Affinage

DHX38

Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 · UniProt Q92620

Length
1227 aa
Mass
140.5 kDa
Annotated
2026-06-09
33 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DHX38 (PRP16) is a DEAH-box RNA-dependent ATPase and RNA helicase that acts as a spliceosomal remodeling factor governing the transition between the two catalytic steps of pre-mRNA splicing (PMID:1825134, PMID:9550699). It associates transiently with the spliceosome late in the pathway, where ATP binding/hydrolysis is coupled to its release and to a conformational rearrangement that protects the 3' splice site and licenses the second transesterification step (PMID:1825134, PMID:1464325); ATPase-deficient motif mutants bind spliceosomes but block step 2 in a dominant-negative manner, establishing that catalysis depends on its NTP hydrolysis (PMID:11856747). Mechanistically, after lariat formation DHX38 destabilizes the first-step factors Cwc25 and Yju2 and disrupts U2-U6 helix I, thereby enabling recruitment of second-step factors Prp22, Prp18, and Slu7 to drive exon ligation (PMID:21098140, PMID:23438600, PMID:24848011). Its sequence-nonspecific helicase activity is targeted to the correct substrate by a non-conserved N-terminal domain and is regulated through functional interaction with the helicase Brr2 (PMID:9769096, PMID:25428373). Beyond promoting forward catalysis, DHX38 proofreads both step 1 and step 2, routing aberrant intermediates to a Prp43-dependent discard pathway, and slowing its ATPase rate permits aberrant intermediates to proceed productively (PMID:8324826, PMID:20705241); it also possesses an ATP-independent activity that promotes usage of aberrant 5' splice sites and mutated branch points via the step-one factor Cwc25 (PMID:21098140, PMID:37858289). In human and zebrafish systems DHX38 controls alternative splicing and splice-site fidelity, and its loss arrests cells in mitotic prometaphase, causes R-loop accumulation and replication-stress-driven DNA damage, and triggers p53-dependent apoptosis in developing retina, inner ear, and hematopoietic progenitors (PMID:35385551, PMID:35929537, PMID:37867960, PMID:39857604). DHX38 additionally associates with centromeric satellite I ncRNA to support chromosome segregation and Aurora B function (PMID:31166646), interacts with G3BP1 to activate MAPK/ERK signaling and EMT in cancer (PMID:37931691), and its own mRNA translation is enhanced by the m6A reader YTHDF1 (PMID:40116022).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1991 High

    Established DHX38/PRP16 as an RNA-dependent ATPase that transiently engages the spliceosome and is specifically required for the second catalytic step, defining the first functional foothold for the protein.

    Evidence Protein purification with in vitro ATPase and splicing complementation assays

    PMID:1825134

    Open questions at the time
    • Did not resolve the molecular substrate of remodeling
    • Helicase activity not yet demonstrated
  2. 1992 High

    Linked ATP hydrolysis to a defined conformational rearrangement of the spliceosome, showing the energy of NTP hydrolysis drives a structural change that protects the 3' splice site for step 2.

    Evidence In vitro splicing with RNase H protection and ATPase assays using NTP analogs

    PMID:1464325

    Open questions at the time
    • Identity of the rearranged RNA elements not defined
    • Helicase mechanism not yet shown
  3. 1993 High

    Revealed a kinetic proofreading function whereby PRP16 ATPase activity discards aberrantly branched intermediates, explaining how splicing fidelity is enforced.

    Evidence Genetic suppressor screen with purified mutant proteins and in vivo intermediate analysis in yeast

    PMID:8324826

    Open questions at the time
    • Downstream discard machinery not identified
    • Direct coupling of ATPase rate to discard not reconstituted
  4. 1994 Medium

    Identified U6 and U2-U6 helix I snRNAs as functional RNA ligands of PRP16's remodeling activity, pointing to the catalytic RNA core as its target.

    Evidence Genetic suppressor screens and site-directed mutagenesis of snRNAs in yeast

    PMID:8088513

    Open questions at the time
    • Genetic interaction does not prove direct physical contact
    • Mechanism of helix I destabilization unresolved at this stage
  5. 1995 High

    Ordered the second-step pathway by showing SLU7 and SSF1 act downstream of PRP16, building a sequential factor map for exon ligation.

    Evidence Glycerol gradient isolation of PRP16-depleted spliceosomes and functional complementation with differential ATP requirements

    PMID:7664739

    Open questions at the time
    • Physical handoff between PRP16 and second-step factors not visualized
    • SSF1 molecular identity not fully defined
  6. 1998 High

    Demonstrated intrinsic ATP-dependent RNA unwinding activity and mapped the structure-function determinants, defining DHX38 as a bona fide helicase whose catalytic motifs and substrate-targeting N-terminus are separable.

    Evidence In vitro RNA duplex unwinding, alanine-scanning and deletion mutagenesis, complementation and localization assays in yeast

    PMID:9550699 PMID:9611193 PMID:9769096

    Open questions at the time
    • How the N-terminal domain recognizes the correct spliceosome state not defined
    • In vivo unwinding substrate not directly captured
  7. 1998 High

    Extended PRP16 function to humans, showing hPrp16 is required for step 2 and is functionally conserved across species.

    Evidence Immunodepletion/add-back in human extracts and cross-species chimera complementation in yeast

    PMID:9524131

    Open questions at the time
    • Human-specific cofactors not identified
    • Structural basis of conservation not addressed
  8. 2002 High

    Established that ATP hydrolysis itself, not merely ATP binding, is mechanistically required for step 2 chemistry, via dominant-negative ATPase-defective mutants.

    Evidence In vivo dominance assay plus purified mutant ATPase, splicing, and spliceosome-binding assays

    PMID:11856747

    Open questions at the time
    • Conformational consequence of hydrolysis not structurally resolved
    • Coupling of motor cycle to factor release not yet shown
  9. 2010 High

    Expanded proofreading to step 1 (5' splice site cleavage) and showed Prp16-mediated rejection is reversible and requires Prp43 to complete discard, integrating DHX38 into a two-step fidelity surveillance system.

    Evidence In vitro splicing with catalytic-center disruption, Prp16 inactivation, and genetic epistasis with Prp43

    PMID:20705241

    Open questions at the time
    • Mechanism of Prp16-to-Prp43 handoff not defined
    • Structural state of rejected intermediates unknown
  10. 2013 Medium

    Defined the substrate of remodeling as the stably bound first-step factors Cwc25 and Yju2, whose displacement by Prp16 (and destabilization of U2-U6 helix I) enables second-step factor binding.

    Evidence In vitro splicing with truncated Yju2, spliceosome-binding and UV cross-linking assays; genetic and cross-linking analysis of helix I

    PMID:21098140 PMID:23438600 PMID:24848011

    Open questions at the time
    • Direct structural snapshot of factor displacement not obtained
    • Antagonism with Cwc2 inferred genetically/biochemically only
  11. 2014 High

    Identified Brr2 as a regulator of Prp16 ATPase activity, and connected Prp16 action to NTR-mediated spliceosome disassembly, embedding DHX38 in a helicase regulatory network.

    Evidence In vitro ATPase modulation with Brr2 Sec63-2 domain, allele-specific genetics, and stage-specific NTR disassembly assays

    PMID:23166295 PMID:25428373

    Open questions at the time
    • Physiological trigger for Brr2 regulation of Prp16 unclear
    • Structural basis of Brr2-Prp16 interplay not resolved
  12. 2019 Medium

    Revealed a splicing-independent role: DHX38 binds centromeric satellite I ncRNA and supports chromosome segregation and Aurora B function, broadening its cellular reach to mitosis.

    Evidence RNA immunoprecipitation, siRNA knockdown, chromosome segregation and Aurora B functional assays in human cells

    PMID:31166646

    Open questions at the time
    • Direct vs splicing-mediated contribution to segregation not separated
    • No reconstitution of the ncRNP complex
  13. 2023 Medium

    Connected DHX38 to genome integrity by showing its loss causes R-loop accumulation and replication-stress-driven DNA damage, defining a DHX38/R-loop/replication-stress axis.

    Evidence CRISPR knockout zebrafish and siRNA knockdown in human cells with R-loop (S9.6) immunostaining and DNA damage markers

    PMID:37867960

    Open questions at the time
    • Whether R-loop control is direct or a downstream consequence of splicing defects unresolved
    • No biochemical demonstration of R-loop resolution by DHX38
  14. 2023 Medium

    Documented cancer-context roles in which DHX38 interacts with G3BP1 to activate MAPK/ERK signaling and EMT, and regulates intron retention of specific transcripts in drug-resistant tumors.

    Evidence Co-IP/LC-MS, knockdown rescue, ERK inhibition, RIP-qPCR and intron-retention RT-PCR in cancer cell lines and tumor assays

    PMID:37506056 PMID:37931691

    Open questions at the time
    • Mechanism linking splicing activity to G3BP1/MAPK not defined
    • Single-lab co-IP without reciprocal structural validation
  15. 2022 Medium

    Tied DHX38 function to development and splice-site fidelity in vertebrates, where loss arrests progenitors in prometaphase, perturbs alternative splicing, and provoked retina/ear/hematopoietic defects with p53-dependent apoptosis.

    Evidence siRNA knockdown with RNA-seq and minigene reporters in human cells; CRISPR knockout zebrafish with cytological, splicing, and p53 analyses

    PMID:35385551 PMID:35929537 PMID:39857604

    Open questions at the time
    • Causal chain from splicing changes to mitotic arrest not fully resolved
    • RP-linked variant mechanism not mapped to a defined biochemical defect
  16. 2025 Medium

    Identified upstream control of DHX38 abundance, with the m6A reader YTHDF1 enhancing Dhx38 mRNA translation, linking epitranscriptomic regulation to DHX38 protein levels and retinal health.

    Evidence MeRIP-seq, RIP-seq, polysome assays, and Ythdf1 knockout mouse retina

    PMID:40116022

    Open questions at the time
    • Direct functional rescue of retinal phenotype by restoring DHX38 not shown
    • Tissue specificity of this regulation not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How DHX38's ATP-driven motor cycle is mechanistically partitioned between forward step-2 catalysis, kinetic proofreading/discard, splicing-independent R-loop suppression, and chromosome segregation remains unresolved.
  • No structural model coupling the helicase cycle to factor release in human spliceosomes
  • Whether mitotic and genome-integrity roles are direct or splicing-dependent is unknown
  • No reconstitution of the proposed nuclear SOS latent-splice-site surveillance role for DHX38

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140657 ATP-dependent activity 4 GO:0003723 RNA binding 3 GO:0016787 hydrolase activity 2 GO:0140098 catalytic activity, acting on RNA 1
Localization
GO:0005634 nucleus 1
Pathway
R-HSA-8953854 Metabolism of RNA 4 R-HSA-1640170 Cell Cycle 2 R-HSA-73894 DNA Repair 2 R-HSA-162582 Signal Transduction 1
Partners
BRR2CWC25G3BP1SLU7YJU2YTHDF1
Complex memberships
spliceosome

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1991 PRP16 (DHX38) is an RNA-dependent ATPase that interacts transiently with the spliceosome and is required specifically for the second catalytic step of pre-mRNA splicing in vitro; ATP binding and/or hydrolysis by PRP16 is concomitant with its release from the spliceosome. Protein purification, in vitro ATPase assay, in vitro splicing complementation assay Nature High 1825134
1992 PRP16 promotes a conformational change in the spliceosome that protects the 3' splice site from oligo-directed RNase H cleavage; this structural rearrangement requires ATP hydrolysis (ATP-γS, a competitive inhibitor, blocks both ATPase activity and 3' splice site protection). PRP16 can hydrolyze all NTPs and dNTPs, linking the nucleotide requirement of step 2 to PRP16. In vitro splicing assay, RNase H protection assay, ATPase activity with NTP analogs The EMBO journal High 1464325
1993 Prp16 ATPase activity governs a discard pathway for aberrantly branched lariat intermediates; suppressor alleles of PRP16 that allow splicing of branch-site mutants all map to the RNA-dependent ATPase region and show reduced ATPase activity in vitro, indicating that slowing ATP hydrolysis gives aberrant intermediates more time to proceed through the productive rather than the discard branch. Genetic suppressor screen, purification of mutant proteins, in vitro ATPase assay, in vivo steady-state splicing intermediate analysis Cell High 8324826
1994 Genetic interactions in yeast between Prp16 and U6 snRNA (single nucleotide deletions upstream of the 5' splice site-interacting sequence) and between Prp16 and U2-U6 helix I suppress prp16 cold-sensitive alleles, providing genetic evidence that U6 and U2 snRNAs are functional RNA ligands for Prp16's ATPase-driven remodeling activity. Genetic suppressor screen with mutagenized U6 snRNA library, site-directed mutagenesis of U2-U6 helix I, overexpression dominance analysis Genetics Medium 8088513
1995 SLU7 protein and the novel activity SSF1 are required together with PRP16 to promote the second catalytic step of splicing; using differential ATP requirements, SLU7 was shown to act after PRP16 in the splicing pathway. Glycerol gradient sedimentation to isolate PRP16-depleted spliceosomes, functional complementation with purified proteins/fractions, differential ATP requirement assay The EMBO journal High 7664739
1998 Prp16 possesses ATP-dependent RNA unwinding (helicase) activity in vitro that is independent of sequence in either strand; the prp16-1 mutation near the ATP-binding motif abolishes both RNA-dependent ATPase and RNA unwinding activities. In vitro RNA duplex unwinding assay with purified protein, ATPase assay, mutant protein analysis Current biology : CB High 9550699
1998 The non-conserved N-terminal domain of Prp16 is essential for viability, required for nuclear localization, and mediates spliceosome binding specifically at the step of Prp16 function; this domain can interact in trans with the catalytic domain to allow complementation, indicating it targets the sequence-nonspecific helicase activity to the correct substrate. Deletion analysis, in vivo complementation, nuclear localization microscopy, spliceosome-binding assay, trans-complementation RNA (New York, N.Y.) High 9769096
1998 Alanine-scanning mutagenesis of Prp16 defined essential residues: Gly-378, Lys-379, Thr-380 in motif I (GETGSGKT); Asp-473 and Glu-474 in the DEAH motif II; and Gln-685, Arg-686, Gly-688, Arg-689, Arg-692 in motif VI are all required for biological activity; the N-terminal 204 amino acids and C-terminal 100 residues are dispensable for in vivo function. Alanine-scanning mutagenesis, in vivo complementation of null strain, deletion analysis Genetics High 9611193
1998 Human DHX38 (hPrp16) is required specifically for the second catalytic step of splicing: immunodepletion of hPrp16 from splicing extracts blocks step II, and activity is fully restored by recombinant hPrp16. hPrp16 associates with the spliceosome late in the splicing pathway. A chimeric yeast-human Prp16 protein rescues a yeast Prp16 knockout, demonstrating functional conservation. Immunodepletion from splicing extracts, recombinant protein complementation, spliceosome association assay, yeast knockout complementation with chimeric protein The EMBO journal High 9524131
2002 Lethal Prp16 mutants in motifs I (G378A, K379A), II (D473A, E474A), and VI (Q685A, G688A, R689A, R692A) are defective for ATP hydrolysis and step 2 transesterification chemistry; these ATPase-defective mutants bind spliceosomes in vitro and block wild-type Prp16 function in trans (dominant-negative), establishing that ATP hydrolysis is mechanistically required for step 2 catalysis. Overexpression dominance assay in vivo, purification of recombinant mutant proteins, ATPase assay, in vitro splicing assay, spliceosome-binding assay The Journal of biological chemistry High 11856747
2010 Prp16 can associate with spliceosomes before 5' splice site cleavage and proofreads 5' splice site cleavage: when Prp16 is disabled, spliceosomes with an inactivated catalytic center can still catalyze 5' splice site cleavage (at reduced rate), but Prp16-mediated rejection is reversible, requiring the downstream discard ATPase Prp43 to complete discard. In vitro splicing assay with metal-ligand disruption at catalytic center, Prp16 inactivation, spliceosome association assay, genetic epistasis with Prp43 Molecular cell High 20705241
2010 Prp16 promotes release of first-step factors Cwc25 and Yju2 from the spliceosome after lariat formation in a Prp16- and ATP-dependent manner, thereby enabling binding of Prp22, Prp18, and Slu7 to promote the second catalytic reaction; additionally, in the absence of ATP, Prp16 has an ATP-independent role in stabilizing Cwc25 binding to spliceosomes containing branch-point mutations to facilitate their splicing. In vitro splicing assay, spliceosome affinity purification, protein binding analysis, ATP-dependency experiments with branch-point mutant pre-mRNAs RNA (New York, N.Y.) High 21098140
2012 NTR complex-mediated spliceosome disassembly is linked to Prp16 action: NTR can disassemble spliceosomes arrested specifically after ATP-dependent action of Prp16 (or Prp2/Prp22), but not before these ATPases act or upon their spliceosome binding; Prp16 and Slu7 (which both interact with Brr2) negatively impact Ntr2 binding to the spliceosome. Affinity purification of spliceosomes arrested at defined stages, NTR disassembly assay, Ntr2 spliceosome binding analysis Molecular and cellular biology High 23166295
2013 Prp16 is required for destabilization of Yju2 and Cwc25 from the spliceosome after the first catalytic step; a truncated Yju2 (Yju2-N) with weak spliceosome affinity can support a low level of second-step splicing even in the absence of Prp16, suggesting that Prp16's role is specifically to displace stably-bound Yju2/Cwc25 to allow second-step factor binding. In vitro splicing complementation with truncated Yju2 fragments, spliceosome-binding assay, UV cross-linking to U2 snRNA Molecular and cellular biology Medium 23438600
2014 Prp16 destabilizes U2-U6 snRNA helix I during spliceosome remodeling between steps 1 and 2; the NTC protein Cwc2 stabilizes U2-U6 helix I, and a prp16-302 mutation stabilizes Cwc2 interactions with U6 snRNA while destabilizing Cwc2 interactions with pre-mRNA, indicating antagonistic functions between Cwc2 and Prp16 at the helix I/active site region. Genetic suppressor analysis, allele-specific epistasis, RNA-protein interaction assays (UV cross-linking), in vivo splicing assays Nucleic acids research Medium 24848011
2014 The C-terminal Sec63-2 domain of Brr2 modulates the ATPase activity of Prp16 in vitro by interfering with Prp16's ability to bind RNA; allele-specific genetic interactions between BRR2 and PRP16 mutations suppress or enhance growth defects, establishing a functional regulatory interaction between these two splicing helicases. In vitro ATPase assay with purified Brr2 Sec63-2 domain and Prp16, allele-specific genetic suppressor/enhancer analysis, physical interaction assay Nucleic acids research High 25428373
2019 DHX38 associates with satellite I noncoding RNA from the human centromere region in an interphase-specific manner; depletion of DHX38 causes defective chromosome segregation (similar to satellite I ncRNA knockdown) and impairs Aurora B function at mitosis, placing DHX38 in an ncRNP complex involved in mitotic regulation. RNA immunoprecipitation (RIP), siRNA knockdown, chromosome segregation assay, Aurora B functional analysis Genes to cells : devoted to molecular & cellular mechanisms Medium 31166646
2022 DHX38 knockdown in human cells causes modulation of ~70 alternative splicing events and affects splicing of retina-specific genes FSCN2 and RHO; overexpression of DHX38 promotes usage of canonical and cryptic 5' splice sites in an HBB splicing reporter; the RP-linked G332D mutation modulates DHX38 splicing activity without detectably changing its spliceosome interaction profile. siRNA knockdown, RNA-seq splicing analysis, minigene splicing reporter assay, co-immunoprecipitation of spliceosomal factors PloS one Medium 35385551
2022 Dhx38 loss in zebrafish arrests erythro-myeloid progenitors (EMPs) and hematopoietic stem/progenitor cells in mitotic prometaphase with chromosome alignment defects; abnormal alternative splicing of genes related to chromosome segregation, microtubule cytoskeleton, cell cycle kinases, and DNA damage occurs in dhx38 mutants, and EMPs/HSPCs undergo p53-dependent apoptosis. CRISPR knockout zebrafish, cytological chromosome alignment analysis, RNA-seq alternative splicing analysis, p53 pathway analysis Development (Cambridge, England) Medium 35929537
2023 Prp16 has an ATP-independent role in promoting usage of aberrant 5' splice sites and mutated branch points: when a 5' splice site mutation is present or when Cwc24 is absent, Prp16 facilitates the branching reaction independently of ATP, and this function is mediated through the step-one factor Cwc25. Additionally, Prp16 prevents use of nearby cryptic branch sites while promoting mutated branch point usage. In vitro splicing assay with ATP analogs and mutant pre-mRNAs, deletion/depletion of Cwc24, Cwc25 interaction assays Nucleic acids research Medium 37858289
2023 DHX38 interacts with G3BP1 (Ras GTPase-activating protein-binding protein) as demonstrated by co-immunoprecipitation; DHX38 regulates G3BP1 expression, leading to activation of the MAPK/ERK signaling pathway and promoting EMT in NSCLC cells. Knockdown of G3BP1 reverses DHX38 overexpression-induced MAPK activation and EMT. Co-immunoprecipitation, LC-MS interactome, siRNA knockdown, ERK inhibitor (SCH772984) treatment, in vitro and in vivo tumor assays Cellular signalling Medium 37931691
2023 DHX38 directly interacts with RELL2 pre-mRNA (confirmed by RIP-qPCR) and regulates retention of intron 4 in RELL2 transcripts in gemcitabine-resistant pancreatic ductal adenocarcinoma cells; altered DHX38 expression causes corresponding changes in RELL2 intron 4 retention. RIP-qPCR, DHX38 knockdown/overexpression, RT-PCR for intron retention PLoS genetics Medium 37506056
2023 DHX38 deficiency in zebrafish and human cell lines causes significant accumulation of R-loops; DNA replication stress is the prerequisite for R-loop-induced DNA damage in DHX38 knockdown cells, establishing a DHX38/R-loop/replication stress/DNA damage regulatory axis in retinal progenitor cells. CRISPR dhx38 knockout zebrafish, R-loop immunofluorescence (S9.6 antibody), DHX38 siRNA knockdown in human cells, DNA damage markers iScience Medium 37867960
2024 dhx38 knockout zebrafish display severe inner ear developmental defects (decrescent otocysts, absent semicircular canal protrusion, smaller otoliths) accompanied by DNA damage, p53-dependent apoptosis in inner ear cells, and abnormal alternative splicing of genes related to DNA damage repair and inner ear morphogenesis. CRISPR knockout zebrafish, bright-field morphology, in situ hybridization, immunofluorescence for apoptosis/DNA damage, RT-PCR alternative splicing analysis Biomedicines Medium 39857604
2025 DHX38 knockdown significantly increases latent splice site (LSS) usage in a luminescence reporter and RNA-seq confirmed widespread LSS activation across hundreds of mRNAs, establishing DHX38 as a component of the nuclear SOS (suppression of splicing) quality control mechanism that prevents inappropriate use of latent splice sites. siRNA screen with luminescence reporter for LSS activation, RNA-seq after DHX38 knockdown bioRxivpreprint Low bio_10.1101_2025.07.20.665773
2025 YTHDF1 binds m6A-modified Dhx38 mRNA at the coding sequence (CDS) and enhances its translational efficiency without altering mRNA levels, as demonstrated by MeRIP-seq and RIP-seq in mouse retina; loss of Ythdf1 reduces Dhx38 protein levels and contributes to retinal degeneration. MeRIP-seq, RIP-seq, Ythdf1 knockout mouse, polysome/translation efficiency assay, single-cell RNA-seq Zoological research Medium 40116022

Source papers

Stage 0 corpus · 33 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1991 PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 301 1825134
1992 A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis. The EMBO journal 185 1464325
1993 A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates. Cell 162 8324826
1995 SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing. The EMBO journal 116 7664739
2010 The DEAH box ATPases Prp16 and Prp43 cooperate to proofread 5' splice site cleavage during pre-mRNA splicing. Molecular cell 104 20705241
1998 The DEAH-box splicing factor Prp16 unwinds RNA duplexes in vitro. Current biology : CB 87 9550699
2010 DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps. RNA (New York, N.Y.) 84 21098140
1998 PRP16, a DEAH-box RNA helicase, is recruited to the spliceosome primarily via its nonconserved N-terminal domain. RNA (New York, N.Y.) 70 9769096
1998 Human homologs of yeast prp16 and prp17 reveal conservation of the mechanism for catalytic step II of pre-mRNA splicing. The EMBO journal 64 9524131
2014 A missense mutation in the splicing factor gene DHX38 is associated with early-onset retinitis pigmentosa with macular coloboma. Journal of medical genetics 54 24737827
2002 Characterization of dominant-negative mutants of the DEAH-box splicing factors Prp22 and Prp16. The Journal of biological chemistry 50 11856747
1998 Mutational analysis of the yeast DEAH-box splicing factor Prp16. Genetics 45 9611193
1994 Genetic interactions between the yeast RNA helicase homolog Prp16 and spliceosomal snRNAs identify candidate ligands for the Prp16 RNA-dependent ATPase. Genetics 40 8088513
2012 Link of NTR-mediated spliceosome disassembly with DEAH-box ATPases Prp2, Prp16, and Prp22. Molecular and cellular biology 35 23166295
2013 A weak spliceosome-binding domain of Yju2 functions in the first step and bypasses Prp16 in the second step of splicing. Molecular and cellular biology 18 23438600
2018 Confirmation of the Role of DHX38 in the Etiology of Early-Onset Retinitis Pigmentosa. Investigative ophthalmology & visual science 16 30208423
2023 DHX38 enhances proliferation, metastasis, and EMT progression in NSCLC through the G3BP1-mediated MAPK pathway. Cellular signalling 14 37931691
2014 Remodeling of U2-U6 snRNA helix I during pre-mRNA splicing by Prp16 and the NineTeen Complex protein Cwc2. Nucleic acids research 13 24848011
2023 An ATP-independent role for Prp16 in promoting aberrant splicing. Nucleic acids research 12 37858289
2014 Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase. Nucleic acids research 12 25428373
1994 The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames. Yeast (Chichester, England) 12 8203164
2022 Retinitis pigmentosa-linked mutation in DHX38 modulates its splicing activity. PloS one 11 35385551
2022 Dhx38 is required for the maintenance and differentiation of erythro-myeloid progenitors and hematopoietic stem cells by alternative splicing. Development (Cambridge, England) 11 35929537
2023 DHX38 restricts chemoresistance by regulating the alternative pre-mRNA splicing of RELL2 in pancreatic ductal adenocarcinoma. PLoS genetics 9 37506056
2019 Early splicing functions of fission yeast Prp16 and its unexpected requirement for gene Silencing is governed by intronic features. RNA biology 9 30810475
2022 The splicing factor DHX38/PRP16 is required for ovarian clear cell carcinoma tumorigenesis, as revealed by a CRISPR-Cas9 screen. FEBS open bio 8 34965029
2023 The splicing factor DHX38 enables retinal development through safeguarding genome integrity. iScience 7 37867960
2019 DEAH box RNA helicase DHX38 associates with satellite I noncoding RNA involved in chromosome segregation. Genes to cells : devoted to molecular & cellular mechanisms 7 31166646
2012 Plasmodium falciparum Prp16 homologue and its role in splicing. Biochimica et biophysica acta 6 22982196
2024 Knockout of dhx38 Causes Inner Ear Developmental Defects in Zebrafish. Biomedicines 4 39857604
2025 Single-cell sequencing analysis reveals the essential role of the m 6A reader YTHDF1 in retinal visual function by regulating TULP1 and DHX38 translation. Zoological research 2 40116022
2023 Correction: Retinitis pigmentosa-linked mutation in DHX38 modulates its splicing activity. PloS one 1 36662708
2022 A Novel Missense Variant C.2571 (P.Ala857=) of the DHX38 Gene in a Saudi Family Causes an Autosomal Recessive Retinitis Pigmentosa. Middle East African journal of ophthalmology 0 35719279

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