber, T. (1996) · Nature Structural Biology · doi:10.1038/nsb1296-1002 · Cited by 89 · see citing works

Energy functions for protein design I: Efficient and accurate continuum electrostatics and solvation

Pokala, N., & Handel, T. M. (2004) · Protein Science · doi:10.1110/ps.03486104 · Cited by 88 · see citing works

Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils

Keating, A. E., Malashkevich, V. N., Tidor, B., & Kim, P. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261563398 · Cited by 86 · see citing works

De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coils 1 1Edited by P. Wright

Wagschal, K. C., Tripet, B., & Hodges, R. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2284 · Cited by 85 · see citing works

Rational design of a nanoscale helical scaffold derived from self-assembly of a dimeric coiled coil motif

Zimenkov, Y., Conticello, V. P., Guo, L., & Thiyagarajan, P. (2004) · Tetrahedron · doi:10.1016/j.tet.2004.06.068 · Cited by 83 · see citing works

Molecular Characterization of tol, a Mediator of Mating-Type-Associated Vegetative Incompatibility in Neurospora crassa

Shiu, P., & Glass, N. L. (1999) · Genetics · doi:10.1093/genetics/151.2.545 · Cited by 82 · see citing works

Peptide-based supramolecular vaccine systems

O’Neill, C. L., Shrimali, P. C., Clapacs, Z., Files, M. A., & Rudra, J. S. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.05.003 · Cited by 80 · see citing works

Redesign of a Four-helix Bundle Protein by Phage Display Coupled with Proteolysis and Structural Characterization by NMR and X-ray Crystallography

Chu, R., Takei, J., Knowlton, J. R., Andrykovitch, M., Pei, W., Kajava, A. V., Steinbach, P. J., Ji, X., & Bai, Y. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00884-7 · Cited by 80 · see citing works

Preferred side-chain constellations at antiparallel coiled-coil interfaces

Hadley, E. B., Testa, O. D., Woolfson, D. N., & Gellman, S. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709068105 · Cited by 79 · see citing works

Potential Functions for Hydrogen Bonds in Protein Structure Prediction and Design

Morozov, A. V., & Kortemme, T. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(05)72001-5 · Cited by 78 · see citing works

A new hydrogen-bonding potential for the design of protein-RNA interactions predicts specific contacts and discriminates decoys

Chen, Y. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh785 · Cited by 78 · see citing works

Achieving stability and conformational specificity in designed proteins via binary patterning11Edited by C. R. Matthews

Marshall, S. A., & Mayo, S. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4319 · Cited by 77 · see citing works

pH-induced folding of an apoptotic coiled coil

Dutta, K., Alexandrov, A., Huang, H., & Pascal, S. M. (2001) · Protein Science · doi:10.1110/ps.28801 · Cited by 76 · see citing works

Polymorphisms in fibronectin binding protein A of Staphylococcus aureus are associated with infection of cardiovascular devices

Lower, S. K., Lamlertthon, S., Casillas-Ituarte, N. N., Lins, R. D., Yongsunthon, R., Taylor, E. S., DiBartola, A. C., Edmonson, C. A., McIntyre, L. M., Reller, L. B., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109071108 · Cited by 75 · see citing works

Synthesis and thermodynamic characterization of self-sorting coiled coils

Bilgiçer, B., & Kumar, K. (2002) · Tetrahedron · doi:10.1016/s0040-4020(02)00260-0 · Cited by 74 · see citing works

Coiled Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled Coils Reveal Configurational Sensitivity to a Single Solvent-Exposed Amino Acid Substitution,

Yadav, M. K., Leman, L. J., Price, D. J., Brooks, C. L., Stout, C. D., & Ghadiri, M. R. (2006) · Biochemistry · doi:10.1021/bi060092q · Cited by 74 · see citing works

A Designed Buried Salt Bridge in a Heterodimeric Coiled Coil

Schneider, J. P., Lear, J. D., & DeGrado, W. F. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970493g · Cited by 74 · see citing works

Peptide Tectonics: Encoded Structural Complementarity Dictates Programmable Self‐Assembly

Lou, S., Wang, X., Yu, Z., & Shi, L. (2019) · Advanced Science · doi:10.1002/advs.201802043 · Cited by 69 · see citing works

Probing the native strain in α1-antitrypsin

Lee, K. N., Park, S. D., & Yu, M. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0696-497 · Cited by 68 · see citing works

Coordination geometry of nonbonded residues in globular proteins

Bahar, İ., & Jernigan, R. L. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00051-x · Cited by 67 · see citing works

Noncovalent self-assembly of a heterotetrameric diiron protein

Marsh, E. N. G., & DeGrado, W. F. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052023199 · Cited by 66 · see citing works

Analysis and design of three-stranded coiled coils and three-helix bundles

Schneider, J. P., Lombardi, A., & DeGrado, W. F. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00011-x · Cited by 66 · see citing works

Peptide hydrogen-bonded organic frameworks

Vijayakanth, T., Dasgupta, S., Ganatra, P., Rencus‐Lazar, S., Desai, A. V., Nandi, S., Jain, R., Bera, S., Nguyen, A. I., Gazit, E., et al. (2024) · Chemical Society Reviews · doi:10.1039/d3cs00648d · Cited by 64 · see citing works

Structure of an Activated Dictyostelium STAT in Its DNA-Unbound Form

Soler‐López, M., Petosa, C., Fukuzawa, M., Ravelli, R. B. G., Williams, J. G., & Müller, C. W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00130-3 · Cited by 64 · see citing works

Metastability in the Inhibitory Mechanism of Human α1-Antitrypsin

Im, H., Seo, E. J., & Yu, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11072 · Cited by 63 · see citing works

Relation Between Protein Stability, Evolution and Structure, as Probed by Carboxylic Acid Mutations

Godoy‐Ruiz, R., Pérez‐Jiménez, R., Ibarra‐Molero, B., & Sánchez‐Ruiz, J. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.048 · Cited by 63 · see citing works

A Set of Computationally Designed Orthogonal Antiparallel Homodimers that Expands the Synthetic Coiled-Coil Toolkit

Negron, C., & Keating, A. E. (2014) · Journal of the American Chemical Society · doi:10.1021/ja507847t · Cited by 59 · see citing works

A Discrete Stage of Baculovirus GP64-mediated Membrane Fusion

Kingsley, D. H., Behbahani, A., Rashtian, A., Blissard, G. W., & Zimmerberg, J. J. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.12.4191 · Cited by 58 · see citing works

Genetic Engineering of Protein-Based Polymers: The Example of Elastinlike Polymers

Rodríguez‐Cabello, J. C., Reguera, J., Girotti, A., Arias, F. J., & Alonso, M. (2005) · Advances in polymer science · doi:10.1007/12_047 · Cited by 58 · see citing works

A Buried Polar Interaction Can Direct the Relative Orientation of Helices in a Coiled Coil

Oakley, M. G., & Kim, P. S. (1998) · Biochemistry · doi:10.1021/bi981269m · Cited by 168 · see citing works

Complementation of Buried Lysine and Surface Polar Residues in a Designed Heterodimeric Coiled Coil

Campbell, K. M., & Lumb, K. J. (2002) · Biochemistry · doi:10.1021/bi025559l · Cited by 21 · see citing works

A Buried Polar Residue in the Hydrophobic Interface of the Coiled-coil Peptide, GCN4-p1, Plays a Thermodynamic, not a Kinetic Role in Folding

Knappenberger, J. A., Smith, J., Thorpe, S. H., Zitzewitz, J. A., & Matthews, C. R. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00592-2 · Cited by 40 · see citing works

Buried polar residues and structural specificity in the GCN4 leucine zipper

Gonzalez, L. C., Woolfson, D. N., & Alber, T. (1996) · Nature Structural Biology · doi:10.1038/nsb1296-1011 · Cited by 215 · see citing works

Buried Polar Residues in Coiled-Coil Interfaces,

Akey, D. L., Malashkevich, V. N., & Kim, P. S. (2001) · Biochemistry · doi:10.1021/bi002829w · Cited by 122 · see citing works