Jonathan P Ling
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Explore the profile of Jonathan P Ling including associated specialties, affiliations and a list of published articles.
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25
Citations
847
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Recent Articles
1.
Ikenaga C, Wilson A, Irwin K, Peethambaran Mallika A, Kilgore C, Sinha I, et al.
Ann Neurol
. 2025 Jan;
97(4):629-641.
PMID: 39757935
Objective: Inclusion body myositis (IBM) is an idiopathic inflammatory myopathy with muscle pathology characterized by endomysial inflammation, rimmed vacuoles, and cytoplasmic mislocalization of transactive response DNA-binding protein 43 (TDP-43). We...
2.
Zhang X, Das T, Chao T, Trinh V, Carmen-Orozco R, Ling J, et al.
iScience
. 2024 Jul;
27(6):110109.
PMID: 38989321
TDP-43 nuclear clearance and cytoplasmic aggregation are hallmarks of TDP-43 proteinopathies. We recently demonstrated that binding to endogenous nuclear GU-rich RNAs sequesters TDP-43 in the nucleus by restricting its passive...
3.
Carmen-Orozco R, Tsao W, Ye Y, Sinha I, Chang K, Trinh V, et al.
Mol Neurodegener
. 2024 Jun;
19(1):45.
PMID: 38853250
Background: Cytoplasmic inclusions and loss of nuclear TDP-43 are key pathological features found in several neurodegenerative disorders, suggesting both gain- and loss-of-function mechanisms of disease. To study gain-of-function, TDP-43 overexpression...
4.
Choi I, Ling J, Zhang J, Helmenstine E, Walter W, Tsakiroglou P, et al.
Blood Adv
. 2024 May;
8(15):3961-3971.
PMID: 38759096
Among the most common genetic alterations in myelodysplastic syndromes (MDS) are mutations in the spliceosome gene SF3B1. Such mutations induce specific RNA missplicing events, directly promote ring sideroblast (RS) formation,...
5.
Sinha I, Sandal P, Burns G, Peethambaran Mallika A, Irwin K, Cruz A, et al.
bioRxiv
. 2024 Apr;
PMID: 38585725
Nuclear clearance and cytoplasmic aggregation of TDP-43 in neurons, initially identified in ALS-FTD, are hallmark pathological features observed across a spectrum of neurodegenerative diseases. We previously found that TDP-43 loss-of-function...
6.
Irwin K, Jasin P, Braunstein K, Sinha I, Garret M, Bowden K, et al.
Nat Med
. 2024 Apr;
30(5):1504.
PMID: 38580817
No abstract available.
7.
Irwin K, Jasin P, Braunstein K, Sinha I, Garret M, Bowden K, et al.
Nat Med
. 2024 Jan;
30(2):382-393.
PMID: 38278991
Although loss of TAR DNA-binding protein 43 kDa (TDP-43) splicing repression is well documented in postmortem tissues of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), whether this abnormality occurs...
8.
Chang K, Ling J, Redding-Ochoa J, An Y, Li L, Dean S, et al.
Acta Neuropathol
. 2023 Dec;
147(1):4.
PMID: 38133681
LATE-NC, the neuropathologic changes of limbic-predominant age-related TAR DNA-binding protein 43 kDa (TDP-43) encephalopathy are frequently associated with Alzheimer's disease (AD) and cognitive impairment in older adults. The association of...
9.
Zhang X, Das T, Chao T, Trinh V, Carmen R, Ling J, et al.
bioRxiv
. 2023 Aug;
PMID: 37577513
TDP-43 nuclear clearance and cytoplasmic aggregation are hallmarks of TDP-43 proteinopathies. We recently demonstrated that binding to endogenous nuclear GU-rich RNAs sequesters TDP-43 in the nucleus by restricting its passive...
10.
Carmen-Orozco R, Tsao W, Ye Y, Sinha I, Chang K, Trinh V, et al.
bioRxiv
. 2023 May;
PMID: 37215013
Cytoplasmic inclusions and loss of nuclear TDP-43 are key pathological features found in several neurodegenerative disorders, suggesting both gain- and loss-of-function mechanisms of disease. To study gain-of-function, TDP-43 overexpression has...