The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“When analyzing the RNA sequence motifs enriched for hnRNPA2B1 binding from the eCLIP experiments in WT and MAPT knockout backgrounds, we detected the known hnRNPA2B1 binding motif, UAGG 34 , overall and for binding windows that overlap with 3'UTRs ( Figure 3B ).”
From Tau is an m 6 A-associated RNA binding protein that causes RNA dysregulation in disease (2026) · cites this paper as [34]
In the citing paper
“Expression or mislocalization of HNRNPA2B1 is also prominent in ALS, muscular diseases and cancers (Martinez et al., 2016) (Kataoka et al., 2015; Pinkus et al., 2014).”
From Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy (2021) · cites this paper as Martinez et al., 2016
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875
Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling
Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620
HNRNPA2B1 Is a Mediator of m6A-Dependent Nuclear RNA Processing Events
Alarcón, C. R., Goodarzi, H., Lee, H., Liu, X., Tavazoie, S., & Tavazoie, S. F. (2015) · Cell · doi:10.1016/j.cell.2015.08.011 · Cited by 1,514
Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335
Self-citationExome Sequencing Reveals VCP Mutations as a Cause of Familial ALS
Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235
Self-citationMolecular biology of amyotrophic lateral sclerosis: insights from genetics
Pasinelli, P., & Brown, R. H. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1971 · Cited by 1,107
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966
Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges
Lovci, M. T., Ghanem, D., Marr, H., Arnold, J., Gee, S., Parra, M., Liang, T. Y., Stark, T. J., Gehman, L. T., Hoon, S., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2699 · Cited by 385
Self-citation
Research works printed but not linked: 54
- Ainger, 1997, Transport and localization elements in myelin basic protein mRNA, J. Cell Biol., 138, 1077, 10.1083/jcb.138.5.1077 · DOI
- Belzil, 2013, RNA-mediated toxicity in neurodegenerative disease, Mol. Cell. Neurosci., 56, 406, 10.1016/j.mcn.2012.12.006 · DOI
- Berson, 2012, Cholinergic-associated loss of hnRNP-A/B in Alzheimer’s disease impairs cortical splicing and cognitive function in mice, EMBO Mol. Med., 4, 730, 10.1002/emmm.201100995 · DOI
- Burkhardt, 2013, A cellular model for sporadic ALS using patient-derived induced pluripotent stem cells, Mol. Cell. Neurosci., 56, 355, 10.1016/j.mcn.2013.07.007 · DOI
- Burnet, 2008, D-amino acid oxidase activity and expression are increased in schizophrenia, Mol. Psychiatry, 13, 658, 10.1038/mp.2008.47 · DOI
- Clower, 2010, The alternative splicing repressors hnRNP A1/A2 and PTB influence pyruvate kinase isoform expression and cell metabolism, Proc. Natl. Acad. Sci. USA, 107, 1894, 10.1073/pnas.0914845107 · DOI · Paper page
- Couthouis, 2011, A yeast functional screen predicts new candidate ALS disease genes, Proc. Natl. Acad. Sci. USA, 108, 20881, 10.1073/pnas.1109434108 · DOI
- Du, 2015, Generation and expansion of highly pure motor neuron progenitors from human pluripotent stem cells, Nat. Commun., 6, 6626, 10.1038/ncomms7626 · DOI
- Fähling, 2006, Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, alpha (I) mRNA stability, J. Biol. Chem., 281, 9279, 10.1074/jbc.M510925200 · DOI
- Horiike, 1994, D-amino-acid oxidase is confined to the lower brain stem and cerebellum in rat brain: regional differentiation of astrocytes, Brain Res., 652, 297, 10.1016/0006-8993(94)90240-2 · DOI
- Huelga, 2012, Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins, Cell Rep., 1, 167, 10.1016/j.celrep.2012.02.001 · DOI · Paper page
- Huppertz, 2014, iCLIP: protein-RNA interactions at nucleotide resolution, Methods, 65, 274, 10.1016/j.ymeth.2013.10.011 · DOI
- Hutchison, 2002, Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor, J. Biol. Chem., 277, 29745, 10.1074/jbc.M203633200 · DOI
- Iguchi, 2013, Loss of TDP-43 causes age-dependent progressive motor neuron degeneration, Brain, 136, 1371, 10.1093/brain/awt029 · DOI
- Kabashi, 2008, TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis, Nat. Genet., 40, 572, 10.1038/ng.132 · DOI · Paper page
- Kapeli, 2016, Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses, Nat. Commun., 7, 12143, 10.1038/ncomms12143 · DOI
- Kawazoe, 2006, Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring, Protein Sci., 15, 2708, 10.1110/ps.062421606 · DOI
- Kedersha, 2000, Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules, J. Cell Biol., 151, 1257, 10.1083/jcb.151.6.1257 · DOI
- Kim, 2013, Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS, Nature, 495, 467, 10.1038/nature11922 · DOI
- Kosturko, 2006, Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs, Mol. Biol. Cell, 17, 3521, 10.1091/mbc.E05-10-0946 · DOI
- Kosuge, 2009, Characterization of chronic glutamate-mediated motor neuron toxicity in organotypic spinal cord culture prepared from ALS model mice, Neurosci. Lett., 454, 165, 10.1016/j.neulet.2009.03.017 · DOI
- Lagier-Tourenne, 2010, TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration, Hum. Mol. Genet., 19, R46, 10.1093/hmg/ddq137 · DOI · Paper page
- Lagier-Tourenne, 2012, Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs, Nat. Neurosci., 15, 1488, 10.1038/nn.3230 · DOI
- Lalmansingh, 2011, TDP-43 is a transcriptional repressor: the testis-specific mouse acrv1 gene is a TDP-43 target in vivo, J. Biol. Chem., 286, 10970, 10.1074/jbc.M110.166587 · DOI
- Lambert, 2014, RNA Bind-n-Seq: quantitative assessment of the sequence and structural binding specificity of RNA binding proteins, Mol. Cell, 54, 887, 10.1016/j.molcel.2014.04.016 · DOI
- Liu-Yesucevitz, 2010, Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue, PLoS ONE, 5, e13250, 10.1371/journal.pone.0013250 · DOI
- Mackenzie, 2007, Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations, Ann. Neurol., 61, 427, 10.1002/ana.21147 · DOI · Paper page
- McGlincy, 2010, Expression proteomics of UPF1 knockdown in HeLa cells reveals autoregulation of hnRNP A2/B1 mediated by alternative splicing resulting in nonsense-mediated mRNA decay, BMC Genomics, 11, 565, 10.1186/1471-2164-11-565 · DOI
- Mitchell, 2010, Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase, Proc. Natl. Acad. Sci. USA, 107, 7556, 10.1073/pnas.0914128107 · DOI
- Mohagheghi, 2016, TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor, Hum. Mol. Genet., 25, 534, 10.1093/hmg/ddv491 · DOI
- Molliex, 2015, Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization, Cell, 163, 123, 10.1016/j.cell.2015.09.015 · DOI · Paper page
- Paul, 2014, The role of D-serine and glycine as co-agonists of NMDA receptors in motor neuron degeneration and amyotrophic lateral sclerosis (ALS), Front. Synaptic Neurosci., 6, 10, 10.3389/fnsyn.2014.00010 · DOI
- Paul, 2014, Pathogenic effects of amyotrophic lateral sclerosis-linked mutation in D-amino acid oxidase are mediated by D-serine, Neurobiol. Aging, 35, 876, 10.1016/j.neurobiolaging.2013.09.005 · DOI
- Polymenidou, 2012, Misregulated RNA processing in amyotrophic lateral sclerosis, Brain Res., 1462, 3, 10.1016/j.brainres.2012.02.059 · DOI · Paper page
- Sasabe, 2007, D-serine is a key determinant of glutamate toxicity in amyotrophic lateral sclerosis, EMBO J., 26, 4149, 10.1038/sj.emboj.7601840 · DOI
- Sasabe, 2012, D-amino acid oxidase controls motoneuron degeneration through D-serine, Proc. Natl. Acad. Sci. USA, 109, 627, 10.1073/pnas.1114639109 · DOI
- Scekic-Zahirovic, 2016, Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss, EMBO J., 35, 1077, 10.15252/embj.201592559 · DOI
- Schwartz, 2012, FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2, Genes Dev., 26, 2690, 10.1101/gad.204602.112 · DOI
- Shan, 2003, A molecular mechanism for mRNA trafficking in neuronal dendrites, J. Neurosci., 23, 8859, 10.1523/JNEUROSCI.23-26-08859.2003 · DOI
- Siomi, 1997, Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins, J. Cell Biol., 138, 1181, 10.1083/jcb.138.6.1181 · DOI
- Skibinski, 2013, Longitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative disease, FEBS Lett., 587, 1139, 10.1016/j.febslet.2013.02.043 · DOI
- Sofola, 2007, RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS, Neuron, 55, 565, 10.1016/j.neuron.2007.07.021 · DOI
- Sun, 2015, ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP, Nat. Commun., 6, 6171, 10.1038/ncomms7171 · DOI
- Thompson, 2012, Paradoxical roles of serine racemase and D-serine in the G93A mSOD1 mouse model of amyotrophic lateral sclerosis, J. Neurochem., 120, 598, 10.1111/j.1471-4159.2011.07601.x · DOI
- Udan-Johns, 2014, Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones, Hum. Mol. Genet., 23, 157, 10.1093/hmg/ddt408 · DOI
- Van Deerlin, 2008, TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis, Lancet Neurol., 7, 409, 10.1016/S1474-4422(08)70071-1 · DOI · Paper page
- Van Nostrand, 2016, Robust transcriptome-wide discovery of RNA-binding protein binding sites with enhanced CLIP (eCLIP), Nat. Methods, 13, 508, 10.1038/nmeth.3810 · DOI · Paper page
- Vance, 2009, Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6, Science, 323, 1208, 10.1126/science.1165942 · DOI
- Wu, 2012, Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice, J. Biol. Chem., 287, 27335, 10.1074/jbc.M112.359000 · DOI
- Xia, 2014, Dynamic analyses of alternative polyadenylation from RNA-seq reveal a 3′-UTR landscape across seven tumour types, Nat. Commun., 5, 5274, 10.1038/ncomms6274 · DOI
- Xiang, 2015, The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei, Cell, 163, 829, 10.1016/j.cell.2015.10.040 · DOI
- Yang, 2013, The DAO gene is associated with schizophrenia and interacts with other genes in the Taiwan Han Chinese population, PLoS ONE, 8, e60099, 10.1371/journal.pone.0060099 · DOI
- Yang, 2014, Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. USA, 111, E1121, 10.1073/pnas.1322641111 · DOI
- Zisoulis, 2010, Comprehensive discovery of endogenous Argonaute binding sites in Caenorhabditis elegans, Nat. Struct. Mol. Biol., 17, 173, 10.1038/nsmb.1745 · DOI
Cited by
Extracellular Vesicles and Nanoparticles: Emerging Complexities
Jeppesen, D. K., Zhang, Q., Franklin, J. L., & Coffey, R. J. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.01.002 · Cited by 705
Hsieh, Y.-C., Guo, C., Yalamanchili, H. K., Abreha, M., Al-Ouran, R., Li, Y., Dammer, E. B., Lah, J. J., Levey, A. I., Bennett, D. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.104 · Cited by 196
Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy
Jiang, L., Lin, W., Zhang, C., Ash, P. E. A., Verma, M., Kwan, J., van Vliet, E., Yang, Z., Cruz, A. L., Boudeau, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.038 · Cited by 177
Deng, Z., Cai, W., Liu, J., Deng, A., Yang, Y., Tu, J., Yuan, C., Xiao, H., & Gao, W. (2021) · Frontiers in Bioscience-Landmark · doi:10.52586/5006 · Cited by 15
Tau is an m 6 A-associated RNA binding protein that causes RNA dysregulation in disease
Dixon, G., Keys, A., Rothamel, K., McKetney, J., Jiang, Y. X., Gordon, L. A., Page, M. L., Liu, C., Hou, K., Flanagan, K., et al. (2026) · doi:10.64898/2026.10.26.762095
Self-citation
Metadata
- Authors
- Martinez, F. J., Pratt, G. A., Van Nostrand, E. L., Batra, R., Huelga, S. C., Kapeli, K., Freese, P., Chun, S. J., Ling, K., Gelboin-Burkhart, C., Fijany, L., Wang, H. C., Nussbacher, J. K., Broski, S. M., Kim, H. J., Lardelli, R., Sundararaman, B., Donohue, J. P., Javaherian, A., Lykke-Andersen, J., Finkbeiner, S., Bennett, C. F., Ares, M., Burge, C. B., Taylor, J. P., Rigo, F., & Yeo, G. W.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 92
- Issue
- 4
- Pages
- 780-795
- ISSN
- 0896-6273
- PMC
- PMC5123850
- Cited by
- 185
- References
- 11
- Language
- en
- Licence
- Funders
- National Institute of General Medical Sciences (T32GM008666)
- NIH (HG004659, NS075449, U54HG007005)
- California Institute of Regenerative Medicine (RB3-05009, RB4-06045)
- ALS Association (VC8K27)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System. https://app.cochat.ai/papers/10.1016/j.neuron.2016.09.050
- The paper
- Martinez, F. J., Pratt, G. A., Van Nostrand, E. L., Batra, R., Huelga, S. C., Kapeli, K., Freese, P., Chun, S. J., Ling, K., Gelboin-Burkhart, C., Fijany, L., Wang, H. C., Nussbacher, J. K., Broski, S. M., Kim, H. J., Lardelli, R., Sundararaman, B., Donohue, J. P., Javaherian, A., . . . Yeo, G. W. (2016). Protein-RNA Networks Regulated by Normal and ALS-Associated Mutant HNRNPA2B1 in the Nervous System. Neuron. https://doi.org/10.1016/j.neuron.2016.09.050
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.