<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(2)</volume><submitter>Li Z</submitter><pubmed_abstract>Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as OX40, plays a crucial role in the regulation of T-cell immune responses under normal physiological conditions. Abnormal expression of OX40 and its cognate ligand OX40L (TNFSF4) have been associated with various autoimmune diseases, indicating that blocking the OX40/OX40L pathway could be a promising strategy for the treatment of a broad range of T cell-mediated autoimmune diseases. Here, we screened and characterized a fully human anti-OX40 antibody (JY007) from a naïve human scFv phage library. JY007 has an affinity constant of 7.71 nmol/L and effectively inhibited the OX40-OX40L interaction at both molecular and cellular levels, with IC&lt;sub>50&lt;/sub> values of 1.088 and 10.12 nmol/L, respectively. Furthermore, JY</pubmed_abstract><journal>Marine life science &amp; technology</journal><pagination>328-339</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12102438</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>A novel anti-OX40 human monoclonal antibody that blocks OX40/OX40L signaling and depletes OX40&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; T cells.</pubmed_title><pmcid>PMC12102438</pmcid><pubmed_authors>Li Z</pubmed_authors><pubmed_authors>Liu L</pubmed_authors><pubmed_authors>Iqbal MO</pubmed_authors><pubmed_authors>Chen J</pubmed_authors><pubmed_authors>Gu Y</pubmed_authors><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Chen X</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Zhang B</pubmed_authors><pubmed_authors>Wu X</pubmed_authors></additional><is_claimable>false</is_claimable><name>A novel anti-OX40 human monoclonal antibody that blocks OX40/OX40L signaling and depletes OX40&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; T cells.</name><description>Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as OX40, plays a crucial role in the regulation of T-cell immune responses under normal physiological conditions. Abnormal expression of OX40 and its cognate ligand OX40L (TNFSF4) have been associated with various autoimmune diseases, indicating that blocking the OX40/OX40L pathway could be a promising strategy for the treatment of a broad range of T cell-mediated autoimmune diseases. Here, we screened and characterized a fully human anti-OX40 antibody (JY007) from a naïve human scFv phage library. JY007 has an affinity constant of 7.71 nmol/L and effectively inhibited the OX40-OX40L interaction at both molecular and cellular levels, with IC&lt;sub>50&lt;/sub> values of 1.088 and 10.12 nmol/L, respectively. Furthermore, JY</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 May</publication><modification>2026-06-01T11:36:50.151Z</modification><creation>2026-04-08T11:56:52.956Z</creation></dates><accession>S-EPMC12102438</accession><cross_references><pubmed>40417257</pubmed><doi>10.1007/s42995-025-00284-y</doi></cross_references></HashMap>