These notes distinguish the independently accessed originals from the preserved publication caches. Quoted text below is anchored to the specified original, not inserted into an abstract-only cache. Additional short source anchors appear once in the review YAML.
PMID:17932509, original PMC article, Table 1 and Results paragraph accompanying Figure 3C. DHX30 is included in the AGO1/AGO2 mRNP complexes. The paragraph's DDX30-containing list “was sensitive to RNase A treatment”. This supports RNA-dependent association, not an independently demonstrated protein-only interface. Selected co-immunoprecipitation Methods and Results were read; the repository cache remains abstract-only.
PMID:18063578, DOI and author-posted original, Table 1 on printed page 3669, DHX30/NP_055781 row. The two native-preparation peptide counts are 6 and 16; the crosslinked-preparation counts are 12 and 5. Target immunoblots corroborate gradient association. Methods describe mitochondrial preparations and formaldehyde treatment; Discussion distinguishes potential protein-protein crosslinks from direct DNA contact. These observations support nucleoid association without establishing nuclear-chromatin binding. The original was read as author-uploaded text, not from the failed publisher/PDF requests; the cache remains abstract-only.
PMID:23275553, original PMC article, Figure 3A/B and Results on mitochondrial nucleic-acid depletion. DHX30 is among “SLIRP, LRPPRC, DHX30, PTCD3, POLRMT and TFAM” reduced under the depletion condition. Figure 3B and its caption were inspected. The separate Figure 2C submitochondrial fractionation is for PABPC5. It must not be described as a direct DHX30 matrix-fractionation experiment.
PMID:34800366, original and Table S1 workbook. In sheet (A) All protein groups, rows 306/307 identify groups 7473/7474. Group 7473 contains Q7L2E3, H7BXY3, Q7L2E3-3 and F6R0H4; it is class 5/cluster 2c and has no topology category. Group 7474 is Q7L2E3-2, class 1/cluster 1, with column BX = Peripheral, BY = 27.001148226379655 and BZ = 90.33085912386213. BY and BZ are integral and membrane-associated percentages, respectively, derived from the extraction/sonication measurements. Sheet (B) All genes, row 279, contains both groups for DHX30. Header rows are 1 and 2; blank/NaN values are not interpreted as negative localization. The database-derived matrix annotation column is not an additional matrix assay.
PMID:29100085, original PMC article, RNA-dependent ATPase and RNA immunoprecipitation Methods/Results. Tagged human DHX30 was assayed from HEK293T cells; U2OS imaging documented cytoplasmic and mitochondrial pools. These experiments establish RNA association and stimulated ATP hydrolysis, not a duplex-unwinding assay. PMID:29304375(https://pubmed.ncbi.nlm.nih.gov/29304375/) corrects an author's surname only.
PMID:34020708, original PMC article, Figure 2 and publisher Supplementary Methods under DOI 10.1186/s13073-021-00900-3. Purified bacterial full-length His6-SUMO human DHX30 unwinds a synthetic radiolabeled RNA duplex in an ATP-dependent native-PAGE assay, with no-ATP and heated-substrate controls. The genuine publisher Methods document was read; an earlier challenge response was not treated as a document. No current-isoform endpoint mapping is supplied by those Methods.
PMID:25683715, original DOI, mitochondrial RNA-granule localization, RNA-IP and ribosome-gradient Results and corresponding human-cell Methods. The separately accessed author-posted original supports large-subunit/monosome assembly and partial nucleoid colocalization. DHX30 RNA-IP was broadly distributed; the study's specific 16S-rRNA result must not be transferred from DDX28/FASTKD2 to DHX30. The preserved cache is abstract-only.
PMID:29100085, DOI 10.1016/j.ajhg.2017.09.014, original publisher supplement, page 15 Figure S5: endogenous human U2OS DHX30 is shown with mitochondria in panel A and with ATXN2/DDX3X in unstressed and stressed cells in panel B. Caption and pixels were inspected; the granule accumulation is partial. The main Results identify heat stress. No quantitative image reanalysis or FMRP identity is claimed.
PMID:34020708, DOI 10.1186/s13073-021-00900-3, Figure 2c and Supplementary Methods describe the full-length His6-SUMO human protein, bacterial expression/purification and radiolabeled RNA-duplex unwinding in ATP-containing reactions. Figures 7/8 and corresponding Methods/Results separately show HEK293T depletion and zebrafish knockout granule phenotypes. These are actual biochemical and cellular observations, but the granule experiments do not resolve the wild-type molecular assembly step.
PDB 2DB2 is a solution-NMR protein construct containing the exact native DHX30 42–148 sequence with terminal tags. The deposition has one protein polymer entity and no RNA polymer entity. IPR056755 and PF24995 identify the divergent dsRNA-binding domain; the literal target match is 48–123. Domain structure and membership corroborate, but do not replace, the direct duplex-substrate experiment or recover the missing PMID:21266579 supplementary target table.