{"public_id":"co_0258c87044dd089828fa5d0fe370f869","status":"active","merged_into_public_id":null,"resolved_public_id":"co_0258c87044dd089828fa5d0fe370f869","name":"phosphophoryn","description":"A highly acidic dentin matrix phosphoprotein implicated in mineralization.","aliases":["PP"],"types":["protein"],"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"origin_summary":{"object_type":"concept","status":"active","confidence":null,"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","concept.status"],"limits":["ledger provenance is aggregated; raw contribution and verifier audit rows are not expanded","entity matching uses settlement bridge refs and edge commands"]},"papers":[{"corpus_id":25359104,"title":"Phosphorylation of Phosphophoryn Is Crucial for Its Function as a Mediator of Biomineralization*","citation_count":168,"url":"https://sah.borca.ai/papers/25359104"}],"claims":[{"public_id":"cl_00d5b917fb02b6a8ada3c955fce4e13b","text":"Phosphophoryn nucleates plate-like apatite crystals in pseudophysiological buffer, but recombinant DMP2 fails to mediate amorphous calcium phosphate transformation to apatite under the same conditions.","corpus_id":25359104,"url":"https://sah.borca.ai/claims/cl_00d5b917fb02b6a8ada3c955fce4e13b"},{"public_id":"cl_56e709075161954104005bc5bd592315","text":"Phosphophoryn promotes collagen aggregate formation, whereas recombinant DMP2 leads to thin fibril formation.","corpus_id":25359104,"url":"https://sah.borca.ai/claims/cl_56e709075161954104005bc5bd592315"},{"public_id":"cl_6d01e28ff4481a219e4dd037282abe51","text":"Phosphate moieties in phosphophoryn are important for its function as a mediator of dentin biomineralization.","corpus_id":25359104,"url":"https://sah.borca.ai/claims/cl_6d01e28ff4481a219e4dd037282abe51"},{"public_id":"cl_ce1ca56fb5145a8f5bcd14b40f42edfe","text":"Phosphophoryn folds into a compact globular structure upon calcium binding, whereas recombinant DMP2 remains unfolded.","corpus_id":25359104,"url":"https://sah.borca.ai/claims/cl_ce1ca56fb5145a8f5bcd14b40f42edfe"}],"related_concepts":[],"resolved_url":"https://sah.borca.ai/concepts/co_0258c87044dd089828fa5d0fe370f869","url":"https://sah.borca.ai/concepts/co_0258c87044dd089828fa5d0fe370f869"}