<HashMap><database>BioModels</database><scores/><additional><submitter>Quentin Thommen</submitter><curationStatus>Non-curated</curationStatus><modellingApproach>differential equation model</modellingApproach><levelVersion>L3V2</levelVersion><full_dataset_link>https://www.ebi.ac.uk/biomodels/MODEL2608180005</full_dataset_link><isPrivate>false</isPrivate><repository>BioModels</repository><modelFormat>SBML</modelFormat><omics_type>Models</omics_type><tokenised_name>Stress priming and thermotolerance model   Pfeuty et al. 2021</tokenised_name><publication_year>2021</publication_year><submissionId>MODEL2608180005</submissionId><publication_authors>Benjamin Pfeuty, Emmanuel Courtade, Thommen Q</publication_authors><first_author>Benjamin Pfeuty</first_author><publication>10.1088/1478-3975/ac02a8,
                            A common signature of cell adaptation to stress is the improved resistance upon priming by prior stress exposure. In the context of hyperthermia, priming or preconditioning with sublethal heat shock can be a useful tool to confer thermotolerance and competitive advantage to cells. In the present study, we develop a data-driven modeling framework that is simple and generic enough to capture a broad set of adaptation behaviors to heat stress at both molecular and cellular levels. The model recovers the main features of thermotolerance and clarifies the tradeoff principles which maximize the thermotolerance effect. It therefore provides an effective predictive tool to design preconditioning and fractionation hyperthermia protocols for therapeutic purpose.. 4, 18.
                            Univ. Lille, CNRS, UMR 8523-PhLAM-Physique des Lasers Atomes et Molécules, F-59000 Lille, France.</publication><submitter_mail>quentin.thommen@univ-lille.fr</submitter_mail><publication_doi>10.1088/1478-3975/ac02a8</publication_doi><submitter_affiliation>Univ. Lille</submitter_affiliation></additional><is_claimable>false</is_claimable><name>Stress priming and thermotolerance model - Pfeuty et al. 2021</name><description>The model describes cellular adaptation to proteotoxic stress through four dynamical variables: protein damage, cell survival, molecular chaperone mRNA and molecular chaperone protein. Heat increases the production of misfolded proteins, which are either degraded or repaired by chaperones. Accumulated damage decreases cell survival and also activates chaperone transcription through a negative-feedback mechanism representing HSF1-mediated regulation. The induced increase in chaperone abundance during a first sublethal heat shock can protect cells against a subsequent stress, thereby reproducing thermotolerance and allowing the effects of priming temperature, duration and recovery time to be explored.</description><dates><last_modification>2026-08-18</last_modification><publication>2026-09-02</publication><submission>2026-08-18</submission></dates><accession>MODEL2608180005</accession><cross_references><doi>10.1088/1478-3975/ac02a8</doi></cross_references></HashMap>