| 2011 |
GEX1A (Herboxidiene) directly targets SAP155 (SF3B1) protein, a subunit of SF3b responsible for pre-mRNA splicing, as identified by photoaffinity-labeling derivatives. GEX1A inhibits pre-mRNA splicing by binding to SAP155/SF3B1, thereby impairing SF3b function. |
Photoaffinity labeling with GEX1A derivatives, in vitro splicing assays, Western blot |
ACS chemical biology |
High |
21138297
|
| 2006 |
SF3B1 (SAP155/SF3b155) N-terminal domain contains multiple U2AF65 binding sites that are distinct from the p14 binding site (mapped to residues 396–424). The N-terminal domain adopts a primarily unfolded structure functioning as a scaffold for multiple protein–protein and protein–RNA interactions required for U2 snRNP recruitment to the branch point during splicing. |
In vitro binding assays, RNA binding studies, inhibition of splicing in vitro, circular dichroism spectroscopy |
Biochemistry |
High |
16906767
|
| 2006 |
DYRK1A phosphorylates SF3B1 (SAP155) at Thr434 in vitro and in cultured cells; overexpression of DYRK1A increases Thr434 phosphorylation of endogenous SF3B1, while DYRK1A knockdown reduces it. Cyclin E/CDK2 phosphorylates SF3B1 at different sites, producing a completely different phosphopeptide pattern. |
In vitro kinase assay, phosphopeptide mapping, mass spectrometry, mutational analysis, co-expression/knockdown in COS-7 and HEK293 cells, Western blot with phospho-specific antibody |
BMC biochemistry |
High |
16512921
|
| 2006 |
SF3B1 (SAP155) binds via its RRM-like domain to the ceramide-responsive RNA cis-element 1 (CRCE1) of Bcl-x pre-mRNA. SAP155 knockdown shifts splicing toward the pro-apoptotic Bcl-x(s) isoform and is required for ceramide-induced activation of the Bcl-x(s) 5' splice site, sensitizing cells to chemotherapeutic agents. |
Mass spectrometry identification, EMSA supershift with anti-SAP155 antibody, RNA interference (RNAi) knockdown, RT-PCR for splice variant quantification, apoptosis assays |
FASEB journal |
High |
16790528
|
| 2006 |
SF3B155 binds to the β-sheet surface of p14 (SF3b14) through a helical peptide (residues 401–415 form the core epitope), occupying the canonical RNA-binding surface of the p14 RRM. SF3B155 simultaneously binds p14 and U2AF65 through non-overlapping regions, potentially stabilizing U2 snRNP association with pre-mRNA. The p14–SF3B155 complex modulates RNA-binding specificity for the branch point. |
NMR spectroscopy, biochemical binding assays, mutagenesis |
RNA |
High |
16495236
|
| 2005 |
SF3b155 contains five functional tryptophan-containing U2AF65-binding sites in its N-terminal domain, each recognized by the U2AF65 UHM domain via a mechanism similar to SF1 but with lower affinity (3.3 kcal/mol less stable than the SF1/U2AF65 complex), consistent with ATP-dependent exchange of these partners during pre-mRNA splicing. |
Intrinsic tryptophan fluorescence spectroscopy, isothermal titration calorimetry, circular dichroism, mutagenesis of SF3b155 variants |
Journal of molecular biology |
High |
16376933
|
| 2002 |
The FHA domain of NIPP1 interacts in vitro and in vivo with the TP dipeptide-rich region of SF3B1 (SAP155) in a phosphorylation-dependent manner; phosphorylated TP motifs in SAP155 compete for binding to the same NIPP1 FHA site. SAP155 kinases in cell lysates are blocked by EGTA and roscovitine (CDK inhibitor). SAP155 phosphorylation is dramatically increased during mitosis. |
GST pulldown, co-immunoprecipitation, phosphopeptide competition, kinase inhibition in cell lysates, mutagenesis |
The Journal of biological chemistry |
High |
12105215
|
| 2008 |
NIPP1 recruits PP1 to Sap155 (SF3B1) and promotes Sap155 dephosphorylation; NIPP1 stimulates Sap155 dephosphorylation by PP1 in vitro by facilitating their interaction. NIPP1 acts as a molecular sensor that recognizes hyperphosphorylated Sap155 through its FHA domain and dissociates after dephosphorylation, linking phosphorylation cycling of Sap155 to splicing regulation. |
Co-immunoprecipitation, in vitro phosphatase assays, siRNA knockdown of NIPP1, overexpression of truncated NIPP1 mutants, splicing assays |
The Journal of biological chemistry |
High |
18842582
|
| 2008 |
The p14–SF3b155 complex has two independent RNA-binding sites: a positively charged groove (requiring Tyr28 and Arg85 of p14) and the C-terminal extension of p14. SF3b155 residues Phe408, Tyr412, Val414, and Leu415 are critical contact points for complex formation with p14. |
NMR chemical shift perturbation, mutagenesis, in vitro binding assays |
Proteins |
High |
18076038
|
| 2010 |
p14 (SF3b14) specifically recognizes the branch adenosine within the bulged U2/branch-point duplex, with the branch nucleotide buried at the p14/SF3b155-peptide interface; this interaction must be disrupted before the first catalytic step of splicing. |
X-ray crystallography (adenine-p14/SF3b155 peptide complex), disulfide cross-linking of protein-RNA complexes, small-angle X-ray scattering (SAXS) |
RNA |
High |
21062891
|
| 2015 |
SF3B1 is strongly associated with nucleosomes at exonic positions in chromatin; disruption of this SF3B1–nucleosome association impairs splicing of short exons flanked by long introns. Co-IP and sedimentation analyses demonstrate SF3B1 physically associates with nucleosomal components, and ChIP-seq shows preferential binding at exonic nucleosomes with differential GC content. |
Co-immunoprecipitation, proteomic analysis, sedimentation analysis, ChIP-seq, RNA-seq, SF3B1–nucleosome binding disruption experiments |
Cell reports |
High |
25892229
|
| 2015 |
Cancer-associated SF3B1 hotspot mutations induce aberrant 3' splice site selection by utilizing a different (upstream) branch point sequence (BPS) compared to wild-type SF3B1. The mutant BPS requires the canonical 3' splice site to enable aberrant splicing during the second step. Approximately 50% of aberrantly spliced mRNAs are degraded by nonsense-mediated decay. |
RNA-seq analysis of cancer cell lines and patient samples, mutagenesis of predicted branchpoints, NMD inhibition experiments, isogenic cell line comparisons |
Cell reports |
High |
26565915
|
| 2016 |
SF3B1 R625/K666 cancer mutations act as change-of-function (not loss-of-function) mutants that promote alternative branchpoint usage, leading to aberrant 3' splice site selection; wild-type SF3B1 knockdown or overexpression does not reproduce the mutant splicing pattern. Mutagenesis of predicted branchpoints confirms that the mutant-specific splicing depends directly on alternative branchpoint utilization. |
RNA-seq of uveal melanoma, isogenic SF3B1-WT and mutant cell lines, SF3B1 knockdown/overexpression, branchpoint mutagenesis |
Nature communications |
High |
26842708
|
| 2016 |
SF3B1 inhibitors (three structurally distinct compounds) all interact with the same site on SF3B1 and interfere with splicing at multiple stages including both early spliceosome assembly and late exon ligation. Inactive analogs of each compound interchangeably compete with active inhibitors to restore splicing, supporting a shared pharmacophore model in which inhibition results not from binding alone but from inducing a conformational change in SF3B1. |
In vitro splicing assays, competition experiments with active and inactive inhibitor analogs, analysis at defined spliceosome assembly stages |
RNA |
High |
26742993
|
| 2016 |
SF3B1 HEAT-repeat mutations (yeast Hsh155 counterparts of human cancer mutations) directly alter the physical interaction between Hsh155 and the spliceosomal ATPase Prp5; this altered interaction changes the fidelity of branch-site (BS)–U2 duplex loading into the SF3B complex during prespliceosome formation, resulting in altered BS selectivity and splicing of suboptimal BS substrates. |
Yeast genetic analysis, in vitro direct binding assays (Hsh155–Prp5 interaction), splicing assays with nonconsensus BS pre-mRNAs, epistasis analysis of Hsh155 and Prp5 mutations |
Genes & development |
High |
28087715
|
| 2016 |
Sf3b1(K700E) knock-in mice develop macrocytic anemia due to terminal erythroid maturation defect and erythroid dysplasia; Sf3b1(K700E) myeloid progenitors show aberrant 3' splice-site selection associated with increased nonsense-mediated decay. Tet2 loss cooperates with Sf3b1(K700E) to worsen erythroid and LT-HSC phenotypes. |
Conditional knock-in mouse model, RNA-seq (aberrant splice site analysis), NMD pathway analysis, genetic epistasis (Sf3b1(K700E) × Tet2 loss), hematopoietic phenotyping |
Cancer cell |
High |
27622333
|
| 2017 |
SF3b1/Hsh155 mutations alter branchsite selection fidelity in yeast, changing how the spliceosome recognizes nonconsensus nucleotides at positions -2, -1, and +1 relative to the branchpoint adenosine. Different HSH155 alleles have disparate effects: some increase and others decrease fidelity of BS selection. The data support a model in which SF3B1 conformational changes promote U2 snRNA association with the BS to drive spliceosome assembly, acting independently of Prp5 ATPase in some contexts. |
Yeast genetic analysis, in vitro splicing assays with nonconsensus BS substrates, single-molecule fluorescence microscopy of spliceosome assembly |
Nucleic acids research |
High |
28062854
|
| 2019 |
Disease-causing SF3B1 hotspot mutations (K700E and others) reduce the level of SUGP1 in mutant spliceosomes. SUGP1 knockdown completely recapitulates SF3B1-mutant splicing errors. SUGP1 overexpression partially rescues aberrant splicing by driving SUGP1 back into mutant spliceosomes. SUGP1 plays an important role in branchsite recognition; loss of SF3B1–SUGP1 interaction is the common molecular defect of disease-causing SF3B1 mutations. |
Purification of wild-type and K700E mutant SF3B1 complexes followed by proteomics, SUGP1 knockdown and overexpression with RNA-seq, analysis across multiple SF3B1 hotspot mutants |
Molecular cell |
High |
31474574
|
| 2019 |
Cus2 (yeast) contains a UHM that binds Hsh155 (yeast SF3b1) through a conserved ULM, enforcing the first ATP-dependent step of pre-spliceosome formation. Disruption of this UHM–ULM interaction allows pre-spliceosome formation without ATP. Crystal structure of the human Tat-SF1 (Cus2 homolog) UHM bound to an Hsh155 ULM at 2.0 Å confirms the interaction is conserved between yeast and humans. |
Crystal structure determination (2.0 Å), mutagenesis of UHM/ULM motifs, yeast splicing extract complementation assays, in vitro binding assays |
RNA |
High |
31110137
|
| 2018 |
Conserved amino acids in SF3B1 (Hsh155) that contact the U2 snRNA backbone in the U2/branch-site duplex are nonessential; however, mutations in the branch-point adenosine-housing pocket, while viable, cause defects in splicing pre-mRNAs with nonconsensus BS sequences. Human SF3B1 HEAT repeats substituted into yeast Hsh155 chimeras confer pladienolide B sensitivity to yeast splicing and alter BS usage. |
Mutational analysis of yeast Hsh155 guided by spliceosome cryo-EM structures, in vitro splicing assays, yeast-human chimeric protein analysis, pladienolide B inhibition assays |
RNA |
High |
29752352
|
| 2019 |
In SF3B1-mutated MDS, mutant SF3B1 generates an alternative ERFE (erythroferrone) transcript in erythroblasts encoding a variant protein that retains capacity to suppress hepcidin transcription, leading to elevated plasma ERFE and iron overload in SF3B1-mutant MDS patients. |
RNA-seq identification of alternative ERFE transcript, induction in primary SF3B1-mutated erythroblasts, hepcidin suppression assays, plasma ERFE measurement |
Science translational medicine |
High |
31292266
|
| 2020 |
SF3B1 hotspot mutations promote decay of PPP2R5A (PP2A subunit) transcripts via aberrant splicing, increasing MYC S62 and BCL2 S70 phosphorylation, which stabilizes MYC protein and impairs apoptosis. Genetic PPP2R5A restoration or pharmacological PP2A activation impaired SF3B1-mutant tumorigenesis. |
RNA-seq across 98 tumors and 12 isogenic cell lines, regulatory network analysis, phosphoprotein analysis, genetic rescue (PPP2R5A restoration), pharmacological PP2A activation in mouse xenograft models |
Cancer discovery |
High |
32188705
|
| 2014 |
CAPERα (a UHM-containing alternative splicing factor) interacts with SF3b155 through a UHM/ULM interaction; crystal structure of the CAPERα UHM bound to a representative SF3b155 ULM at 1.7 Å resolution establishes SF3b155 as the relevant ULM-containing partner of CAPERα in human cell extracts. SF3b155 serves as a platform for coordinated recruitment of multiple UHM-containing splicing factors. |
X-ray crystallography (1.7 Å), isothermal titration calorimetry, pulldown from human cell extracts |
The Journal of biological chemistry |
High |
24795046
|
| 2022 |
CDK11 associates with SF3B1 and phosphorylates threonine residues at its N-terminus during spliceosome activation. This phosphorylation is important for SF3B1 association with U5 and U6 snRNAs in the activated (Bact) spliceosome. Inhibition of CDK11 with OTS964 prevents spliceosomal transition from precatalytic complex B to activated complex Bact, causing widespread intron retention. |
Co-immunoprecipitation (CDK11–SF3B1 association), in vitro kinase assays, OTS964 CDK11 inhibitor treatment, spliceosome complex analysis (B vs Bact), RNA-seq for intron retention, CLIP-seq for snRNA association |
Nature |
High |
36104565
|
| 2022 |
Coordinated missplicing of TMEM14C and ABCB7 by mutant SF3B1 (K700E) sequesters iron in mitochondria causing ring sideroblast (RS) formation in MDS. Functional rescue of both TMEM14C and ABCB7 expression nearly abolished RS formation in iPSC-derived erythroid cells, while rescue of PPOX alone had no effect. |
iPSC model of SF3B1-mutant MDS with in vitro erythroid differentiation, RNA-seq, functional rescue of TMEM14C and ABCB7, ring sideroblast quantification |
Blood |
High |
34861039
|
| 2022 |
SF3B1 K700E mutation induces mis-splicing of MAP3K7, leading to inactivation of the MAP3K7–p38 MAPK pathway, premature downregulation of GATA1, and accelerated erythroid differentiation followed by apoptosis, causing the anemia characteristic of SF3B1-mutant MDS. |
Isogenic SF3B1-WT and mutant cell lines, normal human CD34+ cells, MDS patient cells; p38 MAPK activity assays, GATA1 expression analysis, erythroid differentiation assays |
PNAS |
High |
34930825
|
| 2022 |
CDK12/13 promote the interaction of SF3B1 with Ser2-phosphorylated RNA polymerase II (RNAPII), facilitating SF3B1 association with chromatin and recruitment to 3' splice sites of promoter-proximal introns. CDK12/13 inhibition disrupts the SF3B1–RNAPII interaction and causes selective retention of promoter-proximal introns with weak 3' splice sites. |
Co-IP of SF3B1 with Ser2-phospho-RNAPII, CDK12/13 inhibitor (THZ531) treatment, ChIP-seq for SF3B1 chromatin association, nascent transcript analysis, RNA-seq for intron retention |
Nucleic acids research |
High |
37026485
|
| 2022 |
DHX15 is the RNA helicase required for SUGP1 function in branchpoint recognition. Cancer-causing SF3B1 mutations disrupt the SF3B1–SUGP1 interaction, indirectly depriving SUGP1 of its helicase partner DHX15. Crystal structure of DHX15–SUGP1 G-patch complex reveals the molecular basis of their direct interaction. A DHX15–SUGP1 G-patch fusion protein rescues splicing defects of mutant SF3B1. |
Protein-protein interaction assays (Co-IP, pulldown), crystal structure of DHX15–SUGP1 G-patch complex, RNA-seq, knockdown/overexpression of DHX15, DHX15–SUGP1 fusion rescue experiments |
PNAS |
High |
36459648
|
| 2023 |
Structural modeling and experimental validation show that two regions flanking the SUGP1 G-patch make numerous contacts with the SF3B1 region harboring cancer hotspot mutations. All cancer-associated mutations in these interface regions weaken or disrupt SF3B1–SUGP1 interaction and alter splicing. Structural modeling reveals that the SF3B1–SUGP1 interaction 'loops out' the G-patch for interaction with DHX15. |
Structural modeling (AlphaFold-based), mutagenesis of SF3B1–SUGP1 interface residues, Co-IP, RNA-seq for splicing analysis |
Genes & development |
High |
37977822
|
| 2022 |
SF3B1 K700E mutation promotes centromeric R-loop (cen-R-loop) accumulation, leading to increased chromosome oscillation, impaired chromosome segregation, altered spindle architecture, and aneuploidy. Aberrant splicing of genes involved in R-loop processing underlies cen-R-loop augmentation; overexpression of the normal (not mis-spliced) isoform mitigated mitotic stress. ATM deletion exaggerates these phenotypes. |
R-loop detection (DRIP), chromosome segregation analysis, spindle architecture imaging, isogenic cell lines with SF3B1 mutation, genetic epistasis with ATM deletion, isoform rescue experiments |
The Journal of clinical investigation |
High |
37463047
|
| 2023 |
Mis-splicing of COASY (coenzyme A synthase) by mutant SF3B1 depletes both CoA and succinyl-CoA in erythroblasts, impairing heme biosynthesis and erythropoiesis. Supplementation with vitamin B5 (COASY substrate) rescued CoA/succinyl-CoA concentrations in SF3B1-mutant cells and rescued erythropoiesis differentiation in primary MDS-RS patient cells. |
Splice variant analysis of COASY in patient samples, COASY silencing in erythroid cultures, CoA/succinyl-CoA metabolite measurement, vitamin B5 supplementation in isogenic cells and primary patient cells |
Science translational medicine |
High |
36857430
|
| 2024 |
Cancer-associated SF3B1 mutations reduce RNA polymerase II (RNAPII) elongation rate along gene bodies and decrease RNAPII density at promoters. The elongation defect results from disrupted pre-spliceosome assembly due to impaired protein–protein interactions of mutant SF3B1. Decreased promoter-proximal RNAPII density reduces chromatin accessibility and H3K4me3 at promoters. Sin3/HDAC/H3K4me pathway modulation reverses both transcription and chromatin changes. |
RNAPII ChIP-seq, chromatin accessibility (ATAC-seq), H3K4me3 ChIP-seq, isogenic cell lines, patient samples, mutant mouse model, unbiased epigenetic inhibitor screen |
Molecular cell |
High |
38521065
|
| 2024 |
GPATCH8 is required for mutant SF3B1-induced aberrant splicing activity. GPATCH8 interacts with the RNA helicase DHX15 and functionally opposes SUGP1 in branchpoint quality control. GPATCH8 silencing corrected approximately one-third of mutant SF3B1-dependent splicing defects and improved dysfunctional hematopoiesis in SF3B1-mutant mice and primary human progenitors. |
Synthetic intron screen to identify trans factors, Co-IP (GPATCH8–DHX15 interaction), GPATCH8 knockdown in isogenic cell lines and SF3B1-mutant mice, RNA-seq for splicing correction, hematopoiesis assays |
Molecular cell |
High |
38688280
|
| 2017 |
Upon genotoxic (alkylation) stress, Hsh155 (yeast SF3B1) disassembles from its spliceosomal partners and localizes to intranuclear and cytoplasmic protein quality control aggregates. This sequestration is regulated by molecular chaperones and requires TORC1 signaling through Sfp1 transcription factor, and is associated with intron retention in ribosomal protein gene transcripts and decreased splicing efficiency during stress recovery. |
Cytological screen, live cell imaging, genetic analysis (chaperone mutants, TORC1/Sfp1 pathway), RNA-seq for intron retention, stress recovery assays |
The Journal of cell biology |
Medium |
28978642
|
| 2022 |
Cancer-associated SF3B1 mutations disrupt the interaction between SF3B1 and DDX42 (and DDX46). Overexpression of DDX42 suppresses some SF3B1-mutation-associated aberrant splicing, and this suppression requires DDX42 ATP hydrolysis activity. |
Co-immunoprecipitation of WT and K700E SF3B1 complexes, DDX42 overexpression with RNA-seq for splicing correction, ATPase-dead DDX42 mutant analysis |
Journal of biochemistry |
Medium |
35652295
|
| 2013 |
SAP155 (SF3B1) physically interacts with FIR/FIRΔexon2 (a PUF60 splicing variant), forming a complex that bridges c-Myc transcription and P27 (CDKN1B) expression. SAP155/FIR/FIRΔexon2 knockdown reduces p27 expression and inhibits P27 pre-mRNA splicing, reducing CDK2/Cyclin E expression. |
Co-immunoprecipitation (SAP155–FIR/FIRΔexon2 complex), siRNA knockdown of SAP155/FIR, RT-PCR for P27 splicing, Western blot for CDK2/Cyclin E |
Molecular cancer research |
Medium |
23594796
|
| 2022 |
SF3B1 mutations lead to aberrant retention of full-length exon 6 of IRAK4, producing a longer IRAK4 isoform (IRAK4-long) containing the full death and kinase domains that maximally activates NF-κB. IRAK4-long expression in SF3B1-mutant cells induces TRAF6 activation and K63-linked ubiquitination of CDK2, causing a block in hematopoietic differentiation. IRAK4 inhibition with CA-4948 reduces NF-κB activation and improves myeloid differentiation. |
RNA-seq splicing analysis of SF3B1-mutant MDS samples, IRAK4 isoform functional assays, TRAF6/CDK2 ubiquitination assays, IRAK4 inhibitor in vitro differentiation and xenograft models |
eLife |
Medium |
36040792
|
| 2021 |
SF3B1 protein is stabilized via deubiquitination (post-translational stabilization of the U2 complex component SF3B1). SF3B1 inhibition blocks T-ALL growth in vivo, perturbs exon skipping leading to NMD-mediated reduction of CHEK2 transcripts, and impairs DNA damage response. SF3B1 inhibition also leads to a general decrease in R-loop formation. |
In vivo T-ALL mouse model with SF3B1 inhibitor treatment, deubiquitination assays for SF3B1 stability, RNA-seq for exon skipping/NMD analysis, CHEK2 protein/transcript analysis, R-loop detection |
Science advances |
Medium |
35061527
|
| 2023 |
ALKBH5-driven 5' UTR m6A demethylation fine-tunes SF3B1 translation, and SF3B1 protein abundance levels dynamically regulate MDS-to-leukemia progression in vivo. Changes in SF3B1 levels affect splicing of central DNA repair and epigenetic regulators. |
m6A sequencing, ALKBH5 manipulation in human and murine pre-leukemic MDS cells, SF3B1 translation reporter assays, in vivo MDS-to-leukemia progression monitoring |
Molecular cell |
Medium |
36944332
|
| 2021 |
SF3B1 physically interacts with HIF1α, facilitating binding of the HIF1 complex to hypoxia response elements (HREs) to activate target gene expression. SF3B1 is a HIF-1 target gene, forming a positive feedback loop. Monoallelic Sf3b1 deletion impedes tumor formation and progression via impaired HIF signaling in a mouse pancreatic cancer model. |
Co-IP of SF3B1 with HIF1α, chromatin immunoprecipitation (HIF1 complex binding to HREs), Sf3b1 monoallelic deletion in mouse pancreatic cancer model, tumor formation assays |
Cell reports |
Medium |
36001976
|
| 1998 |
Fission yeast prp10+ (SF3B1 ortholog) is essential for viability and encodes a protein homologous to human SAP155. Prp10p-GFP localizes predominantly to the nuclear DNA region. The N-terminal ~300 amino acids are dispensable for viability, unlike the conserved C-terminal region containing HEAT repeats. |
Complementation cloning, gene disruption, GFP fusion localization, deletion analysis |
Nucleic acids research |
Medium |
9837997
|
| 2012 |
SAP155 (SF3B1) knockdown generates FIRΔexon2 and novel FIR splicing variants (Δ3, Δ4) that lack c-Myc transcriptional repression activity; these variants are found in human colorectal cancer tissues, establishing a role for SAP155 in regulation of FIR pre-mRNA splicing and c-Myc transcriptional control. |
siRNA knockdown of SAP155 in cell lines, RT-PCR identification of FIR splice variants, colorectal cancer tissue analysis |
Cancer science |
Low |
23113893
|
| 2011 |
SF3B1 inhibitor treatment in HNSCC cells promotes generation of pro-apoptotic MCL1-S splice variant while diminishing anti-apoptotic MCL1-L variant, via SF3B1-dependent splicing regulation of MCL1 pre-mRNA. SF3B1 is also involved in the splicing of HPV16 E6 to produce the non-oncogenic E6* isoform. |
RT-PCR and Western blot for MCL1 splice variants upon meayamycin B (SF3B1 inhibitor) treatment, apoptosis assays, pharmacological SF3B1 inhibition |
Scientific reports |
Low |
25139387
|