[1] H. Sung et al., “Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries.,” CA Cancer J Clin, vol. 71, no. 3, pp. 209–249, May 2021.
[2] B. Weigelt, J. L. Peterse, and L. J. van ’t Veer, “Breast cancer metastasis: markers and models.,” Nat Rev Cancer, vol. 5, no. 8, pp. 591–602, Aug. 2005.
[3] A. R. Safa, “Resistance to Cell Death and Its Modulation in Cancer Stem Cells.,” Crit Rev Oncog, vol. 21, no. 3–4, pp. 203–219, 2016.
[4] M. Luo, M. Brooks, and M. S. Wicha, “Epithelial-mesenchymal plasticity of breast cancer stem cells: implications for metastasis and therapeutic resistance.,” Curr Pharm Des, vol. 21, no. 10, pp. 1301–1310, 2015.
[5] B. Dong, D. S. Horowitz, R. Kobayashi, and A. R. Krainer, “Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6.,” Nucleic Acids Res, vol. 21, no. 17, pp. 4085–4092, Aug. 1993.
[6] A. Cléry, M. Blatter, and F. H.-T. Allain, “RNA recognition motifs: boring? Not quite.,” Curr Opin Struct Biol, vol. 18, no. 3, pp. 290–298, Jun. 2008.
[7] G. M. Daubner, A. Cléry, and F. H.-T. Allain, “RRM-RNA recognition: NMR or crystallography…and new findings.,” Curr Opin Struct Biol, vol. 23, no. 1, pp. 100–108, Feb. 2013.
[8] C. M. Clemson et al., “An architectural role for a nuclear noncoding RNA: NEAT1 RNA is essential for the structure of paraspeckles.,” Mol Cell, vol. 33, no. 6, pp. 717–726, Mar. 2009.
[9] X. Dong, J. Sweet, J. R. G. Challis, T. Brown, and S. J. Lye, “Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb.,” Mol Cell Biol, vol. 27, no. 13, pp. 4863–4875, Jul. 2007.
[10] S. Kaneko, O. Rozenblatt-Rosen, M. Meyerson, and J. L. Manley, “The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3’ processing and transcription termination.,” Genes Dev, vol. 21, no. 14, pp. 1779–1789, Jul. 2007.
[11] A. Basu, B. Dong, A. R. Krainer, and C. C. Howe, “The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO.,” Mol Cell Biol, vol. 17, no. 2, pp. 677–686, Feb. 1997.
[12] Y. Kanai, N. Dohmae, and N. Hirokawa, “Kinesin transports RNA: isolation and characterization of an RNA-transporting granule.,” Neuron, vol. 43, no. 4, pp. 513–525, Aug. 2004.
[13] K. V Prasanth et al., “Regulating gene expression through RNA nuclear retention.,” Cell, vol. 123, no. 2, pp. 249–263, Oct. 2005.
[14] Z. Zhang and G. G. Carmichael, “The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs.,” Cell, vol. 106, no. 4, pp. 465–475, Aug. 2001.
[15] R. Peng, B. T. Dye, I. Pérez, D. C. Barnard, A. B. Thompson, and J. G. Patton, “PSF and p54nrb bind a conserved stem in U5 snRNA.,” RNA, vol. 8, no. 10, pp. 1334–1347, Oct. 2002.
[16] L. Jaafar, Z. Li, S. Li, and W. S. Dynan, “SFPQ•NONO and XLF function separately and together to promote DNA double-strand break repair via canonical nonhomologous end joining.,” Nucleic Acids Res, vol. 45, no. 4, pp. 1848–1859, Feb. 2017.
[17] Z. Zhu et al., “p54(nrb)/NONO regulates lipid metabolism and breast cancer growth through SREBP-1A.,” Oncogene, vol. 35, no. 11, pp. 1399–1410, Mar. 2016.
[18] H. Ishiguro, H. Uemura, K. Fujinami, N. Ikeda, S. Ohta, and Y. Kubota, “55 kDa nuclear matrix protein (nmt55) mRNA is expressed in human prostate cancer tissue and is associated with the androgen receptor.,” Int J cancer, vol. 105, no. 1, pp. 26–32, May 2003.
[19] R. Yamamoto et al., “Overexpression of p54(nrb)/NONO induces differential EPHA6 splicing and contributes to castration-resistant prostate cancer growth.,” Oncotarget, vol. 9, no. 12, pp. 10510–10524, Feb. 2018.
[20] S. Schiffner, N. Zimara, R. Schmid, and A.-K. Bosserhoff, “p54nrb is a new regulator of progression of malignant melanoma.,” Carcinogenesis, vol. 32, no. 8, pp. 1176–1182, Aug. 2011.
[21] D. Li et al., “Ets-1 promoter-associated noncoding RNA regulates the NONO/ERG/Ets-1 axis to drive gastric cancer progression.,” Oncogene, vol. 37, no. 35, pp. 4871–4886, Aug. 2018.
[22] X. Z. Zhou and K. P. Lu, “The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.,” Nat Rev Cancer, vol. 16, no. 7, pp. 463–478, Jul. 2016.
[23] E. S. Yeh and A. R. Means, “PIN1, the cell cycle and cancer.,” Nature reviews. Cancer, vol. 7, no. 5. England, pp. 381–388, May-2007.
[24] P.-J. Lu, X. Z. Zhou, Y.-C. Liou, J. P. Noel, and K. P. Lu, “Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function.,” J Biol Chem, vol. 277, no. 4, pp. 2381–2384, Jan. 2002.
[25] Y.-C. Liou, X. Z. Zhou, and K. P. Lu, “Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins.,” Trends Biochem Sci, vol. 36, no. 10, pp. 501–514, Oct. 2011.
[26] Z. Lu and T. Hunter, “Prolyl isomerase Pin1 in cancer.,” Cell Res, vol. 24, no. 9, pp. 1033–1049, Sep. 2014.
[27] T. H. Lee et al., “Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function.,” Mol Cell, vol. 42, no. 2, pp. 147–159, Apr. 2011.
[28] F. Suizu, A. Ryo, G. Wulf, J. Lim, and K. P. Lu, “Pin1 regulates centrosome duplication, and its overexpression induces centrosome amplification, chromosome instability, and oncogenesis.,” Mol Cell Biol, vol. 26, no. 4, pp. 1463–1479, Feb. 2006.
[29] Y. R. Pokharel et al., “Relevance Rank Platform (RRP) for Functional Filtering of High Content Protein-Protein Interaction Data.,” Mol Cell Proteomics, vol. 14, no. 12, pp. 3274–3283, Dec. 2015.
[30] B. A. Lone, F. Ahmad, S. K. L. Karna, and Y. R. Pokharel, “SUPT5H Post-Transcriptional Silencing Modulates PIN1 Expression, Inhibits Tumorigenicity, and Induces Apoptosis of Human Breast Cancer Cells.,” Cell Physiol Biochem Int J Exp Cell Physiol Biochem Pharmacol, vol. 54, no. 5, pp. 928–946, Sep. 2020.
[31] B. A. Lone, S. K. L. Karna, F. Ahmad, N. Shahi, and Y. R. Pokharel, “CRISPR/Cas9 System: A Bacterial Tailor for Genomic Engineering.,” Genet Res Int, vol. 2018, p. 3797214, 2018.
[32] N. E. Sanjana, O. Shalem, and F. Zhang, “Improved vectors and genome-wide libraries for CRISPR screening.,” Nature methods, vol. 11, no. 8. pp. 783–784, Aug-2014.
[33] S. Detre, G. Saclani Jotti, and M. Dowsett, “A ‘quickscore’ method for immunohistochemical semiquantitation: validation for oestrogen receptor in breast carcinomas.,” J Clin Pathol, vol. 48, no. 9, pp. 876–878, Sep. 1995.
[34] P. J. Lu, X. Z. Zhou, M. Shen, and K. P. Lu, “Function of WW domains as phosphoserine- or phosphothreonine-binding modules.,” Science, vol. 283, no. 5406, pp. 1325–1328, Feb. 1999.
[35] C. Smet, J.-M. Wieruszeski, L. Buée, I. Landrieu, and G. Lippens, “Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein.,” FEBS Lett, vol. 579, no. 19, pp. 4159–4164, Aug. 2005.
[36] A. Proteau, S. Blier, A. L. Albert, S. B. Lavoie, A. M. Traish, and M. Vincent, “The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1.,” J Mol Biol, vol. 346, no. 4, pp. 1163–1172, Mar. 2005.
[37] M. R. Kim, H. S. Choi, J. W. Yang, B. C. Park, J.-A. Kim, and K. W. Kang, “Enhancement of vascular endothelial growth factor-mediated angiogenesis in tamoxifen-resistant breast cancer cells: role of Pin1 overexpression.,” Mol Cancer Ther, vol. 8, no. 8, pp. 2163–2171, Aug. 2009.
[38] J. Chen et al., “A 39 amino acid fragment of the cell cycle regulator p21 is sufficient to bind PCNA and partially inhibit DNA replication in vivo.,” Nucleic Acids Res, vol. 24, no. 9, pp. 1727–1733, May 1996.
[39] M. Al-Hajj, M. S. Wicha, A. Benito-Hernandez, S. J. Morrison, and M. F. Clarke, “Prospective identification of tumorigenic breast cancer cells.,” Proc Natl Acad Sci U S A, vol. 100, no. 7, pp. 3983–3988, Apr. 2003.
[40] M.-L. Luo et al., “Prolyl isomerase Pin1 acts downstream of miR200c to promote cancer stem-like cell traits in breast cancer.,” Cancer Res, vol. 74, no. 13, pp. 3603–3616, Jul. 2014.
[41] A. Rustighi et al., “Prolyl-isomerase Pin1 controls normal and cancer stem cells of the breast.,” EMBO Mol Med, vol. 6, no. 1, pp. 99–119, Jan. 2014.
[42] G. Driessens, J. Kline, and T. F. Gajewski, “Costimulatory and coinhibitory receptors in anti-tumor immunity.,” Immunol Rev, vol. 229, no. 1, pp. 126–144, May 2009.
[43] S. L. Topalian, C. G. Drake, and D. M. Pardoll, “Targeting the PD-1/B7-H1(PD-L1) pathway to activate anti-tumor immunity.,” Curr Opin Immunol, vol. 24, no. 2, pp. 207–212, Apr. 2012.
[44] G. S. Herter-Sprie et al., “Synergy of radiotherapy and PD-1 blockade in Kras-mutant lung cancer.,” JCI insight, vol. 1, no. 9, p. e87415, Jun. 2016.
[45] K. Koikawa et al., “Targeting Pin1 renders pancreatic cancer eradicable by synergizing with immunochemotherapy.,” Cell, vol. 184, no. 18, pp. 4753-4771.e27, Sep. 2021.
[46] Z. Hu et al., “Splicing Regulator p54(nrb) /Non-POU Domain-Containing Octamer-Binding Protein Enhances Carcinogenesis Through Oncogenic Isoform Switch of MYC Box-Dependent Interacting Protein 1 in Hepatocellular Carcinoma.,” Hepatology, vol. 72, no. 2, pp. 548–568, Aug. 2020.
[47] F. D. Sigoillot and R. W. King, “Vigilance and validation: Keys to success in RNAi screening.,” ACS Chem Biol, vol. 6, no. 1, pp. 47–60, Jan. 2011.
[48] P. Lassus, J. Rodriguez, and Y. Lazebnik, “Confirming specificity of RNAi in mammalian cells.,” Sci STKE, vol. 2002, no. 147, p. pl13, Aug. 2002.
[49] S. Bélanger, M. Côté, D. Lane, S. L’Espérance, C. Rancourt, and A. Piché, “Bcl-2 decreases cell proliferation and promotes accumulation of cells in S phase without affecting the rate of apoptosis in human ovarian carcinoma cells.,” Gynecol Oncol, vol. 97, no. 3, pp. 796–806, Jun. 2005.
[50] S. F. Mansilla et al., “UV-triggered p21 degradation facilitates damaged-DNA replication and preserves genomic stability.,” Nucleic Acids Res, vol. 41, no. 14, pp. 6942–6951, Aug. 2013.
[51] S. C. Gehen, P. F. Vitiello, R. A. Bambara, P. C. Keng, and M. A. O’Reilly, “Downregulation of PCNA potentiates p21-mediated growth inhibition in response to hyperoxia.,” Am J Physiol Lung Cell Mol Physiol, vol. 292, no. 3, pp. L716-24, Mar. 2007.
[52] C. J. Sherr, “Cancer cell cycles.,” Science, vol. 274, no. 5293, pp. 1672–1677, Dec. 1996.
[53] K. Yang, M. Hitomi, and D. W. Stacey, “Variations in cyclin D1 levels through the cell cycle determine the proliferative fate of a cell.,” Cell Div, vol. 1, p. 32, Dec. 2006.
[54] S. Benchimol, “p53-dependent pathways of apoptosis.,” Cell death and differentiation, vol. 8, no. 11. England, pp. 1049–1051, Nov-2001.
[55] R. Sever and J. S. Brugge, “Signal transduction in cancer.,” Cold Spring Harb Perspect Med, vol. 5, no. 4, Apr. 2015.
[56] H. Li, Z. Qiu, F. Li, and C. Wang, “The relationship between MMP-2 and MMP-9 expression levels with breast cancer incidence and prognosis.,” Oncol Lett, vol. 14, no. 5, pp. 5865–5870, Nov. 2017.
[57] X. Wang et al., “Vimentin plays an important role in the promotion of breast cancer cell migration and invasion by leucine aminopeptidase 3.,” Cytotechnology, vol. 72, no. 5, pp. 639–647, Oct. 2020.
[58] R. A. Battaglia, S. Delic, H. Herrmann, and N. T. Snider, “Vimentin on the move: new developments in cell migration.,” F1000Research, vol. 7, 2018.
[59] U. H. Frixen et al., “E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells.,” J Cell Biol, vol. 113, no. 1, pp. 173–185, Apr. 1991.
[60] G. Berx et al., “E-cadherin is a tumour/invasion suppressor gene mutated in human lobular breast cancers.,” EMBO J, vol. 14, no. 24, pp. 6107–6115, Dec. 1995.
[61] X. Li et al., “Intrinsic resistance of tumorigenic breast cancer cells to chemotherapy.,” J Natl Cancer Inst, vol. 100, no. 9, pp. 672–679, May 2008.