ArticleMetabolic brain disease2025
Acute lipid droplet accumulation induced by the inhibition of the phospholipase DDHD2 does not affect the level, solubility, or phosphoserine-129 status of α-synuclein.
Magdalena M Bolsinger, Tim E Moors, Lisa Brontesi, Silke Nuber, Ulf Dettmer, Nagendran Ramalingam
Abstract read
In one paragraphArticle in Metabolic brain disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registryThe trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
6 authors.
Magdalena M BolsingerAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA.ORCID 0000-0002-3020-9943 Tim E MoorsAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA.
Lisa BrontesiAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA.
Silke NuberAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA.
Ulf DettmerAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA. udettmer@bwh.harvard.edu.ORCID 0000-0001-6676-0107 Nagendran RamalingamAnn Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA. nramalingam@bwh.harvard.edu.ORCID 0000-0002-9459-3593 Funding
How Serine-129 Phosphorylation Status Affects the Spreading of α-Synuclein Pathology in Vivo: a Study in Knock-in AnimalsRF1NS133979 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI DETTMER, ULF, RAMALINGAM, NAGENDRAN · 2023 to 2023
$2.2MPolo-like-kinase-2-dependent α-Synuclein Serine-129 Phosphorylation: a Physiological RoleDuring Synaptic ActivityRF1NS122880 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI DETTMER, ULF, RAMALINGAM, NAGENDRAN · 2022 to 2022
$2.1MBiologically novel mouse models of PD with progressive synucleinopathy and early-onset tremor and motor deficits responsive to L-DOPAR01NS109510 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI NUBER, SILKE · 2019 to 2023
$1.9MPolo-like-kinase-2-dependent α-Synuclein Serine-129 Phosphorylation: a Physiological RoleDuring Synaptic ActivityR01NS122880 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI Ulf Dettmer, Nagendran Ramalingam · 2025 to 2026
$1.4MBiologically Novel Mouse Models of PD with Progressive Synucleinopathy and Early-Onset Tremor and Motor Deficits Responsive to L-DOPARF1NS109510 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI NUBER, SILKE · 2024 to 2024
$1.3MDistinguishing α-Synuclein S129 Phosphorylation in Health and Lewy Body DementiaR21AG085401 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI Nagendran Ramalingam · 2024 to 2026
$433kNIA NIH HHS R21 AG085401NINDS NIH HHS R01 NS109510NINDS NIH HHS R01 NS122880NINDS NIH HHS RF1 NS109510NINDS NIH HHS RF1 NS122880NINDS NIH HHS RF1 NS133979
6 · The paper itselfAbstract
α-Synuclein (αS) is a 140 amino-acid neuronal protein highly enriched in presynaptic nerve terminals. Its progressive accumulation in Lewy bodies and neurites is the hallmark of Parkinson's disease (PD). A growing number of studies highlights a critical interplay between lipid metabolism and αS biology. Some of these works postulate a physical interaction between αS and lipid droplets (LDs), but further clarity is needed, not least because typically exogenous αS and/or heterologous systems have been studied. Here, we investigated the effects of acute LD accumulation on endogenous wild-type αS in primary rat cortical neurons. To induce robust LD accumulation within hours, we inhibited the neuronal triacylglycerol hydrolase DDHD2, a phospholipase, using the compound KLH45. KLH45-induced LD accumulation did not affect total levels, phosphoserine-129 status, or solubility of αS, and no co-localization between LDs and αS was observed under these conditions. These findings suggest that a "second hit" and/or a specific LD lipid composition may be necessary for lipid excess to affect αS homeostasis. Our work thus contributes to the debate on αS structure and lipid interaction.
Indexed as
alpha-SynucleinLipid DropletsNeuronsAnimalsCells, CulturedCerebral CortexLipid MetabolismPhosphorylationRatsSolubilityalpha-SynucleinLipaseLipid metabolismParkinson’s diseaseSynucleinopathies
Identifiers
PMID39853540
PMCPMC12036649
What Socratic holds
Textmetadata
LicenceTDM
Read underepoch 390