Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

PTBP1 and PTBP2 Repress Nonconserved Cryptic Exons
Jonathan P. Ling, Resham Chhabra, Jonathan Merran, et al.
Cell Reports (2016) Vol. 17, Iss. 1, pp. 104-113
Open Access | Times Cited: 59

Showing 1-25 of 59 citing articles:

Heteromeric RNP Assembly at LINEs Controls Lineage-Specific RNA Processing
Jan Attig, Federico Agostini, Clare Gooding, et al.
Cell (2018) Vol. 174, Iss. 5, pp. 1067-1081.e17
Open Access | Times Cited: 152
A Short Tandem Repeat-Enriched RNA Assembles a Nuclear Compartment to Control Alternative Splicing and Promote Cell Survival
Karen Yap, Svetlana Mukhina, Gen Zhang, et al.
Molecular Cell (2018) Vol. 72, Iss. 3, pp. 525-540.e13
Open Access | Times Cited: 141
Roles of PTBP1 in alternative splicing, glycolysis, and oncogensis
Wei Zhu, Bolun Zhou, Lijuan Rong, et al.
Journal of Zhejiang University SCIENCE B (2020) Vol. 21, Iss. 2, pp. 122-136
Open Access | Times Cited: 116
The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis
Alexander Bampton, Lauren M. Gittings, Pietro Fratta, et al.
Acta Neuropathologica (2020) Vol. 140, Iss. 5, pp. 599-623
Open Access | Times Cited: 94
Splicing repression is a major function of TDP-43 in motor neurons
Aneesh Donde, Mingkuan Sun, Jonathan P. Ling, et al.
Acta Neuropathologica (2019) Vol. 138, Iss. 5, pp. 813-826
Open Access | Times Cited: 79
ASCOT identifies key regulators of neuronal subtype-specific splicing
Jonathan P. Ling, Christopher Wilks, Rone Charles, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 74
Neurodegenerative diseases: a hotbed for splicing defects and the potential therapies
Dunhui Li, Craig S. McIntosh, Frank Mastaglia, et al.
Translational Neurodegeneration (2021) Vol. 10, Iss. 1
Open Access | Times Cited: 70
Genetic loss of function of Ptbp1 does not induce glia-to-neuron conversion in retina
Thanh Hoang, Dong Won Kim, Haley Appel, et al.
Cell Reports (2022) Vol. 39, Iss. 11, pp. 110849-110849
Open Access | Times Cited: 53
Loss of TDP-43 function and rimmed vacuoles persist after T cell depletion in a xenograft model of sporadic inclusion body myositis
Kyla A. Britson, Jonathan P. Ling, Kerstin E. Braunstein, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 628
Open Access | Times Cited: 50
TDP-43 and other hnRNPs regulate cryptic exon inclusion of a key ALS/FTD risk gene, UNC13A
Yuka Koike, Sarah Pickles, Virginia Estades Ayuso, et al.
PLoS Biology (2023) Vol. 21, Iss. 3, pp. e3002028-e3002028
Open Access | Times Cited: 27
Tdp-43 cryptic exons are highly variable between cell types
Yun Ha Jeong, Jonathan P. Ling, Sophie Lin, et al.
Molecular Neurodegeneration (2017) Vol. 12, Iss. 1
Open Access | Times Cited: 79
The Splicing Factor hnRNP M Is a Critical Regulator of Innate Immune Gene Expression in Macrophages
Kelsi O West, Haley M. Scott, Sylvia Torres-Odio, et al.
Cell Reports (2019) Vol. 29, Iss. 6, pp. 1594-1609.e5
Open Access | Times Cited: 73
Cryptic exon incorporation occurs in Alzheimer’s brain lacking TDP-43 inclusion but exhibiting nuclear clearance of TDP-43
Mingkuan Sun, William R. Bell, Katherine D. LaClair, et al.
Acta Neuropathologica (2017) Vol. 133, Iss. 6, pp. 923-931
Open Access | Times Cited: 65
Multiple functions of heterogeneous nuclear ribonucleoproteins in the positive single-stranded RNA virus life cycle
Jingming Wang, Di Sun, Mingshu Wang, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 35
Long-read proteogenomics to connect disease-associated sQTLs to the protein isoform effectors of disease
Abdullah Abood, Larry D. Mesner, Erin D. Jeffery, et al.
The American Journal of Human Genetics (2024) Vol. 111, Iss. 9, pp. 1914-1931
Open Access | Times Cited: 7
Molecular mechanisms linking loss of TDP-43 function to amyotrophic lateral sclerosis/frontotemporal dementia-related genes
Yuka Koike
Neuroscience Research (2024) Vol. 208, pp. 1-7
Open Access | Times Cited: 6
Autoregulation of RBM10 and cross-regulation of RBM10/RBM5 via alternative splicing-coupled nonsense-mediated decay
Yue Sun, Yufang Bao, Wenjian Han, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 14, pp. 8524-8540
Open Access | Times Cited: 53
SON drives oncogenic RNA splicing in glioblastoma by regulating PTBP1/PTBP2 switching and RBFOX2 activity
Jung‐Hyun Kim, Kyuho Jeong, Jianfeng Li, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 38
HnRNP K mislocalisation is a novel protein pathology of frontotemporal lobar degeneration and ageing and leads to cryptic splicing
Alexander Bampton, Ariana Gatt, Jack Humphrey, et al.
Acta Neuropathologica (2021) Vol. 142, Iss. 4, pp. 609-627
Open Access | Times Cited: 36
Alternative splicing coupled to nonsense-mediated decay coordinates downregulation of non-neuronal genes in developing mouse neurons
Anna Zhuravskaya, Karen Yap, Fursham Hamid, et al.
Genome biology (2024) Vol. 25, Iss. 1
Open Access | Times Cited: 5
Matrin3 binds directly to intronic pyrimidine-rich sequences and controls alternative splicing
Yuri Uemura, Takuya Oshima, Munetaka Yamamoto, et al.
Genes to Cells (2017) Vol. 22, Iss. 9, pp. 785-798
Open Access | Times Cited: 48
TDP43 and RNA instability in amyotrophic lateral sclerosis
Kaitlin Weskamp, Sami J. Barmada
Brain Research (2018) Vol. 1693, pp. 67-74
Open Access | Times Cited: 46
CRISPR whole-genome screening identifies new necroptosis regulators and RIPK1 alternative splicing
Marinella Callow, Colin Watanabe, Katherine E. Wickliffe, et al.
Cell Death and Disease (2018) Vol. 9, Iss. 3
Open Access | Times Cited: 42
The Diverse Roles of RNA-Binding Proteins in Glioma Development
Mitzli X. Velasco, Adam Kosti, Luiz O. F. Penalva, et al.
Advances in experimental medicine and biology (2019), pp. 29-39
Closed Access | Times Cited: 40
An ancient germ cell-specific RNA-binding protein protects the germline from cryptic splice site poisoning
Ingrid Ehrmann, James H. Crichton, Matthew R. Gazzara, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 38
Page 1 - Next Page

Scroll to top