Cited by 136Protein Structure and DynamicsChemical Synthesis and AnalysisRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.

Molecular basis of coiled-coil formation

Open access

Steinmetz, Michel O., Jelesarov, Ilian, Matousek, William M., Honnappa, Srinivas, Jahnke, Wolfgang, Missimer, John H., Frank, Sabine, Alexandrescu, Andrei T., Kammerer, Richard A.·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0700321104PMC PMC1855353

Open this paper in CoChat — free account

Abstract

Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed “trigger sequence,” that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.

Integrity signals

Registry

Crossref · 10.1073/pnas.0700321104

Cites

61 of 61 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D. S., Bigam, C. G., Yao, J. S., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,361
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,635
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturants
Santoro, M. M., & Bolen, D. W. (1988) · Biochemistry · doi:10.1021/bi00421a014 · Cited by 1,585
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 1,444
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
Coiled coils: a highly versatile protein folding motif.
Burkhard, P., Stetefeld, J., & Strelkov, S. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01898-5 · Cited by 1,055
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211764 · Cited by 1,012
A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G
Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M. D., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816
Coiled Coil Domains: Stability, Specificity, and Biological Implications
Mason, J., & Arndt, K. M. (2004) · ChemBioChem · doi:10.1002/cbic.200300781 · Cited by 756

Show all 61 references

Sorted by citations

Definition and testing of the GROMOS force-field versions 54A7 and 54B7
Schmid, N., Eichenberger, A. P., Choutko, A., Riniker, S., Winger, M., Mark, A. E., & van Gunsteren, W. F. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0700-9 · Cited by 2,535
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A. O., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 334
Kinetic Advantage of Intrinsically Disordered Proteins in Coupled Folding–Binding Process: A Critical Assessment of the “Fly-Casting” Mechanism
Huang, Y., & Liu, Z. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.010 · Cited by 276
Essential role of coiled-coils for aggregation and activity of Q/N-rich prions and polyQ proteins
Fiumara, F., Fioriti, L., Kandel, E., & Hendrickson, W. (2010) · Cell · doi:10.1016/j.cell.2010.11.042 · Cited by 249
Synthetic beta cells for fusion-mediated dynamic insulin secretion
Chen, Z., Wang, J., Sun, W., Ogunnaike, E. A., Kahkoska, A. R., Zhang, X., Lü, Y., Ligler, F. S., Buse, J. B., & Gu, Z. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2511 · Cited by 250
STIM1 couples to ORAI1 via an intramolecular transition into an extended conformation
Muik, M., Fahrner, M., Schindl, R., Stathopulos, P. B., Frischauf, I., Derler, I., Plenk, P., Lackner, B., Groschner, K., Ikura, M., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.79 · Cited by 235
The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer
Sanchez, J. G., Okreglicka, K. M., Chandrasekaran, V., Welker, J. M., Sundquist, W. I., & Pornillos, O. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318962111 · Cited by 197
Mixing MARTINI: Electrostatic Coupling in Hybrid Atomistic–Coarse-Grained Biomolecular Simulations
Wassenaar, T. A., Ingólfsson, H. I., Prieß, M., Marrink, ‪. J., & Schäfer, L. V. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp311533p · Cited by 167
p66α–MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2–NuRD complex
Gnanapragasam, M. N., Scarsdale, J. N., Amaya, M. L., Webb, H. D., Desai, M. A., Walavalkar, N. M., Wang, S. Z., Zu Zhu, S., Ginder, G. D., & Williams, D. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015341108 · Cited by 148
Dynamics and mechanisms of coupled protein folding and binding reactions
Kiefhaber, T., Bachmann, A., & Jensen, K. S. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.09.010 · Cited by 136
Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
Ellena, J. F., Liang, B., Wiktor, M., Stein, A., Cafiso, D. S., Jahn, R., & Tamm, L. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908317106 · Cited by 115
Testing of the GROMOS Force-Field Parameter Set 54A8: Structural Properties of Electrolyte Solutions, Lipid Bilayers, and Proteins
Reif, M., Winger, M., & Oostenbrink, C. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct300874c · Cited by 105
The Coarse-Grained OPEP Force Field for Non-Amyloid and Amyloid Proteins
Chebaro, Y., Pasquali, S., & Derreumaux, P. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp301665f · Cited by 107
Structural Insights into the Organization of the Cavin Membrane Coat Complex
Kovtun, O., Tillu, V. A., Jung, W., Leneva, N., Ariotti, N., Chaudhary, N., Mandyam, R. A., Ferguson, C., Morgan, G., Johnston, W. A., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.10.002 · Cited by 102
Hydrogen exchange of monomeric α‐synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli
Croke, R. L., Sallum, C. O., Watson, E., Watt, E. D., & Alexandrescu, A. T. (2008) · Protein Science · doi:10.1110/ps.033803.107 · Cited by 99
Self-citation
Molecular basis of coiled-coil oligomerization-state specificity
Ciani, B., Bjelić, S., Srinivas, H., Jawhari, H., Jaussi, R., Payapilly, A., Jowitt, T. A., Steinmetz, M. O., & Kammerer, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008502107 · Cited by 80
Self-citation
An Effective Strategy for Stabilizing Minimal Coiled Coil Mimetics
Wuo, M. G., Mahon, A. B., & Arora, P. S. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05525 · Cited by 78
Modulation of Coiled-Coil Dimer Stability through Surface Residues while Preserving Pairing Specificity
Drobnak, I., Gradišar, H., Ljubetič, A., Merljak, E., & Jerala, R. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b01690 · Cited by 79
Structural Basis for Plant MADS Transcription Factor Oligomerization
Lai, X., Daher, H., Galien, A., Hugouvieux, V., & Zubieta, C. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.06.014 · Cited by 74
NMR determination of pKa values in α‐synuclein
Croke, R. L., Patil, S. M., Quevreaux, J., Kendall, D. A., & Alexandrescu, A. T. (2010) · Protein Science · doi:10.1002/pro.556 · Cited by 70
Self-citation
An effective all-atom potential for proteins
Irbäck, A., Mitternacht, S., & Mohanty, S. (2009) · PMC Biophysics · doi:10.1186/1757-5036-2-2 · Cited by 66
Highly Anisotropic Stability and Folding Kinetics of a Single Coiled Coil Protein under Mechanical Tension
Gao, Y., Sirinakis, G., & Zhang, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja204005r · Cited by 65
Probing the Interaction between the Coiled Coil Leucine Zipper of cGMP-dependent Protein Kinase Iα and the C Terminus of the Myosin Binding Subunit of the Myosin Light Chain Phosphatase
Sharma, A. K., Zhou, G., Kupferman, J., Surks, H. K., Christensen, E. N., Chou, J. J., Mendelsohn, M. E., & Rigby, A. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804916200 · Cited by 63
Electrostatic Contributions to the Stability of the GCN4 Leucine Zipper Structure
Matousek, W. M., Ciani, B., Fitch, C. A., Bertrand García‐Moreno, E., Kammerer, R. A., & Alexandrescu, A. T. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.007 · Cited by 58
Self-citation
Coiled-coil domains are sufficient to drive liquid-liquid phase separation in protein models
Ramirez, D. A., Hough, L. E., & Shirts, M. R. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.02.007 · Cited by 53
More than a syllable in fib-ROS-is: The role of ROS on the fibrotic extracellular matrix and on cellular contacts
Grosche, J., Meißner, J., & Eble, J. A. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.03.005 · Cited by 53
What lessons can be learned from studying the folding of homologous proteins?
Nickson, A. A., & Clarke, J. (2010) · Methods · doi:10.1016/j.ymeth.2010.06.003 · Cited by 54
Peptide Tertiary Structure Nucleation by Side‐Chain Crosslinking with Metal Complexation and Double “Click” Cycloaddition
Torres, O. B., Yüksel, D., Bernardina, M., Kumar, K., & Bong, D. T.-Y. (2008) · ChemBioChem · doi:10.1002/cbic.200800040 · Cited by 54
Biomolecular structure refinement using the GROMOS simulation software
Schmid, N., Allison, J. R., Dolenc, J., Eichenberger, A. P., Kunz, A. E., & A, W. F. V. G. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9534-0 · Cited by 50
Slow, Reversible, Coupled Folding and Binding of the Spectrin Tetramerization Domain
Shammas, S. L., Rogers, J. M., Hill, S. A., & Clarke, J. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.10.012 · Cited by 46
Identification, recombinant production and structural characterization of four silk proteins from the Asiatic honeybee Apis cerana
Shi, J., Lua, S., Du, N., Liu, X., & Song, J. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.03.020 · Cited by 46
Evidence for a Coiled-coil Interaction Mode of Disordered Proteins from Bacterial Type III Secretion Systems
Gazi, A. D., Bastaki, M. N., Charova, S. N., Gkougkoulia, E. A., Kapellios, E. A., Panopoulos, N. J., & Kokkinidis, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803408200 · Cited by 43
TolA Modulates the Oligomeric Status of YbgF in the Bacterial Periplasm
Krachler, A. M., Sharma, A., Cauldwell, A. V., Papadakos, G. A., & Kleanthous, C. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.050 · Cited by 42
Self-assembly of stimuli-responsive coiled-coil fibrous hydrogels
Meleties, M., Katyal, P., Lin, B., Britton, D., & Montclare, J. K. (2021) · Soft Matter · doi:10.1039/d1sm00780g · Cited by 42
CCDC134, a novel secretory protein, inhibits activation of ERK and JNK, but not p38 MAPK
Huang, J., Shi, T., Ma, T., Zhang, Y., Ma, X., Lu, Y., Song, Q., Liu, W., Ma, D., & Qiu, X. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7448-5 · Cited by 39
Asynchronous replica exchange software for grid and heterogeneous computing
Gallicchio, E., Xia, J., Flynn, W. F., Zhang, B., Samlalsingh, S., Mentes, A., & Levy, R. M. (2015) · Computer Physics Communications · doi:10.1016/j.cpc.2015.06.010 · Cited by 38
Unique Features of the Anti-parallel, Heterodimeric Coiled-coil Interaction between Methyl-cytosine Binding Domain 2 (MBD2) Homologues and GATA Zinc Finger Domain Containing 2A (GATAD2A/p66α)
Walavalkar, N. M., Gordon, N. C., & Williams, D. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431346 · Cited by 38
Control of microtubule dynamics using an optogenetic microtubule plus end–F-actin cross-linker
Adikes, R. C., Hallett, R. A., Saway, B. F., Kuhlman, B. A., & Slep, K. C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201705190 · Cited by 36
Cardiomyopathy Mutations in the Tail of β-Cardiac Myosin Modify the Coiled-coil Structure and Affect Integration into Thick Filaments in Muscle Sarcomeres in Adult Cardiomyocytes
Wolny, M., Colegrave, M., Colman, L., White, E., Knight, P. J., & Peckham, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.513291 · Cited by 36
Deriving Structural Information from Experimentally Measured Data on Biomolecules
A, W. F. V. G., Allison, J. R., Daura, X., Dolenc, J., Hansen, N., Mark, A. E., Oostenbrink, C., Rusu, V. H., & Smith, L. J. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601828 · Cited by 35
A Coiled Coil Trigger Site Is Essential for Rapid Binding of Synaptobrevin to the SNARE Acceptor Complex
Wiederhold, K., Kloepper, T. H., Walter, A. M., Stein, A., Kienle, N., Sørensen, J. B., & Fasshauer, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105148 · Cited by 33
Conformational Dynamics of Asparagine at Coiled-Coil Interfaces
Thomas, F., Niitsu, A., Oregioni, A., Bartlett, G. J., & Woolfson, D. N. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00848 · Cited by 33
Structure of monomeric full‐length ARC sheds light on molecular flexibility, protein interactions, and functional modalities
Hallin, E. I., Eriksen, M. S., Baryshnikov, S., Nikolaienko, O., Grødem, S., Hosokawa, T., Hayashi, Y., Bramham, C. R., & Kursula, P. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14556 · Cited by 30
Methods of NMR structure refinement: molecular dynamics simulations improve the agreement with measured NMR data of a C-terminal peptide of GCN4-p1
Dolenc, J., Missimer, J. H., Steinmetz, M. O., & A, W. F. V. G. (2010) · Journal of Biomolecular NMR · doi:10.1007/s10858-010-9425-9 · Cited by 32
Self-citation
Coiled-Coil Formation on Lipid Bilayers—Implications for Docking and Fusion Efficiency
Pähler, G., Panse, C. H., Diederichsen, U., & Janshoff, A. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.08.053 · Cited by 31
Dissecting the behavior and function of MBD3 in DNA methylation homeostasis by single-molecule spectroscopy and microscopy
Cui, Y., & Irudayaraj, J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv098 · Cited by 30
Polymorphism in tropomyosin structure and function
Janco, M., Suphamungmee, W., Li, X., Lehman, W., Lehrer, S. S., & Geeves, M. A. (2013) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-013-9353-x · Cited by 30
The SNARE Motif of Synaptobrevin Exhibits an Aqueous–Interfacial Partitioning That Is Modulated by Membrane Curvature
Liang, B., Dawidowski, D., Ellena, J. F., Tamm, L. K., & Cafiso, D. S. (2014) · Biochemistry · doi:10.1021/bi401638u · Cited by 30
Peptide encapsulation regulated by the geometry of carbon nanotubes
Zhang, Z., Kang, Y., Liang, L., Liu, Y., Wu, T., & Wang, Q. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.11.041 · Cited by 28
Intrinsic disorder and coiled‐coil formation in prostate apoptosis response factor 4
Libich, D. S., Schwalbe, M., Kate, S., Venugopal, H., Claridge, J. K., Edwards, P. J. B., Dutta, K., & Pascal, S. M. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07087.x · Cited by 27
DEF6, a Novel Substrate for the Tec Kinase ITK, Contains a Glutamine-rich Aggregation-prone Region and Forms Cytoplasmic Granules that Co-localize with P-bodies
Hey, F., Czyzewicz, N., Jones, P., & Sablitzky, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346767 · Cited by 26
Molecular dynamics guided study of salt bridge length dependence in both fluorinated and non‐fluorinated parallel dimeric coiled‐coils
Pendley, S. S., Yu, Y. B., & Cheatham, T. E. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22177 · Cited by 26
Evidence for an Elongated Dimeric Structure of Heparin-Binding Hemagglutinin from Mycobacterium tuberculosis
Esposito, C., Pethoukov, M. V., Svergun, D. I., Ruggiero, A., Pedone, C., Pedone, E. M., & Berisio, R. (2008) · Journal of Bacteriology · doi:10.1128/jb.01988-07 · Cited by 25
Simulative and experimental investigation on the cleavage site that generates the soluble human LOX-1
Biocca, S., Arcangeli, T., Tagliaferri, E., Testa, B., Vindigni, G., Oteri, F., Giorgi, A., Iacovelli, F., Novelli, G., Desideri, A., et al. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.10.001 · Cited by 21
Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper
Sheftic, S. R., Snell, J. M., Jha, S., & Alexandrescu, A. T. (2012) · European Biophysics Journal · doi:10.1007/s00249-012-0846-0 · Cited by 20
Self-citation
Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments
Ramm, B., Stigler, J., Hinczewski, M., Thirumalai, D., Herrmann, H. O., Woehlke, G., & Rief, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403122111 · Cited by 20
Molecular studies on structural changes and oligomerisation of violaxanthin de-epoxidase associated with the pH-dependent activation
Hallin, E. I., Hasan, M., Guo, K., & Åkerlund, H. (2016) · Photosynthesis Research · doi:10.1007/s11120-016-0261-y · Cited by 20
Use of danazol for treatment of corticosteroid-resistant immune-mediated thrombocytopenia in a dog
Bloom, J. C., Meunier, L. D., Thiem, P. A., & Sellers, T. S. (1989) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.1989.194.01.76 · Cited by 19
Dihedral Angle Entropy Measures for Intrinsically Disordered Proteins
Cukier, R. I. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp5102412 · Cited by 18
Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination
Esposito, C., Carullo, P., Pedone, E. M., Graziano, G., Vecchio, P. D., & Berisio, R. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.044 · Cited by 16
Predicting the Effect of Ions on the Conformation of the H-NS Dimerization Domain
Vreede, J., & Dame, R. T. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.05.040 · Cited by 16
Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
Simm, D., Hatje, K., & Kollmar, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174639 · Cited by 16
Probing the Structure and Dynamics of Proteins by Combining Molecular Dynamics Simulations and Experimental NMR Data.
Allison, J. R., Hertig, S., Missimer, J., Smith, L. J., Steinmetz, M., & Dolenc, J. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300393b · Cited by 13
Self-citation
Electrostatic Contributions to the Stabilities of Native Proteins and Amyloid Complexes
Sheftic, S. R., Croke, R. L., Larochelle, J., & Alexandrescu, A. T. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)66010-9 · Cited by 15
Self-citation
Acidic pH triggers conformational changes at the NH2-terminal propeptide of the precursor of pulmonary surfactant protein B to form a coiled coil structure
Bañares-Hidalgo, Á., Pérez‐Gil, J., & Estrada, P. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.03.016 · Cited by 15
Dimerization of Tropomyosins
Gimona, M. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-85766-4_6 · Cited by 15
Specific sequence combinations at parallel and antiparallel helix–helix interfaces
Kurochkina, N. A. (2008) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2008.08.020 · Cited by 14
Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4
Buth, S. A., Menin, L., Shneider, M. M., Engel, J., Boudko, S. P., & Leiman, P. G. (2015) · Viruses · doi:10.3390/v7082839 · Cited by 14
A new set of atomic radii for accurate estimation of solvation free energy by Poisson–Boltzmann solvent model
Yamagishi, J., Okimoto, N., Morimoto, G., & Taiji, M. (2014) · Journal of Computational Chemistry · doi:10.1002/jcc.23728 · Cited by 14
Hamiltonian Replica Exchange Method Studies of a Leucine Zipper Dimer
Su, L., & Cukier, R. I. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp900309q · Cited by 14
Distribution of counterions and interaction between two similarly charged dielectric slabs: Roles of charge discreteness and dielectric inhomogeneity
Pezeshkian, W., Nikoofard, N., Norouzi, D., Mohammad-Rafiee, F., & Fazli, H. (2012) · Physical Review E · doi:10.1103/physreve.85.061925 · Cited by 13
Direct inhibition of NF-κB activation by peptide targeting the NOA ubiquitin binding domain of NEMO
Chiaravalli, J., Fontan, É., Fsihi, H., Coïc, Y., Baleux, F., Véron, M., & Agou, F. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.083 · Cited by 13
Transmission of Stability Information through the N-domain of Tropomyosin Is Interrupted by a Stabilizing Mutation (A109L) in the Hydrophobic Core of the Stability Control Region (Residues 97–118)
Kirwan, J. P., & Hodges, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507236 · Cited by 12
Coiled coils as possible models of protein structure evolution
Gáspári, Z., & Nyitray, L. (2011) · BioMolecular Concepts · doi:10.1515/bmc.2011.015 · Cited by 12
Exploring the trigger sequence of the GCN4 coiled‐coil: Biased molecular dynamics resolves apparent inconsistencies in NMR measurements
Missimer, J. H., Dolenc, J., Steinmetz, M. O., & A, W. F. V. G. (2010) · Protein Science · doi:10.1002/pro.528 · Cited by 11
Self-citation
The Disulfide Bonds within BST-2 Enhance Tensile Strength during Viral Tethering
Pont, K. E. D., McKenzie, A. M., Kokhan, O., Sumner, I., & Berndsen, C. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01362 · Cited by 10
Retention of Coiled-Coil Dimer Formation in the Absence of Ion Pairing at Positions Flanking the Hydrophobic Core
Biok, N. A., Passow, A. D., Wang, C., Bingman, C. A., Abbott, N. L., & Gellman, S. H. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00668 · Cited by 9
Critical interactions in the stability control region of tropomyosin
Kirwan, J. P., & Hodges, R. S. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.01.020 · Cited by 9
Designed Protein Origami
Drobnak, I., Ljubetič, A., Gradišar, H., Pisanski, T., & Jerala, R. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-39196-0_2 · Cited by 9
Bestimmung von Strukturinformation aus experimentellen Messdaten für Biomoleküle
A, W. F. V. G., Allison, J. R., Daura, X., Dolenc, J., Hansen, N., Mark, A. E., Oostenbrink, C., Rusu, V. H., & Smith, L. J. (2016) · Angewandte Chemie · doi:10.1002/ange.201601828 · Cited by 8
The trigger sequence in the GCN4 leucine zipper: α-helical propensity and multistate dynamics of folding and dimerization
Chapagain, P. P., Liu, Y., & Gerstman, B. S. (2008) · The Journal of Chemical Physics · doi:10.1063/1.3006421 · Cited by 8
Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix
Kaplan, A. R., Brady, M. R., Maciejewski, M. W., Kammerer, R. A., & Alexandrescu, A. T. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b00634 · Cited by 8
Self-citation
An EB1-binding motif acts as a microtubule tip localization signal
Honnappa, S., Gouveia, S. M., Weisbrich, A., Damberger, F. F., Bhavesh, N. S., Jawhari, H., Grigoriev, I., van Rijssel, F. J. A., Buey, R. M., Lawera, A., et al. (2009) · Cell · doi:10.1016/j.cell.2009.04.065 · Cited by 611
Self-citation
Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction
Weidner, P., Saar, D., Söhn, M., Schroeder, T., Yu, Y., Zöllner, F. G., Ponelies, N., Zhou, X., Zwicky, A., Rohrbacher, F. N., et al. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216783 · Cited by 7
Complementary Peptide Interactions Support the Ultra-Rigidity of Polymers of De Novo Designed Click-Functionalized Bundlemers
Yang, D.-B., Zhang, T., Blum, J. E., Kloxin, C. J., Pochan, D. J., & Saven, J. G. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c06403 · Cited by 7
A Hamiltonian replica exchange method for building protein–protein interfaces applied to a leucine zipper
Cukier, R. I. (2011) · The Journal of Chemical Physics · doi:10.1063/1.3548074 · Cited by 7
Heterotrimeric Coiled Coils with Core Residue Urea Side Chains
Diss, M. L., & Kennan, A. J. (2008) · The Journal of Organic Chemistry · doi:10.1021/jo802379p · Cited by 7
Simulations of Temperature and Salt Concentration Effects on bZIP, a Basic Region Leucine Zipper
Cukier, R. I. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp300836t · Cited by 7
Rationally designed coiled-coil DNA looping peptides control DNA topology
Gowetski, D. B., Kodis, E. J., & Kahn, J. D. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt553 · Cited by 6
Structural basis of RNA binding by leucine zipper GCN4
Nikolaev, Y., & Pervushin, K. V. (2012) · Protein Science · doi:10.1002/pro.2051 · Cited by 6
Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc
Hallin, E. I., Markússon, S., Böttger, L., Torda, A. E., Bramham, C. R., & Kursula, P. (2021) · PLoS ONE · doi:10.1371/journal.pone.0251459 · Cited by 6
Insight into the Role of the Hv1 C-Terminal Domain in Dimer Stabilization
Boonamnaj, P., & Sompornpisut, P. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b08669 · Cited by 6
GCN4 enhances the stability of the pore domain of potassium channel KcsA
Yuchi, Z., Pau, V. P. T., & Yang, D. S. C. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06747.x · Cited by 6
Identifying the genetic and epigenetic basis for asymmetric bZIP expression in temperature-stressed bread wheat
Kaur, R., Singh, D., Singh, P. K., Kaur, G., Shah, K., Pandey, H., Devi, S. G., Pandey, A. K., & Rishi, V. (2024) · Plant Growth Regulation · doi:10.1007/s10725-024-01129-x · Cited by 5
A modular approach for organizing dimeric coiled coils on peptoid oligomer scaffolds
Jiang, L., & Kirshenbaum, K. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00453g · Cited by 5
Spatially organized nanoassembly of single-chain TRAIL that induces optimal death receptor clustering and cancer-specific apoptosis
Shin, G., Lee, J. E., Lee, D.-H., Lee, D.-H., & Lim, S. I. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.105638 · Cited by 4
Structural Basis for the Oligomerization-State Switch from a Dimer to a Trimer of an Engineered Cortexillin-1 Coiled-Coil Variant
Bjelić, S., Wieser, M. M., FREY, D. J., Stirnimann, C. U., Chance, M. R., Jaussi, R., Steinmetz, M. O., & Kammerer, R. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063370 · Cited by 4
Self-citation
Nanomaterials based on peptides
Rodina, E. V. (2012) · Polymer Science Series C · doi:10.1134/s1811238212050025 · Cited by 4
Stabilization of Native and Non-native Structures by Salt Bridges in a Lattice Model of the GCN4 Leucine Dimer
Liu, Y., Chapagain, P. P., & Gerstman, B. S. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp909872a · Cited by 4
Supramolecular replication of peptide and DNA patterned arrays
Laromaine, A., Akbulut, Ö., Stellacci, F., & Stevens, M. M. (2009) · Journal of Materials Chemistry · doi:10.1039/b915803k · Cited by 4

Authors: Steinmetz, M. O., Jelesarov, I., Matousek, W. M., Honnappa, S., Jahnke, W., Missimer, J. H., Frank, S., Alexandrescu, A. T., & Kammerer, R. A.
Affiliations: Paul Scherrer Institute (CH)
University of Zurich (CH)
University of Connecticut (US)
*Biomolecular Research, Structural Biology, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;
Novartis (Switzerland) (CH)
F. Hoffmann-La Roche AG (CH)
Wellcome Centre for Cell-Matrix Research (GB)
ORCID: Steinmetz, Michel O.
Jelesarov, Ilian
Jahnke, Wolfgang
Missimer, John H.
Frank, Sabine
Alexandrescu, Andrei T.
Kammerer, Richard A.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-04-24
Volume: 104
Issue: 17
Pages: 7062-7067
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0700321104
PMC: PMC1855353
OpenAlex: W2032892814
Cited by: 136
References: 61
Citations by year: 2026: 2 · 2025: 6 · 2024: 9 · 2022: 1 · 2021: 2 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 7 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 13 · 2012: 15
FWCI: 4.91
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
DORA PSI (Paul Scherrer Institute) (submittedVersion)
Research Explorer (The University of Manchester) (submittedVersion)
Funders: Wellcome Trust
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (109423)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: GCN4, leucine zipper, helix stabilization, hydrogen bonding, electrostatic interactions, protein folding mechanism, dimerization
MeSH terms: Arginine, DNA-Binding Proteins, Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy, Peptides, Solutions, Thermodynamics, Transcription Factors, Leucine Zippers, Protein Folding, Amino Acid Substitution, Saccharomyces cerevisiae Proteins, Mutant Proteins, Basic-Leucine Zipper Transcription Factors

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Molecular basis of coiled-coil formation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks