<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang C</submitter><funding>The Open Foundation of Key Laboratory of Taihu Basin Water Resources Management, Ministry of Water Resources</funding><funding>National Natural Science Foundation of China</funding><pagination>499</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12899096</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(3)</volume><pubmed_abstract>Thermophilic cyanobacteria are key models for thermotolerance and a promising source of thermophilic bioresources. Yet the subcellular basis of their stress resilience remains poorly resolved. Here, we focus on intracellular polyphosphate (polyP)-rich granules, termed "stabilisomes," which have been implicated in stress adaptation. The lack of a high-purity, structure-preserving isolation method has been a major technical bottleneck hindering the elucidation of this resilience mechanism. This study describes a robust, structure-preserving purification strategy, boosting the granule-to-protein yield by over 10,000-fold compared with conventional methods. The specificity and structural integrity of this method are supported by the specific enrichment of complex proteomic (937 proteins) and m</pubmed_abstract><journal>Plants (Basel, Switzerland)</journal><pubmed_title>High-Purity Isolation of Polyphosphate-Rich Stabilisomes Defines Their Conserved Chemical Architecture in Thermophilic Cyanobacteria.</pubmed_title><pmcid>PMC12899096</pmcid><funding_grant_id>Yk922001-C2</funding_grant_id><funding_grant_id>42307172</funding_grant_id><funding_grant_id>41871082</funding_grant_id><pubmed_authors>Wang M</pubmed_authors><pubmed_authors>Yang L</pubmed_authors><pubmed_authors>Wang C</pubmed_authors><pubmed_authors>Zhou C</pubmed_authors><pubmed_authors>Song X</pubmed_authors><pubmed_authors>Yin J</pubmed_authors></additional><is_claimable>false</is_claimable><name>High-Purity Isolation of Polyphosphate-Rich Stabilisomes Defines Their Conserved Chemical Architecture in Thermophilic Cyanobacteria.</name><description>Thermophilic cyanobacteria are key models for thermotolerance and a promising source of thermophilic bioresources. Yet the subcellular basis of their stress resilience remains poorly resolved. Here, we focus on intracellular polyphosphate (polyP)-rich granules, termed "stabilisomes," which have been implicated in stress adaptation. The lack of a high-purity, structure-preserving isolation method has been a major technical bottleneck hindering the elucidation of this resilience mechanism. This study describes a robust, structure-preserving purification strategy, boosting the granule-to-protein yield by over 10,000-fold compared with conventional methods. The specificity and structural integrity of this method are supported by the specific enrichment of complex proteomic (937 proteins) and m</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Feb</publication><modification>2026-07-06T03:22:26.84Z</modification><creation>2026-07-06T03:11:12.815Z</creation></dates><accession>S-EPMC12899096</accession><cross_references><pubmed>41681662</pubmed><doi>10.3390/plants15030499</doi></cross_references></HashMap>