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

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196 · see citing works

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,157 · see citing works

The Pfam Protein Families Database

Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,062 · see citing works

SCOP: A structural classification of proteins database for the investigation of sequences and structures

Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,412 · 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

The SWISS-PROT protein sequence data bank and its supplement TrEMBL

Bairoch, A., & Apweiler, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.31 · Cited by 3,594 · see citing works

The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998

Bairoch, A. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.38 · Cited by 3,275 · see citing works

The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000

Bairoch, A. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.45 · Cited by 3,118 · see citing works

Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Abrahams, J. P., Leslie, A. G. W., Lutter, R., & Walker, J. E. (1994) · Nature · doi:10.1038/370621a0 · Cited by 3,004 · see citing works

CATH – a hierarchic classification of protein domain structures

Orengo, C., Michie, A. D., Jones, S., Jones, D., Swindells, M. B., & Thornton, J. M. (1997) · Structure · doi:10.1016/s0969-2126(97)00260-8 · Cited by 2,608 · see citing works

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417 · see citing works

Core Structure of gp41 from the HIV Envelope Glycoprotein

Chan, D. C., Fass, D., Berger, J. M., & Kim, P. S. (1997) · Cell · doi:10.1016/s0092-8674(00)80205-6 · Cited by 1,961 · see citing works

The PROSITE database, its status in 1995

Bairoch, A., Bucher, P., & Hofmann, K. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.1.189 · Cited by 1,929 · see citing works

The packing of α-helices: simple coiled-coils

Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578 · 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 · cited 16× · 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

Profile analysis: detection of distantly related proteins.

Gribskov, M., McLachlan, A. D., & Eisenberg, D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.13.4355 · Cited by 1,325 · see citing works

MIPS: a database for genomes and protein sequences

Mewes, H. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.37 · Cited by 1,276 · see citing works

The Pfam Protein Families Database

Bateman, A. G. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.263 · Cited by 1,253 · see citing works

Coiled coils: new structures and new functions.

Lupas, A. (1996) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(96)10052-9 · Cited by 1,191 · see citing works

The PROSITE database, its status in 1999

Hofmann, K., Bücher, P., Falquet, L., & Bairoch, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.215 · Cited by 1,092 · see citing works

Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions

Kissinger, C. R., Liu, B., Martı́n-Blanco, E., Kornberg, T. B., & Pabo, C. O. (1990) · Cell · doi:10.1016/0092-8674(90)90453-l · Cited by 986 · see citing works

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions

Das, A. K., Cohen, P. T. W., & Barford, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1192 · Cited by 832 · see citing works

Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 å resolution: cofactors and protein-cofactor interactions

Ermler, U., Fritzsch, G., Buchanan, S. K., & Michel, H. (1994) · Structure · doi:10.1016/s0969-2126(94)00094-8 · Cited by 792 · see citing works

Enlarged representative set of protein structures

Hobohm, U., & Sander, C. (1994) · Protein Science · doi:10.1002/pro.5560030317 · Cited by 788 · see citing works

The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution

Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90472-8 · Cited by 770 · see citing works

Crystal structure of the heterodimeric bZIP transcription factor c-Fos–c-Jun bound to DNA

Glover, J. N. M., & Harrison, S. C. (1995) · Nature · doi:10.1038/373257a0 · Cited by 750 · see citing works

Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer

Stowell, M. H. B., McPhillips, T., Rees, D. C., Soltis, S. M., Abresch, E. C., & Fehér, G. (1997) · Science · doi:10.1126/science.276.5313.812 · Cited by 725 · see citing works

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

Wolf, E., Kim, P. S., & Berger, B. (1997) · Protein Science · doi:10.1002/pro.5560060606 · Cited by 720 · see citing works

Three-Dimensional Structure of the Armadillo Repeat Region of β-Catenin

Huber, A. H., Nelson, W. J., & Weis, W. I. (1997) · Cell · doi:10.1016/s0092-8674(00)80352-9 · Cited by 706 · see citing works

Predicting coiled coils by use of pairwise residue correlations.

Berger, B., Wilson, D. B., Wolf, E., Tonchev, T., Milla, M. E., & Kim, P. S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8259 · Cited by 622 · see citing works

Crystallographic refinement at 2.3 Å Resolution and Refined Model of the Photosynthetic Reaction Centre fromRhodopseudomonas viridis

Deisenhofer, J., Epp, O., Sinning, I., & Michel, H. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0097 · Cited by 612 · see citing works

Proton Transfer Pathways in Bacteriorhodopsin at 2.3 Angstrom Resolution

Luecke, H., Richter, H.-T., & Lanyi, J. Κ. (1998) · Science · doi:10.1126/science.280.5371.1934 · Cited by 585 · see citing works

PQS: a protein quaternary structure file server

Henrick, K. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01253-5 · Cited by 540 · see citing works

Helix to helix packing in proteins.

Chothia, C., Levitt, M., & Richardson, D. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90341-7 · Cited by 537 · see citing works

Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target

Chan, D. C., Chutkowski, C. T., & Kim, P. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15613 · Cited by 477 · see citing works

[9] Profile analysis

Gribskov, M., Lothy, R., & Eisenberg, D. S. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)83011-w · Cited by 476 · 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

How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution

Mancia, F., Keep, N. H., Nakagawa, A., Leadlay, P. F., McSweeney, S. M., Rasmussen, B. F., secke, P. B., Diat, O., & Evans, P. R. (1996) · Structure · doi:10.1016/s0969-2126(96)00037-8 · Cited by 460 · see citing works

High-Resolution Protein Design with Backbone Freedom

Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T., & Kim, P. S. (1998) · Science · doi:10.1126/science.282.5393.1462 · Cited by 458 · 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

Crystal Structure of Recombinant Farnesyl Diphosphate Synthase at 2.6-.ANG. Resolution

Tarshis, L. C., Yan, M., Poulter, C. D., & Sacchettini, J. C. (1994) · Biochemistry · doi:10.1021/bi00202a004 · Cited by 424 · 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

Structural basis for self-association and receptor recognition of human TRAF2

Park, Y. C., Burkitt, V., Villa, A. R., Tong, L., & Wu, H. (1999) · Nature · doi:10.1038/19110 · Cited by 359 · see citing works

Sticky-End Assembly of a Designed Peptide Fiber Provides Insight into Protein Fibrillogenesis

Pandya, M. J., Spooner, G. M., Sunde, M., Thorpe, J. R., Rodger, A., & Woolfson, D. N. (2000) · Biochemistry · doi:10.1021/bi000246g · Cited by 344 · see citing works

Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design.

Vinson, C. R., Hai, T., & Boyd, S. M. (1993) · Genes & Development · doi:10.1101/gad.7.6.1047 · Cited by 336 · see citing works

Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions.

Yeates, T. O., Komiya, H., Chirino, A. J., Rees, D. C., Allen, J. P., & Fehér, G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.7993 · Cited by 318 · see citing works

Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides

Chang, C. H., El-Kabbani, O. A. L., Tiede, D. M., Norris, J. R., & Schiffer, M. (1991) · Biochemistry · doi:10.1021/bi00236a005 · Cited by 317 · see citing works

Analysis of the Saccharomyces Spindle Pole by Matrix-assisted Laser Desorption/Ionization (MALDI) Mass Spectrometry

Wigge, P. A., Jensen, O. N., Holmes, S., Souès, S., Mann, M., & Kilmartin, J. V. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.967 · Cited by 316 · see citing works

Trimeric structure of a C-type mannose-binding protein

Weis, W. I., & Drickamer, K. (1994) · Structure · doi:10.1016/s0969-2126(94)00124-3 · Cited by 307 · see citing works

The Crystal Structure of a Five-Stranded Coiled Coil in COMP: A Prototype Ion Channel?

Malashkevich, V. N., Kammerer, R. A., Efimov, V. P., Schulthess, T., & Engel, J. (1996) · Science · doi:10.1126/science.274.5288.761 · Cited by 301 · see citing works

The Structural Basis for the Recognition of Diverse Receptor Sequences by TRAF2

Ye, H., Park, Y. C., Kreishman, M., Kieff, E. D., & Wu, H. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80334-2 · Cited by 292 · 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

The high‐resolution X‐ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis

Bode, W., Papamokos, E., & Müsil, D. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13566.x · Cited by 287 · see citing works

Heptad breaks in α-helical coiled coils: Stutters and stammers

Brown, J. H., Cohen, C., & Parry, D. A. D. (1996) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199610)26:2 · Cited by 268 · see citing works

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

Lumb, K. J., & Kim, P. S. (1995) · Biochemistry · doi:10.1021/bi00027a013 · Cited by 266 · see citing works

Crystal structure of colicin Ia

Wiener, M. C., Freymann, D. M., Ghosh, P., & Stroud, R. M. (1997) · Nature · doi:10.1038/385461a0 · Cited by 254 · see citing works

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

Lumb, K. J., & Kim, P. S. (1998) · Biochemistry · doi:10.1021/bi9850468 · Cited by 250 · 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 216 · see citing works

Predicting oligomerization states of coiled coils

Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214 · see citing works

A structural motif in the variant surface glycoproteins of Trypanosoma brucei

Blum, M. L., Down, J. A., Gurnett, A. M., Carrington, M., Turner, M. J., & Wiley, D. C. (1993) · Nature · doi:10.1038/362603a0 · Cited by 211 · see citing works

Structure, Function, and Dynamics of Keratin Intermediate Filaments

Steinert, P. M. (1993) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12475665 · Cited by 198 · see citing works

The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB

Lancaster, C. R. D., & Michel, H. (1997) · Structure · doi:10.1016/s0969-2126(97)00285-2 · Cited by 192 · see citing works

α-Helical Protein Assembly Motifs

Kohn, W. D., Mant, C. T., & Hodges, R. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2583 · Cited by 185 · see citing works

The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum

Alzari, P. M., Souchon, H., & Domínguez, R. (1996) · Structure · doi:10.1016/s0969-2126(96)00031-7 · Cited by 179 · see citing works

An autonomous folding unit mediates the assembly of two-stranded coiled coils

Kammerer, R. A., Schulthess, T., Landwehr, R., Lustig, A., Engel, J., Aebi, U., & Steinmetz, M. O. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13419 · Cited by 174 · see citing works

A generalized profile syntax for biomolecular sequence motifs and its function in automatic sequence interpretation.

Bucher, P., & Bairoch, A. (1994) · PubMed · Cited by 172 · 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

Crystal Structures at 2.5 Angstrom Resolution of Seryl-tRNA Synthetase Complexed with Two Analogs of Seryl Adenylate

Belrhali, H., Yaremchuk, A. D., Tukalo, M. A., Larsen, K. S., Berthet-Colominas, C., LEBERMAN, R., Beijer, B., Sproat, B. S., Als-Nielsen, J., Grübel, G., et al. (1994) · Science · doi:10.1126/science.8128224 · Cited by 163 · see citing works

Crystallographic Analyses of Site-Directed Mutants of the Photosynthetic Reaction Center from Rhodobacter sphaeroides

Chirino, A. J., Lous, E. J., Huber, M., Allen, J. P., Schenck, C. C., Paddock, M. L., Fehér, G., & Rees, D. C. (1994) · Biochemistry · doi:10.1021/bi00181a020 · Cited by 152 · 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 145 · see citing works

A Designed Heterotrimeric Coiled Coil

Nautiyal, S., Woolfson, D. N., King, D., & Alber, T. (1995) · Biochemistry · doi:10.1021/bi00037a001 · Cited by 143 · see citing works

Crystal structure of the GreA transcript cleavage factor from Escherichia coli

Stebbins, C. E., Borukhov, S. I., Orlova, M., Polyakov, A., Goldfarb, A., & Darst, S. A. (1995) · Nature · doi:10.1038/373636a0 · Cited by 137 · see citing works

X-ray structure of an anti-fungal chitosanase from streptomyces N174

Marcotte, E. M., Monzingo, A. F., Ernst, S. R., Brzeziński, R., & Robertas, J. D. (1996) · Nature Structural Biology · doi:10.1038/nsb0296-155 · Cited by 136 · see citing works

Principles of Helix-Helix Packing in Proteins: The Helical Lattice Superposition Model

Walther, D. M., Eisenhaber, F., & Argos, P. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0044 · Cited by 127 · see citing works

Structure of spheroidene in the photosynthetic reaction center from YRhodobacter sphaeroides

Arnoux, B., Ducruix, A. F., Reiss‐Husson, F., Lutz, M., Norris, J. R., Schiffer, M., & Chang, C. H. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81612-6 · Cited by 125 · see citing works

The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

Burkhard, P., Kammerer, R. A., Steinmetz, M. O., Bourenkov, G. P., & Aebi, U. (2000) · Structure · doi:10.1016/s0969-2126(00)00100-3 · Cited by 121 · see citing works

A distinct 14 residue site triggers coiled‐coil formation in cortexillin I

Steinmetz, M. O., Stock, A., Schulthess, T., Landwehr, R., Lustig, A., Faix, J., Gerisch, G., Aebi, U., & Kammerer, R. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.1883 · Cited by 119 · 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

Structure of a replication-terminator protein complexed with DNA

Kamada, K., Horiuchi, T., Ohsumi, K., Shimamoto, N., & Morikawa, K. (1996) · Nature · doi:10.1038/383598a0 · Cited by 106 · see citing works

2·9 Å resolution structure of the N-terminal domain of a variant surface glycoprotein from Trypanosoma brucei

Freymann, D. M., Down, J. A., Carrington, M., Roditi, I. J., Turner, M., & Wiley, D. C. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80066-x · Cited by 99 · see citing works

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

Kohn, W., Kay, C., & Hodges, R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2125 · Cited by 90 · see citing works

Crystal structure of the CDK4/6 inhibitory protein p18INK4c provides insights into ankyrin-like repeat structure/function and tumor-derived p16INK4 mutations

Venkataramani, R. N., Swaminathan, K., & Marmorstein, R. (1998) · Nature Structural Biology · doi:10.1038/nsb0198-74 · Cited by 89 · see citing works

Three-stranded α-fibrous proteins: the heptad repeat and its implications for structure

Conway, J. F., & Parry, D. A. D. (1991) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(91)90004-e · Cited by 80 · see citing works

Accessibility to internal cavities and ligand binding sites monitored by protein crystallographic thermal factors

Carugo, O., & Argos, P. (1998) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19980501)31:2 · Cited by 72 · see citing works

Structural Studies of Wild-Type and Mutant Reaction Centers from an Antenna-Deficient Strain of Rhodobacter sphaeroides: Monitoring the Optical Properties of the Complex from Bacterial Cell to Crystal

McAuley-Hecht, K. E., Fyfe, P. K., Ridge, J. P., Prince, S. M., Hunter, C. N., Isaacs, N. W., Cogdell, R. J., & Jones, M. R. (1998) · Biochemistry · doi:10.1021/bi971717a · Cited by 68 · see citing works

Coiled-coil assembly by peptides with non-heptad sequence motifs

Hicks, M. R., Holberton, D. V., Kowalczyk, C., & Woolfson, D. N. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00021-7 · Cited by 64 · see citing works

Crystal structure of a designed, thermostable, heterotrimeric coiled coil

Nautiyal, S., & Alber, T. (1999) · Protein Science · doi:10.1110/ps.8.1.84 · Cited by 61 · see citing works

Construction of an atomic model for tropomyosin and implications for interactions with actin

Phillips, G. N. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90469-9 · Cited by 52 · see citing works

Open‐and‐shut cases in coiled‐coil assembly: α‐sheets and α‐cylinders

Walshaw, J., & Woolfson, D. N. (2001) · Protein Science · doi:10.1110/ps.36901 · Cited by 50 · see citing works

The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: Structural refinement using heteronuclear multidimensional NMR spectroscopy

Andersen, K. V., & Poulsen, F. M. (1993) · Journal of Biomolecular NMR · doi:10.1007/bf00212514 · Cited by 49 · see citing works

The structure of ColE1 rop in solution

Eberle, W., Pastore, A., Sander, C., & ROSCH, P. J. (1991) · Journal of Biomolecular NMR · doi:10.1007/bf01874570 · Cited by 48 · see citing works

Complementary packing of α‐helices in proteins

Efimov, A. V. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01507-0 · Cited by 35 · see citing works

Crystals of a gragment of influenza haemagglutinin in the low pH induced conformation

Bullough, P. A., Hughson, F. M., Treharne, A., Ruigrok, R. W. H., Skehel, J. J., & Wiley, D. C. (1994) · Journal of Molecular Biology · doi:10.1016/0022-2836(94)90027-2 · Cited by 35 · see citing works

Sequence-based design of a peptide probe for the APC tumor suppressor protein.

Sharma, V. A., Logan, J., King, D. S., White, R., & Alber, T. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70324-0 · Cited by 33 · see citing works

Structure of the Reaction Center from Rhodobacter sphaeroides R-26 and 2.4.1

Allen, J. P., Fehér, G., Yeates, T. O., Komiya, H., & Rees, D. C. (1988) · Springer eBooks · doi:10.1007/978-1-4899-0815-5_2 · Cited by 28 · see citing works

Solution structure of the antitermination protein NusB of Escherichia coli: a novel all‐helical fold for an RNA‐binding protein

Huenges, M., Rölz, C., Gschwind, R. M., Peteranderl, R., Berglechner, F., Richter, G., Bacher, A., Kessler, H., & Gemmecker, G. (1998) · The EMBO Journal · doi:10.1093/emboj/17.14.4092 · Cited by 21 · see citing works

Coiled Coil Domains: Stability, Specificity, and Biological Implications

Mason, J., & Arndt, K. M. (2004) · ChemBioChem · doi:10.1002/cbic.200300781 · Cited by 756 · see citing works

The Structure of α-Helical Coiled Coils

Lupas, A. N., & Gruber, M. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(05)70003-6 · Cited by 668 · 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

An HMM model for coiled-coil domains and a comparison with PSSM-based predictions

Delorenzi, M., & Speed, T. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.4.617 · Cited by 479 · see citing works

Paircoil2: improved prediction of coiled coils from sequence.

McDonnell, A. V., Jiang, T., Keating, A. E., & Berger, B. (2006) · Bioinformatics · doi:10.1093/bioinformatics/bti797 · Cited by 424 · see citing works

Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme

Rosenberg, O. S., Deindl, S., Sung, R.-J., Nairn, A. C., & Kuriyan, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.029 · Cited by 333 · see citing works

Computational design of water-soluble α-helical barrels

Thomson, A. R., Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L., & Woolfson, D. N. (2014) · Science · doi:10.1126/science.1257452 · Cited by 330 · see citing works

Peptide Design and Self-assembly into Targeted Nanostructure and Functional Materials

Sinha, N. J., Langenstein, M. G., Pochan, D. J., Kloxin, C. J., & Saven, J. G. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00712 · Cited by 328 · see citing works

Protein Design: From the Aspect of Water Solubility and Stability

Qing, R., Hao, S.-L., Smorodina, E., Jin, D., Zalevsky, A. O., & Zhang, S.-G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 287 · see citing works

Smart Self‐Assembled Hybrid Hydrogel Biomaterials

Kopec̆ek, J., & Yang, J. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201040 · Cited by 312 · see citing works

Structural specificity in coiled-coil interactions

Grigoryan, G., & Keating, A. E. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.04.008 · Cited by 290 · see citing works

Conformational Flexibility in the Multidrug Efflux System Protein AcrA

Mikolosko, J., Bobyk, K. D., Zgurskaya, H. I., & Ghosh, P. (2006) · Structure · doi:10.1016/j.str.2005.11.015 · Cited by 279 · see citing works

Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors

Alexander, R. P., & Zhulin, I. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609359104 · Cited by 268 · 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

The 2.8 Å crystal structure of the dynein motor domain

Kon, T., Oyama, T., Shimo‐Kon, R., Imamula, K., Shima, T., Sutoh, K., & Kurisu, G. (2012) · Nature · doi:10.1038/nature10955 · Cited by 260 · see citing works

Engineering nanoscale order into a designed protein fiber

Papapostolou, D., Smith, A. M., Atkins, E. D. T., Oliver, S., Ryadnov, M. G., Serpell, L. C., & Woolfson, D. N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700801104 · Cited by 246 · see citing works

Analysis of α-Helical Coiled Coils with the Program TWISTER Reveals a Structural Mechanism for Stutter Compensation

Strelkov, S. V., & Burkhard, P. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4454 · Cited by 246 · see citing works

Probing Designability via a Generalized Model of Helical Bundle Geometry

Grigoryan, G., & DeGrado, W. F. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.058 · Cited by 232 · see citing works

A seven-helix coiled coil

Liu, J., Zheng, Q., Deng, Y., Cheng, C.-S., Kallenbach, N. R., & Lu, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604871103 · Cited by 227 · 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 217 · 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

A Periodic Table of Coiled-Coil Protein Structures

Moutevelis, E., & Woolfson, D. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.028 · Cited by 204 · see citing works

STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry

Stathopulos, P. B., Schindl, R., Fahrner, M., Zheng, L., Gasmi-Seabrook, G. M. C., Muik, M., Romanin, C., & Ikura, M. (2013) · Nature Communications · doi:10.1038/ncomms3963 · Cited by 203 · see citing works

De novo designed peptides for biological applications

Boyle, A. L., & Woolfson, D. N. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00152j · Cited by 192 · see citing works

A de novo peptide hexamer with a mutable channel

Zaccai, N. R., Chi, B., Thomson, A. R., Boyle, A. L., Bartlett, G. J., Bruning, M., Linden, N., Sessions, R. B., Booth, P. J., Brady, R. L., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.692 · Cited by 192 · see citing works

DeepCoil—a fast and accurate prediction of coiled-coil domains in protein sequences

Ludwiczak, J., Winski, A., Szczepaniak, K., Alva, V., & Dunin-Horkawicz, S. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty1062 · Cited by 184 · see citing works

Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A

Scott, A., Gaspar, J., Stuchell‐Brereton, M. D., Alam, S. L., Skalicky, J. J., & Sundquist, W. I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502165102 · Cited by 183 · see citing works

A brief history of de novo protein design: minimal, rational, and computational.

Woolfson, D. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167160 · Cited by 139 · see citing works

Mechanism of Tc toxin action revealed in molecular detail

Meusch, D., Gatsogiannis, C., Efremov, R. G., Lang, A. E., Hofnagel, O., Vetter, I. R., Aktories, K., & Raunser, S. (2014) · Nature · doi:10.1038/nature13015 · Cited by 166 · see citing works

Comparative analysis of coiled-coil prediction methods

Gruber, M., Söding, J., & Lupas, A. N. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.03.009 · Cited by 161 · see citing works

The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation

Lee, M., Sadowska, A., Bekere, I., Ho, D., Gully, B. S., Lü, Y., Iyer, K. S., Trewhella, J., Fox, A. H., & Bond, C. S. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv156 · Cited by 160 · see citing works

CC+: a relational database of coiled-coil structures

Testa, O. D., Moutevelis, E., & Woolfson, D. N. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn675 · Cited by 158 · see citing works

De novo protein design: how do we expand into the universe of possible protein structures?

Woolfson, D. N., Bartlett, G. J., Burton, A. J., Heal, J. W., Niitsu, A., Thomson, A. R., & Wood, C. W. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.05.009 · Cited by 155 · see citing works

Structural Basis for the Actin-Binding Function of Missing-in-Metastasis

Lee, S. H., Kerff, F., Chéreau, D., Ferrón, F., Klug, A., & Domínguez, R. (2007) · Structure · doi:10.1016/j.str.2006.12.005 · Cited by 151 · see citing works

Coiled-Coil Design: Updated and Upgraded

Woolfson, D. N. (2017) · Subcellular Biochemistry · doi:10.1007/978-3-319-49674-0_2 · Cited by 149 · see citing works

The structure of bovine IF1, the regulatory subunit of mitochondrial F‐ATPase

Cabezón, E., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.6990 · Cited by 146 · see citing works

An atlas of protein homo-oligomerization across domains of life

Schweke, H., Pacesa, M., Levin, T., Goverde, C. A., Kumar, P., Duhoo, Y., Dornfeld, L. J., Dubreuil, B., Georgeon, S., Ovchinnikov, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.01.022 · Cited by 144 · see citing works

Historical review: Another 50th anniversary – new periodicities in coiled coils

Gruber, M. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.008 · Cited by 141 · 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 140 · see citing works

The KCNQ1 (Kv7.1) COOH Terminus, a Multitiered Scaffold for Subunit Assembly and Protein Interaction

Wiener, R., Haitin, Y., Shamgar, L., Fernández‐Alonso, M. C., Martos, A., Chomsky-Hecht, O., Rivas, G., Attali, B., & Hirsch, J. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707541200 · Cited by 134 · see citing works

C CB uilder 2.0: Powerful and accessible coiled‐coil modeling

Wood, C. W., & Woolfson, D. N. (2017) · Protein Science · doi:10.1002/pro.3279 · Cited by 129 · see citing works

De novo design of a hyperstable non-natural protein–ligand complex with sub-Å accuracy

Polizzi, N. F., Wu, Y., Lemmin, T., Maxwell, A. M., Zhang, S., Rawson, J., Beratan, D. N., Therien, M. J., & DeGrado, W. F. (2017) · Nature Chemistry · doi:10.1038/nchem.2846 · Cited by 125 · see citing works

Constructing ion channels from water-soluble α-helical barrels

Scott, A. J., Niitsu, A., Kratochvil, H. T., Lang, E. J. M., Sengel, J. T., Dawson, W., Mahendran, K. R., Mravic, M., Thomson, A. R., Brady, R. L., et al. (2021) · Nature Chemistry · doi:10.1038/s41557-021-00688-0 · Cited by 125 · see citing works

Molecular basis of fibrin clot elasticity.

Lim, B. C. B., Lee, E. H., Sotomayor, M., & Schulten, K. (2008) · Structure · doi:10.1016/j.str.2007.12.019 · Cited by 128 · see citing works

Crystal Structure of a vFlip-IKKγ Complex: Insights into Viral Activation of the IKK Signalosome

Bagnéris, C., Ageichik, A. V., Cronin, N., Wallace, B. A., Collins, M. K., Boshoff, C., Waksman, G., & Barrett, T. E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.029 · Cited by 124 · see citing works

A monodisperse transmembrane α-helical peptide barrel

Mahendran, K. R., Niitsu, A., Kong, L., Thomson, A. R., Sessions, R. B., Woolfson, D. N., & Bayley, H. (2016) · Nature Chemistry · doi:10.1038/nchem.2647 · Cited by 123 · see citing works

Structural Basis for Mitotic Centrosome Assembly in Flies

Feng, Z., Caballe, A., Wainman, A., Johnson, S., Haensele, A. F. M., Cottee, M. A., Conduit, P. T., Lea, S. M., & Raff, J. W. (2017) · Cell · doi:10.1016/j.cell.2017.05.030 · Cited by 123 · see citing works

Coiled coil protein origami: from modular design principles towards biotechnological applications.

Lapenta, F., Aupič, J., Strmšek, Ž., & Jerala, R. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00822h · Cited by 74 · see citing works

The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

Kühnel, K., Jarchau, T., Wolf, E., Schlichting, I., Walter, U., Wittinghofer, A., & Strelkov, S. V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403069101 · Cited by 122 · see citing works

Complete Predicted Three-Dimensional Structure of the Facilitator Transmembrane Protein and Hepatitis C Virus Receptor CD81: Conserved and Variable Structural Domains in the Tetraspanin Superfamily

Seigneuret, M. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.069666 · Cited by 122 · see citing works

De novo design of orthogonal peptide pairs forming parallel coiled‐coil heterodimers

Gradišar, H., & Jerala, R. (2010) · Journal of Peptide Science · doi:10.1002/psc.1331 · Cited by 122 · see citing works

Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies

Egelman, E. H., Xu, C., DiMaio, F., Magnotti, E. L., Modlin, C., Yu, X., Wright, E., Baker, D. A., & Conticello, V. P. (2015) · Structure · doi:10.1016/j.str.2014.12.008 · Cited by 120 · see citing works

Rational Design of Helical Nanotubes from Self-Assembly of Coiled-Coil Lock Washers

Xu, C., Liu, R., Mehta, A. K., Guerrero-Ferreira, R., Wright, E. R., Dunin-Horkawicz, S., Morris, K. L., Serpell, L. C., Zuo, X., Wall, J. S., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4074529 · Cited by 119 · see citing works

The Structure and Topology of α-Helical Coiled Coils

Lupas, A. N., Baßler, J., & Dunin-Horkawicz, S. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-49674-0_4 · Cited by 116 · see citing works

CCBuilder: an interactive web-based tool for building, designing and assessing coiled-coil protein assemblies

Wood, C. W., Bruning, M., Ibarra, A. Á., Bartlett, G. J., Thomson, A. R., Sessions, R. B., Brady, R. L., & Woolfson, D. N. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu502 · Cited by 110 · see citing works

Atomic structure of vimentin coil 2

Nicolet, S., Herrmann, H. O., Aebi, U., & Strelkov, S. V. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.02.012 · Cited by 107 · 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

Extended knobs-into-holes packing in classical and complex coiled-coil assemblies☆

Walshaw, J., & Woolfson, D. N. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.014 · Cited by 104 · see citing works

A conserved trimerization motif controls the topology of short coiled coils

Kammerer, R. A., Kostrewa, D., Progias, P., Srinivas, H., Avila, D. W., Lustig, A., Winkler, F. K., Pieters, J., & Steinmetz, M. O. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502390102 · Cited by 105 · see citing works

Wavelet transforms for the characterization and detection of repeating motifs

Murray, K. B., Gorse, D., & Thornton, J. M. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5332 · Cited by 105 · 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 104 · see citing works

LOGICOIL—multi-state prediction of coiled-coil oligomeric state

Vincent, T. L., Green, P. J., & Woolfson, D. N. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts648 · Cited by 103 · see citing works

Vimentin Coil 1A—A Molecular Switch Involved in the Initiation of Filament Elongation

Meier, M., Padilla‐Meier, G. P., Herrmann, H. O., Wedig, T., Hergt, M., Patel, T. R., Stetefeld, J., Aebi, U., & Burkhard, P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.067 · Cited by 101 · see citing works

Structural basis for the enhanced stability of highly fluorinated proteins

Buer, B. C., Meagher, J. L., Stuckey, J. A., & Marsh, E. N. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120112109 · Cited by 99 · see citing works

Engineered Socket Study of Signaling through a Four-Helix Bundle: Evidence for a Yin−Yang Mechanism in the Kinase Control Module of the Aspartate Receptor

Swain, K. E., Gonzalez, M. A., & Falke, J. J. (2009) · Biochemistry · doi:10.1021/bi901020d · Cited by 99 · see citing works

The evolution and structure prediction of coiled coils across all genomes.

Rackham, O. J. L., Madera, M., Armstrong, C. T., Vincent, T. L., Woolfson, D. N., & Gough, J. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.032 · 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

Multicoil2: Predicting Coiled Coils and Their Oligomerization States from Sequence in the Twilight Zone

Trigg, J., Gutwin, K., Keating, A. E., & Berger, B. (2011) · PLoS One · doi:10.1371/journal.pone.0023519 · Cited by 91 · see citing works

Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations

Schubert, H., Zhai, Q., Sandrin, V., Eckert, D. M., Garcia‐Maya, M., Saul, L., Sundquist, W. I., Steiner, R. A., & Hill, C. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008206107 · Cited by 95 · see citing works

Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein.Preprint

Liu, Y., Salter, H. K., Holding, A. N., Johnson, C. M., Stephens, E., Lukavsky, P., Walshaw, J., & Bullock, S. (2013) · Genes & Development · doi:10.1101/gad.212381.112 · Cited by 98 · see citing works

Structure of the Conserved HAMP Domain in an Intact, Membrane-Bound Chemoreceptor: A Disulfide Mapping Study

Swain, K. E., & Falke, J. J. (2007) · Biochemistry · doi:10.1021/bi701832b · Cited by 92 · see citing works

Interhead tension determines processivity across diverse N-terminal kinesins

Shastry, S., & Hancock, W. O. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102628108 · Cited by 89 · see citing works

Crystal Structure of the Nipah Virus Phosphoprotein Tetramerization Domain

Bruhn, J. F., Barnett, K. C., Bibby, J., Thomas, J. M. H., Keegan, R. M., Rigden, D. J., Bornholdt, Z. A., & Saphire, E. O. (2013) · Journal of Virology · doi:10.1128/jvi.02294-13 · Cited by 88 · see citing works

Designing heterodimeric two‐stranded α‐helical coiled‐coils: the effect of chain length on protein folding, stability and specificity

Litowski, J. R., & Hodges, R. S. (2001) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2001.10972.x · Cited by 84 · see citing works

Redesign of protein nanocages: the way from 0D, 1D, 2D to 3D assembly

Lv, C., Zhang, X., Liu, Y., Zhang, T., Chen, H., Zang, J., Zheng, B., & Zhao, G. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01349h · Cited by 84 · see citing works

Sequence and Structural Duality: Designing Peptides to Adopt Two Stable Conformations

Pandya, M. J., Cerasoli, E., Joseph, A., Stoneman, R. G., Waite, E., & Woolfson, D. N. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045568c · Cited by 83 · see citing works

The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled‐coil

Conners, R., Hill, D. J., Borodina, E. V., Agnew, C., Daniell, S. J., Burton, N. M., Sessions, R. B., Clarke, A. R., Catto, L. E., Lammie, D., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.101 · Cited by 83 · see citing works

Macromolecular therapeutics

Yang, J., & Kopec̆ek, J. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.04.013 · Cited by 79 · 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

Structural and Biophysical Analysis of BST-2/Tetherin Ectodomains Reveals an Evolutionary Conserved Design to Inhibit Virus Release

Swiecki, M. K., Scheaffer, S. M., Allaire, M., Fremont, D. H., Colonna, M., & Brett, T. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190538 · Cited by 78 · see citing works

The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition

Casal, E., Federici, L., Zhang, W., Fernandez-Recio, J., Priego, E.-M., Miguel, R. N., DuHadaway, J. B., Prendergast, G. C., Luisi, B. F., & Laue, E. D. (2006) · Biochemistry · doi:10.1021/bi060717k · Cited by 77 · see citing works

Protein–Protein Interactions Mediated by Helical Tertiary Structure Motifs

Watkins, A. M., Wuo, M. G., & Arora, P. S. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05527 · Cited by 77 · see citing works

The Structure of the Coiled-Coil Domain of Ndel1 and the Basis of Its Interaction with Lis1, the Causal Protein of Miller-Dieker Lissencephaly

Derewenda, U., Tarricone, C., Choi, W. C., Cooper, D. R., Lukasik, S., Perrina, F., Tripathy, A., Kim, M. H., Cafiso, D. S., Musacchio, A., et al. (2007) · Structure · doi:10.1016/j.str.2007.09.015 · Cited by 74 · see citing works

Coiled coil-based therapeutics and drug delivery systems.

Utterström, J., Naeimipour, S., Selegård, R., & Aili, D. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.012 · Cited by 68 · see citing works

Hantavirus Nucleocapsid Protein Coiled-Coil Domains

Alfadhli, A., Steel, E. A., Finlay, L. A., Bächinger, H. P., & Barklis, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203395200 · Cited by 71 · see citing works

The use of coiled-coil proteins in drug delivery systems

McFarlane, A. A., Orriss, G. L., & Stetefeld, J. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.05.034 · Cited by 70 · see citing works

Polar Assembly in a Designed Protein Fiber

Smith, A. M., Acquah, S. F. A., Bone, N. M., Kroto, H. W., Ryadnov, M. G., Stevens, M. S. P., Walton, D. R. M., & Woolfson, D. N. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200461599 · Cited by 70 · see citing works

Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design

Zottig, X., Côté‐Cyr, M., Arpin, D., Archambault, D., & Bourgault, S. (2020) · Nanomaterials · doi:10.3390/nano10051008 · Cited by 69 · see citing works

On the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins

Wong, E. T. C., Na, D., & Gsponer, J. A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003192 · Cited by 68 · see citing works

Core-directed protein design

Woolfson, D. N. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00234-7 · Cited by 68 · see citing works

Structures of Dimeric GIT1 and Trimeric β-PIX and Implications for GIT–PIX Complex Assembly

Schlenker, O., & Rittinger, K. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.050 · Cited by 65 · see citing works

Sequence Comparisons of Intermediate Filament Chains: Evidence of a Unique Functional/Structural Role for Coiled-Coil Segment 1A and Linker L1

Smith, T. A., Strelkov, S. V., Burkhard, P., Aebi, U., & Parry, D. A. D. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4438 · Cited by 65 · see citing works

Crystal structure of the signaling helix coiled-coil domain of the β1 subunit of the soluble guanylyl cyclase

Ma, X., Beuve, A. V., & van den Akker, F. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-2 · Cited by 63 · see citing works

Crystal Structure of a Core Domain of Stomatin from Pyrococcus horikoshii Illustrates a Novel Trimeric and Coiled-Coil Fold

Yokoyama, H., Fujii, S., & Matsui, I. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.024 · Cited by 61 · see citing works

A Fungal Sarcolemmal Membrane-Associated Protein (SLMAP) Homolog Plays a Fundamental Role in Development and Localizes to the Nuclear Envelope, Endoplasmic Reticulum, and Mitochondria

Nordzieke, S., Zobel, T., Fränzel, B., Wolters, D. A., Kück, U., & Teichert, I. (2014) · Eukaryotic Cell · doi:10.1128/ec.00241-14 · Cited by 61 · see citing works

Generalized Crick Equations for Modeling Noncanonical Coiled Coils

Offer, G., Hicks, M. R., & Woolfson, D. N. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4448 · Cited by 59 · see citing works

Parallel Coiled-coil Association of the RhoA-binding Domain in Rho-kinase

Shimizu, T., Ihara, K., Maesaki, R., Amano, M., Kaibuchi, K., & Hakoshima, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306458200 · Cited by 59 · see citing works

Structural Insights into the Molecular Mechanisms of Cauliflower Mosaic Virus Transmission by Its Insect Vector

Hoh, F., Uzest, M., Drucker, M., Plisson‐Chastang, C., Bron, P., Blanc, S., & Dumas, C. (2010) · Journal of Virology · doi:10.1128/jvi.02662-09 · Cited by 55 · see citing works

Crystal Structure of the Marburg Virus VP35 Oligomerization Domain

Bruhn, J. F., Kirchdoerfer, R. N., Urata, S. M., Li, S., Tickle, I. J., Bricogne, G., & Saphire, E. O. (2016) · Journal of Virology · doi:10.1128/jvi.01085-16 · Cited by 55 · see citing works

Engineering protein stability with atomic precision in a monomeric miniprotein

Baker, E. G., Williams, C., Hudson, K. L., Bartlett, G. J., Heal, J. W., Goff, K. L. P., Sessions, R. B., Crump, M. P., & Woolfson, D. N. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2380 · Cited by 55 · see citing works

<scp> CC ⁺ </scp> : A searchable database of validated coiled coils in <scp>PDB</scp> structures and <scp>AlphaFold2</scp> models

Kumar, P., Petrenas, R., Dawson, W. M., Schweke, H., Levy, E. D., & Woolfson, D. N. (2023) · Protein Science · doi:10.1002/pro.4789 · Cited by 11 · see citing works

<i>Socket2</i>: a program for locating, visualizing and analyzing coiled-coil interfaces in protein structures

Kumar, P., & Woolfson, D. N. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab631 · Cited by 51 · see citing works

Applying graph theory to protein structures: an Atlas of coiled coils

Heal, J. W., Bartlett, G. J., Wood, C. W., Thomson, A. R., & Woolfson, D. N. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty347 · Cited by 22 · see citing works

PS-Coils: A new method for coiled-coil prediction that expolits both single sequence and evolutionary information

Bartoli, L., Fariselli, P., & Casadio, R. (2009) · Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna)

CC+: a relational database of coiled-coil structures

Testa, O. D., Moutevelis, E., & Woolfson, D. N. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn675 · Cited by 158 · see citing works