Cited by 422Protein Structure and DynamicsGenomics and Chromatin DynamicsChemical Synthesis and Analysis

The DOI matches its Crossref record; 25 of the 26 references it cites were found in a registry or an index.

Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

O'Shea, Erin K., Rutkowski, Rheba, Kim, Peter S.·1992·Cell

Open this paper in CoChat — free account

Abstract

Fos and Jun, the protein products of the nuclear proto-oncogenes c-fos and c-jun, associate preferentially to form a heterodimer that binds to DNA and modulates transcription of a wide variety of genes in response to mitogenic stimuli. Both Fos and Jun contain a single leucine zipper region. Previous studies have shown that the leucine zippers of Fos and Jun are necessary and sufficient to mediate preferential heterodimer formation. The leucine zipper regions from Fos and Jun are also known to fold autonomously, most likely as two-stranded, parallel coiled coils. We show here that 8 amino acids from Fos and from Jun are sufficient to mediate preferential heterodimer formation in a background of the GCN4 leucine zipper sequence. Using pH titration and amino acid replacements, we also show that destabilization of the Fos homodimer by acidic residues provides a major thermodynamic driving force for preferential heterodimer formation.

Integrity signals

Registry

Crossref · 10.1016/0092-8674(92)90145-3

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, 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?

The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438
Biophysical chemistry
Spragg, S. P. (1979) · Nature · doi:10.1038/278085a0 · Cited by 1,707
Fos and jun: The AP-1 connection
Curran, T., & Franza, B. R. (1988) · Cell · doi:10.1016/0092-8674(88)90024-4 · Cited by 1,595
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
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
Self-citation
Human Proto-Oncogene c- jun Encodes a DNA Binding Protein with Structural and Functional Properties of Transcription Factor AP-1
Bohmann, D., Bos, T. J., Admon, A., Nishimura, T., Vogt, P. K., & Tjian, R. (1987) · Science · doi:10.1126/science.2825349 · Cited by 1,321
Evidence That the Leucine Zipper Is a Coiled Coil
O’Shea, E. K., Rutkowski, R., & Kim, P. S. (1989) · Science · doi:10.1126/science.2911757 · Cited by 837
Self-citation
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
Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral and cellular fos gene products have different carboxy termini
Beveren, C. V., van Straaten, F., Curran, T., Müller, R., & Verma, I. M. (1983) · Cell · doi:10.1016/0092-8674(83)90306-9 · Cited by 524

Show all 26 references

Sorted by citations

Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
Moi, P., Chan, K., Asunis, I., Cao, A., & Kan, Y. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9926 · Cited by 1,607
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
Protein-protein interactions: methods for detection and analysis
Phizicky, E. M., & Fields, S. (1995) · Microbiological Reviews · doi:10.1128/mr.59.1.94-123.1995 · Cited by 977
A spring-loaded mechanism for the conformational change of influenza hemagglutinin
Carr, C. M., & Kim, P. S. (1993) · Cell · doi:10.1016/0092-8674(93)90260-w · Cited by 857
Self-citation
Life without white fat: a transgenic mousePreprint
Moitra, J., Mason, M. M., Olive, M., Krylov, D. Y., Gavrilova, O., Marcus‐Samuels, B., Feigenbaum, L., Lee, E., Aoyama, T., Eckhaus, M., et al. (1998) · Genes & Development · doi:10.1101/gad.12.20.3168 · Cited by 776
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex
Ellenberger, T. E., Brandl, C. J., Struhl, K., & Harrison, S. C. (1992) · Cell · doi:10.1016/s0092-8674(05)80070-4 · Cited by 972
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 734
Genomic Survey and Gene Expression Analysis of the Basic Leucine Zipper Transcription Factor Family in Rice
Nijhawan, A., Jain, M., Tyagi, A. K., & Khurana, J. P. (2007) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.112821 · Cited by 720
The AP2 domain of APETALA2 defines a large new family of DNA binding proteins in Arabidopsis
Okamuro, J. K., Caster, B., Villarroel, R., MONTAGU, M. V., & Jofuku, K. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.7076 · Cited by 682
Do salt bridges stabilize proteins? A continuum electrostatic analysis
Hendsch, Z. S., & Tidor, B. (1994) · Protein Science · doi:10.1002/pro.5560030206 · Cited by 634
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
Self-citation
Proteomics Analysis of A33 Immunoaffinity-purified Exosomes Released from the Human Colon Tumor Cell Line LIM1215 Reveals a Tissue-specific Protein Signature
Mathivanan, S., Lim, J. W. E., Tauro, B. J., Ji, H. L., Moritz, R. L., & Simpson, R. J. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900152-mcp200 · Cited by 614
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
Hybrid hydrogels assembled from synthetic polymers and coiled-coil protein domains
Wang, C., Stewart, R. J., & Kopec̆ek, J. (1999) · Nature · doi:10.1038/17092 · Cited by 583
Oncogenic activity of the c-Myc protein requires dimerization with Max
Amati, B. B., Brooks, M. W., Levy-Strumpf, N., Littlewood, T. D., Evan, G. I., & Land, H. (1993) · Cell · doi:10.1016/0092-8674(93)90663-b · Cited by 566
Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472
Self-citation
Cyclic Adenosine 3′,5′-Monophosphate Response Element Binding Protein (CREB) and Related Transcription-Activating Deoxyribonucleic Acid-Binding Proteins*
MEYER, T. E., & Habener, J. F. (1993) · Endocrine Reviews · doi:10.1210/edrv-14-3-269 · Cited by 470
Distinct roles of Jun : Fos and Jun : ATF dimers in oncogenesis
van Dam, H., & Castellazzi, M. (2001) · Oncogene · doi:10.1038/sj.onc.1204239 · Cited by 462
Comprehensive Identification of Human bZIP Interactions with Coiled-Coil Arrays
Newman, J. R. S., & Keating, A. E. (2003) · Science · doi:10.1126/science.1084648 · Cited by 449
Classification of Human B-ZIP Proteins Based on Dimerization Properties
Vinson, C., Myakishev-Rempel, M., Acharya, A., Mir, A. A., Moll, J. R., & Bonovich, M. T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6321-6335.2002 · Cited by 464
Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer.Preprint
Ellenberger, T., Fass, D., Arnaud, M., & Harrison, S. C. (1994) · Genes & Development · doi:10.1101/gad.8.8.970 · Cited by 445
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 439
Self-citation
A Coiled-Coil Oligomerization Domain of Bcr Is Essential for the Transforming Function of Bcr-Abl Oncoproteins
McWhirter, J. R., Galasso, D. L., & Wang, J. Y. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7587 · Cited by 422
Transcriptional regulation in the immune system: all roads lead to AP-1
Foletta, V. C., Segal, D., & Cohén, D. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.63.2.139 · Cited by 393
Molecular Genetics of Mating Recognition in Basidiomycete Fungi
Casselton, L. A., & Olesnicky, N. S. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.55-70.1998 · Cited by 353
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
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
Small-molecule antagonists of Myc/Max dimerization inhibit Myc-induced transformation of chicken embryo fibroblasts
Berg, T., Cohen, S. B., Desharnais, J., Sonderegger, C. K., Maslyar, D. J., Goldberg, J., Boger, D. L., & Vogt, P. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062036999 · Cited by 326
JunB differs from c-Jun in its DNA-binding and dimerization domains, and represses c-Jun by formation of inactive heterodimers.Preprint
Deng, T., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.3.479 · Cited by 328
DIMERIZATION AS A REGULATORY MECHANISM IN SIGNAL TRANSDUCTION
Klemm, J. D., Schreiber, S. L., & Crabtree, G. R. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.569 · Cited by 323
New protein engineering approaches to multivalent and bispecific antibody fragments
Plückthun, A., & Pack, P. (1997) · Immunotechnology · doi:10.1016/s1380-2933(97)00067-5 · Cited by 322
Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras
Pfarr, C. M., Mechta‐Grigoriou, F., Spyrou, G., Lallemand, D., Carillo, S., & Yaniv, M. (1994) · Cell · doi:10.1016/0092-8674(94)90513-4 · Cited by 311
Structure of the leucine zipper
Alber, T. (1992) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(05)80275-8 · Cited by 277
Optimizing the stability of single-chain proteins by linker length and composition mutagenesis
Robinson, C. R., & Sauer, R. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5929 · Cited by 271
Multiallelic recognition: Nonself-dependent dimerization of the bE and bW homeodomain proteins in ustilago maydis
Kämper, J., Reichmann, M., Romeis, T., Bölker, M., & Kahmann, R. (1995) · Cell · doi:10.1016/0092-8674(95)90372-0 · Cited by 270
A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.
Krylov, D., Mikhailenko, I., & Vinson, C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06579.x · Cited by 269
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
Self-citation
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
Peptide conformation and protein folding
Dyson, H. J., & Wright, P. E. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90203-w · Cited by 235
Modular Design in Natural and Biomimetic Soft Materials
Kushner, A. M., & Guan, Z. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201006496 · Cited by 231
Laminins and other strange proteins
Engel, J. (1992) · Biochemistry · doi:10.1021/bi00159a001 · Cited by 203
Promoter Specificity and Biological Activity of Tethered AP-1 Dimers
Bakiri, L., Matsuo, K., Wisniewska, M. B., Wagner, E. F., & Yaniv, M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4952-4964.2002 · Cited by 205
Immunochemical Characterization and Transacting Properties of Upstream Stimulatory Factor Isoforms
Viollet, B., Lefrançois‐Martinez, A., Henrion‐Caude, A., Kahn, A., Raymondjean, M., & Martinez, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1405 · Cited by 196
Fos and Jun repress transcription activation by NF-IL6 through association at the basic zipper region
Hsu, W., Kerppola, T. K., Chen, P., Curran, T., & Chen‐Kiang, S. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.268 · Cited by 199
Interactions of coiled coils in transcription factors: where is the specificity?
Baxevanis, A. D., & Vinson, C. (1993) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(93)90035-n · Cited by 182
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 185
Genome-wide systematic characterization of the bZIP transcriptional factor family in tomato (Solanum lycopersicum L.)
Li, D., Fu, F., Zhang, H., & Song, F. (2015) · BMC Genomics · doi:10.1186/s12864-015-1990-6 · Cited by 180
Coiled-coils: stability, specificity, and drug delivery potential
Yu, Y. B. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00058-3 · Cited by 176
The Role of Activator Protein-1 (AP-1) Family Members in CD30-Positive Lymphomas
Alonso, I. G. D. L. F., Liang, H.-C., Turner, S. D., Lagger, S., Merkel, O., & Kenner, L. (2018) · Cancers · doi:10.3390/cancers10040093 · Cited by 167
Coiled‐Coil Peptide‐Based Assembly of Gold Nanoparticles
Stevens, M. M., Flynn, N. T., Wang, C., Tirrell, D. A., & Langer, R. (2004) · Advanced Materials · doi:10.1002/adma.200306430 · Cited by 170
Electrostatic Interactions Control the Parallel and Antiparallel Orientation of .alpha.-Helical Chains in Two-Stranded .alpha.-Helical Coiled-Coils
Monera, O. D., Kay, C. M., & Hodges, R. S. (1994) · Biochemistry · doi:10.1021/bi00179a010 · Cited by 170
Programmed Self-Sorting of Coiled Coils with Leucine and Hexafluoroleucine Cores
Bilgiçer, B., Xing, X., & Kumar, K. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016767o · Cited by 169
Fortuitous convergences: the beginnings of JUN
Vogt, P. K. (2002) · Nature reviews. Cancer · doi:10.1038/nrc818 · Cited by 169
The basic region of AP-1 specifies glucocorticoid receptor activity at a composite response element.Preprint
Miner, J. N., & Yamamoto, K. R. (1992) · Genes & Development · doi:10.1101/gad.6.12b.2491 · Cited by 156
Measurement of Interhelical Electrostatic Interactions in the GCN4 Leucine Zipper
Lumb, K. J., & Kim, P. S. (1995) · Science · doi:10.1126/science.7716550 · Cited by 156
Self-citation
De novo design of α-helical proteins: basic research to medical applications
Hodges, R. S. (1996) · Biochemistry and Cell Biology · doi:10.1139/o96-015 · Cited by 155
DNA-binding and dimerization preferences of Arabidopsis homeodomain-leucine zipper transcription factors in vitro
Johannesson, H., Wang, Y., & Engström, P. (2001) · Plant Molecular Biology · doi:10.1023/a:1006423324025 · Cited by 154
Small-molecule inhibitors of the Myc oncoprotein
Fletcher, S., & Prochownik, E. V. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.005 · Cited by 160
Designed heterodimerizing leucine zippers with a ranger of pIs and stabilities up to 10−15 M
Moll, J. R., Ruvinov, S., Pastan, I., & Vinson, C. (2001) · Protein Science · doi:10.1110/ps.39401 · Cited by 153
Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design
Mason, J. M., Schmitz, M. A., Müller, K. M., & Arndt, K. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509880103 · Cited by 151
Synthesis and Characterization of Dimaleimide Fluorogens Designed for Specific Labeling of Proteins
Girouard, S., Houle, M.-H., Grandbois, A., Keillor, J. W., & Michnick, S. W. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045742x · Cited by 149
A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae
Newman, J. R., Wolf, E., & Kim, P. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13203 · Cited by 150
Self-citation
c-fos proto-oncogene regulation and function
Piechaczyk, M., & Blanchard, J. (1994) · Critical Reviews in Oncology/Hematology · doi:10.1016/1040-8428(94)90021-3 · Cited by 151
Kinetics of Folding of Leucine Zipper Domains
Wendt, H., Berger, C. E. M., Baici, A., Thomas, R. M., & Bosshard, H. R. (1995) · Biochemistry · doi:10.1021/bi00012a028 · Cited by 147
A Designed Heterotrimeric Coiled Coil
Nautiyal, S., Woolfson, D. N., King, D., & Alber, T. (1995) · Biochemistry · doi:10.1021/bi00037a001 · Cited by 141
Inter-helical interactions in the leucine zipper coiled coil dimer: ph and salt dependence of coupling energy between charged amino acids
Krylov, D. Y., Barchi, J., & Vinson, C. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1762 · Cited by 136
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
Cross-Species Annotation of Basic Leucine Zipper Factor Interactions: Insight into the Evolution of Closed Interaction Networks
Deppmann, C. D., Alvania, R. S., & Taparowsky, E. J. (2006) · Molecular Biology and Evolution · doi:10.1093/molbev/msl022 · Cited by 136
Pharmaceutical research in molecular oncology
Gibbs, J. (1994) · Cell · doi:10.1016/0092-8674(94)90189-9 · Cited by 132
Identification, molecular cloning, and characterization of dual leucine zipper bearing kinase. A novel serine/threonine protein kinase that defines a second subfamily of mixed lineage kinases.
Holzman, L. B., Merritt, S. E., & Fan, G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47353-x · Cited by 128
Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 å resolution
PÁRRAGA, A., Bellsolell, L., Ferré-D’Amaré, A. R., & Burley, S. K. (1998) · Structure · doi:10.1016/s0969-2126(98)00067-7 · Cited by 126
Computational approaches to identify leucine zippers
Bornberg‐Bauer, E. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.11.2740 · Cited by 128
Getting a grip on DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains
Ellenberger, T. (1994) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(94)90054-x · Cited by 124
Radiolytic Modification of Basic Amino Acid Residues in Peptides: Probes for Examining Protein−Protein Interactions
Xu, G., Takamoto, K., & Chance, M. R. (2003) · Analytical Chemistry · doi:10.1021/ac035104h · Cited by 126
Selective Dimerization of a C2H2 Zinc Finger Subfamily
McCarty, A. S., Kleiger, G., Eisenberg, D. S., & Smale, S. T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00043-1 · Cited by 126
Barstar is electrostatically optimized for tight binding to barnase.
Tidor, B., & Lee, L. (2001) · Nature Structural Biology · doi:10.1038/83082 · Cited by 125
Isolation of cDNA encoding the human NF-E2 protein.
Chan, J. Y., Han, X. L., & Kan, Y. W. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11366 · Cited by 123
Protein destabilization by electrostatic repulsions in the two‐stranded α‐helical coiled‐coil/leucine zipper
Kohn, W. D., Kay, C. M., & Hodges, R. S. (1995) · Protein Science · doi:10.1002/pro.5560040210 · Cited by 124
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
The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils
Dieckmann, G. R., McRorie, D. K., Lear, J. D., Sharp, K. A., DeGrado, W. F., & Pecoraro, V. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1891 · Cited by 122
Studies on p40, the leucine zipper motif-containing protein encoded by the first open reading frame of an active human LINE-1 transposable element.
Holmes, S. E., Singer, M., & Swergold, G. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)88618-0 · Cited by 121
SMiLE-seq identifies binding motifs of single and dimeric transcription factors
Isakova, A., Groux, R., Imbeault, M., Rainer, P. Y., Alpern, D., Dainese, R., Ambrosini, G., Trono, D., Bücher, P., & Deplancke, B. (2017) · Nature Methods · doi:10.1038/nmeth.4143 · Cited by 118
Review: Protein Design—Where We Were, Where We Are, Where We're Going
Pokala, N., & Handel, T. M. (2001) · Journal of Structural Biology · doi:10.1006/jsbi.2001.4349 · Cited by 120
Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a comparison to Homo sapiens B-ZIP motifs
Deppmann, C. D. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh653 · Cited by 117
A bZIP protein, sisterless-a, collaborates with bHLH transcription factors early in Drosophila development to determine sex.Preprint
Erickson, J. W., & Cline, T. W. (1993) · Genes & Development · doi:10.1101/gad.7.9.1688 · Cited by 119
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
MULTIPROTEIN-DNA COMPLEXES IN TRANSCRIPTIONAL REGULATION
Wolberger, C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.29 · Cited by 117
Genome-wide analysis of the basic leucine zipper (bZIP) transcription factor gene family in six legume genomes
Wang, Z., Cheng, K., Wan, L., Yan, L., Jiang, H., Liu, S., Lei, Y. H., & Liao, B. (2015) · BMC Genomics · doi:10.1186/s12864-015-2258-x · Cited by 116
Salt effects on protein stability: two-strandedα-helical coiled-coils containing inter- or intrahelical ion pairs
Kohn, W. D., Kay, C. M., & Hodges, R. S. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0930 · Cited by 117
Defective dorsal closure and loss of epidermal decapentaplegic expression in Drosophila fos mutants
Zeitlinger, J., Kockel, L., Peverali, F. A., Jackson, D. B., Mlodzik, M., & Bohmann, D. (1997) · The EMBO Journal · doi:10.1093/emboj/16.24.7393 · Cited by 115
Autocrine growth and anchorage independence: two complementing Jun-controlled genetic programs of cellular transformationPreprint
van Dam, H., Huguier, S., Kooistra, K., Baguet, J., Vial, E., van der Eb, A. J., Herrlich, P. A., Angel, P. E., & Castellazzi, M. (1998) · Genes & Development · doi:10.1101/gad.12.8.1227 · Cited by 112
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 114
Interferon‐inducible Mx proteins in fish
Leong, J. C., Trobridge, G. D., Kim, C. H., Johnson, M. C., & Simon, B. E. (1998) · Immunological Reviews · doi:10.1111/j.1600-065x.1998.tb01275.x · Cited by 111
Interferon-induced Mx proteins form oligomers and contain a putative leucine zipper.
Melén, K., Ronni, T., Broni, B. A., Krug, R. M., von Bonsdorff, C. ‐., & Julkunen, I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35693-x · Cited by 110
A Heterodimer of the Zn2Cys6 Transcription Factors Pip2p and Oaf1p Controls Induction of Genes Encoding Peroxisomal Proteins in Saccharomyces Cerevisiae
Rottensteiner, H., Kal, A. J., Hamilton, B., Ruis, H., & Tabak, H. F. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00776.x · Cited by 109
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
Transcription factor AP‐1, and the role of Fra‐2
Foletta, V. C. (1996) · Immunology and Cell Biology · doi:10.1038/icb.1996.17 · Cited by 109
The rat hepatic leukemia factor (HLF) gene encodes two transcriptional activators with distinct circadian rhythms, tissue distributions and target preferences.
Falvey, E., Fleury-Olela, F., & Schibler, U. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00105.x · Cited by 105
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 105

Authors: O'Shea, E. K., Rutkowski, R., & Kim, P. S.
Affiliations: Howard Hughes Medical Institute (US)
Massachusetts Institute of Technology (US)
ORCID: Kim, Peter S.
Venue: Cell
Publisher: Elsevier BV
Published: 1992-02
Volume: 68
Issue: 4
Pages: 699-708
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(92)90145-3
OpenAlex: W2066101080
Cited by: 422
References: 26
Citations by year: 2026: 1 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 8 · 2018: 3 · 2017: 9 · 2016: 5 · 2015: 7 · 2014: 7 · 2013: 7 · 2012: 14
FWCI: 13.51
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Rita Allen Foundation
Allen Foundation
National Institutes of Health (2r01gm044162-10)
National Institute of General Medical Sciences (GM44162)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: Fos-Jun heterodimer, leucine zipper, c-fos, c-Jun, protein-protein interaction specificity, coiled coil, GCN4 leucine zipper, acidic residues, pH titration, amino acid substitutions, transcriptional regulation, mitogenic signaling
MeSH terms: Amino Acid Sequence, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Conformation, Thermodynamics, Molecular Structure, Leucine Zippers, Proto-Oncogene Proteins c-jun, Proto-Oncogene Proteins c-fos

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

Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

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