This guide separates the biological evidence from the material actually accessed. A native publication cache may contain only an abstract even when selected original sections were read elsewhere. The table below records the actual native cache and the scoped original reading separately. Genuine acquisition refreshed the target UniProt and GOA files without reseeding the inherited review. Forty existing normal sources remain byte-identical; 23 previously absent sources were fetched with native functions.
PMID:24971490(https://pubmed.ncbi.nlm.nih.gov/24971490/) supports human FXN-assisted sulfur transfer and initial [2Fe-2S] formation through radiolabel and CD measurements. PMID:38627381(https://doi.org/10.1038/s41467-024-47310-8) connects FXN binding with rearrangement of the ISCU site and faster persulfide transfer; exact constructs delegated to its unrecovered Supplementary Table 3 remain unspecified. PMID:31101807(https://doi.org/10.1038/s41467-019-09989-y) resolves contacts to NFS1/ISCU using human FXN 81-210 and bacterial ACP-containing preparations. BLI measures the assembled complex; the thermal-stability experiment is not an isolated binary affinity assay. PMID:29097656(https://doi.org/10.1038/s41467-017-01497-1) distinguishes human crystallographic components from fungal FXN-containing SAXS assemblies. PMID:29491838(https://pubmed.ncbi.nlm.nih.gov/29491838/) explicitly adds human FXN to a fly core complex and therefore supplies direct target evidence within that mixed-species experiment.
PMID:12785837(https://pubmed.ncbi.nlm.nih.gov/12785837/) reports both ferrous and ferric binding and assembly on ISU; an ISU-bound cluster is not itself proof of an FXN-bound cluster. PMID:29576242(https://pubmed.ncbi.nlm.nih.gov/29576242/) reports condition-dependent ferrous binding and release while leaving ISCU uptake and alternative physiological iron sources unresolved. Its ferric-negative experiment includes five-fold FeCl3, a precipitation check and oxidation of previously bound Fe2+. These directly challenge earlier positive ferric reports; the conflict remains unresolved because the older complete experimental conditions were not recovered. No assay-condition explanation is established. PMID:15123683(https://pubmed.ncbi.nlm.nih.gov/15123683/) positively supports human holoFXN-human FECH association and reconstituted iron delivery. PMID:15641778(https://pubmed.ncbi.nlm.nih.gov/15641778/) supports ferroxidase activity of assembled human protein, separately from the unresolved cellular peroxide-response assertion.
The exact positive HuRI and Haenig partner contexts are retained as yeast-assay evidence. Original supplementary joins identify all ten FXN Haenig partners, but none occurs in the retained mammalian-validation subset. Study-wide validation rates are not assigned to those pairs. PMID:15961414(https://doi.org/10.1093/hmg/ddi214) explicitly reports human frataxin association with human succinate dehydrogenase subunits in its authentic abstract. Current reasons omit fragment ranges, antibody details and host attribution from the earlier contemporaneous reading whose complete successful response was not retained. PMID:26702583(https://pubmed.ncbi.nlm.nih.gov/26702583/) explicitly names FXN among HSPA9-associated proteins in its abstract; inaccessible Methods are not filled in from interaction databases.
Human-cell studies distinguish mitochondrial and contextual cytosolic pools. Processing, mutant targeting, rescue and fractionation experiments do not establish that every tested fragment is a natural splice product. Official UniProt Q16595 declares three products whose 210/171/196-residue sequences were checked against the official FASTAs. The retained HPA location record reports mitochondrial and cytosolic labels for CAB022164 samples; individual images were not independently scored.
All six incoming PAINT nodes were checked on the actual PTHR16821 tree and alignment. Literal IBD donors, including human self-evidence, are preserved. Node validity does not independently resolve inaccessible molecular chemistry. The ISS matrix donor is the separately verified yeast Q07540 record, not an IBA or a newly read donor experiment.
The successful retained complex R-HSA-1362398 page lists human FXN 81-210 and links the complex to UQCRFS1 insertion within complex III assembly. The immutable event summary is also available. Direct event and FXN-component requests returned 404; no successful event HTML, resolved component accession or direct FXN-to-UQCRFS1 transfer assay is claimed. Inclusion in a modeled transfer complex does not by itself assign that chemical step to each subunit.
The inherited source baseline is accepted commit 7d80d6aef16b7ef0246a8833cf3e51a8e262b4dd. The actual native acquisition and source hashes are recorded in FXN-review-evidence.json. External URLs are locators for the read source, not a claim that every full article or supplement was retrieved. The complete private provenance retains exact source pins. Historical unquoted findings and all quotations remain in the original-review archive; current assessments below govern the claims.
| Reference and original locator | Native cache at snapshot | Actual reading and limits |
|---|---|---|
| GO_REF:0000002 | Official method description or inherited provider file; no new native acquisition. | The official InterPro-to-GO method maps curated family/domain/site signatures to GO assertions after sequence matching. It explains FXN’s signature-derived rows; the method page is not itself an experiment establishing every mapped function. The actual IPR017789 biological scope is assessed separately. |
| GO_REF:0000024 | Official method description or inherited provider file; no new native acquisition. | The official method describes curator-judged transfer from experimentally annotated similar proteins, retaining the donor accession and excluding NOT source assertions. It explains the literal Q07540 ISS source. The FXN-specific donor identity and matrix IDA were separately verified; reading the method does not claim a fresh experimental read of that donor paper. |
| GO_REF:0000033 | Official method description or inherited provider file; no new native acquisition. | The authentic official PAINT method describes curated ancestral functions supported by experimental descendants. Independent retained PTHR16821 tree/MSA, AN/PTN lookup and literal IBD data establish all six incoming FXN nodes on the actual 210-residue human lineage, with exact donor sets. Target self-membership is valid experimental grounding. This verifies propagation provenance rather than pairwise similarity; it does not independently resolve inaccessible cluster-binding chemistry. |
| GO_REF:0000043 | Official method description or inherited provider file; no new native acquisition. | The retained official metadata identifies the historical UniProt keyword-to-GO mapping method and explicitly says that a formerly all-species pipeline is now restricted to viruses. Preserve this as historical reference provenance without treating the current restriction as evidence that a past human biological assertion was false. No current FXN assay or keyword-specific function is established by the method description. |
| GO_REF:0000044 | Official method description or inherited provider file; no new native acquisition. | The official method maps the UniProt subcellular-location controlled vocabulary to GO, with different underlying manual and automated annotation routes. This explains the cytosol mapping source, not a newly performed localization experiment. Human FXN fractionation and current HPA metadata provide separate biological support; natural-product specificity is not inferred from the mapping. |
| GO_REF:0000052 | Official method description or inherited provider file; no new native acquisition. | The official HPA method describes antibody-based confocal localization curation and literature-support grading. Its identity is verified. Current FXN metadata and sample labels were separately inspected, but no individual image was independently scored and no isoform specificity is established merely by the method citation. |
| GO_REF:0000107 | Official method description or inherited provider file; no new native acquisition. | The official Ensembl Compara method automatically transfers eligible experimental annotations across qualifying orthology relationships, excluding NOT and generic protein-binding transfer. It explains inherited automated provenance. Reading this method is not an independent audit of every historical donor alignment or assay; each biological assertion still requires its own scope assessment. |
| GO_REF:0000117 | Official method description or inherited provider file; no new native acquisition. | The official ARBA method uses reviewed manual annotations to learn rules, including ontology-based augmentation with broader GO terms, and assigns electronic predictions. It explains the broad homeostasis rules cited by FXN. Method identity does not establish that a particular rule correctly captures FXN’s mechanism or that a predicted process is core. |
| GO_REF:0000120 | Official method description or inherited provider file; no new native acquisition. | The official combined-IEA method merges identical annotations from several electronic pipelines and retains their sources in WITH/FROM. It is a deduplication/provenance method rather than an independent experiment or a count of independent confirmations. Preserve the literal FXN source identifiers and assess the biological scope separately. |
| PMID:12785837(https://pubmed.ncbi.nlm.nih.gov/12785837/); original locator | Existing source preserved; full_text_available: false. | Authentic abstract verifies the reported positive ferrous/ferric binding, iron donation and [2Fe-2S] assembly measurements. The ferric-specific finding conflicts with controlled negative human NMR evidence in PMID:29576242 and is recorded as DISPUTED below; the full older experiment was inaccessible. The separate FXN-bound cluster and autoprocessing claims remain unverified. Neither the identifier nor all findings are rejected. |
| PMID:15123683(https://pubmed.ncbi.nlm.nih.gov/15123683/); original locator | Existing source preserved; full_text_available: false. | The original abstract explicitly identifies human holofrataxin-human ferrochelatase association, iron transfer and heme formation. Full Methods, exact constructs and binding conditions were not recovered. The positive reconstituted capability supports bounded binding and iron-delivery annotations but does not establish an obligatory physiological iron-donor mechanism. |
| PMID:15509595(https://pubmed.ncbi.nlm.nih.gov/15509595/); original locator | Existing source preserved; full_text_available: false. | Human HeLa RNA-interference experiments directly address FXN-dependent Fe-S client maturation. Enzyme specificity, IRP1 readouts and reversibility support the maturation role; this is not evidence that FXN must cleave itself. The early depletion interval did not produce every expected iron phenotype, which limits universal physiological claims. Access: Selected indexed original Results and Methods, beyond the abstract-only normal cache. |
| PMID:15581888(https://pubmed.ncbi.nlm.nih.gov/15581888/); original locator | Genuinely fetched; full_text_available: false. | The abstract explicitly includes human-heart mitochondrial fractions alongside recombinant frataxin assembly experiments. It supports the basic localization context, but detailed fraction purity and physiological oligomer stoichiometry were not independently checked. No full-text access or native fixed oligomer claim is made. Access: Authentic official abstract; article page offers requested full text rather than recovered original. |
| PMID:15641778(https://pubmed.ncbi.nlm.nih.gov/15641778/); original locator | Existing source preserved; full_text_available: false. | The intended original abstract directly supports ferroxidase activity and radical protection of assembled recombinant human frataxin, with monomeric material distinguished. Exact constructs and complete Methods were unavailable. The separate cellular response-to-hydrogen-peroxide annotation cannot be verified from that biochemical abstract and remains UNDECIDED; this does not reject the positive assembled-protein activity or claim that the full paper lacks a cellular assay. |
| PMID:15961414(https://pubmed.ncbi.nlm.nih.gov/15961414/); original locator; original locator | Existing source preserved; full_text_available: false. | The authentic abstract explicitly supports association of human frataxin with human succinate dehydrogenase subunits. The earlier indexed author-page reading was contemporaneous, but its successful full response body was not retained. Current claims therefore use only the retrievable abstract and original partner provenance, without fragment ranges, antibody details, host attribution or isolated binary affinity. The saved 403 response is excluded. Citation identity and the bounded association are verified; detailed full-text assays are not independently reproducible from the retained material. |
| PMID:16091420(https://pubmed.ncbi.nlm.nih.gov/16091420/); original locator | Genuinely fetched; full_text_available: false. | Endogenous human Caco-2 cells retain mitochondrial FXN and gain an additional cytosolic pool during differentiation. Fractionation and confocal observations are supported by mitochondrial-marker controls. Cytosolic IscU1 co-immunoprecipitation is an association assay, not proof of purified binary affinity or a current splice-product assignment. Access: Selected indexed original Methods and Results with figure captions; no figure-pixel or supplement inspection. |
| PMID:16608849(https://pubmed.ncbi.nlm.nih.gov/16608849/); original locator | Existing source preserved; full_text_available: false. | Human patient lymphoblast and cell-line experiments support conditional survival and cytochrome-c release phenotypes and nonexclusive FXN localization. Full-length and engineered targeting-deficient constructs are distinct; the tested protection is not universal across stimuli. No current natural isoform or measured export mechanism is inferred. Access: Selected indexed original Methods, Results, Discussion and captions; normal cache is abstract-only. |
| PMID:17285345(https://pubmed.ncbi.nlm.nih.gov/17285345/); original locator | Existing source preserved; full_text_available: false. | The original abstract reports human 56-210 iron binding and iron-associated self-cleavage, with altered acidic-surface accessibility and ISU association. This is a processed-fragment experiment, not a declared natural splice product. The source supplies background mitochondrial context rather than a direct localization experiment in the accessed material; its proposed physiological cleavage significance remains a hypothesis. |
| PMID:17468497(https://pubmed.ncbi.nlm.nih.gov/17468497/); original locator | Existing source preserved; full_text_available: false. | Human-cell processing experiments, fractionation and N-terminal sequencing support mature 81–210 FXN and its mitochondrial/cytosolic distribution. Engineered cleavage-site mutants and separately expressed fragments are not interchangeable with currently declared natural splice products. The selected experiments do not independently establish mitochondrial export. Access: Selected indexed original Results, Discussion and Methods; normal cache is abstract-only. |
| PMID:18160053(https://pubmed.ncbi.nlm.nih.gov/18160053/); original locator | Existing source preserved; full_text_available: false. | The abstract directly concerns FXN-silenced human HeLa cells and rescue by mitochondrial ferritin, with iron distribution and Fe-S/oxidative endpoints. It supports a physiological iron-homeostasis context without isolating a dedicated FXN homeostatic mechanism. Full Methods and detailed rescue controls were not recovered. Access: Authentic official and immutable-cache abstract; attempted HAL full-text route returned an access challenge. |
| PMID:18424449(https://pubmed.ncbi.nlm.nih.gov/18424449/); original locator | Existing source preserved; full_text_available: true. | Human HEK293 and patient-derived cellular experiments test iron-dependent FXN expression and precursor/intermediate/mature protein behavior. DFO-sensitive expression satisfies the broad response-to-iron definition without demonstrating autonomous FXN iron sensing. Reporter and protein-stability experiments are kept distinct. Access: Selected full original text from immutable main cache. |
| PMID:18537827(https://pubmed.ncbi.nlm.nih.gov/18537827/) | Existing source preserved; full_text_available: false. | Authentic abstract supports altered mutant stability, aggregation and iron-binding behavior, but ferric-specific full assay conditions were not accessible. This IDA specificity remains unresolved in light of conflicting human ferric-binding studies; positive mutant folding observations are retained. |
| PMID:18725397(https://pubmed.ncbi.nlm.nih.gov/18725397/); original locator | Genuinely fetched; full_text_available: false. | The abstract explicitly covers human FXN mitochondrial processing and mature-form rescue experiments. It supports the basic mitochondrial location; detailed fractionation and host/construct conditions were not fully reassessed. An exclusivity statement is not generalized over other directly measured human-cell cytosolic pools. Access: Authentic official abstract; indexed article page did not provide the original full text. |
| PMID:20053667(https://pubmed.ncbi.nlm.nih.gov/20053667/); original locator | Existing source preserved; full_text_available: false. | Human HEK293 and patient-cell experiments distinguish mature mitochondrial and cytosolic FXN. Co-immunoprecipitation and aconitase rescue support association and functional activation, respectively. Full-length versus engineered cytosolic constructs are explicit; the proposed Fe-S repair and mitochondrial export mechanisms were not directly demonstrated. Access: Selected indexed original Results, Discussion and Methods, beyond the abstract-only cache. |
| PMID:21298097(https://pubmed.ncbi.nlm.nih.gov/21298097/); original locator | Existing source preserved; full_text_available: true. | Human FXN complex experiments in HeLa mitochondrial material and human-construct rescue in mouse fibroblasts support mitochondrial assembly function. Bacterial coexpression uses specified mammalian components and does not establish direct binary interaction for every pair or one universal native stoichiometry. Human-protein experiments are not mislabeled as mouse-only evidence. Access: Selected full original Results, Discussion and Methods from immutable main cache. |
| PMID:24971490(https://pubmed.ncbi.nlm.nih.gov/24971490/) | Existing source preserved; full_text_available: true. | Original Europe PMC XML identity and selected Methods plus Results sections were read. Human protein reconstitution, sulfur radiolabel tracking and CD experiments support FXN activation of sulfur transfer and [2Fe-2S] assembly. The paper distinguishes bound cluster signal from iron/sulfide solution chemistry. Figure captions were read; full supplementary and image inspection was not performed. |
| PMID:26702583(https://pubmed.ncbi.nlm.nih.gov/26702583/); original locator | Existing source preserved; full_text_available: false. | The authentic abstract explicitly identifies frataxin among proteins interacting with and stabilized by HSPA9. It distinguishes disease-variant effects but does not supply the detailed assay, constructs or comparison controls. Full text remained inaccessible; the positive target-specific statement supports bounded association only. |
| PMID:27519411(https://pubmed.ncbi.nlm.nih.gov/27519411/); original locator | Existing source preserved; full_text_available: false. | The abstract describes a recombinant human FXN42–210/NFS1/ISD11/ISCU architecture assembled in bacteria. It informs the mitochondrial assembly context but does not directly measure endogenous cellular localization or prove a fixed native 24-mer. The basic NAS mitochondrial assertion has independent human-cell support. Access: Authentic immutable-cache abstract only; no full Methods or figure inspection claimed. |
| PMID:28634302(https://pubmed.ncbi.nlm.nih.gov/28634302/) | Existing source preserved; full_text_available: false. | Original cached PubMed abstract identifies the NFS1/ISD11/ACP architecture and the rationale for FXN activation. Selected indexed original discussion corroborates that mechanistic framing. Europe PMC full-text retrieval failed, PMC returned a browser challenge, and an HTTP200 NCBI response was HTML rather than article XML. Therefore no full-text kinetic-table or construct verification is claimed. |
| PMID:29097656(https://pubmed.ncbi.nlm.nih.gov/29097656/); original locator | Existing source preserved; full_text_available: true. | Original XML selected Results and Methods distinguish human NFS1/ISD11/ISCU crystallography with co-purified bacterial ACP from Chaetomium thermophilum FXN-containing SAXS assemblies. The crystallographic ISCU M107I construct is engineered. Retain the core-complex evidence without calling the fungal SAXS arrangement an all-human structure. |
| PMID:29491838(https://pubmed.ncbi.nlm.nih.gov/29491838/) | Existing source preserved; full_text_available: true. | Original XML section on the Drosophila Nfs1/Isd11/IscU/frataxin complex and Figure3 explicitly report HUMAN FXN added to purified fly components, with larger complexes and enhanced sulfide production. Thus the target is experimentally assayed despite the Drosophila-focused title. Its localization discussion is distinct from a direct human cell-localization experiment. |
| PMID:29576242(https://pubmed.ncbi.nlm.nih.gov/29576242/) | Existing source preserved; full_text_available: true. | Selected retained original Results1.1-1.6, Discussion and Methods3.1 were read, and Results1.3 re-read for the conflict. Human FXN81-210 bound Fe2+ but not Fe3+ in NMR; a five-fold FeCl3 challenge, no observed precipitation, and loss of the iron-bound spectral response after oxidation directly challenge earlier ferric-binding claims. The cited XAS corroboration is described as yeast in this source, not independently verified human replication here. The physiological iron donor and separate [4Fe-4S] experiment remain unresolved. |
| PMID:31101807(https://pubmed.ncbi.nlm.nih.gov/31101807/); original locator | Existing source preserved; full_text_available: true. | Selected original structural Results and expression/BLI/thermal-stability Methods were read. Human FXN81–210 contacts NFS1 and ISCU in a complex containing bacterial ACP. BLI measures the assembled complex. Table 1 thermal measurements are differential scanning fluorimetry of FXN variants, so the retained IntAct calorimetry label must not be presented as an isolated binary affinity assay. |
| PMID:32296183(https://pubmed.ncbi.nlm.nih.gov/32296183/) | Existing source preserved; full_text_available: true. | Original HuRI Methods were reused with exact official FXN partner/publication joins. A6NEM1 and DAPP1 contacts are positive yeast two-hybrid records with the retained construct features. Study-wide orthogonal-validation statistics do not demonstrate mammalian validation of these particular pairs; no physiological or natural-product-specific inference is made. |
| PMID:32814053(https://pubmed.ncbi.nlm.nih.gov/32814053/) | Existing source preserved; full_text_available: false. | Original Methods and exact Table S1/S2/S4 workbooks were read and joined. All ten FXN partners occur in NN1.0 and NN1.0ext; the FXN clone entry is CCSB_10735. None of these FXN pairs occurs in the retained Table S4 mammalian-validation sample. Preserve the positive yeast assay evidence, partner suffixes and tested fragments without inventing endogenous or pathway functions. |
| PMID:34800366(https://pubmed.ncbi.nlm.nih.gov/34800366/); original locator | Existing source preserved; full_text_available: true. | MitoCoP combines quantitative analysis of human-cell fractions, import-related evidence and curation. The source supports the broad high-throughput mitochondrial mapping context. The incoming FXN assertion is retained with independent FXN-specific evidence; no claim is made that its individual supplementary measurements were re-audited. Access: Selected full main-text strategy and Figure 1 caption from immutable cache; exact target supplement row not independently extracted. |
| PMID:38627381(https://pubmed.ncbi.nlm.nih.gov/38627381/); original locator | Existing source preserved; full_text_available: true. | Original XML selected structural Results, rapid persulfidation Results, figure captions and assay Methods were read. FXN-dependent ISCU rearrangement and faster NFS1-to-ISCU sulfur transfer support a direct activation role. Protein expression refers exact construct details to SupplementaryTable3, which was not recovered; no unverified construct length is assigned. Full figure images and supplements were not inspected. |
| PMID:9241270(https://pubmed.ncbi.nlm.nih.gov/9241270/); original locator | Genuinely fetched; full_text_available: false. | The abstract explicitly distinguishes human epitope-tagged FXN mitochondrial localization from yeast loss-of-function/iron experiments. This supports the basic human location without guessing tag or cell details, assigning yeast phenotypes to human cells, or claiming full original Methods access. Access: Authentic official abstract only. |
| PMID:9302253(https://pubmed.ncbi.nlm.nih.gov/9302253/); original locator | Genuinely fetched; full_text_available: false. | Human and mouse frataxin localization is explicitly studied by immunofluorescence and immunoelectron microscopy. The broad mitochondrial conclusion is supported. Detailed topology, universal exclusivity and natural splice-product specificity are not established from the abstract alone. Access: Authentic official abstract only. |
| Reactome:R-HSA-1362408 | Existing source preserved; curated source summary. | Immutable source summary explicitly describes the matrix FXN/NFS1/ISD11/ISCU [2Fe-2S] assembly reaction and alternative iron-donor versus activation interpretations. Read as a curated reaction model, not an additional experiment proving one physiological iron source. |
| Reactome:R-HSA-1362409 | Existing source preserved; curated source summary. | Immutable pathway summary distinguishes initial ISCU [2Fe-2S] assembly from downstream larger-cluster maturation and targeting. It supports pathway and matrix context while not assigning every downstream chemical step to FXN. |
| Reactome:R-HSA-1362416 | Existing source preserved; curated source summary. | Immutable source models frataxin ferrous binding and describes sulfur-production activation. Its fixed stoichiometry and alternative interaction models are source-specific, not a resolution of assay differences among primary papers. A fresh ContentService request was inaccessible; no refreshed API result is claimed. |
| Reactome:R-HSA-9854405 | Existing source preserved; curated source summary. | Immutable source describes proposed iron delivery to mitochondrial aconitase and places FXN in the matrix. The cached reaction summary was read; its cited detailed primary repair assays were not independently inspected in this pass. Used for bounded pathway/localization context. |
| Reactome:R-HSA-9854984 | Existing source preserved; curated source summary. | Immutable summary concerns respiratory complexII maturation. The official R-HSA-1362398 participant page independently links the FXN-containing cluster complex as an input of this event. This confirms model inclusion, not a direct measurement that FXN itself inserts the SDHB clusters. |
| Reactome:R-HSA-9865881; original locator | Existing source preserved; curated source summary. | The retained official Complex III assembly pathway page explicitly includes the UQCRFS1 cluster-insertion event. Its linked complex R-HSA-1362398 lists human FXN81-210 as a component and an input of that event, establishing actual model inclusion. The pathway states that the human assembly process is inferred from yeast evidence. Retain this bounded downstream assembly context as non-core; this model is not an independent experiment demonstrating an FXN-specific iron-transfer step, direct respiratory catalysis, or participation in every stage of complex III assembly. Later direct pathway/event requests returned404 and do not supersede the successful retained participant-page reading. |
| Reactome:R-HSA-9866272; original locator | Existing source preserved; curated source summary. | The immutable event summary attributes UQCRFS1 cluster insertion to an FXN-containing transfer complex. The successfully retained official R-HSA-1362398 participant page explicitly lists human FXN81-210 in the matrix complex and links it as an input of the UQCRFS1 insertion event within pathway9865881. Thus FXN is not absent from the model. Direct event-page and FXN-component-page requests returned404; no successful event HTML or resolved FXN-component-to-accession fetch is claimed. The detailed cited primary transfer experiments were not inspected. Specific attribution of iron-chaperone chemistry to FXN in UQCRFS1 maturation remains unresolved; matrix location is independently supported. |
| file:human/FXN/FXN-deep-research-falcon.md | Official method description or inherited provider file; no new native acquisition. | Inherited provider output is preserved as provenance and research context. Its model-header string is a literal inherited quotation but provides no biological evidence. Individual scientific assertions are evaluated against original publications; the provider output is not independently certified as a primary source. |
The native --no-seed acquisition preserved the complete inherited 79-row review. The fresh 92-context QuickGO response, all 16 exported TSV columns and the native parser projection agree exactly with the approved mapping. No new PENDING seed is claimed. Three original contexts retain five extension atoms, and the three natural product sequences remain distinct from processed experimental constructs. Native reference titles are used where cached; manual assessments retain their original access and claim limits. Default validation, strict GOA reconciliation, status audit and native EDIT history validation passed. Status is DRAFT with 21 advisories: 17 supported generic-binding rows, three source-specific mixed-action terms and the unused inherited provider file. Structured propagation metadata records the unresolved cluster-binding IBA without changing its biological judgment. The ontology cache is unchanged.
The prior acquisition and validation section records the initial publication. Default validation and strict GOA reconciliation passed for all 92 contexts. The native EDIT history, status audit and private rendered preview passed. Status is DRAFT with 20 advisories: 16 supported generic-binding rows, three source-specific mixed-action terms and the unused inherited provider file. The ferric and cluster-binding IBA metadata distinguish verified ancestry from unresolved experimental claims. The ontology cache is unchanged. It retains all 92 original contexts and the 20 active plus 48 historical inherited quotation occurrences. Six short, exact-cache occurrences are added with reference-specific provenance; the two original activation-core quotations remain unchanged. The whole inherited review and source archive remain intact.
The FECH interaction is refined to GO:0034986 iron chaperone activity, matching the original human iron-delivery observation without promoting that capability to an obligatory physiological core role. Four ferric-binding rows are UNDECIDED; the contradictory paper supports that review judgment. The positive finding from PMID:12785837 carries a claim-specific DISPUTED assessment and an explicitly attributed negative excerpt from PMID:29576242.
The exact mouse O35943 donor chain distinguishes its independent IDA involved_in row from its human-derived ISO acts_upstream_of row. PMID:25597503(https://pubmed.ncbi.nlm.nih.gov/25597503/) remains the literal donor reference; its accepted manuscript reports sulfur-transfer experiments and cites the earlier assembly study. The two transferred [4Fe-4S] annotation reasons now use the authentic cached abstract of PMID:23265191(https://pubmed.ncbi.nlm.nih.gov/23265191/): a cluster forms within the quaternary ISCU/NFS1/ISD11/FXN complex and can activate mammalian aconitase after transfer; the ternary complex without FXN assembles an Fe-S cluster but transfers it inefficiently. These observations support bounded non-core ortholog transfer, without resolving the separate human acts_upstream_of annotation.
External experimental reading is separate from those abstract-grounded reasons. The complete official ACS supplement for DOI:10.1021/ja308736e was retained and read. Pages 2–3 and 8 identify murine constructs; pages 4–7 describe anaerobic reconstitution, transfer and spectroscopy methods; Table S2 on page 15 reports cluster-species fractions at different iron amounts and incubation times. Cluster-species fractions and aconitase-transfer efficiency are distinct observables. The Table S2 comparisons are not used as negative evidence against the abstract’s transfer result. Both native donor-paper caches are abstract-only, and the main 23265191 article body was inaccessible; the linked external supplement supplies the additional assay and organism scope. This source was retained, unlike the unrecovered successful 15961414 author-page response.
| Added reference | Native cache | External material actually read |
|---|---|---|
| PMID:25597503(https://pubmed.ncbi.nlm.nih.gov/25597503/) | Genuinely fetched; full_text_available: false. | Accepted original manuscript, selected Results/Discussion/Methods. |
| PMID:23265191(https://pubmed.ncbi.nlm.nih.gov/23265191/) | Genuinely fetched; full_text_available: false. | Official abstract and complete ACS supplement; main article body inaccessible. |
The two GO:0004322 rows are MARK_AS_OVER_ANNOTATED. The PMID:15641778 abstract positively reports ferroxidase activity of assembled recombinant human frataxin. The PMID:15581888 abstract also reports human-heart mitochondrial species ranging from monomers to large polymers. Thus physiological assembly is supported; it is the physiological use of iron-oxidation chemistry that remains unestablished. The measured activity and its existing quotations remain intact. No quantitative inefficiency, noise, promiscuity, absent oligomerization or unreported assay condition is inferred from the abstract-only access. The question about physiological settings requiring this activity remains open.