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46 results for “protein aggregation”

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geo20/100

Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation

GEO Series GSE84636. Homo sapiens. 21 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenJul 2016View details →
zenodo20/100

An improved marker for cytoplasmic protein aggregation in the budding yeast Saccharomyces cerevisiae

<p>CUP1-<span>&Delta;</span>ssCPY*-mGFP cytoplasmic aggregates characterisation (confocal images)</p>

opencc-by-4.0Dec 2023View details →
geo16/100

A glycosylation-driven protein complex assembly governs mRNA homeostasis and ensures protein aggregates clearance in cells and organs

GEO Series GSE292672. Homo sapiens. 3 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenAug 2025View details →
geo16/100

Distinct sub-cellular autophagy impairments occur independently of protein aggregation in aged induced neurons from patients with Huntington’s disease

GEO Series GSE167104. Homo sapiens. 15 samples. Type: Methylation profiling by genome tiling array.

openGEO-OpenFeb 2022View details →
geo16/100

Mitochondrial protein import stress augments alpha-synuclein aggregation and neurodegeneration independent of bioenergetics

GEO Series GSE236975. Mus musculus. 72 samples. Type: Expression profiling by high throughput sequencing.

openGEO-OpenOct 2023View details →
zenodo12/100

Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution

<p>Scalone E, Broggini L, Visentin C, Erba D, Bačić Toplek F, Peqini K, Pellegrino S, Ricagno S, Paissoni C, Camilloni C. Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution. Proc Natl Acad Sci U S A. 2022 Jun 28;119(26):e2203181119. doi: 10.1073/pnas.2203181119. Epub 2022 Jun 23. PMID: 35737839; PMCID: PMC9245614.</p> <p>Abstract</p> <p>Protein aggregation into amyloid fibrils is the archetype of aberrant biomolecular self-assembly processes, with more than 50 associated diseases that are mostly uncurable. Understanding aggregation mechanisms is thus of fundamental importance and goes in parallel with the structural characterization of the transient oligomers formed during the process. Oligomers have been proven elusive to high-resolution structural techniques, while the large sizes and long time scales, typical of aggregation processes, have limited the use of computational methods to date. To surmount these limitations, we here present multi-<em>e</em>GO, an atomistic, hybrid structure-based model which, leveraging the knowledge of monomers conformational dynamics and of fibril structures, efficiently captures the essential structural and kinetics aspects of protein aggregation. Multi-<em>e</em>GO molecular dynamics simulations can describe the aggregation kinetics of thousands of monomers. The concentration dependence of the simulated kinetics, as well as the structural features of the resulting fibrils, are in qualitative agreement with in vitro experiments carried out on an amyloidogenic peptide from Transthyretin, a protein responsible for one of the most common cardiac amyloidoses. Multi-<em>e</em>GO simulations allow the formation of primary nuclei in a sea of transient lower-order oligomers to be observed over time and at atomic resolution, following their growth and the subsequent secondary nucleation events, until the maturation of multiple fibrils is achieved. Multi-<em>e</em>GO, combined with the many experimental techniques deployed to study protein aggregation, can provide the structural basis needed to advance the design of molecules targeting amyloidogenic diseases.</p>

restrictedJan 2023View details →

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Allen Brain Atlas

Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.

allen-brain-atlas
neuroscienceopenDocumentation, web resources, and API references are available online.
Last verified 2026-04-30Open record

Annotated Behaviour and Observability Dataset (ABODe)

ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.

abode-home-cage
behavioral-neuroscienceopenThe DataShare record exposes download links for annotations, documentation, license text, and the zipped per-snippet data directory.
Last verified 2026-04-30Open record

DANDI Archive for NWB datasets

DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.

dandi-nwb
electrophysiologyopenPublished Dandiset metadata and archive endpoints are available through the production DANDI API.
Last verified 2026-04-30Open record

International Brain Laboratory public data

The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.

ibl
behavioral-neuroscienceopenPublic sessions can be searched and loaded from the IBL public data server through ONE.
Last verified 2026-04-29Open record

OpenNeuro

OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.

openneuro
neuroscienceopenPublished datasets are available on demand over the internet.
Last verified 2026-04-29Open record