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ProteomicsTitin BioID - protein and peptide pull-down
Proximity proteomics has greatly advanced the analysis of native protein complexes and subcellular structures in culture, but has not been amenable to study development and disease in vivo. Here, we generated a knock-in mouse with the biotin ligase (BioID) inserted at titin’s Z-disc region to identi...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-18 | PXD017341 | Pride
Mouse Titin Biotinylation sites Bioid 
TranscriptomicsThe smooth muscle titin filament system regulates uterus contractility and implantation.
We investigated the impact of smooth-muscle–specific deletion of titin M-band exons 1–2. Understanding how disruption of titin M-band signaling alters uterine smooth-muscle physiology provides insight into the molecular mechanisms controlling coordinated uterine peristalsis, embryo positioning, and ...
ORGANISM(S): Mus musculus 
2026-09-16 | E-MTAB-17587 | biostudies-arrayexpress
TranscriptomicsHeart RNA-seq of control mice and a mouse model of cardiometabolic heart failure (HFpEF) treated with Rbm20 antisense oligonucleotides
We report the heart RNA-sequencing of control animals (C57BL/6N genetic background, wild type) and animals of a mouse model of cardiometabolic heart failure (HFpEF) treated or not with RBM20 antisense oligonucleotide. HFpEF was induced using a 2-hit regimen, in which male mice were fed with a high-f...
ORGANISM(S): Mus musculus 
2026-03-19 | E-MTAB-14882 | biostudies-arrayexpress
TranscriptomicsHeart RNA-seq of therapeutic RBM20 antisense oligonucleotide (ASO) treatment in a mouse model of heart failure with preserved ejection fraction (HFpEF)
We report the heart RNA-sequencing of control animals and animals of a mouse model of heart failure treated or not with RBM20 antisense oligonucleotide. This study aims to investigate the therapeutic effect of antisense oligonucleotide (ASO)-mediated downregulation of the cardiac splice factor RBM20...
ORGANISM(S): Mus musculus 
2021-12-06 | E-MTAB-9361 | biostudies-arrayexpress
UnknownStructural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.
Not available
S-EPMC4968714 | biostudies-literature
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