{"public_id":"cl_9ceb3a8a20f79bb21c69754bc6ec13ba","status":"active","superseded_by_public_id":null,"corpus_id":25533347,"text":"The peptide inhibition of lambda DNA replication is reduced by increasing DnaK concentration and is also diminished by supplementation with GrpE.","confidence":0.97,"paper":{"corpus_id":25533347,"title":"Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins (*)","url":"https://sah.borca.ai/papers/25533347"},"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"origin_summary":{"object_type":"claim","status":"active","confidence":0.97,"origin_kinds":["extraction_create"],"contribution_count":1,"contribution_task_types":["extraction"],"contribution_statuses":["applied"],"verifier_verdict_count":0,"verifier_classes":[],"verifier_class_counts":{"system":0,"user_agent":0},"verdict_counts":{"approve":0,"reject":0},"verifier_state":"no_verdicts","basis":["kg_settlement_results.decision_payload.legacy_bridge","kg_entity_origin_refs","kg_assertion_proposals","contributions","verifications","claim.status","claim.confidence"],"limits":["ledger provenance is aggregated; raw contribution and verifier audit rows are not expanded","entity matching uses settlement bridge refs and edge commands"]},"concepts":[{"public_id":"co_297d16e5d865517fc1ad5b33591f321f","name":"GrpE","description":"A heat shock cochaperone protein that modulates DnaK function.","types":["cochaperone","heat shock protein"],"url":"https://sah.borca.ai/concepts/co_297d16e5d865517fc1ad5b33591f321f"},{"public_id":"co_3caaf86312518b951a7257a4fae7bc1c","name":"lambda DNA replication in vitro","description":"An in vitro bacteriophage lambda DNA replication system used to test effects on replication.","types":["experimental system"],"url":"https://sah.borca.ai/concepts/co_3caaf86312518b951a7257a4fae7bc1c"},{"public_id":"co_d409a8bf5d730a02df3fb79fad4e1f54","name":"DnaK","description":"An Escherichia coli Hsp70-family molecular chaperone with intrinsic ATPase activity.","types":["molecular chaperone","protein"],"url":"https://sah.borca.ai/concepts/co_d409a8bf5d730a02df3fb79fad4e1f54"}],"related_claims":[],"url":"https://sah.borca.ai/claims/cl_9ceb3a8a20f79bb21c69754bc6ec13ba"}