| 2013 |
hnRNPA2B1 specifically binds exosomal miRNAs through recognition of specific sequence motifs (EXO motifs), controlling their loading into exosomes. In exosomes, hnRNPA2B1 is sumoylated, and sumoylation controls its binding to miRNAs. Mutagenesis of identified motifs or changes in hnRNPA2B1 expression levels modulate miRNA loading into exosomes. |
RNA immunoprecipitation, sumoylation assays, mutagenesis of miRNA motifs, modulation of hnRNPA2B1 expression |
Nature communications |
High |
24356509
|
| 2015 |
HNRNPA2B1 binds m6A-bearing RNAs in vivo and in vitro with a biochemical footprint matching the m6A consensus motif, acting as a nuclear reader of the m6A mark. It mediates alternative splicing of nuclear transcripts similarly to the m6A writer METTL3, binds m6A marks in primary miRNA transcripts, interacts with the Microprocessor complex protein DGCR8, and promotes primary miRNA processing. |
RNA immunoprecipitation (in vivo and in vitro), alternative splicing assays, HNRNPA2B1 and METTL3 knockdown with pri-miRNA processing readout, Co-IP with DGCR8 |
Cell |
High |
26321680
|
| 2013 |
Pathogenic missense mutations in the prion-like domain (PrLD) of hnRNPA2B1 (e.g., D290V) strengthen a steric zipper motif, exacerbating formation of self-seeding fibrils that cross-seed wild-type hnRNP polymerization. Wild-type hnRNPA2 shows intrinsic tendency to assemble into self-seeding fibrils. Disease mutations promote excess incorporation into stress granules and drive cytoplasmic inclusion formation in animal models. |
Fibril assembly assays, seeding experiments, stress granule imaging in cells and animal models, mutagenesis |
Nature |
High |
23455423
|
| 2018 |
The hnRNPA2 low-complexity (LC) domain is compact and intrinsically disordered as a monomer and retains predominant disorder in a liquid-liquid phase-separated form. Disease mutations D290V and P298L induce aggregation by enhancing and extending the aggregation-prone region respectively. The hnRNPA2 LC domain directly interacts with and induces phase separation of TDP-43. Arginine methylation reduces hnRNPA2 phase separation by disrupting arginine-mediated contacts. |
NMR spectroscopy, in vitro phase separation assays, mutagenesis, arginine methylation assays |
Molecular cell |
High |
29358076
|
| 2019 |
Upon DNA virus infection, nuclear hnRNPA2B1 senses viral DNA, homodimerizes, and is then demethylated at arginine-226 by the arginine demethylase JMJD6. This leads to hnRNPA2B1 translocation to the cytoplasm where it activates the TBK1-IRF3 pathway, inducing IFN-α/β production. Additionally, hnRNPA2B1 facilitates m6A modification and nucleocytoplasmic trafficking of CGAS, IFI16, and STING mRNAs to amplify cytoplasmic antiviral signaling. |
Co-IP, demethylation assays identifying JMJD6 as writer/eraser, nuclear-cytoplasmic fractionation, TBK1-IRF3 pathway activation assays, m6A RIP on CGAS/IFI16/STING mRNAs |
Science (New York, N.Y.) |
High |
31320558
|
| 2015 |
The LC domain of hnRNPA2 adopts a similar conformation in hydrogel polymers, liquid-like droplets, and isolated nuclei, forming amyloid-like cross-β fibers. A molecular footprinting technique applied to native hnRNPA2 in isolated nuclei showed its LC domain exists in a similar polymeric conformation to recombinant polymers, suggesting biologic utility for LC domain polymerization in information transfer. |
Molecular footprinting of polymeric LC domain state, hydrogel polymer preparation, electron microscopy, analysis of isolated nuclei |
Cell |
High |
26544936
|
| 2016 |
Transcriptome-wide CLIP in mouse spinal cord identified UAGG motifs enriched within ~2,500 hnRNP A2/B1 binding sites and revealed a role for hnRNP A2/B1 in alternative polyadenylation. hnRNP A2/B1 loss causes alternative splicing changes including skipping of an exon in ALS-associated D-amino acid oxidase (DAO) that reduces D-serine metabolism. ALS-associated D290V mutant shows increased nuclear-insoluble hnRNP A2/B1 and abnormal splicing in patient fibroblasts and iPSC-derived motor neurons. |
CLIP-seq in mouse spinal cord, RNA-seq upon KD, patient fibroblast and iPSC-MN analysis, nuclear fractionation |
Neuron |
High |
27773581
|
| 2020 |
CryoEM structure of the hnRNPA2 LCD fibril core revealed chains kinked in a cross-β conformation enabling non-covalent cross-linking of fibrils, distinguishing them from pathogenic amyloid. The D290V disease mutation fundamentally alters fibril structure to a more stable energetic state, as shown by crystal structure of the D290V-containing segment forming a steric zipper. |
CryoEM structure determination, crystal structure of D290V segment, hydrogel formation assay, energetic calculations |
Nature communications |
High |
32796831
|
| 2018 |
Solid-state NMR with segmental isotope labeling showed that both wild-type hnRNPA2 LC and the D290V mutant form labile polymers in an in-register cross-β conformation. Aspartic acid 290 is charged at physiological pH and immobilized within the polymer core; D290V mutation removes destabilizing electrostatic interactions, making polymers thermodynamically more stable. |
Solid-state NMR spectroscopy with segmental isotope labeling, electron microscopy, thermodynamic stability measurements |
Proceedings of the National Academy of Sciences of the United States of America |
High |
30279180
|
| 2021 |
Optogenetically induced tau oligomers (oTau) associate with HNRNPA2B1 (identified by proteomics and validated in neurons, animal models, and human Alzheimer brain). HNRNPA2B1 functions as a linker connecting oTau with m6A-modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau from associating with m6A or reducing protein synthesis and reduces oTau-induced neurodegeneration. |
Optogenetic tau oligomerization (Cry2-based), proteomics, Co-IP in neurons and animal models, HNRNPA2B1 knockdown with neurodegeneration readout, m6A association assay |
Molecular cell |
High |
34453888
|
| 2014 |
HNRNPA2B1 (hnRNP A2 and B1 proteins encoded by HNRNPA2B1) interacts with oncogenic KRAS G12V in PDAC cells as shown by mass spectrometry and Co-IP. This interaction requires KRAS phosphorylation at serine 181. Knockdown of HNRNPA2B1 inactivates AKT-mTOR signaling, reduces interaction between KRAS and PI3K, and reduces KRAS-dependent PDAC cell survival and tumor formation. |
Mass spectrometry pulldown, Co-IP, Phos-tag phosphorylation analysis, shRNA knockdown, xenograft tumor models |
Gastroenterology |
High |
24998203
|
| 2018 |
The SH3 domain of Fyn kinase (Fyn-SH3) interacts with the hnRNPA2 low-complexity domain despite hnRNPA2 lacking canonical SH3-binding sequences. Fyn-SH3 induces hnRNPA2 LC phase separation and is incorporated into in vitro phase-separated granules. NMR identified hnRNPA2 LC interaction sites on the surface of Fyn-SH3. |
In vitro microscopy, solution NMR spectroscopy, in vitro phase separation assays |
The Journal of biological chemistry |
High |
30397184
|
| 2020 |
In vitro tyrosine phosphorylation of hnRNPA2 by Fyn reduces hnRNPA2 phase separation, prevents partitioning of hnRNPF and ch-TOG into hnRNPA2 LC droplets, and decreases aggregation of hnRNPA2 disease variants. Transport granule components hnRNPF and ch-TOG interact weakly with hnRNPA2 but partition specifically into LC droplets. Expression of Fyn kinase in C. elegans reduces neurodegeneration associated with chimeric hnRNPA2 D290V. |
In vitro phase separation assays, tyrosine phosphorylation assays, C. elegans neurodegeneration model with Fyn expression, NMR |
The EMBO journal |
High |
33349959
|
| 2016 |
Drosophila model expressing disease-homologous hnRNPA2B1 mutations (Hrb98DE) in fly muscle causes progressive cytoplasmic inclusion pathology containing stress granule marker ROX8 and additional RNA-binding proteins including TDP-43. Overexpression of DNAJB6/MRJ rescues inclusion formation and prevents RBP aggregation after heat shock through a physical interaction; wild-type but not disease-mutant MRJ interacted with RBPs after heat shock. |
Drosophila genetic model with disease-homologous mutations, immunofluorescence for inclusions, genetic epistasis (MRJ overexpression/KO), co-immunoprecipitation after heat shock |
Human molecular genetics |
High |
26744327
|
| 2022 |
Heterozygous frameshift variants in HNRNPA2B1 that extend the reading frame with a novel neomorphic C-terminal sequence (escaping NMD and translated) have reduced affinity for the nuclear import receptor karyopherin β2, resulting in cytoplasmic accumulation of hnRNPA2 protein in cells and animal models, causing early-onset oculopharyngeal muscular dystrophy. |
Frameshift variant characterization, nuclear import receptor binding assay (karyopherin β2), cellular localization by immunofluorescence, animal models |
Nature communications |
High |
35484142
|
| 2023 |
SUMOylated HNRNPA2B1 (HNRNPA2B1SUMO) acts as an endogenous inhibitor of RPA during normal DNA replication. HNRNPA2B1SUMO associates with RPA through recognizing the SUMO-interacting motif (SIM) of RPA, inhibiting RPA accumulation at replication forks and impeding local ATR activation. DNA damage reduces HNRNPA2B1SUMO, releasing nuclear soluble RPA to chromatin and enabling ATR activation. HNRNPA2B1 hinders homologous recombination repair by limiting RPA availability. |
Co-IP identifying SIM-mediated interaction, chromatin fractionation, ATR activation assays, HR repair assays, PARP inhibitor sensitivity assays |
Molecular cell |
High |
36702126
|
| 2020 |
Solution NMR showed that the two RRMs of hnRNPA2 move independently in solution without RNA. hnRNPA2 RRMs bind the minimal A2RE11 RNA weakly, with NMR shifts in both RRMs upon binding. Short A2RE RNAs or longer RNAs containing this sequence completely prevent in vitro phase separation of full-length hnRNPA2 and aggregation of disease-associated mutants. |
Solution NMR spectroscopy, biophysical RNA binding assays, in vitro phase separation assays with RNA addition |
Nucleic acids research |
High |
32870271
|
| 2011 |
In pancreatic cancer cells, inhibition of Fyn kinase activity downregulated hnRNPA2B1 expression. hnRNPA2B1 binds Bcl-x mRNA and affects its splicing, promoting formation of anti-apoptotic Bcl-xL (downregulation of hnRNPA2B1 increased pro-apoptotic Bcl-xS formation and apoptosis). Overexpression of hnRNPA2B1 rescued cells from apoptosis. |
Kinase-dead Fyn expression, RNA interference knockdown, Bcl-x splicing assay by RT-PCR, apoptosis assays |
Carcinogenesis |
Medium |
21642356
|
| 2010 |
Under mitochondrial respiratory stress, Akt1 phosphorylates hnRNPA2, and this phosphorylation is a crucial step for recruitment of hnRNPA2 as a transcriptional coactivator to stress target promoters (including NFκB/cRel:p50, C/EBPδ, CREB, NFAT pathways), culminating in transcription activation of nuclear genes including Cathepsin L, RyR1, Glut4 and Akt1. |
In vivo phosphorylation assays, chromatin immunoprecipitation at stress target promoters, transcription activation assays with dominant-negative constructs |
Biochimica et biophysica acta |
Medium |
20153290
|
| 2015 |
hnRNPA2/B1 binds the COX-2 core promoter to activate COX-2 expression in non-small-cell lung cancer. hnRNPA2/B1 interacts directly with the transcriptional co-activator p300, which acetylates hnRNPA2/B1. Acetylation by p300 (requiring its HAT domain) enhances hnRNPA2/B1 binding to the COX-2 promoter and promotes COX-2 expression and tumor growth. |
ChIP (promoter binding), Co-IP (hnRNPA2B1-p300 interaction), acetylation assays with p300 HAT domain deletion mutant, shRNA/siRNA knockdown with functional readouts |
Molecular oncology |
Medium |
26774881
|
| 2018 |
hnRNPA2 functions as a lysine acetyltransferase (KAT) that acetylates histone H4 at lysine 8 (H4K8) at telomeres under mitochondrial dysfunction. This H4K8 acetylation is associated with telomere attrition. Expression of a KAT-mutant hnRNPA2 rescued telomere length, suggesting impaired H4K8 acetylation is responsible. |
KAT activity assay, histone acetylation assay (H4K8), telomere length measurement, KAT-mutant hnRNPA2 expression rescue |
PloS one |
Medium |
30427907
|
| 2019 |
hnRNPA2B1 binds the 3'-UTR of HIF-1α mRNA through its C-terminal glycine-rich domain, promoting HIF-1α translation. The small molecule MO-460 inhibits initiation of HIF-1α translation by binding to the C-terminal glycine-rich domain of hnRNPA2B1 and blocking its binding to HIF-1α mRNA 3'-UTR. |
RNA immunoprecipitation showing hnRNPA2B1-HIF-1α mRNA 3'UTR interaction, chemical proteomics identifying MO-460 binding site, translation assays |
Experimental & molecular medicine |
Medium |
30755586
|
| 2019 |
M1 muscarinic receptor signaling controls hnRNPA2/B1 protein levels by regulating mRNA translation via nonsense-mediated decay regulation, not by altering mRNA levels, protein aggregation, or degradation. Genetic mouse models with decreased or increased cholinergic tone show corresponding changes in hnRNPA2/B1 protein levels. |
Genetic mouse models (cholinergic tone manipulation), M1 muscarinic receptor knockout, translation assays, NMD pathway analysis |
The Journal of neuroscience |
Medium |
27277805
|
| 2019 |
hnRNPA2/B1 localization shifts from nucleus to cytoplasm during mammalian embryonic development, regulated by METTL3-dependent m6A RNA methylation. METTL3 KD blastocysts show increased mislocalization of hnRNPA2/B1, and hnRNPA2/B1 KD causes developmental arrest after the 4-cell stage with decreased OCT4 and SOX2 inner cell mass markers. |
Immunofluorescence localization in embryos, hnRNPA2/B1 and METTL3 knockdown with developmental readout, RNA-seq in KD blastocysts |
Scientific reports |
Medium |
31201338
|
| 2020 |
In uninfected HEp-2 cells, hnRNPA2B1 is localized in the nucleus and is not a component of exosomes. Upon HSV-1 infection, hnRNPA2B1 is quantitatively exported to the cytoplasm where a fraction colocalizes with a Golgi marker. In ΔhnRNPA2B1 cells, there is a >10-fold reduction in HSV-1 released through the apical surface, but no significant impact on basolateral cell-to-cell transfer. |
Subcellular fractionation, immunofluorescence colocalization with Golgi marker, hnRNPA2B1 knockout cells, viral yield quantification |
Journal of virology |
Medium |
32295924
|
| 2020 |
Epirubicin disrupts the interaction between hnRNPA2B1 and miR-503 in endothelial cells, leading to hnRNPA2B1 relocalization to the nucleus while miR-503 and ANXA2 are sorted into exosomes. hnRNPA2B1 negatively regulates exosomal sorting of miR-503, establishing that RNA-binding proteins can inhibit exosomal miRNA export. |
Biotinylated miR-503 pulldown with mass spectrometry identification, western blotting validation, knockdown systems with pulldown analysis, localization assays |
Cellular and molecular life sciences |
Medium |
31894362
|
| 2024 |
hnRNPA2B1 is associated with stress granules (SGs) and represses their disassembly. hnRNPA2B1 absence specifically enhances arsenite-induced SG disassembly via the ubiquitin-proteasome system (not autophagy). hnRNPA2B1 interacts with core SG proteins G3BP1, G3BP2, USP10, and Caprin-1; its depletion reduces the G3BP1-USP10/Caprin-1 interaction and elevates G3BP1 ubiquitination. Hnrnpa2b1 KO in mice causes Sertoli cell-only syndrome and complete male infertility. |
Co-IP identifying SG protein interactions, ubiquitination assays, proteasome inhibitor experiments, autophagy inhibitor experiments, Hnrnpa2b1 KO mouse model with fertility phenotype |
Cell reports |
High |
38363675
|
| 2022 |
In PAH pulmonary arterial smooth muscle cells, hnRNPA2B1 expression and nuclear localization are increased. hnRNPA2B1 promotes expression of mRNAs carrying three defined binding motifs involved in different aspects of the cell cycle. RNA immunoprecipitation confirmed binding to target mRNAs. hnRNPA2B1 silencing decreased target mRNA levels and reduced proliferation and resistance to apoptosis in PAH-PASMC. In vivo hnRNPA2B1 inhibition in lungs rescued pulmonary hypertension in rats. |
RNA immunoprecipitation, bioinformatics motif analysis, hnRNPA2B1 silencing with proliferation/apoptosis readouts, immunofluorescence localization, monocrotaline rat model |
Circulation |
Medium |
35993245
|
| 2024 |
hnRNPA2B1 mediates nuclear export of m6A-tagged mRNAs through the ALYREF/NXF1 complex. ISGylation of hnRNPA2B1 (mediated by PCAT6 serving as scaffold between ISG15 and hnRNPA2B1) protects hnRNPA2B1 from ubiquitination-mediated proteasomal degradation, enhancing its ability to selectively export m6A-modified mRNAs. |
Co-IP (PCAT6-ISG15-hnRNPA2B1 complex, hnRNPA2B1-ALYREF/NXF1), ISGylation assay, ubiquitination assay, nuclear mRNA export assay, hnRNPA2B1 knockdown |
Advanced science (Weinheim, Baden-Wurttemberg, Germany) |
Medium |
38626369
|
| 2022 |
hnRNPA2B1 mediates microRNA processing (specifically miR-92a-2-5p and miR-373-3p) via interaction with DGCR8 (confirmed by Co-IP). These processed miRNAs are transported in exosomes to recipient monocytes or mesenchymal stem cells to activate osteoclastogenesis and suppress osteoblastogenesis by inhibiting IRF8 or RUNX2. |
RNA pull-down, RIP assays for hnRNPA2B1-pri-miRNA interaction, Co-IP for hnRNPA2B1-DGCR8, exosome isolation and characterization, luciferase assay for miRNA targets |
Theranostics |
Medium |
36451863
|
| 2020 |
HNRNPA2B1 interacts with KRAS mRNA and facilitates its nuclear export and translation in colorectal cancer. The lncRNA CRNDE maintains HNRNPA2B1 protein stability by inhibiting E3 ubiquitin ligase TRIM21-mediated K63 ubiquitination-dependent degradation. The CRNDE/hnRNPA2B1 axis activates MAPK signaling through KRAS. |
RNA immunoprecipitation for KRAS mRNA binding, nuclear export assay, ubiquitination assay identifying TRIM21 as E3 ligase, Co-IP, CRISPR KO experiments |
Cell death & disease |
Medium |
37716979
|
| 2020 |
Linc01232 physically interacts with the RNA recognition motif 2 domain of HNRNPA2B1 (680-890 nt fragment) and inhibits its ubiquitin-mediated degradation, stabilizing HNRNPA2B1. Stabilized HNRNPA2B1 participates in alternative splicing of A-Raf, regulating the MAPK/ERK signaling pathway. |
RNA pull-down, RIP assays, domain mapping of HNRNPA2B1 interaction region, ubiquitination assays, RNA-seq for alternative splicing |
Cancer letters |
Medium |
32814086
|
| 2022 |
hnRNPA2/B1 regulates copper homeostasis by modulating the abundance of Cu(I)-transporter ATP7A via the 3' UTR of the ATP7A transcript in an isoform-dependent manner. Downregulation of B1 and B1b isoforms is sufficient to elevate ATP7A, while overexpression of either hnRNPA2 or hnRNPB1 isoforms decreases ATP7A mRNA levels. |
siRNA knockdown of specific isoforms, isoform-specific overexpression, 3'UTR reporter assay, mRNA and protein quantification, copper level measurement |
Frontiers in molecular biosciences |
Medium |
36545508
|
| 2025 |
hnRNPA2B1 is a sensor for the metabolite adenine in the nucleus. Adenine directly binds and activates hnRNPA2B1, which is then recruited to Il1b enhancers. hnRNPA2B1 increases Il1b enhancer chromatin accessibility by binding and recruiting nucleolin and the demethylase FTO to mediate Il1b enhancer DNA N6-methyladenosine (6mA) demethylation, thereby increasing IL-1β production during bacterial infection. |
Large-scale metabolite-hnRNPA2B1 interaction screen, direct binding assay (adenine-hnRNPA2B1), ChIP at Il1b enhancers, chromatin accessibility assay, Co-IP with nucleolin and FTO, myeloid-specific cKO mice with bacterial infection |
Cell metabolism |
High |
39814017
|
| 2022 |
A hnRNPA2B1 agonist compound PAC5 binds near Asp49 in the RNA recognition motif of hnRNPA2B1, activating it and promoting its translocation to the cytoplasm where it initiates the TBK1-IRF3 pathway, leading to type I IFN production with antiviral activity against HBV and SARS-CoV-2. |
Binding site characterization by structural analysis (near Asp49 in RRM), nuclear-cytoplasmic fractionation, TBK1-IRF3 activation assay, in vivo HBV and hamster SARS-CoV-2 models |
Protein & cell |
Medium |
36726760
|
| 2024 |
hnRNPA2B1 stabilizes SREBP2 mRNA via m6A modification and similarly stabilizes LDLR mRNA in an m6A-dependent manner, triggering de novo cholesterol synthesis through HMGCR induction and promoting glioma stemness. |
RNA immunoprecipitation for SREBP2/LDLR mRNA binding, m6A MeRIP sequencing, RNA stability assay, hnRNPA2B1 ablation with transcriptome and lipidomic readouts |
Neuro-oncology |
Medium |
38070488
|
| 2017 |
HNRNPA2B1 mediates exclusion of cassette exon 11 from MST1R pre-mRNA (validated by minigene model), generating the RON∆165 isoform that activates Akt/PKB signaling in head and neck cancer. Depletion of HNRNPA2B1 by CRISPR/Cas9 causes exon 11 inclusion, reducing RON∆165 and inhibiting Akt/PKB signaling, leading to reduced EMT. |
CRISPR/Cas9 knockout, MST1R-minigene splicing assay, isoform-specific RT-PCR, Akt/PKB signaling assays |
Laboratory investigation |
Medium |
32669614
|
| 2017 |
Nm23-H1 increases the protein stability of hnRNPA2/B1 and both are co-recruited to the 5'UTR of Sp1 mRNA to regulate its cap-independent (IRES-mediated) translational activity in lung cancer cells. |
Co-IP of Nm23-H1 and hnRNPA2/B1, RNA immunoprecipitation of 5'UTR of Sp1 mRNA, IRES-based reporter assay, protein stability assay |
Scientific reports |
Medium |
28831131
|
| 2014 |
hnRNP-A2/B1 binds directly to the ASCL1 mRNA 5'- and 3'-UTRs (identified by RNA pulldown and MALDI/TOF-MS) and functions as a key positive regulator of ASCL1 expression. Downregulation of hnRNP-A2/B1 during hypoxia is associated with post-transcriptional suppression of hASH1 synthesis. |
RNA pulldown with MALDI/TOF-MS identification, reporter gene assays for 5'- and 3'-UTR function, siRNA knockdown, hypoxia exposure |
The Journal of biological chemistry |
Medium |
25124043
|
| 2023 |
CSNK1D (casein kinase 1 delta) phosphorylates HNRNPA2B1 to enhance its stability. Phosphorylated/stabilized HNRNPA2B1 promotes maturation of miR-25-3p and miR-93-5p by recognizing m6A marks on primary miR-25/93 transcripts. miR-93-5p targets BAMBI to activate TGF-β pathway; miR-25-3p targets FOXO3 to inactivate FOXO pathway. |
Mass spectrometry identifying CSNK1D as kinase, phosphorylation and stability assays, m6A RIP for pri-miRNA binding, pri-miRNA processing assay |
Cellular and molecular life sciences |
Medium |
37208565
|
| 2013 |
PARP1 and HNRNPA2B1 specifically bind DNA sequences at the termini of 'forum domains' — chromosomal regions of 50-250 kb flanked by DNA double-strand break hot spots that contain coordinately expressed genes, suggesting a structural role in coordinated transcription of gene clusters. |
Genome-wide mapping of blunt-ended DSBs, ChIP-seq for PARP1 and HNRNPA2B1 binding at domain termini |
PLoS genetics |
Medium |
23593027
|
| 2024 |
hnRNPA2B1 interacts with PABPC1, and this complex coordinates with the cap-binding eIF4F complex to facilitate translation of CIP2A, DLAT, and GPX1 mRNAs independent of m6A modification in gastric cancer cells. H. pylori infection induces hnRNPA2B1 upregulation through NF-κB recruitment to its promoter. |
Mass spectrometry and Co-IP for hnRNPA2B1-PABPC1 interaction, Ribo-seq and polysome profiling for translational regulation, RIP-seq for mRNA targets, m6A epitranscriptomic microarray |
Advanced science (Weinheim, Baden-Wurttemberg, Germany) |
Medium |
38887155
|