Publications by authors named "Sergio R Labra"
Alzheimer's disease (AD) is the most common form of dementia worldwide. Despite extensive progress, the cellular and molecular mechanisms of AD remain incompletely understood, partially due to inadequate disease models. To illuminate the earliest changes in hereditary (familial) Alzheimer's disease, we developed an isogenic AD cerebrocortical organoid (CO) model.
View Article and Find Full Text PDFDetecting Boolean Asymmetric Relationships With a Loop Counting Technique and its Implications for Analyzing Heterogeneity Within Gene Expression Datasets.
IEEE Trans Comput Biol Bioinform
January 2025
Article Synopsis
- Traditional methods for analyzing gene relationships often focus on symmetric correlations; however, this study introduces a technique to detect 'boolean-asymmetric' relationships (BARs) in gene expression data.
- The proposed method identifies biclusters enriched with these asymmetric relationships, revealing regulatory influences of certain genes on others that are not apparent in typical analyses.
- When applied to single-cell RNA sequencing data, the BAR-biclusters provided new insights regarding different cell subsets and gene pathways, leading to improved predictive models compared to those using only symmetric data.
Article Synopsis
- - The immune system plays a key role in sporadic Alzheimer's disease (sAD), with genetic risk factors highlighting its importance in the disorder's mechanisms.
- - Studies of microglia in human brains show that their activation is linked to the progression of Alzheimer's, particularly when beta-Amyloid and tau pathology are present together.
- - Variants in the TREM2 gene lead to altered microglial responses, which may affect treatment strategies for sAD due to significant differences in immune activation across brain regions and genetic backgrounds.
Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.
Biochim Biophys Acta Proteins Proteom
October 2019
Intrinsically disordered proteins (IDPs) are ubiquitous in proteomes and serve in a range of cellular functions including signaling, regulation, transport and enzyme function. IDP misfunction and aggregation are also associated with several diseases including neurodegenerative diseases and cancer. During the past decade, single-molecule methods have become popular for detailed biophysical and structural studies of these complex proteins.
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