{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:32:34Z","timestamp":1786977154684,"version":"build-2736575974"},"reference-count":27,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,7,19]],"date-time":"2014-07-19T00:00:00Z","timestamp":1405728000000},"content-version":"vor","delay-in-days":18,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100009740","name":"SUNY Downstate Medical Center","doi-asserted-by":"crossref","award":["921372"],"award-info":[{"award-number":["921372"]}],"id":[{"id":"10.13039\/100009740","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2014,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Peptides with enhanced resistance to proteolysis, based on the amino acid sequence of the F11 receptor molecule (F11R, aka JAM\u2010A\/Junctional adhesion molecule\u2010A), were designed, prepared, and examined as potential candidates for the development of anti\u2010atherosclerotic and anti\u2010thrombotic therapeutic drugs. A sequence at the N\u2010terminal of F11R together with another sequence located in the first Ig\u2010loop of this protein, were identified to form a steric active\u2010site operating in the F11R\u2010dependent adhesion between cells that express F11R molecules on their external surface. In silico modeling of the complex between two polypeptide chains with the sequences positioned in the active\u2010site was used to generate peptide\u2010candidates designed to inhibit homophilic interactions between surface\u2010located F11R molecules. The two lead F11R peptides were modified with D\u2010Arg and D\u2010Lys at selective sites, for attaining higher stability to proteolysis in vivo. Using molecular docking experiments we tested different conformational states and the putative binding affinity between two selected D\u2010Arg and D\u2010Lys\u2010modified F11R peptides and the proposed binding pocket. The inhibitory effects of the F11R peptide\n                    <jats:bold>\n                      <jats:sub>2<\/jats:sub>\n                      HN\u2010(dK)\u2010SVT\u2010(dR)\u2010EDTGTYTC\u2010CONH\n                      <jats:sub>2<\/jats:sub>\n                    <\/jats:bold>\n                    on antibody\u2010induced platelet aggregation and on the adhesion of platelets to cytokine\u2010inflammed endothelial cells are reported in detail, and the results point out the significant potential utilization of F11R peptides for the prevention and treatment of atherosclerotic plaques and associated thrombotic events. \u00a9 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 322\u2013334, 2014.\n                  <\/jats:p>","DOI":"10.1002\/bip.22503","type":"journal-article","created":{"date-parts":[[2014,5,7]],"date-time":"2014-05-07T05:24:51Z","timestamp":1399440291000},"page":"322-334","source":"Crossref","is-referenced-by-count":13,"title":["Development of new antiatherosclerotic and antithrombotic drugs utilizing F11 receptor (F11R\/JAM\u2010A) peptides"],"prefix":"10.1002","volume":"102","author":[{"given":"A.","family":"Babinska","sequence":"first","affiliation":[{"name":"Division of Nephrology, Department of Medicine State University of New York, Downstate Medical Center Brooklyn NY 11203"},{"name":"Department of Cell Biology and Medicine State University of New York, Downstate Medical Center Brooklyn NY 11203"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. C.","family":"Clement","sequence":"additional","affiliation":[{"name":"Department of Chemistry Lehman College of the City University of New York Bronx  NY 10468"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M.","family":"Swiatkowska","sequence":"additional","affiliation":[{"name":"Department of Molecular and Medical Biophysics Medical University of Lodz 92\u2010215 Lodz Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J.","family":"Szymanski","sequence":"additional","affiliation":[{"name":"Department of Molecular and Medical Biophysics Medical University of Lodz 92\u2010215 Lodz Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Shon","sequence":"additional","affiliation":[{"name":"Division of Nephrology, Department of Medicine State University of New York, Downstate Medical Center Brooklyn NY 11203"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y. H.","family":"Ehrlich","sequence":"additional","affiliation":[{"name":"Program in Neuroscience College of Staten Island of the City University of New York Staten Island NY 10314"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E.","family":"Kornecki","sequence":"additional","affiliation":[{"name":"Division of Nephrology, Department of Medicine State University of New York, Downstate Medical Center Brooklyn NY 11203"},{"name":"Department of Cell Biology and Medicine State University of New York, Downstate Medical Center Brooklyn NY 11203"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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