Aitor Franco

Aitor Franco

PhD in Molecular Biology and Biomedicine

About

8
Publications
1,367
Reads
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81
Citations
Additional affiliations
February 2021 - present
Biofisika Institute (UPV-EHU/CSIC)
Position
  • PostDoc Position
January 2017 - January 2021
Biofisika Institute (UPV-EHU/CSIC)
Position
  • PhD Student
Education
October 2016 - December 2020
Universidad del País Vasco / Euskal Herriko Unibertsitatea
Field of study
  • Molecular Biology and Biomedicine
September 2015 - June 2016
Universidad del País Vasco / Euskal Herriko Unibertsitatea
Field of study
  • Molecular Biology and Biomedicine
September 2011 - July 2015

Publications

Publications (8)
Article
Full-text available
Protein aggregation is a hallmark of major neurodegenerative disorders. Increasing data suggest that smaller aggregates cause higher toxic response than filamentous aggregates (fibrils). However, the size of small aggregates has challenged their detection within biologically relevant environments. Here, we report approaches to quantitatively super-...
Article
Full-text available
The aggregation of α-synuclein is the hallmark of a collective of neurodegenerative disorders known as synucleinopathies. The tendency to aggregate of this protein, the toxicity of its ag-gregation intermediates and the ability of the cellular protein quality control system to clear these intermediates seems to be regulated, among other factors, by...
Article
Full-text available
Neurodegenerative diseases (NDs) are increasingly positioned as leading causes of global deaths. The accelerated aging of the population and its strong relationship with neurodegeneration forecast these pathologies as a huge global health problem in the upcoming years. In this scenario, there is an urgent need for understanding the basic molecular...
Article
Significance Although the human disaggregase machinery has been shown to disassemble mature α-synuclein amyloid fibrils, the molecular mechanism that drives the process has remained elusive. In this work, we show that amyloid disassembly is initiated by the destabilization of the fibril ends, followed by the fast propagation of protofilament unzipp...
Article
Full-text available
Nucleoplasmin (NP) is a pentameric histone chaperone that regulates the condensation state of chromatin in different cellular processes. We focus here on the interaction of NP with the histone octamer, showing that NP could bind sequentially the histone components to assemble an octamer-like particle, and crosslinked octamers with high affinity. Th...
Chapter
Cells have evolved an ingenious way to tightly pack the genetic information in a nucleoprotein complex called chromatin. The functional unit of chromatin is the nucleosome, which is made of DNA wrapped around histones. Dynamic modulation of nucleosome structure by regulating the association/dissociation of histones to/from DNA is essential for DNA...
Article
Full-text available
Nucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A–H2B histone chaperone, and recently it has been shown that it can also interact with H3-H4. However, its interaction with different ty...

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