Sung H, et al. Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin. 2021;71:209–49.
Alvarez RH. Present and future evolution of advanced breast cancer therapy. Breast Cancer Res. 2010;12 Suppl 2:S1.
Ferrari P, et al. Molecular mechanisms, biomarkers and emerging therapies for chemotherapy resistant TNBC. Int J Mol Sci. 2022;23:1665.
Pernas S, Tolaney SM. HER2-positive breast cancer: new therapeutic frontiers and overcoming resistance. Ther Adv Med Oncol. 2019;11:1758835919833519.
Lin NU, Winer EP. Advances in adjuvant endocrine therapy for postmenopausal women. J Clin Oncol. 2008;26:798–805.
Pan H, et al. 20-year risks of breast-cancer recurrence after stopping endocrine therapy at 5 years. N Engl J Med. 2017;377:1836–46.
Hanker AB, Sudhan DR, Arteaga CL. Overcoming endocrine resistance in breast cancer. Cancer Cell. 2020;37:496–513.
Slamon DJ, et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N Engl J Med. 2001;344:783–92.
Romond EH, et al. Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer. N Engl J Med. 2005;353:1673–84.
Schmid P, et al. Atezolizumab and nab-paclitaxel in advanced triple-negative breast cancer. N Engl J Med. 2018;379:2108–21.
Angelucci A. Targeting tyrosine kinases in cancer: lessons for an effective targeted therapy in the clinic. Cancers. 2019;11:490.
Roskoski R Jr. Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors. Pharmacol Res. 2015;94:9–25.
Elsberger B. Translational evidence on the role of Src kinase and activated Src kinase in invasive breast cancer. Crit Rev Oncol Hematol. 2014;89:343–51.
Kato G. Regulatory roles of the N-terminal intrinsically disordered region of modular Src. Int J Mol Sci. 2022;23:2241.
Ia KK, et al. Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases. Growth Factors. 2010;28:329–50.
Song RX, Zhang Z, Santen RJ. Estrogen rapid action via protein complex formation involving ERalpha and Src. Trends Endocrinol Metab. 2005;16:347–53.
Boonyaratanakornkit V, et al. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol Cell. 2001;8:269–80.
Ballare C, et al. Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells. Mol Cell Biol. 2003;23:1994–2008.
Dwyer AR, Truong TH, Ostrander JH, Lange CA. 90 YEARS OF PROGESTERONE: steroid receptors as MAPK signaling sensors in breast cancer: let the fates decide. J Mol Endocrinol. 2020;65:T35–48.
Feng W, et al. Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway. Mol Endocrinol. 2001;15:32–45.
Aggelis V, Johnston SRD. Advances in endocrine-based therapies for Estrogen receptor-positive metastatic breast cancer. Drugs. 2019;79:1849–66.
Rasha F, Sharma M, Pruitt K. Mechanisms of endocrine therapy resistance in breast cancer. Mol Cell Endocrinol. 2021;532: 111322.
Hiscox S, et al. Dual targeting of Src and ER prevents acquired antihormone resistance in breast cancer cells. Breast Cancer Res Treat. 2009;115:57–67.
Chen Y, et al. Combined Src and ER blockade impairs human breast cancer proliferation in vitro and in vivo. Breast Cancer Res Treat. 2011;128:69–78.
Poulard C, et al. Activation of rapid oestrogen signalling in aggressive human breast cancers. EMBO Mol Med. 2012;4:1200–13.
Fan P, et al. c-Src modulates estrogen-induced stress and apoptosis in estrogen-deprived breast cancer cells. Cancer Res. 2013;73:4510–20.
Muthuswamy SK, Siegel PM, Dankort DL, Webster MA, Muller WJ. Mammary tumors expressing the neu proto-oncogene possess elevated c-Src tyrosine kinase activity. Mol Cell Biol. 1994;14:735–43.
Guy CT, Muthuswamy SK, Cardiff RD, Soriano P, Muller WJ. Activation of the c-Src tyrosine kinase is required for the induction of mammary tumors in transgenic mice. Genes Dev. 1994;8:23–32.
Tan M, et al. ErbB2 promotes Src synthesis and stability: novel mechanisms of Src activation that confer breast cancer metastasis. Can Res. 2005;65:1858–67.
Smith HW, et al. An ErbB2/c-Src axis links bioenergetics with PRC2 translation to drive epigenetic reprogramming and mammary tumorigenesis. Nat Commun. 2019;10:2901.
Wilson GR, et al. Activated c-SRC in ductal carcinoma in situ correlates with high tumour grade, high proliferation and HER2 positivity. Br J Cancer. 2006;95:1410–4.
Muthuswamy SK. Trastuzumab resistance: all roads lead to SRC. Nat Med. 2011;17:416–8.
Zhang S, et al. Combating trastuzumab resistance by targeting SRC, a common node downstream of multiple resistance pathways. Nat Med. 2011;17:461–9.
Peiro G, et al. Src, a potential target for overcoming trastuzumab resistance in HER2-positive breast carcinoma. Br J Cancer. 2014;111:689–95.
Bianchini G, Balko JM, Mayer IA, Sanders ME, Gianni L. Triple-negative breast cancer: challenges and opportunities of a heterogeneous disease. Nat Rev Clin Oncol. 2016;13:674–90.
Myoui A, et al. C-SRC tyrosine kinase activity is associated with tumor colonization in bone and lung in an animal model of human breast cancer metastasis. Can Res. 2003;63:5028–33.
Finn RS, et al. Dasatinib, an orally active small molecule inhibitor of both the src and abl kinases, selectively inhibits growth of basal-type/"triple-negative" breast cancer cell lines growing in vitro. Breast Cancer Res Treat. 2007;105:319–26.
Tryfonopoulos D, et al. Src: a potential target for the treatment of triple-negative breast cancer. Ann Oncol Off J Eur Soc Med Oncol. 2011;22:2234–40.
Finn RS, et al. Dasatinib as a single agent in triple-negative breast cancer: results of an open-label phase 2 study. Clin Cancer Res Off J Am Assoc Cancer Res. 2011;17:6905–13.
Giatromanolaki A, Sivridis E, Fiska A, Koukourakis MI. The CD44+/CD24- phenotype relates to “triple-negative” state and unfavorable prognosis in breast cancer patients. Med Oncol. 2011;28:745–52.
Tian J, et al. Dasatinib sensitises triple negative breast cancer cells to chemotherapy by targeting breast cancer stem cells. Br J Cancer. 2018;119:1495–507.
Lou L, Yu Z, Wang Y, Wang S, Zhao Y. c-Src inhibitor selectively inhibits triple-negative breast cancer overexpressed Vimentin in vitro and in vivo. Cancer Sci. 2018;109:1648–59.
Kohale IN, et al. Identification of Src family kinases as potential therapeutic targets for chemotherapy-resistant triple negative breast cancer. Cancers. 2022;14:4220.
Parsons JT, Parsons SJ. Src family protein tyrosine kinases: cooperating with growth factor and adhesion signaling pathways. Curr Opin Cell Biol. 1997;9:187–92.
Biscardi JS, et al. c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function. J Biol Chem. 1999;274:8335–43.
Ishizawar RC, Miyake T, Parsons SJ. c-Src modulates ErbB2 and ErbB3 heterocomplex formation and function. Oncogene. 2007;26:3503–10.
Bottinger EP, Jakubczak JL, Haines DC, Bagnall K, Wakefield LM. Transgenic mice overexpressing a dominant-negative mutant type II transforming growth factor beta receptor show enhanced tumorigenesis in the mammary gland and lung in response to the carcinogen 7,12-dimethylbenz-[a]-anthracene. Can Res. 1997;57:5564–70.
Galliher AJ, Schiemann WP. Src phosphorylates Tyr284 in TGF-beta type II receptor and regulates TGF-beta stimulation of p38 MAPK during breast cancer cell proliferation and invasion. Can Res. 2007;67:3752–8.
van Roy F, Berx G. The cell-cell adhesion molecule E-cadherin. Cell Mol Life Sci CMLS. 2008;65:3756–88.
Behrens J, et al. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J Cell Biol. 1993;120:757–66.
Kinch MS, Clark GJ, Der CJ, Burridge K. Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J Cell Biol. 1995;130:461–71.
Vlahov N, et al. Alternate RASSF1 transcripts control SRC activity, E-cadherin contacts, and YAP-mediated invasion. Curr Biol CB. 2015;25:3019–34.
Mukherjee M, et al. Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin. EMBO J. 2012;31:1308–19.
Rolland Y, et al. The CDC42-interacting protein 4 controls epithelial cell cohesion and tumor dissemination. Dev Cell. 2014;30:553–68.
Bhatt AS, Erdjument-Bromage H, Tempst P, Craik CS, Moasser MM. Adhesion signaling by a novel mitotic substrate of src kinases. Oncogene. 2005;24:5333–43.
Wong CH, et al. Phosphorylation of the SRC epithelial substrate Trask is tightly regulated in normal epithelia but widespread in many human epithelial cancers. Clin Cancer Res Off J Am Assoc Cancer Res. 2009;15:2311–22.
Spassov DS, Baehner FL, Wong CH, McDonough S, Moasser MM. The transmembrane src substrate Trask is an epithelial protein that signals during anchorage deprivation. Am J Pathol. 2009;174:1756–65.
Leroy C, et al. CUB-domain-containing protein 1 overexpression in solid cancers promotes cancer cell growth by activating Src family kinases. Oncogene. 2015;34:5593–8.
Nelson LJ, et al. Src kinase is biphosphorylated at Y416/Y527 and activates the CUB-domain containing protein 1/protein kinase C delta pathway in a subset of triple-negative breast cancers. Am J Pathol. 2020;190:484–502.
Sakai T, Jove R, Fassler R, Mosher DF. Role of the cytoplasmic tyrosines of beta 1A integrins in transformation by v-src. Proc Natl Acad Sci USA. 2001;98:3808–13.
Datta A, Huber F, Boettiger D. Phosphorylation of beta3 integrin controls ligand binding strength. J Biol Chem. 2002;277:3943–9.
Schumacher S, Vazquez Nunez R, Biertumpfel C, Mizuno N. Bottom-up reconstitution of focal adhesion complexes. FEBS J. 2022;289:3360–73.
Mishra YG, Manavathi B. Focal adhesion dynamics in cellular function and disease. Cell Signal. 2021;85: 110046.
Benlimame N, et al. FAK signaling is critical for ErbB-2/ErbB-3 receptor cooperation for oncogenic transformation and invasion. J Cell Biol. 2005;171:505–16.
Lahlou H, et al. Mammary epithelial-specific disruption of the focal adhesion kinase blocks mammary tumor progression. Proc Natl Acad Sci USA. 2007;104:20302–7.
Bianchi-Smiraglia A, Paesante S, Bakin AV. Integrin beta5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways. Oncogene. 2013;32:3049–58.
Lee JJ, et al. Inhibition of epithelial cell migration and Src/FAK signaling by SIRT3. Proc Natl Acad Sci USA. 2018;115:7057–62.
Fatherree JP, Guarin JR, McGinn RA, Naber SP, Oudin MJ. Chemotherapy-induced collagen IV drives cancer cell motility through activation of Src and focal adhesion kinase. Can Res. 2022;82:2031–44.
Mekhdjian AH, et al. Integrin-mediated traction force enhances paxillin molecular associations and adhesion dynamics that increase the invasiveness of tumor cells into a three-dimensional extracellular matrix. Mol Biol Cell. 2017;28:1467–88.
Wang S, et al. CCM3 is a gatekeeper in focal adhesions regulating mechanotransduction and YAP/TAZ signalling. Nat Cell Biol. 2021;23:758–70.
Qian X, et al. The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell. 2009;16:246–58.
Courtneidge SA, Azucena EF, Pass I, Seals DF, Tesfay L. The SRC substrate Tks5, podosomes (invadopodia), and cancer cell invasion. Cold Spring Harb Symp Quant Biol. 2005;70:167–71.
Joshi B, et al. Phosphocaveolin-1 is a mechanotransducer that induces caveola biogenesis via Egr1 transcriptional regulation. J Cell Biol. 2012;199:425–35.
Yoon HJ, Kim DH, Kim SJ, Jang JH, Surh YJ. Src-mediated phosphorylation, ubiquitination and degradation of Caveolin-1 promotes breast cancer cell stemness. Cancer Lett. 2019;449:8–19.
Ngan E, et al. LPP is a Src substrate required for invadopodia formation and efficient breast cancer lung metastasis. Nat Commun. 2017;8:15059.
Centonze G, et al. p130Cas/BCAR1 and p140Cap/SRCIN1 Adaptors: The Yin Yang in Breast Cancer? Front Cell Dev Biol. 2021;9: 729093.
Wu MH, et al. MCT-1 expression and PTEN deficiency synergistically promote neoplastic multinucleation through the Src/p190B signaling activation. Oncogene. 2014;33:5109–20.
Sausgruber N, et al. Tyrosine phosphatase SHP2 increases cell motility in triple-negative breast cancer through the activation of SRC-family kinases. Oncogene. 2015;34:2272–8.
Tognoli ML, et al. RASSF1C oncogene elicits amoeboid invasion, cancer stemness, and extracellular vesicle release via a SRC/Rho axis. EMBO J. 2021;40: e107680.
Lu Y, et al. Src family protein-tyrosine kinases alter the function of PTEN to regulate phosphatidylinositol 3-kinase/AKT cascades. J Biol Chem. 2003;278:40057–66.
Hirsch DS, Shen Y, Dokmanovic M, Wu WJ. pp60c-Src phosphorylates and activates vacuolar protein sorting 34 to mediate cellular transformation. Can Res. 2010;70:5974–83.
Li H, et al. Phosphatidylethanolamine-binding protein 4 is associated with breast cancer metastasis through Src-mediated Akt tyrosine phosphorylation. Oncogene. 2014;33:4589–98.
Jiang T, Qiu Y. Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation. J Biol Chem. 2003;278:15789–93.
Ma X, et al. Characterization of the Src-regulated kinome identifies SGK1 as a key mediator of Src-induced transformation. Nat Commun. 2019;10:296.
Si Y, et al. Src inhibits the hippo tumor suppressor pathway through tyrosine phosphorylation of lats1. Can Res. 2017;77:4868–80.
Lamar JM, et al. SRC tyrosine kinase activates the YAP/TAZ axis and thereby drives tumor growth and metastasis. J Biol Chem. 2019;294:2302–17.
Garcia-Higuera I, et al. Genomic stability and tumour suppression by the APC/C cofactor Cdh1. Nat Cell Biol. 2008;10:802–11.
Han T, et al. Interplay between c-Src and the APC/C co-activator Cdh1 regulates mammary tumorigenesis. Nat Commun. 2019;10:3716.
Easton DF, et al. Genome-wide association study identifies novel breast cancer susceptibility loci. Nature. 2007;447:1087–93.
Maretzky T, et al. Src stimulates fibroblast growth factor receptor-2 shedding by an ADAM15 splice variant linked to breast cancer. Can Res. 2009;69:4573–6.
Jin L, et al. Phosphorylation-mediated activation of LDHA promotes cancer cell invasion and tumour metastasis. Oncogene. 2017;36:3797–806.
Phan J, Reue K. Lipin, a lipodystrophy and obesity gene. Cell Metab. 2005;1:73–83.
Song L, et al. Proto-oncogene Src links lipogenesis via lipin-1 to breast cancer malignancy. Nat Commun. 2020;11:5842.
Silva CM. Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis. Oncogene. 2004;23:8017–23.
Garcia R, et al. Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells. Oncogene. 2001;20:2499–513.
Kloth MT, et al. STAT5b, a mediator of synergism between c-Src and the epidermal growth factor receptor. J Biol Chem. 2003;278:1671–9.
Lu H, et al. Chemotherapy-induced Ca(2+) release stimulates breast cancer stem cell enrichment. Cell Rep. 2017;18:1946–57.
Jiang L, et al. NCAPG confers trastuzumab resistance via activating SRC/STAT3 signaling pathway in HER2-positive breast cancer. Cell Death Dis. 2020;11:547.
Calvo F, et al. Mechanotransduction and YAP-dependent matrix remodelling is required for the generation and maintenance of cancer-associated fibroblasts. Nat Cell Biol. 2013;15:637–46.
Sorrentino G, et al. Glucocorticoid receptor signalling activates YAP in breast cancer. Nat Commun. 2017;8:14073.
Liu Q, et al. HOMER3 facilitates growth factor-mediated beta-Catenin tyrosine phosphorylation and activation to promote metastasis in triple negative breast cancer. J Hematol Oncol. 2021;14:6.
Kim H, Son S, Ko Y, Shin I. CTGF regulates cell proliferation, migration, and glucose metabolism through activation of FAK signaling in triple-negative breast cancer. Oncogene. 2021;40:2667–81.
Lu G, et al. Phosphorylation of ETS1 by Src family kinases prevents its recognition by the COP1 tumor suppressor. Cancer Cell. 2014;26:222–34.
Arnold SF, Vorojeikina DP, Notides AC. Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element. J Biol Chem. 1995;270:30205–12.
Arnold SF, Obourn JD, Jaffe H, Notides AC. Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol Endocrinol. 1995;9:24–33.
Ma L, et al. Kindlin-2 promotes Src-mediated tyrosine phosphorylation of androgen receptor and contributes to breast cancer progression. Cell Death Dis. 2022;13:482.
Chu I, et al. p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2. Cell. 2007;128:281–94.
Marcotte R, Smith HW, Sanguin-Gendreau V, McDonough RV, Muller WJ. Mammary epithelial-specific disruption of c-Src impairs cell cycle progression and tumorigenesis. Proc Natl Acad Sci USA. 2012;109:2808–13.
Richard S, et al. Sam68 haploinsufficiency delays onset of mammary tumorigenesis and metastasis. Oncogene. 2008;27:548–56.
Fraser C, et al. Rapid discovery and structure-activity relationships of pyrazolopyrimidines that potently suppress breast cancer cell growth via SRC kinase inhibition with exceptional selectivity over ABL kinase. J Med Chem. 2016;59:4697–710.
Jallal H, et al. A Src/Abl kinase inhibitor, SKI-606, blocks breast cancer invasion, growth, and metastasis in vitro and in vivo. Can Res. 2007;67:1580–8.
Vultur A, et al. SKI-606 (bosutinib), a novel Src kinase inhibitor, suppresses migration and invasion of human breast cancer cells. Mol Cancer Ther. 2008;7:1185–94.
Hebbard L, et al. Control of mammary tumor differentiation by SKI-606 (bosutinib). Oncogene. 2011;30:301–12.
Campone M, et al. Phase II study of single-agent bosutinib, a Src/Abl tyrosine kinase inhibitor, in patients with locally advanced or metastatic breast cancer pretreated with chemotherapy. Ann Oncol Off J Eur Soc Med Oncol. 2012;23:610–7.
Moy B, et al. Bosutinib in combination with the aromatase inhibitor letrozole: a phase II trial in postmenopausal women evaluating first-line endocrine therapy in locally advanced or metastatic hormone receptor-positive/HER2-negative breast cancer. Oncologist. 2014;19:348–9.
Moy B, et al. Bosutinib in combination with the aromatase inhibitor exemestane: a phase II trial in postmenopausal women with previously treated locally advanced or metastatic hormone receptor-positive/HER2-negative breast cancer. Oncologist. 2014;19:346–7.
Isakoff SJ, et al. Bosutinib plus capecitabine for selected advanced solid tumours: results of a phase 1 dose-escalation study. Br J Cancer. 2014;111:2058–66.
Beetham H, et al. Loss of integrin-linked kinase sensitizes breast cancer to SRC inhibitors. Can Res. 2022;82:632–47.
Lombardo LJ, et al. Discovery of N-(2-chloro-6-methyl- phenyl)-2-(6-(4-(2-hydroxyethyl)- piperazin-1-yl)-2-methylpyrimidin-4- ylamino)thiazole-5-carboxamide (BMS-354825), a dual Src/Abl kinase inhibitor with potent antitumor activity in preclinical assays. J Med Chem. 2004;47:6658–61.
Mayer EL, et al. A phase 2 trial of dasatinib in patients with advanced HER2-positive and/or hormone receptor-positive breast cancer. Clin Cancer Res Off J Am Assoc Cancer Res. 2011;17:6897–904.
Herold CI, et al. Phase II trial of dasatinib in patients with metastatic breast cancer using real-time pharmacodynamic tissue biomarkers of Src inhibition to escalate dosing. Clin Cancer Res Off J Am Assoc Cancer Res. 2011;17:6061–70.
Schott AF, et al. Phase II studies of two different schedules of dasatinib in bone metastasis predominant metastatic breast cancer: SWOG S0622. Breast Cancer Res Treat. 2016;159:87–95.
Pusztai L, et al. Gene signature-guided dasatinib therapy in metastatic breast cancer. Clin Cancer Res Off J Am Assoc Cancer Res. 2014;20:5265–71.
Fornier MN, et al. A phase I study of dasatinib and weekly paclitaxel for metastatic breast cancer. Ann Oncol Off J Eur Soc Med Oncol. 2011;22:2575–81.
Morris PG, et al. Phase II study of paclitaxel and dasatinib in metastatic breast cancer. Clin Breast Cancer. 2018;18:387–94.
Somlo G, et al. Dasatinib plus capecitabine for advanced breast cancer: safety and efficacy in phase I study CA180004. Clin Cancer Res Off J Am Assoc Cancer Res. 2013;19:1884–93.
Paul D, et al. Randomized phase-II evaluation of letrozole plus dasatinib in hormone receptor positive metastatic breast cancer patients. NPJ Breast Cancer. 2019;5:36.
Soriano P, Montgomery C, Geske R, Bradley A. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell. 1991;64:693–702.
Mitri Z, et al. TBCRC-010: phase I/II study of dasatinib in combination with zoledronic acid for the treatment of breast cancer bone metastasis. Clin Cancer Res Off J Am Assoc Cancer Res. 2016;22:5706–12.
Ocana A, et al. A phase I study of the SRC kinase inhibitor dasatinib with trastuzumab and paclitaxel as first line therapy for patients with HER2-overexpressing advanced breast cancer: GEICAM/2010–04 study. Oncotarget. 2017;8:73144–53.
Ocana A, et al. Efficacy and safety of dasatinib with trastuzumab and paclitaxel in first line HER2-positive metastatic breast cancer: results from the phase II GEICAM/2010-04 study. Breast Cancer Res Treat. 2019;174:693–701.
Herynk MH, et al. Cooperative action of tamoxifen and c-Src inhibition in preventing the growth of estrogen receptor-positive human breast cancer cells. Mol Cancer Ther. 2006;5:3023–31.
Jain S, et al. Src inhibition blocks c-Myc translation and glucose metabolism to prevent the development of breast cancer. Can Res. 2015;75:4863–75.
Gucalp A, et al. Phase II trial of saracatinib (AZD0530), an oral SRC-inhibitor for the treatment of patients with hormone receptor-negative metastatic breast cancer. Clin Breast Cancer. 2011;11:306–11.
Temps C, et al. A Conformation selective mode of inhibiting SRC improves drug efficacy and tolerability. Can Res. 2021;81:5438–50.
Cortes J, et al. Pembrolizumab plus chemotherapy versus placebo plus chemotherapy for previously untreated locally recurrent inoperable or metastatic triple-negative breast cancer (KEYNOTE-355): a randomised, placebo-controlled, double-blind, phase 3 clinical trial. Lancet. 2020;396:1817–28.
Schmid P, et al. Atezolizumab plus nab-paclitaxel as first-line treatment for unresectable, locally advanced or metastatic triple-negative breast cancer (IMpassion130): updated efficacy results from a randomised, double-blind, placebo-controlled, phase 3 trial. Lancet Oncol. 2020;21:44–59.