{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T16:08:59Z","timestamp":1789056539334,"version":"build-2803163510"},"reference-count":78,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.biochi.2026.08.002","type":"journal-article","created":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T23:35:48Z","timestamp":1786059348000},"page":"161-170","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["F11 Receptor\/Junctional Adhesion Molecule-A: a novel therapeutic target in breast cancer"],"prefix":"10.1016","volume":"249","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4505-9498","authenticated-orcid":false,"given":"Rados\u0142aw","family":"Bednarek","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"\u015awi\u0105tkowska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2026.08.002_bib1","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1016\/S0140-6736(16)31891-8","article-title":"Breast cancer","volume":"389","author":"Harbeck","year":"2017","journal-title":"Lancet"},{"key":"10.1016\/j.biochi.2026.08.002_bib3","unstructured":"Wojciechowska U, Didkowska J. Zachorowania i zgony na nowotwory z\u0142o\u015bliwe w Polsce. Nowotwory piersi u kobiet (C50). In: Krajowy Rejestr Nowotwor\u00f3w, Centrum Onkologii-Instytut im. Marii Sk\u0142odowskiej-Curie. https:\/\/onkologia.org.pl\/en\/report\/. Accessed June 19, 2026."},{"key":"10.1016\/j.biochi.2026.08.002_bib4","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1126\/science.1203543","article-title":"A perspective on cancer cell metastasis","volume":"331","author":"Chaffer","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.biochi.2026.08.002_bib5","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/s41392-025-02148-4","article-title":"Invasion and metastasis in cancer: molecular insights and therapeutic targets","volume":"10","author":"Li","year":"2025","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.biochi.2026.08.002_bib6","doi-asserted-by":"crossref","first-page":"797","DOI":"10.3892\/ijo.2015.3075","article-title":"The role of inflammation in progression of breast cancer: friend or foe?","volume":"47","author":"Allen","year":"2015","journal-title":"Int. J. Oncol."},{"key":"10.1016\/j.biochi.2026.08.002_bib7","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1038\/nrc3628","article-title":"Crossing the endothelial barrier during metastasis","volume":"13","author":"Reymond","year":"2013","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.biochi.2026.08.002_bib8","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1186\/bcr2876","article-title":"Breast cancer growth and metastasis: interplay between cancer stem cells, embryonic signaling pathways and epithelial-to-mesenchymal transition","volume":"13","author":"Takebe","year":"2011","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2022.113774","article-title":"EMT mechanism in breast cancer metastasis and drug resistance: revisiting molecular interactions and biological functions","volume":"155","author":"Hashemi","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.biochi.2026.08.002_bib10","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1084\/jem.20120662","article-title":"Deficiency for endoglin in tumor vasculature weakens the endothelial barrier to metastatic dissemination","volume":"210","author":"Anderberg","year":"2013","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.biochi.2026.08.002_bib11","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1007\/s00441-014-1820-1","article-title":"Tight junction dynamics: the role of junctional adhesion molecules (JAMs)","volume":"355","author":"Garrido-Urbani","year":"2014","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib12","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1038\/s41572-019-0111-2","article-title":"Breast cancer","volume":"5","author":"Harbeck","year":"2019","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.biochi.2026.08.002_bib13","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1038\/35021093","article-title":"Molecular portraits of human breast tumours","volume":"406","author":"Perou","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2026.08.002_bib14","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/nature10983","article-title":"The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups","volume":"486","author":"Curtis","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2026.08.002_bib15","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1093\/annonc\/mdy024","article-title":"Unravelling triple-negative breast cancer molecular heterogeneity using an integrative multiomic analysis","volume":"29","author":"Bareche","year":"2018","journal-title":"Ann. Oncol."},{"key":"10.1016\/j.biochi.2026.08.002_bib16","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1007\/s12032-023-02111-9","article-title":"Extensive review on breast cancer its etiology, progression, prognostic markers, and treatment","volume":"40","author":"Swaminathan","year":"2023","journal-title":"Med. Oncol."},{"key":"10.1016\/j.biochi.2026.08.002_bib17","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1002\/stem.2021","article-title":"Development of a fluorescent reporter system to delineate cancer stem cells in triple-negative breast cancer","volume":"33","author":"Thiagarajan","year":"2015","journal-title":"Stem Cell."},{"key":"10.1016\/j.biochi.2026.08.002_bib18","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.celrep.2013.11.043","article-title":"High-throughput flow cytometry screening reveals a role for junctional adhesion molecule a as a cancer stem cell maintenance factor","volume":"6","author":"Lathia","year":"2014","journal-title":"Cell Rep."},{"key":"10.1016\/j.biochi.2026.08.002_bib19","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1128\/MCB.06678-11","article-title":"Relocalization of junctional adhesion molecule A during inflammatory stimulation of brain endothelial cells","volume":"32","author":"Stamatovic","year":"2012","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.biochi.2026.08.002_bib20","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1083\/jcb.142.1.117","article-title":"Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration","volume":"142","author":"Mart\u00ecn-Padura","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.biochi.2026.08.002_bib21","doi-asserted-by":"crossref","first-page":"10042","DOI":"10.1016\/S0021-9258(19)38776-9","article-title":"Activation of human platelets by a stimulatory monoclonal antibody","volume":"265","author":"Kornecki","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2026.08.002_bib22","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1182\/blood.V95.8.2600","article-title":"Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation","volume":"95","author":"Sobocka","year":"2000","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2026.08.002_bib23","doi-asserted-by":"crossref","first-page":"4094","DOI":"10.1002\/(SICI)1521-4141(199812)28:12<4094::AID-IMMU4094>3.0.CO;2-2","article-title":"CTX, a Xenopus thymocyte receptor, defines a molecular family conserved throughout vertebrates","volume":"28","author":"Chr\u00e9tien","year":"1998","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.biochi.2026.08.002_bib24","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamem.2020.183299","article-title":"Physiological functions of junctional adhesion molecules (JAMs) in tight junctions","volume":"1862","author":"Hartmann","year":"2020","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.biochi.2026.08.002_bib25","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s11010-021-04259-2","article-title":"The F11 Receptor (F11R)\/Junctional Adhesion Molecule-A (JAM-A) (F11R\/JAM-A) in cancer progression","volume":"477","author":"Czubak-Prowizor","year":"2022","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.biochi.2026.08.002_bib26","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1152\/physrev.00004.2017","article-title":"Junctional adhesion molecules (JAMs): cell adhesion receptors with pleiotropic functions in cell physiology and development","volume":"97","author":"Ebnet","year":"2017","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.biochi.2026.08.002_bib27","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1007\/s00018-017-2729-0","article-title":"Junctional adhesion molecule-A: functional diversity through molecular promiscuity","volume":"75","author":"Steinbacher","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.biochi.2026.08.002_bib28","doi-asserted-by":"crossref","first-page":"D444","DOI":"10.1093\/nar\/gkae1082","article-title":"InterPro: the protein sequence classification resource in 2025","volume":"53","author":"Blum","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib29","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.1093\/emboj\/20.16.4391","article-title":"X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif","volume":"20","author":"Kostrewa","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2026.08.002_bib30","doi-asserted-by":"crossref","first-page":"5366","DOI":"10.1073\/pnas.0937718100","article-title":"Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding","volume":"100","author":"Prota","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2026.08.002_bib31","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1091\/mbc.e14-01-0018","article-title":"Trans-dimerization of JAM-A regulates Rap2 and is mediated by a domain that is distinct from the cis-dimerization interface","volume":"25","author":"Monteiro","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.biochi.2026.08.002_bib32","doi-asserted-by":"crossref","first-page":"2194","DOI":"10.1158\/0008-5472.CAN-07-3057","article-title":"Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion","volume":"68","author":"Naik","year":"2008","journal-title":"Cancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib33","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1002\/ijc.24498","article-title":"JAM-A expression positively correlates with poor prognosis in breast cancer patients","volume":"125","author":"McSherry","year":"2009","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.biochi.2026.08.002_bib34","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1038\/onc.2012.276","article-title":"Junctional adhesion molecule-A is co-expressed with HER2 in breast tumors and acts as a novel regulator of HER2 protein degradation and signaling","volume":"32","author":"Brennan","year":"2013","journal-title":"Oncogene"},{"key":"10.1016\/j.biochi.2026.08.002_bib35","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0021242","article-title":"Abrogation of junctional adhesion molecule-A expression induces cell apoptosis and reduces breast cancer progression","volume":"6","author":"Murakami","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2026.08.002_bib36","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1186\/s13058-018-1064-1","article-title":"Cleavage of the extracellular domain of junctional adhesion molecule-A is associated with resistance to anti-HER2 therapies in breast cancer settings","volume":"20","author":"Leech","year":"2018","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib37","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.7314\/APJCP.2016.17.4.1609","article-title":"HER-2 positive breast cancer - a mini-review","volume":"17","author":"Asif","year":"2016","journal-title":"Asian Pac. J. Cancer Prev. APJCP"},{"key":"10.1016\/j.biochi.2026.08.002_bib38","doi-asserted-by":"crossref","first-page":"646","DOI":"10.3390\/cancers11050646","article-title":"Gene expression and miRNAs profiling: function and regulation in human epidermal growth factor receptor 2 (HER2)-positive breast cancer","volume":"11","author":"Sareyeldin","year":"2019","journal-title":"Cancers"},{"key":"10.1016\/j.biochi.2026.08.002_bib39","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.critrevonc.2019.05.001","article-title":"Resistance mechanisms to anti-HER2 therapies in HER2-positive breast cancer: current knowledge, new research directions and therapeutic perspectives","volume":"139","author":"Vernieri","year":"2019","journal-title":"Crit. Rev. Oncol. Hematol."},{"key":"10.1016\/j.biochi.2026.08.002_bib40","doi-asserted-by":"crossref","DOI":"10.1016\/j.critrevonc.2025.104624","article-title":"Challenges and prospects in HER2-positive breast cancer-targeted therapy","volume":"207","author":"Li","year":"2025","journal-title":"Crit. Rev. Oncol. Hematol."},{"key":"10.1016\/j.biochi.2026.08.002_bib41","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/s10549-022-06790-2","article-title":"Synthesis and evaluation of naphthalene derivatives as potent STAT3 inhibitors and agents against triple-negative breast cancer growth and metastasis","volume":"197","author":"Yang","year":"2023","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.biochi.2026.08.002_bib42","doi-asserted-by":"crossref","first-page":"1796","DOI":"10.3390\/pharmaceutics15071796","article-title":"Triple negative breast cancer treatment options and limitations: future outlook","volume":"15","author":"Obidiro","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.biochi.2026.08.002_bib43","doi-asserted-by":"crossref","first-page":"1595","DOI":"10.2217\/pgs-2017-0117","article-title":"Triple-negative breast cancer and the potential for targeted therapy","volume":"18","author":"Jhan","year":"2017","journal-title":"Pharmacogenomics"},{"key":"10.1016\/j.biochi.2026.08.002_bib44","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.21873\/anticanres.13230","article-title":"Antibiotic Tetrocarcin-A down-regulates JAM-A, IAPs and induces apoptosis in triple-negative breast cancer models","volume":"39","author":"Vellanki","year":"2019","journal-title":"Anticancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib45","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1080\/13543784.2020.1818067","article-title":"The dawn of targeted therapies for triple negative breast cancer (TNBC): a snapshot of investigational drugs in phase I and II trials","volume":"29","author":"Huynh","year":"2020","journal-title":"Expert Opin. Invest. Drugs"},{"key":"10.1016\/j.biochi.2026.08.002_bib46","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.3390\/diagnostics13111949","article-title":"New biomarkers and treatment advances in triple-negative breast cancer","volume":"13","author":"El Hejjioui","year":"2023","journal-title":"Diagnostics"},{"key":"10.1016\/j.biochi.2026.08.002_bib47","doi-asserted-by":"crossref","DOI":"10.1177\/17588359231183679","article-title":"Antibody-drug conjugates: the evolving field of targeted chemotherapy for breast cancer treatment","volume":"15","author":"Nader-Marta","year":"2023","journal-title":"Ther. Adv. Med. Oncol."},{"key":"10.1016\/j.biochi.2026.08.002_bib48","doi-asserted-by":"crossref","first-page":"221","DOI":"10.32604\/or.2023.028525","article-title":"Targeting triple-negative breast cancer: a clinical perspective","volume":"31","author":"Popovic","year":"2023","journal-title":"Oncol. Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib49","article-title":"Targeted therapeutic strategies for triple-negative breast cancer","volume":"11","author":"Li","year":"2021","journal-title":"Front. Oncol."},{"key":"10.1016\/j.biochi.2026.08.002_bib50","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2018961118","article-title":"Targeting the tetraspanin CD81 reduces cancer invasion and metastasis","volume":"118","author":"Vences-Catal\u00e1n","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2026.08.002_bib51","doi-asserted-by":"crossref","first-page":"6569","DOI":"10.1038\/onc.2010.386","article-title":"miR-145-dependent targeting of junctional adhesion molecule A and modulation of fascin expression are associated with reduced breast cancer cell motility and invasiveness","volume":"29","author":"G\u00f6tte","year":"2010","journal-title":"Oncogene"},{"key":"10.1016\/j.biochi.2026.08.002_bib52","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/ijc.27772","article-title":"A novel role for junctional adhesion molecule-A in tumor proliferation: modulation by an anti-JAM-A monoclonal antibody","volume":"132","author":"Goetsch","year":"2013","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.biochi.2026.08.002_bib53","first-page":"184","article-title":"Paradigms lost-an emerging role for over-expression of tight junction adhesion proteins in cancer pathogenesis","volume":"3","author":"Leech","year":"2015","journal-title":"Ann. Transl. Med."},{"key":"10.1016\/j.biochi.2026.08.002_bib54","article-title":"Generation and characterization of mAb 61H9 against junctional adhesion molecule-a with potent antitumor activity","volume":"12","author":"Liu","year":"2024","journal-title":"PeerJ"},{"key":"10.1016\/j.biochi.2026.08.002_bib55","doi-asserted-by":"crossref","first-page":"5135","DOI":"10.7150\/jca.47470","article-title":"Antibiotics for cancer treatment: a double-edged sword","volume":"11","author":"Gao","year":"2020","journal-title":"J. Cancer"},{"key":"10.1016\/j.biochi.2026.08.002_bib56","doi-asserted-by":"crossref","first-page":"244","DOI":"10.7164\/antibiotics.33.244","article-title":"A new antibiotic, antlermicin a","volume":"33","author":"Kobinata","year":"1980","journal-title":"J. Antibiot."},{"key":"10.1016\/j.biochi.2026.08.002_bib57","doi-asserted-by":"crossref","first-page":"232","DOI":"10.3390\/md17040232","article-title":"Marine spirotetronates: biosynthetic edifices that inspire drug discovery","volume":"17","author":"Braddock","year":"2019","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.biochi.2026.08.002_bib58","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1271\/bbb1961.47.59","article-title":"Mechanism of action of tetrocarcin A","volume":"47","author":"Tamaoki","year":"1983","journal-title":"Agric. Biol. Chem."},{"key":"10.1016\/j.biochi.2026.08.002_bib59","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1021\/np500757w","article-title":"Spirotetronate polyketides as leads in drug discovery","volume":"78","author":"Lacoske","year":"2015","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.biochi.2026.08.002_bib60","first-page":"1229","article-title":"Tetrocarcin A inhibits mitochondrial functions of Bcl-2 and suppresses its anti-apoptotic activity","volume":"60","author":"Nakashima","year":"2000","journal-title":"Cancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib61","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.canlet.2018.09.032","article-title":"Natural compound Tetrocarcin-A downregulates Junctional Adhesion Molecule-A in conjunction with HER2 and inhibitor of apoptosis proteins and inhibits tumor cell growth","volume":"440\u2013441","author":"Vellanki","year":"2019","journal-title":"Cancer Lett."},{"key":"10.1016\/j.biochi.2026.08.002_bib62","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1096\/fj.02-0020fje","article-title":"Stressful death of T-ALL tumor cells after treatment with the anti-tumor agent Tetrocarcin-A","volume":"16","author":"Tinhofer","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.biochi.2026.08.002_bib63","doi-asserted-by":"crossref","first-page":"4561","DOI":"10.1182\/blood-2002-08-2501","article-title":"Tetrocarcin-A-induced ER stress mediates apoptosis in B-CLL cells via a Bcl-2-independent pathway","volume":"101","author":"Anether","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2026.08.002_bib64","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.bbrc.2007.02.136","article-title":"Apoptosis and inactivation of the PI3-kinase pathway by tetrocarcin A in breast cancers","volume":"356","author":"Nakajima","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2026.08.002_bib65","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1002\/bip.22503","article-title":"Development of new antiatherosclerotic and antithrombotic drugs utilizing F11 receptor (F11R\/JAM-A) peptides","volume":"102","author":"Babinska","year":"2014","journal-title":"Biopolymers"},{"key":"10.1016\/j.biochi.2026.08.002_bib66","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1055\/s-0037-1613070","article-title":"Two regions of the human platelet F11-receptor (F11R) are critical for platelet aggregation, potentiation and adhesion","volume":"87","author":"Babinska","year":"2002","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.biochi.2026.08.002_bib80","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.biochi.2026.08.002_bib67","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.atherosclerosis.2019.02.014","article-title":"A peptide antagonist of F11R\/JAM-A reduces plaque formation and prolongs survival in an animal model of atherosclerosis","volume":"284","author":"Babinska","year":"2019","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.biochi.2026.08.002_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.dib.2020.105516","article-title":"In vivo data: treatment with the F11R\/JAM-A peptide 4D decreases mortality and reduces the generation of atherosclerotic plaques in ApoE-deficient mice","volume":"30","author":"Babinska","year":"2020","journal-title":"Data Brief"},{"key":"10.1016\/j.biochi.2026.08.002_bib69","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/s10549-019-05471-x","article-title":"Functional inhibition of F11 receptor (F11R\/junctional adhesion molecule-A\/JAM-A) activity by a F11R-derived peptide in breast cancer and its microenvironment","volume":"179","author":"Bednarek","year":"2020","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.biochi.2026.08.002_bib70","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1186\/bcr2889","article-title":"Choosing the right cell line for breast cancer research","volume":"13","author":"Holliday","year":"2011","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.biochi.2026.08.002_bib71","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1186\/1471-2407-8-228","article-title":"Imagable 4T1 model for the study of late stage breast cancer","volume":"8","author":"Tao","year":"2008","journal-title":"BMC Cancer"},{"key":"10.1016\/j.biochi.2026.08.002_bib72","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1186\/s12935-023-03023-4","article-title":"Triple negative breast cancer metastasis is hindered by a peptide antagonist of F11R\/JAM-A protein","volume":"23","author":"Bednarek","year":"2023","journal-title":"Cancer Cell Int."},{"key":"10.1016\/j.biochi.2026.08.002_bib73","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.3390\/cancers14051303","article-title":"Functional antagonism of Junctional Adhesion Molecule-A (JAM-A), Overexpressed in Breast Ductal Carcinoma In Situ (DCIS), reduces HER2-Positive tumor progression","volume":"14","author":"Smith","year":"2022","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.biochi.2026.08.002_bib74","doi-asserted-by":"crossref","DOI":"10.1111\/ejh.70225","article-title":"Junctional Adhesion Molecule-A (JAM-A) associates with high-risk disease in multiple myeloma patients and a structure-based rationally-designed peptide inhibitor attenuates tumorigenic features in vitro and in vivo","author":"McAuley","year":"2026","journal-title":"Eur. J. Haematol."},{"key":"10.1016\/j.biochi.2026.08.002_bib75","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1182\/blood-2008-04-152330","article-title":"Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases","volume":"113","author":"Koenen","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.biochi.2026.08.002_bib76","doi-asserted-by":"crossref","first-page":"8896","DOI":"10.1002\/anie.201412070","article-title":"Structure-based design of inhibitors of protein-protein interactions: mimicking peptide binding epitopes","volume":"54","author":"Pelay-Gimeno","year":"2015","journal-title":"Angew Chem. Int. Ed. Engl."},{"key":"10.1016\/j.biochi.2026.08.002_bib77","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.tibtech.2014.02.003","article-title":"Chemically programmed antibodies","volume":"32","author":"Rader","year":"2014","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.biochi.2026.08.002_bib78","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1111\/j.1476-5381.2010.01127.x","article-title":"Principles of early drug discovery","volume":"162","author":"Hughes","year":"2011","journal-title":"Br. J. Pharmacol."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908426001781?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908426001781?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T15:39:09Z","timestamp":1789054749000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908426001781"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":78,"alternative-id":["S0300908426001781"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2026.08.002","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"F11 Receptor\/Junctional Adhesion Molecule-A: a novel therapeutic target in breast cancer","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2026.08.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}