Mechanism of specificity in the Fos-Jun oncoprotein heterodimer

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

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

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

The leucine zipper may induce electrophoretic mobility anomalies without DNA bending

McCormick, R. J., Badalian, T. M., & Fisher, D. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14434 · Cited by 20

Molecular characterization of EAP-300: a high molecular weight, embryonic polypeptide contning an amino acid repeat comprised of multiple leucine-zipper motifs

Kelly, M. M., Phanhthourath, C., Brees, D. K., McCabe, C. F., & Cole, G. J. (1995) · Developmental Brain Research · doi:10.1016/0165-3806(94)00185-3 · Cited by 20

Mcm10 Self-Association Is Mediated by an N-Terminal Coiled-Coil Domain

Du, W., Josephrajan, A., Adhikary, S., Bowles, T. M., Bielinsky, A., & Eichman, B. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070518 · Cited by 19

Co-regulation by Notch and Fos is required for cell fate specification of intermediate precursors duringC. elegansuterine development

Oommen, K. S., & Newman, A. P. (2007) · Development · doi:10.1242/dev.002741 · Cited by 19

How kinesin-2 forms a stalk

Vukajlovic, M., Dietz, H., Schliwa, M., & Ökten, Z. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0112 · Cited by 19

Plant Disease Resistance: Commonality and Novelty in Multicellular Innate Immunity

Fluhr, R., & Kaplan‐Levy, R. N. (2002) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-59430-4_2 · Cited by 19

The AP-1 family of transcription factors are important regulators of gene expression within Leydig cells

Nguyen, H. T., Najih, M., & Martin, L. J. (2021) · Endocrine · doi:10.1007/s12020-021-02888-7 · Cited by 18

The Steroidogenic Acute Regulatory Protein (StAR)

Clark, B. J., & Stocco, D. M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1112-7_2 · Cited by 19

Multiple Forms of C/EBPβ Bind the EFII Enhancer Sequence in the Rous Sarcoma Virus Long Terminal Repeat

Sears, R. C., & Sealy, L. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4855-4871.1994 · Cited by 18

Tunable Energy Transfer Rates via Control of Primary, Secondary, and Tertiary Structure of a Coiled Coil Peptide Scaffold

Wilger, D. J., Bettis, S. E., Materese, C. K., Minakova, M., Papoian, G. A., Papanikolas, J. M., & Waters, M. L. (2012) · Inorganic Chemistry · doi:10.1021/ic300669t · Cited by 17

JNK-Dependent cJun Phosphorylation Mitigates TGFβ- and EGF-Induced Pre-Malignant Breast Cancer Cell Invasion by Suppressing AP-1-Mediated Transcriptional Responses

Sundqvist, A., Voytyuk, O., Hamdi, M., Popeijus, H. E., van der Burgt, C., Janssen, J. M., Martens, J. W. M., Moustakas, A., Heldin, C., ten Dijke, P., et al. (2019) · Cells · doi:10.3390/cells8121481 · Cited by 17

Alzheimer's Disease Aβ Peptide Fragment 10–30 Forms a Spectrum of Metastable Oligomers with Marked Preference for N to N and C to C Monomer Termini Proximity

Jabłonowska, A., Bakun, M., Kupniewska-Kozak, A., & Dadlez, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.083 · Cited by 17

DNA binding and transactivation properties of Fos variants with homodimerization capacity

Porte, D. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.15.3026 · Cited by 17

Dissecting the Role of Leucine Zippers in the Binding of bZIP Domains of Jun Transcription Factor to DNA

Seldeen, K., McDonald, C. B., Deegan, B. J., Bhat, V., & Farooq, A. (2010) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2010.03.116 · Cited by 15

A Heterospecific Leucine Zipper Tetramer

Deng, Y., Liu, J., Zheng, Q., Li, Q., Kallenbach, N. R., & Lu, M. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.07.008 · Cited by 16

Predicting Protein Secondary and Supersecondary Structure

Singh, M. (2005) · Chapman & Hall/CRC computer and information science series · doi:10.1201/9781420036275.pt7 · Cited by 17

Evidence that the bZIP domains of the Jun transcription factor bind to DNA as monomers prior to folding and homodimerization

Seldeen, K. L., McDonald, C. B., Deegan, B. J., & Farooq, A. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.010 · Cited by 15

Change in oligomerization specificity of the p53 tetramerization domain by hydrophobic amino acid substitutions

Stavridi, E. S., Caruso, L. C., Chehab, N. H., & Halazonetis, T. D. (1999) · Protein Science · doi:10.1110/ps.8.9.1773 · Cited by 15

Solvent-exposed Residues in the Tet repressor (TetR) Four-helix Bundle Contribute to Subunit Recognition and Dimer Stability

Schnappinger, D., Schubert, P., Berens, C., Pfleiderer, K., & Hillen, W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6405 · Cited by 15

Self-assembly of the bZIP transcription factor ΔFosB

Zhou, Y., Venkannagari, H., Lynch, H. M., Aglyamova, G. V., Bhandari, M., Machius, M., Nestler, E. J., Robison, A. J., & Rudenko, G. (2019) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2019.12.001 · Cited by 14

FOS gene associated immune infiltration signature in perivascular adipose tissues of abdominal aortic aneurysm

Ding, S., Gan, T., Xiang, Y., Zhu, X., Jin, Y., Ning, H., Guo, T., Zhao, S., Xie, J., & Yuan, Z. (2022) · Gene · doi:10.1016/j.gene.2022.146576 · Cited by 14

Acid-Induced Polymerization of the Group 5 Mite Allergen from Dermatophagoides pteronyssinus

Liaw, S., Chen, H.-Z., Liu, G.-G., & Chua, K.-Y. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5184 · Cited by 14

Polyionic fusion peptides function as specific dimerization motifs

Richter, S. A., Stubenrauch, K. G., Lilie, H., & Rudolph, R. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.10.775 · Cited by 14

[18] Molecular applications of fusions to leucine zippers

Rieker, J. D., & Hu, J. C. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)28403-6 · Cited by 14

Modulares Design in natürlichen und biomimetischen elastischen Materialien

Kushner, A. M., & Guan, Z. (2011) · Angewandte Chemie · doi:10.1002/ange.201006496 · Cited by 13

Homodimerization and Heterodimerization of Minimal Zinc(II)-Binding-Domain Peptides of T-Cell Proteins CD4, CD8α, and Lck

Davis, A. M., & Berg, J. M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9028928 · Cited by 13

A Modular and Noncovalent Transduction System for Leucine‐Zipper‐Tagged Proteins

Hansen, M. B., Verdurmen, W. P. R., Leunissen, E. H. P., Minten, I. J., van Hest, J. C. M., Brock, R. E., & Löwik, D. W. P. M. (2011) · ChemBioChem · doi:10.1002/cbic.201100481 · Cited by 13

Structural and Biochemical Analysis of Signal Transduction by the TRAF Family of Adapter ProteinsPreprint

McWhirter, S. M., Pullen, S. S., WERNEBURG, B. G., Labadia, M. E., Ingraham, R. H., Crute, J. J., Kehry, M. R., & Alber, T. (1999) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1999.64.551 · Cited by 14

Transcription Factors as Molecular Mediators in Cell Death

Soares, H. D., Curran, T., & MORGAN, J. I. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44408.x · Cited by 13

Cloning of a gene encoding a human leukocyte protein characterised by extensive heptad repeats

Print, C. G., Leung, E. Y., Harrison, J. E. B., Watson, J. D., & Krissansen, G. W. (1994) · Gene · doi:10.1016/0378-1119(94)90381-6 · Cited by 13

Structure and dynamic association of an assembly platform subcomplex of the bacterial type II secretion system

Dazzoni, R., Li, Y., López‐Castilla, A., Brier, S., Méchaly, A., Cordier, F., Haouz, A., Nilges, M., Francetić, O., Bardiaux, B., et al. (2022) · Structure · doi:10.1016/j.str.2022.12.003 · Cited by 12

Impact of Lactational Exposure to Polychlorinated Biphenyl Causes Epigenetic Modification and Impairs Sertoli Cells Functional Regulators in F1 Progeny

Priya, E. S., Kumar, T. S., Singh, P., Balakrishnan, S., & Arunakaran, J. (2017) · Reproductive Sciences · doi:10.1177/1933719117699707 · Cited by 12

Improving the interaction of Myc‐interfering peptides with Myc using molecular dynamics simulations

Jouaux, E. M., Timm, B., Arndt, K. M., & Exner, T. E. (2008) · Journal of Peptide Science · doi:10.1002/psc.1078 · Cited by 13

Contribution of the Transcription Factors Sp1/Sp3 and AP-1 to Clusterin Gene Expression during Corneal Wound Healing of Tissue-Engineered Human Corneas

Gross, C., Le‐Bel, G., Desjardins, P., Benhassine, M., Germain, L., & Guérin, S. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212426 · Cited by 11

A novel type of dimerization motif, related to leucine zippers, is present in plant homeodomain proteins

Palena, C., Chan, R. L., & González, D. H. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(97)00012-2 · Cited by 11

α-helical coiled coils: simple models for self-associating peptide and protein systemss

Thomas, R. M., Wendt, H., Zampieri, A., & Bosshard, H. R. (2007) · Steinkopff eBooks · doi:10.1007/bfb0114066 · Cited by 11

Characterization of the Joining Chain (J‐Chain) Promoter

Sigvardsson, M., OLSSON, L., Högbom, E., & Leanderson, T. (1993) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1993.tb02581.x · Cited by 10

Analysis of CYS3 regulator function inNeurospora crassaby modification of leucine zipper dimerization specificity

Paietta, J. V. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.6.1044 · Cited by 10

Biochemical and Molecular Dynamic Simulation Analysis of a Weak Coiled Coil Association between Kinesin-II Stalks

Doodhi, H., Jana, S. C., Devan, P., Mazumdar, S., & Ray, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045981 · Cited by 10

Leucine Zippers

Hakoshima, T. (2005) · Wiley eBooks · doi:10.1038/npg.els.0005049 · Cited by 11

NF-Y Binding Site Architecture Defines a C-Fos Targeted Promoter Class

Haubrock, M., Hartmann, F., & Wingender, E. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160803 · Cited by 9

Trichomonas vaginalis Repair of Iron Centres Proteins: The Different Role of Two Paralogs

Nobre, L. S., Meloni, D., Teixeira, M. S., Viscogliosi, É., & Saraiva, L. M. (2016) · Protist · doi:10.1016/j.protis.2016.03.001 · Cited by 9

Phylogenetic profiling of protein interaction networks in eukaryotic transcription factors reveals focal proteins being ancestral to hubs

Amoutzias, G. D., Weiner, J. M., & Bornberg‐Bauer, E. (2005) · Gene · doi:10.1016/j.gene.2004.12.031 · Cited by 9

Leucine Zippers

Hakoshima, T. (2014) · Wiley eBooks · doi:10.1002/9780470015902.a0005049.pub2 · Cited by 11

Encapsulation of BSA in hybrid PEG hydrogels: stability and controlled release

Tourné‐Péteilh, C., Barège, M., Lions, M., Martínez, J., Devoisselle, J., Aubert‐Pouëssel, A., Subra, G., & Mehdi, A. (2021) · RSC Advances · doi:10.1039/d1ra03547a · Cited by 8

The transcription factors Junb and Fosl2 cooperate to regulate Cdh3 expression in 15P‐1 Sertoli cells

Nguyen, H. T., & Martin, L. J. (2022) · Molecular Reproduction and Development · doi:10.1002/mrd.23656 · Cited by 8

Molecular Characterization and Phylogenetic Analysis of BZIP Protein in Plants

Shanmughanandhan, D., Arul, Balasubramanian, P., & Ramalingam, S. (2010) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000144 · Cited by 8

Site‐specific experiments on folding/unfolding of Jun coiled coils: Thermodynamic and kinetic parameters from spin inversion transfer nuclear magnetic resonance at leucine‐18

d’Avignon, D. A., Bretthorst, G. L., Holtzer, M. E., Schwarz, K., Angeletti, R. H., Mints, L., & Holtzer, A. M. (2006) · Biopolymers · doi:10.1002/bip.20555 · Cited by 8

Lack of association of G-protein β2- and γ2-subunit N-terminal fragments provides evidence against the coiled-coil model of subunit-βγ assembly

Marin, E. P., & Neubig, R. R. (1995) · Biochemical Journal · doi:10.1042/bj3090377 · Cited by 8

Platelet-derived growth factor regulation of fos stability correlates with growth induction.

Jackson, J. A., Holt, J. T., & Pledger, W. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41946-1 · Cited by 8

Role of c‐Jun NH2‐terminal kinase‐mediated mitogen‐activated protein kinase pathway in response to pesticides in Apis cerana cerana

Niu, X., Wang, L., Meng, H., Wang, H., Xu, B., & Wang, C. (2022) · Insect Science · doi:10.1111/1744-7917.13053 · Cited by 7

Controlling leucine-zipper partner recognition in cells through modification of a–g interactions

Azuma, Y., Kükenshöner, T., Ma, G., Yasunaga, J., Imanishi, M., Tanaka, G., Nakase, I., Maruno, T., Kobayashi, Y., Arndt, K. M., et al. (2014) · Chemical Communications · doi:10.1039/c4cc00555d · Cited by 7

On-Surface Assembly of Coiled-Coil Heterodimers

White, S. J., Morton, D. W. A., Cheah, B. C., Bronowska, A. K., Davies, A. G., Stockley, P. G., Wälti, C., & Johnson, S. (2012) · Langmuir · doi:10.1021/la3025149 · Cited by 7

Self-Assembling Protein Systems: A Model for Materials Science

McGrath, K. P., & Butler, M. M. (1997) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4612-4094-5_8 · Cited by 7

Identification of a functional site on the type I TGF‐β receptor by mutational analysis of its ectodomain

Guimond, A., Sulea, T. I., Zwaagstra, J. C., Ekiel, I. H., & O'Connor‐McCourt, M. D. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03231-8 · Cited by 7

Towards predicting coiled-coil protein interactions

Singh, M., & Kim, P. S. (2001) · doi:10.1145/369133.369238 · Cited by 7

Proliferation and differentiation properties of bipotent glial progenitor cell lines immortalized with the adenovirus E1A gene

Galiana, E., Bernard, R., Borde, I., Rouget, P., & Evrard, C. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490360204 · Cited by 7

Involvement of calmodulin-dependent protein kinase I in the regulation of the expression of connexin 43 in MA-10 tumor Leydig cells

Najih, M., Nguyen, H. T., & Martin, L. J. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04553-7 · Cited by 6

Interleukin 6 induces DNA binding activity of AP1 in M1 myeloblastic cells but not in a growth resistant cell derivative.

Melamed, D., Resnitzky, D., Haimov, I., Levy, N., Pfarr, C. M., Yaniv, M., & Kimchi, A. (1993) · PubMed · Cited by 6

A synthetic leucine zipper-based dimerization system for combining multiple promoter specificities

Jérôme, V., & Müller, R. (2001) · Gene Therapy · doi:10.1038/sj.gt.3301443 · Cited by 5

Controlling leucine zipper specificity with interfacial hydrophobic residues

Bains, N. P. S., Wilce, M. C. J., Mackay, L. G., & King, G. F. (1999) · International Journal of Peptide Research and Therapeutics · doi:10.1007/bf02443435 · Cited by 5

Solution Structure of O-glycosylated C-terminal Leucine Zipper Domain of Human Salivary Mucin (MUC7)

Narasimhamurthy, S., Naganagowda, G. A., Janagani, S., Gururaja, T., & Levine, M. J. (2000) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2000.10506654 · Cited by 4

Design of Polypeptides

Gutte, B., & Klauser, S. (1995) · Elsevier eBooks · doi:10.1016/b978-012310920-0/50010-3 · Cited by 5

Leucine Zipper

Krylov, D. Y., & Vinson, C. (2001) · Encyclopedia of Life Sciences · doi:10.1038/npg.els.0003001 · Cited by 5

The Role of Interhelical Ionic Interactions in Myosin Rod Assembly

Arrizubieta, M. J., & Bandman, E. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8105 · Cited by 4

Response of Djun and Dfos mRNA abundance to signal transduction pathways in cultured cells of Drosophila melanogaster

Xia, X., & Goldstein, E. S. (1999) · Molecular Biology Reports · doi:10.1023/a:1006906419110 · Cited by 4

Electrostatic Interactions in Leucine Zippers: Effects on Stability and Specificity of Interaction

McGrath, K. P., Butler, M. M., DiGirolamo, C. M., Kaplan, D. L., Petka, W. A., & Laue, T. M. (2000) · Journal of Bioactive and Compatible Polymers · doi:10.1177/088391150001500405 · Cited by 4

Regulation of α-Helical Coiled-coil Dimerization in Chicken Skeletal Muscle Light Meromyosin

Arrizubieta, M. J., & Bandman, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13847 · Cited by 4

FAM210A: An emerging regulator of mitochondrial homeostasis

Wang, Y., & Yue, F. (2024) · BioEssays · doi:10.1002/bies.202400090 · Cited by 3

Analysis of star promoter in common carp and catfish testis: Role of c-jun and its association with testicular function as a transcription factor

Tenugu, S., & Senthilkumaran, B. (2025) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2025.106817 · Cited by 3

Analysis of Selected and Designed Chimeric D- and L-α-Helix Assemblies

Kükenshöner, T., Hagemann, U. B., Wohlwend, D., Räuber, C., Baumann, T., Keller, S., Einsle, O., Müller, K. M., & Arndt, K. M. (2014) · Biomacromolecules · doi:10.1021/bm5006883 · Cited by 3

Regulation of Cdh2 by the AP-1 family transcription factor Junb in TM4 Sertoli cells

Nguyen, H. T., & Martin, L. J. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.078 · Cited by 3

Influential Mutations in the SMAD4 Trimer Complex Can Be Detected from Disruptions of Electrostatic Complementarity

Nolan, B. E., Levenson, E., & Chen, B. Y. (2017) · Journal of Computational Biology · doi:10.1089/cmb.2016.0162 · Cited by 3

Isolating Influential Regions of Electrostatic Focusing in Protein and DNA Structure

Blumenthal, S., Tang, Y., Yang, W., & Chen, B. Y. (2013) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2013.124 · Cited by 3

Functional analysis of homeodomain-leucine zipper transcription factors in Arabidopsis thaliana

Johannesson, H. (2000) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 3

The Role of the C-terminal Coiled-coil in the Cellular Localization and in the Osmotic Stress Response of Transporter ProP

Marom, D. (2015) · The Atrium (University of Guelph) · Cited by 3

High-throughput thermodynamic and kinetic measurements of transcription factor/DNA mutations reveal how conformational heterogeneity can shape motif selectivityPreprint

Hastings, R., Aditham, A. K., DelRosso, N. V., Suzuki, P., & Fordyce, P. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.13.566946 · Cited by 4

Exclusive Characteristics of the p.E555K Dominant-Negative Variant in Autosomal Dominant E47 Deficiency

Utsumi, T., Tsumura, M., Yashiro, M., Kato, Z., Noma, K., Sakura, F., Kagawa, R., Mizoguchi, Y., Karakawa, S., Ohnishi, H., et al. (2024) · Journal of Clinical Immunology · doi:10.1007/s10875-024-01758-x · Cited by 2

The Activation of the CCND1 Promoter by AP-1 and SOX Transcription Factors in PC3 Prostate Cancer Cells Can Be Prevented by Anacardic Acid Analogs

Brunie, M., Robichaud, M., Touaibia, M., & Martin, L. J. (2024) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-024-01646-6 · Cited by 2

Alternative splicing of bunched confers a dual role in hippo pathway-dependent growth and tumorigenesis

Guo, P., Song, S., Niu, Y., Kuang, X., Zhou, D., Zhou, Z., Zhang, Y., & Ma, X. (2025) · Oncogene · doi:10.1038/s41388-025-03348-6 · Cited by 2

A volumetric method for representing and comparing regions of electrostatic focusing in molecular structure

Chen, B. Y., & Paul, D. (2012) · ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics (ACM-BCB) · doi:10.1145/2382936.2382967 · Cited by 2

Peptide models of bZIP proteins: Quantitative analysis of DNA affinity and specificity

Metallo, S., & Schepartz, A. (1995) · Techniques in protein chemistry · doi:10.1016/s1080-8914(06)80047-5 · Cited by 1

Les protéines artificielles

Michon, T., & Tirrell, D. A. (2000) · Biofutur · doi:10.1016/s0294-3506(00)88138-7 · Cited by 2

3.11 Protein Switches

Christensen, T., Hassouneh, W., Callahan, D. J., & Chilkoti, A. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00316-7 · Cited by 1

Engineering and characterization of a pH ‐sensitive homodimeric antiparallel coiled coil

Nagarkar, R. P., Fichman, G., & Schneider, J. P. (2020) · Peptide Science · doi:10.1002/pep2.24180 · Cited by 1

Predicting and testing determinants of histidine-kinase functions by leveraging protein sequence information

Ashenberg, O. (2012) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 1

Protein Secondary Structure Prediction

Krystek, S. R., Metzler, W. J., & Novotný, J. (1995) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0203s00 · Cited by 1

Biological Self-Assembly: A Paradigm for Materials Science

McGrath, K. P., & Kaplan, D. L. (1993) · MRS Proceedings · doi:10.1557/proc-330-61 · Cited by 1

Transcription Factors in Sertoli Cells

Chaudhary, J., & Skinner, M. K. (2005) · Elsevier eBooks · doi:10.1016/b978-012647751-1/50016-7 · Cited by 1

Interaction Between AP-1 Proteins and Glucocorticoid Receptors in Regulation of Lymphokine Activated Killer (LAK) Cell Activity in the Equine Species.

Bu, J. (1996) · doi:10.31390/gradschool_disstheses.6178 · Cited by 1

Transgenic mice studies of immediate-early genes: from markers to mutants

Kasof, G. M., Curran, T., & Morgan, J. I. (1995) · Springer eBooks · doi:10.1007/978-3-642-79562-6_7

Running head: bZIP Transcription Factors in Rice

Khurana, J. P. (2007)

SVM Classification to Predict Two Stranded Anti-parallel Coiled Coils based on Protein Sequence Data

Huang, Z., Li, Y., & Hu, X. (2005) · Lecture notes in computer science · doi:10.1007/11424857_40

BIOPHYSICAL ANALYSIS OF THE AP1-DNA INTERACTION

Seldeen, K. L. (2009)

Characterizing antigen-specific CD4⁺ T cells using HLA-DR oligomers

Cameron, T. O. (2002) · DSpace@MIT (Massachusetts Institute of Technology)

Activating Protein‐1

Vinson, C. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm1246

Estudo da interação entre domínios C-terminais de septinas humanas: implicação na formação e estabilidade do filamento

Sala, F. A. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.75.2015.tde-10082015-140053

Solution assembly of cytokine receptor ectodomain complexes

Wu, Z., Johnson, K. W., Goldstein, B., Laue, T. M., & Ciardelli, T. L. (1996) · Techniques in protein chemistry · doi:10.1016/s1080-8914(96)80008-1

Artificial Protein Hydrogel Materials

Petka, W. A., Harden, J. L., Sakata, J. K., & Tirrell, D. A. (1998) · MRS Proceedings · doi:10.1557/proc-550-23

Computational Enzyme Design

Bolon, D. N. A. (2002) · doi:10.7907/w7f3-ds14

Preferential Heterodimer Formation by Isolated Leucine Zippers from Fos and Jun

O’Shea, E. K., Rutkowski, R., Stafford, W. F., & Kim, P. S. (1989) · Science · doi:10.1126/science.2503872 · Cited by 471

Different requirements for formation of Jun: Jun and Jun: Fos complexes.Preprint

Smeal, T., Angel, P. E., Meek, J., & Karin, M. (1989) · Genes & Development · doi:10.1101/gad.3.12b.2091 · Cited by 263

fos andjun interaction: The role of the leucine zipper

Ransone, L. J., Visvader, J. E., Lamph, W. W., Sassone‐Corsi, P., & Verma, I. M. (1989) · International Journal of Cancer · doi:10.1002/ijc.2910440705 · Cited by 19

Fos-Jun interaction: mutational analysis of the leucine zipper domain of both proteins.Preprint

Ransone, L. J., Visvader, J. E., Sassone‐Corsi, P., & Verma, I. M. (1989) · Genes & Development · doi:10.1101/gad.3.6.770 · Cited by 153

Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding Domains

Gentz, R., Rauscher, F. J., Abate, C., & Curran, T. (1989) · Science · doi:10.1126/science.2494702 · Cited by 559