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 Osteopontin and Metastasis

N. Zhang et al., Osteopontin accelerates the development and metastasis of bladder cancer via activating JAK1/STAT1 pathway. Genes Genomics 42, 467 (2020). https://www.ncbi.nlm.nih.gov/pubmed/32088853

D. Raineri et al., Osteopontin binds ICOSL promoting tumor metastasis. Commun Biol 3, 615 (2020). https://www.ncbi.nlm.nih.gov/pubmed/33106594

F. Villanueva et al., The cancer-related transcription factor RUNX2 modulates expression and secretion of the matricellular protein osteopontin in osteosarcoma cells to promote adhesion to endothelial pulmonary cells and lung metastasis. J Cell Physiol 234, 13659 (2019). https://www.ncbi.nlm.nih.gov/pubmed/30637720

J. Tao et al., Therapeutic effect of combined hyperbaric oxygen and radiation therapy for single brain metastasis and its influence on osteopontin and MMP-9. Exp Ther Med 17, 465 (2019). https://www.ncbi.nlm.nih.gov/pubmed/30651823

X. Pang et al., Osteopontin as a multifaceted driver of bone metastasis and drug resistance. Pharmacol Res 144, 235 (2019). https://www.ncbi.nlm.nih.gov/pubmed/31028902

M. Kovacheva et al., Conditional Knockdown of Osteopontin Inhibits Breast Cancer Skeletal Metastasis. Int J Mol Sci20,  (2019). https://www.ncbi.nlm.nih.gov/pubmed/31590218

J. Chiou et al., Follistatin-like Protein 1 Inhibits Lung Cancer Metastasis by Preventing Proteolytic Activation of Osteopontin. Cancer Res 79, 6113 (2019). https://www.ncbi.nlm.nih.gov/pubmed/31653686

Y. Zhu et al., C-C chemokine receptor type 1 mediates osteopontin-promoted metastasis in hepatocellular carcinoma. Cancer Sci 109, 710 (2018). https://www.ncbi.nlm.nih.gov/pubmed/29285854

Y. Zheng et al., Osteopontin promotes metastasis of intrahepatic cholangiocarcinoma through recruiting MAPK1 and mediating Ser675 phosphorylation of beta-Catenin. Cell Death Dis 9, 179 (2018). https://www.ncbi.nlm.nih.gov/pubmed/29415992

X. Yang et al., Capn4 Enhances Osteopontin Expression through Activation of the Wnt/beta-Catenin Pathway to Promote Epithelial Ovarian Carcinoma Metastasis. Cell Physiol Biochem 42, 185 (2017). https://www.ncbi.nlm.nih.gov/pubmed/28535511

C. Xu et al., Osteopontin is involved in TLR4 pathway contributing to ovarian cancer cell proliferation and metastasis. Oncotarget 8, 98394 (2017). https://www.ncbi.nlm.nih.gov/pubmed/29228698

C. G. Kang et al., Plumbagin reduces osteopontin-induced invasion through inhibiting the Rho-associated kinase signaling pathway in A549 cells and suppresses osteopontin-induced lung metastasis in BalB/c mice. Bioorg Med Chem Lett 27, 1914 (2017). https://www.ncbi.nlm.nih.gov/pubmed/28359791

I. Giopanou et al., Tumor-derived osteopontin isoforms cooperate with TRP53 and CCL2 to promote lung metastasis. Oncoimmunology 6, e1256528 (2017). https://www.ncbi.nlm.nih.gov/pubmed/28197374

K. Xu et al., The fibroblast Tiam1-osteopontin pathway modulates breast cancer invasion and metastasis. Breast Cancer Res 18, 14 (2016). https://www.ncbi.nlm.nih.gov/pubmed/26821678

C. Q. Wang et al., Interleukin-6 enhances cancer stemness and promotes metastasis of hepatocellular carcinoma via up-regulating osteopontin expression. Am J Cancer Res 6, 1873 (2016). https://www.ncbi.nlm.nih.gov/pubmed/27725896

R. Jia et al., Osteopontin facilitates tumor metastasis by regulating epithelial-mesenchymal plasticity. Cell Death Dis 7, e2564 (2016). https://www.ncbi.nlm.nih.gov/pubmed/28032860

M. Ahmed et al., An Osteopontin/CD44 Axis in RhoGDI2-Mediated Metastasis Suppression. Cancer Cell 30, 432 (2016). https://www.ncbi.nlm.nih.gov/pubmed/27593345

H. Zhao et al., [Correlation of osteopontin expression and laryngeal squamous cell carcinoma infiltration and metastasis]. Lin Chung Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 29, 1530 (2015). https://www.ncbi.nlm.nih.gov/pubmed/26647537

J. Song et al., Hepatic stellate cells activated by acidic tumor microenvironment promote the metastasis of hepatocellular carcinoma via osteopontin. Cancer Lett 356, 713 (2015). https://www.ncbi.nlm.nih.gov/pubmed/25449435

L. Ng et al., Post-operative plasma osteopontin predicts distant metastasis in human colorectal cancer. PLoS One 10, e0126219 (2015). https://www.ncbi.nlm.nih.gov/pubmed/25961724

X. Hou et al., Osteopontin is a useful predictor of bone metastasis and survival in patients with locally advanced nasopharyngeal carcinoma. Int J Cancer 137, 1672 (2015). https://www.ncbi.nlm.nih.gov/pubmed/25824984

X. Q. Zhao et al., Osteopontin promoter polymorphisms at locus -443 are associated with metastasis and poor prognosis of human intrahepatic cholangiocarcinoma in Chinese population. Int J Clin Exp Pathol 7, 6914 (2014). https://www.ncbi.nlm.nih.gov/pubmed/25400775

T. C. Xue et al., Spatial localization of the JAG1/Notch1/osteopontin cascade modulates extrahepatic metastasis in hepatocellular carcinoma. Int J Oncol 45, 1883 (2014). https://www.ncbi.nlm.nih.gov/pubmed/25176314

L. Qin, Osteopontin is a promoter for hepatocellular carcinoma metastasis: a summary of 10 years of studies. Front Med 8, 24 (2014). https://www.ncbi.nlm.nih.gov/pubmed/24464486

T. K. Kwak et al., Inhibitory effect of ethanol extract of Ocimum sanctum on osteopontin mediated metastasis of NCI-H460 non-small cell lung cancer cells. BMC Complement Altern Med 14, 419 (2014). https://www.ncbi.nlm.nih.gov/pubmed/25345853

T. E. Kruger et al., Bone sialoprotein and osteopontin in bone metastasis of osteotropic cancers. Crit Rev Oncol Hematol 89, 330 (2014). https://www.ncbi.nlm.nih.gov/pubmed/24071501

T. C. Xue et al., Transmembrane receptor CXCR7 increases the risk of extrahepatic metastasis of relatively well-differentiated hepatocellular carcinoma through upregulation of osteopontin. Oncol Rep 30, 105 (2013). https://www.ncbi.nlm.nih.gov/pubmed/23636305

B. S. Sun et al., Osteopontin knockdown suppresses non-small cell lung cancer cell invasion and metastasis. Chin Med J (Engl) 126, 1683 (2013). https://www.ncbi.nlm.nih.gov/pubmed/23652051

S. Kumar et al., Functional characterization of stromal osteopontin in melanoma progression and metastasis. PLoS One8, e69116 (2013). https://www.ncbi.nlm.nih.gov/pubmed/23935934

Q. Z. Dong et al., Osteopontin promoter polymorphisms at locus -443 significantly affect the metastasis and prognosis of human hepatocellular carcinoma. Hepatology 57, 1024 (2013). https://www.ncbi.nlm.nih.gov/pubmed/23079960

Y. Chen et al., Osteopontin genetic variants are associated with overall survival in advanced non-small-cell lung cancer patients and bone metastasis. J Exp Clin Cancer Res 32, 45 (2013). https://www.ncbi.nlm.nih.gov/pubmed/23883434

F. Zhao et al., Genetic polymorphisms in the osteopontin promoter increases the risk of distance metastasis and death in Chinese patients with gastric cancer. BMC Cancer 12, 477 (2012). https://www.ncbi.nlm.nih.gov/pubmed/23072570

Y. Wu et al., Breast cancer metastasis suppressor 1 regulates hepatocellular carcinoma cell apoptosis via suppressing osteopontin expression. PLoS One 7, e42976 (2012). https://www.ncbi.nlm.nih.gov/pubmed/22927944

L. Sun et al., Combination of haptoglobin and osteopontin could predict colorectal cancer hepatic metastasis. Ann Surg Oncol 19, 2411 (2012). https://www.ncbi.nlm.nih.gov/pubmed/22219064

Y. Li et al., Elevated content of osteopontin in plasma and tumor tissues of patients with laryngeal and hypopharyngeal carcinoma associated with metastasis and prognosis. Med Oncol 29, 1429 (2012). https://www.ncbi.nlm.nih.gov/pubmed/21706367

J. Huang et al., Osteopontin-enhanced hepatic metastasis of colorectal cancer cells. PLoS One 7, e47901 (2012). https://www.ncbi.nlm.nih.gov/pubmed/23112867

C. H. Chen et al., FLJ10540 is associated with tumor progression in nasopharyngeal carcinomas and contributes to nasopharyngeal cell proliferation, and metastasis via osteopontin/CD44 pathway. J Transl Med 10, 93 (2012). https://www.ncbi.nlm.nih.gov/pubmed/22591637

S. J. Zhang et al., [Inhibition of invasive growth and metastasis of hepatic alveolar echinococcosis by anti-osteopontin antibody]. Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 29, 410 (2011). https://www.ncbi.nlm.nih.gov/pubmed/24822337

L. Zhang et al., [The correlation between osteopontin and metastasis of hepatic Echinococcus multilocularis infection]. Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 29, 33 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21823321

Z. M. Wang et al., Lentiviral-mediated siRNA targeted against osteopontin suppresses the growth and metastasis of gastric cancer cells. Oncol Rep 25, 997 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21286666

H. Y. Sun et al., [Identification of metastasis-related osteopontin expression and glycosylation in hepatocellular carcinoma]. Zhonghua Gan Zang Bing Za Zhi 19, 904 (2011). https://www.ncbi.nlm.nih.gov/pubmed/22525502

G. Platzer et al., The metastasis-associated extracellular matrix protein osteopontin forms transient structure in ligand interaction sites. Biochemistry 50, 6113 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21609000

Z. Mi et al., Osteopontin promotes CCL5-mesenchymal stromal cell-mediated breast cancer metastasis. Carcinogenesis32, 477 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21252118

J. G. Lu et al., Overexpression of osteopontin and integrin alphav in laryngeal and hypopharyngeal carcinomas associated with differentiation and metastasis. J Cancer Res Clin Oncol 137, 1613 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21853313

F. Lin et al., Overexpression of osteopontin in hepatocellular carcinoma and its relationships with metastasis, invasion of tumor cells. Mol Biol Rep 38, 5205 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21188534

Y. Liang et al., Elevated circulating levels of osteopontin are associated with metastasis in advanced non-small cell lung cancer. Chin J Cancer Res 23, 64 (2011). https://www.ncbi.nlm.nih.gov/pubmed/23467432

R. X. Chen et al., Down-regulation of osteopontin inhibits metastasis of hepatocellular carcinoma cells via a mechanism involving MMP-2 and uPA. Oncol Rep 25, 803 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21174062

G. Berge et al., Osteopontin--an important downstream effector of S100A4-mediated invasion and metastasis. Int J Cancer 129, 780 (2011). https://www.ncbi.nlm.nih.gov/pubmed/20957651

M. S. Beausoleil et al., Deletion of the thrombin cleavage domain of osteopontin mediates breast cancer cell adhesion, proteolytic activity, tumorgenicity, and metastasis. BMC Cancer 11, 25 (2011). https://www.ncbi.nlm.nih.gov/pubmed/21247495

K. N. Yu et al., Aerosol delivery of small hairpin osteopontin blocks pulmonary metastasis of breast cancer in mice. PLoS One 5, e15623 (2010). https://www.ncbi.nlm.nih.gov/pubmed/21203518

L. A. Shevde et al., Osteopontin: an effector and an effect of tumor metastasis. Curr Mol Med 10, 71 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20205680

K. Ohno et al., Inhibition of osteopontin reduces liver metastasis of human pancreatic cancer xenografts injected into the spleen in a mouse model. Surg Today 40, 347 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20339989

B. J. Metge et al., Elevated osteopontin levels in metastatic melanoma correlate with epigenetic silencing of breast cancer metastasis suppressor 1. Oncology 78, 75 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20215788

G. Kou et al., A bispecific antibody effectively inhibits tumor growth and metastasis by simultaneous blocking vascular endothelial growth factor A and osteopontin. Cancer Lett 299, 130 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20826049

M. Imano et al., Increased osteopontin-positive macrophage expression in colorectal cancer stroma with synchronous liver metastasis. World J Surg 34, 1930 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20414778

V. Elazar et al., Sustained delivery and efficacy of polymeric nanoparticles containing osteopontin and bone sialoprotein antisenses in rats with breast cancer bone metastasis. Int J Cancer 126, 1749 (2010). https://www.ncbi.nlm.nih.gov/pubmed/19739076

J. Dai et al., A humanized anti-osteopontin antibody inhibits breast cancer growth and metastasis in vivo. Cancer Immunol Immunother 59, 355 (2010). https://www.ncbi.nlm.nih.gov/pubmed/19690854

D. Courter et al., The RGD domain of human osteopontin promotes tumor growth and metastasis through activation of survival pathways. PLoS One 5, e9633 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20224789

R. X. Chen et al., Osteopontin, a single marker for predicting the prognosis of patients with tumor-node-metastasis stage I hepatocellular carcinoma after surgical resection. J Gastroenterol Hepatol 25, 1435 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20659235

H. J. Chen, J. R. Xiao, W. Yuan, Loss of p16INK4, alone and with overexpression of osteopontin, correlates with survival of patients with spinal metastasis from hepatocellular carcinoma. Med Oncol 27, 1005 (2010). https://www.ncbi.nlm.nih.gov/pubmed/19813107

P. H. Anborgh et al., Role of the metastasis-promoting protein osteopontin in the tumour microenvironment. J Cell Mol Med 14, 2037 (2010). https://www.ncbi.nlm.nih.gov/pubmed/20597997

G. Song et al., Osteopontin promotes gastric cancer metastasis by augmenting cell survival and invasion through Akt-mediated HIF-1alpha up-regulation and MMP9 activation. J Cell Mol Med 13, 1706 (2009). https://www.ncbi.nlm.nih.gov/pubmed/19602039

Z. Mi et al., RNA aptamer blockade of osteopontin inhibits growth and metastasis of MDA-MB231 breast cancer cells. Mol Ther 17, 153 (2009). https://www.ncbi.nlm.nih.gov/pubmed/18985031

F. Lin et al., [Interference of osteopontin expression inhibits the invasion and metastasis of human hepatocellular carcinoma cell lines]. Zhonghua Gan Zang Bing Za Zhi 17, 422 (2009). https://www.ncbi.nlm.nih.gov/pubmed/19567019

Y. Liang et al., [The expression of galectin-3 and osteopontin in occult metastasis of non-small cell lung cancer]. Zhonghua Wai Ke Za Zhi 47, 1061 (2009). https://www.ncbi.nlm.nih.gov/pubmed/19781269

J. Zhao et al., Thirty-kilodalton Tat-interacting protein suppresses tumor metastasis by inhibition of osteopontin transcription in human hepatocellular carcinoma. Hepatology 48, 265 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18537194

J. Zhao et al., Down-regulation of osteopontin suppresses growth and metastasis of hepatocellular carcinoma via induction of apoptosis. Gastroenterology 135, 956 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18555021

P. Y. Wai, P. C. Kuo, Osteopontin: regulation in tumor metastasis. Cancer Metastasis Rev 27, 103 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18049863

B. S. Sun et al., Lentiviral-mediated miRNA against osteopontin suppresses tumor growth and metastasis of human hepatocellular carcinoma. Hepatology 48, 1834 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18972404

E. B. Schulze et al., The thrombin inhibitor Argatroban reduces breast cancer malignancy and metastasis via osteopontin-dependent and osteopontin-independent mechanisms. Breast Cancer Res Treat 112, 243 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18097747

B. D. Hedley et al., Downregulation of osteopontin contributes to metastasis suppression by breast cancer metastasis suppressor 1. Int J Cancer 123, 526 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18470911

S. Emani et al., RNA stability regulates differential expression of the metastasis protein, osteopontin, in hepatocellular cancer. Surgery 143, 803 (2008). https://www.ncbi.nlm.nih.gov/pubmed/18549897

R. S. Samant et al., Breast cancer metastasis suppressor 1 (BRMS1) inhibits osteopontin transcription by abrogating NF-kappaB activation. Mol Cancer 6, 6 (2007). https://www.ncbi.nlm.nih.gov/pubmed/17227585

L. R. Rodrigues et al., The role of osteopontin in tumor progression and metastasis in breast cancer. Cancer Epidemiol Biomarkers Prev 16, 1087 (2007). https://www.ncbi.nlm.nih.gov/pubmed/17548669

H. Rangaswami, G. C. Kundu, Osteopontin stimulates melanoma growth and lung metastasis through NIK/MEKK1-dependent MMP-9 activation pathways. Oncol Rep 18, 909 (2007). https://www.ncbi.nlm.nih.gov/pubmed/17786354

A. Ramankulov et al., Plasma osteopontin in comparison with bone markers as indicator of bone metastasis and survival outcome in patients with prostate cancer. Prostate 67, 330 (2007). https://www.ncbi.nlm.nih.gov/pubmed/17192877

C. Hayashi et al., Serum osteopontin, an enhancer of tumor metastasis to bone, promotes B16 melanoma cell migration. J Cell Biochem 101, 979 (2007). https://www.ncbi.nlm.nih.gov/pubmed/17390343

B. K. Cui et al., [Osteopontin as a potential biomarker of metastasis and recurrence for hepatocellular carcinoma]. Ai Zheng 25, 876 (2006). https://www.ncbi.nlm.nih.gov/pubmed/16831281

A. L. Allan et al., Role of the integrin-binding protein osteopontin in lymphatic metastasis of breast cancer. Am J Pathol169, 233 (2006). https://www.ncbi.nlm.nih.gov/pubmed/16816376

P. Y. Wai et al., Osteopontin silencing by small interfering RNA suppresses in vitro and in vivo CT26 murine colon adenocarcinoma metastasis. Carcinogenesis 26, 741 (2005). https://www.ncbi.nlm.nih.gov/pubmed/15661802

P. Y. Wai, P. C. Kuo, The role of Osteopontin in tumor metastasis. J Surg Res 121, 228 (2004). https://www.ncbi.nlm.nih.gov/pubmed/15501463

V. E. Moye et al., Osteopontin expression correlates with adhesive and metastatic potential in metastasis-inducing DNA-transfected rat mammary cell lines. Br J Cancer 90, 1796 (2004). https://www.ncbi.nlm.nih.gov/pubmed/15150606

K. A. Jessen et al., Molecular analysis of metastasis in a polyomavirus middle T mouse model: the role of osteopontin. Breast Cancer Res 6, R157 (2004). https://www.ncbi.nlm.nih.gov/pubmed/15084239

H. Adwan, T. J. Bauerle, M. R. Berger, Downregulation of osteopontin and bone sialoprotein II is related to reduced colony formation and metastasis formation of MDA-MB-231 human breast cancer cells. Cancer Gene Ther 11, 109 (2004). https://www.ncbi.nlm.nih.gov/pubmed/14647232

G. Zhang, B. He, G. F. Weber, Growth factor signaling induces metastasis genes in transformed cells: molecular connection between Akt kinase and osteopontin in breast cancer. Mol Cell Biol 23, 6507 (2003). https://www.ncbi.nlm.nih.gov/pubmed/12944477

H. W. Pan et al., Overexpression of osteopontin is associated with intrahepatic metastasis, early recurrence, and poorer prognosis of surgically resected hepatocellular carcinoma. Cancer 98, 119 (2003). https://www.ncbi.nlm.nih.gov/pubmed/12833464

G. Carlinfante et al., Differential expression of osteopontin and bone sialoprotein in bone metastasis of breast and prostate carcinoma. Clin Exp Metastasis 20, 437 (2003). https://www.ncbi.nlm.nih.gov/pubmed/14524533

E. V. Ariztia et al., Osteopontin contributes to hepatocyte growth factor-induced tumor growth and metastasis formation. Exp Cell Res 288, 257 (2003). https://www.ncbi.nlm.nih.gov/pubmed/12915117

V. Urquidi et al., Contrasting expression of thrombospondin-1 and osteopontin correlates with absence or presence of metastatic phenotype in an isogenic model of spontaneous human breast cancer metastasis. Clin Cancer Res 8, 61 (2002). https://www.ncbi.nlm.nih.gov/pubmed/11801541

P. S. Rudland et al., Prognostic significance of the metastasis-associated protein osteopontin in human breast cancer. Cancer Res 62, 3417 (2002). https://www.ncbi.nlm.nih.gov/pubmed/12067984

M. M. Rashid, [Cooperative role of osteopontin with type I collagen on the metastasis of murine melanoma cells]. Hokkaido Igaku Zasshi 77, 341 (2002). https://www.ncbi.nlm.nih.gov/pubmed/12187830

S. J. Hotte et al., Plasma osteopontin: associations with survival and metastasis to bone in men with hormone-refractory prostate carcinoma. Cancer 95, 506 (2002). https://www.ncbi.nlm.nih.gov/pubmed/12209742

G. F. Weber, The metastasis gene osteopontin: a candidate target for cancer therapy. Biochim Biophys Acta 1552, 61 (2001). https://www.ncbi.nlm.nih.gov/pubmed/11825687

H. Nemoto et al., Osteopontin deficiency reduces experimental tumor cell metastasis to bone and soft tissues. J Bone Miner Res 16, 652 (2001). https://www.ncbi.nlm.nih.gov/pubmed/11315992

K. A. Furger et al., The functional and clinical roles of osteopontin in cancer and metastasis. Curr Mol Med 1, 621 (2001). https://www.ncbi.nlm.nih.gov/pubmed/11899236

M. El-Tanani et al., Metastasis-inducing dna regulates the expression of the osteopontin gene by binding the transcription factor Tcf-4. Cancer Res 61, 5619 (2001). https://www.ncbi.nlm.nih.gov/pubmed/11454716

G. F. Weber, S. Ashkar, H. Cantor, Interaction between CD44 and osteopontin as a potential basis for metastasis formation. Proc Assoc Am Physicians 109, 1 (1997). https://www.ncbi.nlm.nih.gov/pubmed/9010911

A. J. Oates, R. Barraclough, P. S. Rudland, The role of osteopontin in tumorigenesis and metastasis. Invasion Metastasis 17, 1 (1997). https://www.ncbi.nlm.nih.gov/pubmed/9425320

A. J. Oates, R. Barraclough, P. S. Rudland, The identification of osteopontin as a metastasis-related gene product in a rodent mammary tumour model. Oncogene 13, 97 (1996). https://www.ncbi.nlm.nih.gov/pubmed/8700559

B. Feng, E. E. Rollo, D. T. Denhardt, Osteopontin (OPN) may facilitate metastasis by protecting cells from macrophage NO-mediated cytotoxicity: evidence from cell lines down-regulated for OPN expression by a targeted ribozyme. Clin Exp Metastasis 13, 453 (1995). https://www.ncbi.nlm.nih.gov/pubmed/7586803

D. T. Denhardt, A. F. Chambers, Overcoming obstacles to metastasis--defenses against host defenses: osteopontin (OPN) as a shield against attack by cytotoxic host cells. J Cell Biochem 56, 48 (1994). https://www.ncbi.nlm.nih.gov/pubmed/7528752