14-3-3 proteins: A historic overview

Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor

Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594

Serine Phosphorylation of Death Agonist BAD in Response to Survival Factor Results in Binding to 14-3-3 Not BCL-XL

Zha, J., Harada, H., Yang, E., Jockel, J., & Korsmeyer, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81382-3 · Cited by 2,595

The p53 pathway: positive and negative feedback loops

Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967

The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity

Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604

Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine

Muslin, A. J., Tanner, J. W., Allen, P. M., & Shaw, A. S. (1996) · Cell · doi:10.1016/s0092-8674(00)81067-3 · Cited by 1,381

Is a p53-Regulated Inhibitor of G2/M Progression

Hermeking, H., Lengauer, C., Polyak, K., He, T.-C., Zhang, L., Thiagalingam, S., Kinzler, K. W., & Vogelstein, B. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80002-7 · Cited by 1,251

14-3-3σ is required to prevent mitotic catastrophe after DNA damage

Chan, T. A., Hermeking, H., Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1999) · Nature · doi:10.1038/44188 · Cited by 895

Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia

Ren, R. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1567 · Cited by 878

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

Das, A. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1192 · Cited by 825

Activation of AKT Kinases in Cancer: Implications for Therapeutic Targeting

(2005) · Advances in Cancer Research · doi:10.1016/s0065-230x(05)94002-5 · Cited by 823

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891

Brassinosteroid Signal Transduction from Receptor Kinases to Transcription Factors

Kim, T.-W., & Wang, Z.-Y. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.043008.092057 · Cited by 655

The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development

Morrison, D. K. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.10.003 · Cited by 605

Functions of OsBZR1 and 14-3-3 proteins in brassinosteroid signaling in rice

Bai, M.-Y., Zhang, L.-Y., Gampala, S. S., Zhu, S.-W., Song, W.-Y., Chong, K., & Wang, Z.-Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706386104 · Cited by 461

A Systems Level Analysis of Transcriptional Changes in Alzheimer's Disease and Normal Aging

Miller, J. A., Oldham, M. C., & Geschwind, D. H. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4098-07.2008 · Cited by 385

Arylalkylamine N-Acetyltransferase: “the Timezyme”

Klein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.r600036200 · Cited by 422

Bioinformatic and experimental survey of 14-3-3-binding sites

Johnson, C., Crowther, S., Stafford, M. J., Campbell, D. G., Toth, R., & MacKintosh, C. (2010) · Biochemical Journal · doi:10.1042/bj20091834 · Cited by 334

Regulation of Pichia pastoris promoters and its consequences for protein production

Vogl, T., & Glieder, A. (2013) · New Biotechnology · doi:10.1016/j.nbt.2012.11.010 · Cited by 332

Structural basis of 14-3-3 protein functions

Obsil, T., & Obsilova, V. (2011) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2011.09.001 · Cited by 273

14-3-3 fusion oncogenes in high-grade endometrial stromal sarcoma

Lee, C.-H., Ou, W.-B., Mariño-Enriquez, A., Zhu, M., Mayeda, M., Wang, Y., Guo, X., Brunner, A. L., Amant, F., French, C. A., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115528109 · Cited by 259

Structure/function relationships underlying regulation of FOXO transcription factors

Obsil, T., & Obsilova, V (2008) · Oncogene · doi:10.1038/onc.2008.20 · Cited by 254

Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor

Zhao, J., Du, Y., Horton, J. R., Upadhyay, A. K., Lou, B., Bai, Y., Zhang, X., Du, L., Li, M., Wang, B., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100012108 · Cited by 105

The Mechanism of SARS-CoV-2 Nucleocapsid Protein Recognition by the Human 14-3-3 Proteins

Tugaeva, K. V., Hawkins, D. E. D. P., Smith, J. L. R., Bayfield, O. W., Ker, D.-S., Sysoev, A. A., Klychnikov, O. I., Antson, A. A., & Sluchanko, N. N. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166875 · Cited by 95

Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms

Gogl, G., Tugaeva, K. V., Eberling, P., Kostmann, C., Trave, G., & Sluchanko, N. N. (2021) · Nature Communications · doi:10.1038/s41467-021-21908-8 · Cited by 91

Stabilization and Inhibition of Protein–Protein Interactions: The 14-3-3 Case Study

Milroy, L.-G., Brunsveld, L., & Ottmann, C. (2013) · ACS Chemical Biology · doi:10.1021/cb300599t · Cited by 88

Small molecules targeting protein–protein interactions for cancer therapy

Wu, D., Li, Y., Zheng, L., Xiao, H., Ouyang, L., Wang, G., & Sun, Q. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.05.035 · Cited by 71

Quantitative Proteomics Analysis Reveals BAG3 as a Potential Target To Suppress Severe Acute Respiratory Syndrome Coronavirus Replication

Zhang, L., Zhang, Z.-P., Zhang, X.-E., Lin, F.-S., & Ge, F. (2010) · Journal of Virology · doi:10.1128/jvi.00213-10 · Cited by 60

Liquid-liquid phase separation of protein tau: An emerging process in Alzheimer's disease pathogenesis

Ainani, H., Bouchmaa, N., Ben Mrid, R., & El Fatimy, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106011 · Cited by 54

Hormone-induced 14-3-3γ adaptor protein regulates steroidogenic acute regulatory protein activity and steroid biosynthesis in MA-10 Leydig cells

Aghazadeh, Y., Rone, M. B., Blonder, J., Ye, X., Veenstra, T. D., Hales, D. B., Culty, M., & Papadopoulos, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.339580 · Cited by 46

Induction of Androgen Formation in the Male by a TAT-VDAC1 Fusion Peptide Blocking 14-3-3ɛ Protein Adaptor and Mitochondrial VDAC1 Interactions

Aghazadeh, Y., Martinez-Arguelles, D. B., Fan, J., Culty, M., & Papadopoulos, V. (2014) · Molecular Therapy · doi:10.1038/mt.2014.116 · Cited by 43

Liquid-liquid phase separation in Alzheimer’s disease

Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33

Proteomic clusters underlie heterogeneity in preclinical Alzheimer’s disease progression

Wisch, J. K., Butt, O. H., Gordon, B. A., Schindler, S. E., Fagan, A. M., Henson, R. L., Yang, C., Boerwinkle, A. H., Benzinger, T. L. S., Holtzman, D. M., et al. (2023) · Brain · doi:10.1093/brain/awac484 · Cited by 11

Phosphorylation Code of Human Nucleophosmin Includes Four Cryptic Sites for Hierarchical Binding of 14-3-3 Proteins

Kapitonova, A. A., Perfilova, K. V., Cooley, R. B., & Sluchanko, N. N. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168592 · Cited by 9