PDCD4 is a CSL associated protein with a transcription repressive function in cancer associated fibroblast activation

The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism

Kopan, R., & Ilagan, M. X. G. (2009) · Cell · doi:10.1016/j.cell.2009.03.045 · Cited by 3,631 · see citing works

TGF-ß Signaling in Fibroblasts Modulates the Oncogenic Potential of Adjacent Epithelia

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The reverse Warburg effect: Aerobic glycolysis in cancer associated fibroblasts and the tumor stroma

Pavlides, S., Whitaker-Menezes, D., Castello-Cros, R., Flomenberg, N., Witkiewicz, A. K., Frank, P. G., Casimiro, M. C., Wang, C., Fortina, P., Addya, S., et al. (2009) · Cell Cycle · doi:10.4161/cc.8.23.10238 · Cited by 1,391 · see citing works

TUMOR STROMA AND REGULATION OF CANCER DEVELOPMENT

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Cellular senescence: putting the paradoxes in perspective

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The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation

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Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKα kinasesPreprint

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Dynamic binding of RBPJ is determined by Notch signaling statusPreprint

Castel, D., Mourikis, P., Bartels, S. J. J., Brinkman, A. B., Tajbakhsh, S., & Stunnenberg, H. G. (2013) · Genes & Development · doi:10.1101/gad.211912.112 · Cited by 256 · see citing works

Notch tumor suppressor function

Dotto, G. P. (2008) · Oncogene · doi:10.1038/onc.2008.225 · Cited by 245 · see citing works

Combined CSL and p53 downregulation promotes cancer-associated fibroblast activation

Procopio, M.-G., Laszlo, C., Al Labban, D., Kim, D. E., Bordignon, P., Jo, S.-H., Goruppi, S., Menietti, E., Ostano, P., Ala, U., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3228 · Cited by 223 · see citing works

Isolation of a novel mouse gene MA-3 that is induced upon programmed cell death

Shibahara, K., Asano, M., Ishida, Y., Aoki, T., Koike, T., & Honjo, T. (1995) · Gene · doi:10.1016/0378-1119(95)00607-9 · Cited by 223 · see citing works

PTF1 Is an Organ-Specific and Notch-Independent Basic Helix-Loop-Helix Complex Containing the Mammalian Suppressor of Hairless (RBP-J) or Its Paralogue, RBP-L

Beres, T. M., Masui, T., Swift, G. H., Shi, L., Henke, R., & MacDonald, R. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.117-130.2006 · Cited by 216 · see citing works

Mechanistic Insights into Notch Receptor Signaling from Structural and Biochemical Studies

Kovall, R. A., & Blacklow, S. C. (2010) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(10)92002-4 · Cited by 213 · see citing works

Epidermal Expression of the Translation Inhibitor Programmed Cell Death 4 Suppresses Tumorigenesis

Jansen, A. P., Camalier, C. E., & Colburn, N. H. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-2119 · Cited by 212 · see citing works

A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development

Mulligan, P., Yang, F., Stefano, L. D., Ji, J., Ouyang, J., Nishikawa, J. L., Toiber, D., Kulkarni, M., Wang, Q., Najafi-Shoushtari, S. H., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.020 · Cited by 211 · see citing works

Multifocal Epithelial Tumors and Field Cancerization from Loss of Mesenchymal CSL Signaling

Hu, B., Castillo, E., Harewood, L., Ostano, P., Reymond, A., Dummer, R., Raffoul, W., Hoetzenecker, W., Hofbauer, G. F. L., & Dotto, G. P. (2012) · Cell · doi:10.1016/j.cell.2012.03.048 · Cited by 211 · see citing works

Multifocal epithelial tumors and field cancerization: stroma as a primary determinant

Dotto, G. P. (2014) · Journal of Clinical Investigation · doi:10.1172/jci72589 · Cited by 169 · see citing works

Translational Regulation of Autoimmune Inflammation and Lymphoma Genesis by Programmed Cell Death 4

Hilliard, A., Hilliard, B., Zheng, S.-J., Sun, H., Miwa, T., Song, W., Göke, R., & Chen, Y. H. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.8095 · Cited by 167 · see citing works

More complicated than it looks: assembly of Notch pathway transcription complexes

Kovall, R. A. (2008) · Oncogene · doi:10.1038/onc.2008.223 · Cited by 161 · see citing works

Twist1 Is a Key Regulator of Cancer-Associated Fibroblasts

Lee, K.-W., Yeo, S.-Y., Sung, C. O., & Kim, S. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0350 · Cited by 140 · see citing works

Transformation suppressor protein Pdcd4 interferes with JNK-mediated phosphorylation of c-Jun and recruitment of the coactivator p300 by c-Jun

Bitomsky, N., Böhm, M., & Klempnauer, K.-H. (2004) · Oncogene · doi:10.1038/sj.onc.1208064 · Cited by 134 · see citing works

Programmed Cell Death Protein 4 Down-regulates Y-Box Binding Protein-1 Expression via a Direct Interaction with Twist1 to Suppress Cancer Cell Growth

Shiota, M., Izumi, H., Tanimoto, A., Takahashi, M., Miyamoto, N., Kashiwagi, E., Kidani, A., Hirano, G., Masubuchi, D., Fukunaka, Y., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2334 · Cited by 134 · see citing works

Micro‐RNA‐21 regulates TGF‐β‐induced myofibroblast differentiation by targeting PDCD4 in tumor‐stroma interaction

Yao, Q., Cao, S., Li, C., Mengesha, A., Kong, B., & Wei, M. (2010) · International Journal of Cancer · doi:10.1002/ijc.25506 · Cited by 120 · see citing works

IRF6 is a mediator of Notch pro‐differentiation and tumour suppressive function in keratinocytes

Restivo, G., Nguyen, B.-C., Dziunycz, P., Ristorcelli, E., Ryan, R. J. H., Yalcin-Ozuysal, Ö., Piazza, M., Radtke, F., Dixon, M. J., Hofbauer, G. F. L., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.325 · Cited by 118 · see citing works

DDX5 is a positive regulator of oncogenic NOTCH1 signaling in T cell acute lymphoblastic leukemia

Lin, S., Tian, L., Shen, H., Gu, Y., Li, J., Chen, Z., Sun, X., You, M. J., & Wu, L. (2012) · Oncogene · doi:10.1038/onc.2012.482 · Cited by 91 · see citing works

RITA, a novel modulator of Notch signalling, acts via nuclear export of RBP‐J

Wacker, S., Alvarado, C., von Wichert, G., Knippschild, U., Wiedenmann, J., Clauß, K., Nienhaus, G. U., Hameister, H., Baumann, B., Borggrefe, T., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.289 · Cited by 68 · see citing works

RNA helicase Ddx5 and the noncoding RNA SRA act as coactivators in the Notch signaling pathway

Jung, C., Mittler, G., Oswald, F., & Borggrefe, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.032 · Cited by 60 · see citing works

Targeting the eIF4A RNA helicase blocks translation of the MUC1-C oncoprotein

Jin, C., Rajabi, H. N., Rodrigo, C. M., Porco, J. A. J., & Kufe, D. W. (2012) · Oncogene · doi:10.1038/onc.2012.236 · Cited by 48 · see citing works

Dicer1 imparts essential survival cues in Notch-driven T-ALL via miR-21–mediated tumor suppressor Pdcd4 repression

Junker, F., Chabloz, A., Koch, U., & Radtke, F. (2015) · Blood · doi:10.1182/blood-2014-12-618892 · Cited by 45 · see citing works

Notch-independent functions of CSL.

Johnson, J. E., & MacDonald, R. J. (2011) · Current Topics in Developmental Biology · doi:10.1016/b978-0-12-385975-4.00009-7 · Cited by 43 · see citing works

Structure of the Tandem MA-3 Region of Pdcd4 Protein and Characterization of Its Interactions with eIF4A and eIF4G

Waters, L. C., Strong, S. L., Ferlemann, E., Oka, O., Muskett, F. W., Veverka, V., Banerjee, S., Schmedt, T., Henry, A. J., Klempnauer, K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166157 · Cited by 38 · see citing works

Notch Signaling in Development, Tissue Homeostasis, and Disease

Siebel, C., & Lendahl, U. (2017) · Physiological Reviews · doi:10.1152/physrev.00005.2017 · Cited by 968 · see citing works

Mechanisms of the Epithelial–Mesenchymal Transition and Tumor Microenvironment in Helicobacter pylori-Induced Gastric Cancer

Baj, J., Korona‐Głowniak, I., Forma, A., Maani, A., Sitarz, R., Rahnama, M., Radzikowska, E., & Portincasa, P. (2020) · Cells · doi:10.3390/cells9041055 · Cited by 173 · see citing works

Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions

Matsuhashi, S., Manirujjaman, M., Hamajima, H., & Ozaki, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092304 · Cited by 143 · see citing works

CREBBP and STAT6 co-mutation and 16p13 and 1p36 loss define the t(14;18)-negative diffuse variant of follicular lymphoma

Xian, R. R., Xie, Y., Haley, L. M., Yonescu, R., Pallavajjala, A., Pittaluga, S., Jaffe, E. S., Duffield, A. S., McCall, C. M., Gheith, S. M. F., et al. (2020) · Blood Cancer Journal · doi:10.1038/s41408-020-0335-0 · Cited by 55 · see citing works

Transcriptional regulation of metabolism in disease: From transcription factors to epigenetics

Hawkins, L. J., Al-attar, R., & Storey, K. B. (2018) · PeerJ · doi:10.7717/peerj.5062 · Cited by 16 · see citing works

Metastasis and cancer associated fibroblasts: taking it up a NOTCH

Ghosh, A., & Mitra, A. K. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1277076 · Cited by 12 · see citing works

PDCD4 expression in coronary atherosclerosis rat models and its mechanism

Gao, Y., Li, H., Zhou, Y., Lv, H., & Chen, Y. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7296 · Cited by 12 · see citing works

Neuronal activity regulates the nuclear proteome to promote activity-dependent transcription

Herbst, W. A., Deng, W., Wohlschlegel, J. A., Achiro, J. M., & Martin, K. C. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202103087 · Cited by 11 · see citing works

The proteomic study of serially passaged human skin fibroblast cells uncovers down-regulation of the chromosome condensin complex proteins involved in replicative senescence

Meng, Q., Gao, J., Zhu, H., He, H., Lu, Z. H., Hong, M., & Zhou, H. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.10.065 · Cited by 10 · see citing works

The bright and dark side of skin senescence. Could skin rejuvenation anti-senescence interventions become a "bright" new strategy for the prevention of age-related skin pathologies?

Georgakopoulou, E. A., Valsamidi, C., Veroutis, D., & Havaki, S. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111409 · Cited by 10 · see citing works

Multiple Genetic Loci Associated with Pug Dog Thoracolumbar Myelopathy

Brander, G., Rohdin, C., Bianchi, M., Bergvall, K., Andersson, G., Ljungvall, I., Jäderlund, K. H., Häggström, J. U., Hedhammar, Å. A., Lindblad‐Toh, K., et al. (2023) · Genes · doi:10.3390/genes14020385 · Cited by 8 · see citing works

Induction of premature senescence and a less-fibrogenic phenotype by programmed cell death 4 knockdown in the human hepatic stellate cell line Lieming Xu-2

Perveen, R., Ozaki, I., Manirujjaman, M., Mine, K., Murata, Y., Tanaka, K., Xia, J., Takahashi, H., Anzai, K., & Matsuhashi, S. (2022) · Human Cell · doi:10.1007/s13577-022-00844-9 · Cited by 3 · see citing works

Single-cell spatial multi-omics molecular pathology enabled by SuperFocusPreprint

Lu, Y., Tian, X., Vicari, M., Enninful, A., Bao, S., Bai, Z., Liu, C., Zhang, X., Andrén, P. E., Lundeberg, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.26.696575 · Cited by 1 · see citing works

Combined CSL and p53 downregulation promotes cancer-associated fibroblast activation

Procopio, M.-G., Laszlo, C., Al Labban, D., Kim, D. E., Bordignon, P., Jo, S.-H., Goruppi, S., Menietti, E., Ostano, P., Ala, U., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3228 · Cited by 223 · see citing works

A multistep process of cancer associated fibroblasts determination under CSL-p53 control

Procopio, M.-G. (2015) · IRIS

Abstract IA10: Convergent control of cancer associated fibroblast activation and field cancerization by Notch/CSL and p53 signaling

Dotto, G. P., & Dotto, G. P. (2016) · Cancer Research · doi:10.1158/1538-7445.tme16-ia10

CSL and NOTCH1 determine genomic stability and expansion of Cancer Associated Fibroblasts in human skin

Bottoni, G. (2018) · IRIS

CSL controls telomere maintenance and genome stability in human dermal fibroblasts

Bottoni, G., Katarkar, A., Tassone, B., Ghosh, S., Clocchiatti, A., Goruppi, S., Bordignon, P., Jafari, P., Tordini, F., Lunardi, T., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11785-7 · Cited by 25 · see citing works