Stress‐induced mRNP granules: Form and function of processing bodies and stress granules

AR Guzikowski, YS Chen, BM Zid - Wiley Interdisciplinary …, 2019 - Wiley Online Library
In response to stress, cells must quickly reprogram gene expression to adapt and survive.
This is achieved in part by altering levels of mRNAs and their translation into proteins …

Relevance of electrostatic charges in compactness, aggregation, and phase separation of intrinsically disordered proteins

G Bianchi, S Longhi, R Grandori, S Brocca - International Journal of …, 2020 - mdpi.com
The abundance of intrinsic disorder in the protein realm and its role in a variety of
physiological and pathological cellular events have strengthened the interest of the scientific …

Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities

CPJ Maury - Cellular and Molecular Life Sciences, 2018 - Springer
A crucial stage in the origin of life was the emergence of the first molecular entity that was
able to replicate, transmit information, and evolve on the early Earth. The amyloid world …

Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex

RB Davis, A Supakar, AK Ranganath… - Nature …, 2024 - nature.com
Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic
acid-binding proteins including those involved in transcription and RNA processing. PLDs of …

Protein assembly systems in natural and synthetic biology

G Chiesa, S Kiriakov, AS Khalil - BMC biology, 2020 - Springer
The traditional view of protein aggregation as being strictly disease-related has been
challenged by many examples of cellular aggregates that regulate beneficial biological …

What makes a protein sequence a prion?

R Sabate, F Rousseau, J Schymkowitz… - PLoS computational …, 2015 - journals.plos.org
Typical amyloid diseases such as Alzheimer's and Parkinson's were thought to exclusively
result from de novo aggregation, but recently it was shown that amyloids formed in one cell …

Prion-like domains in eukaryotic viruses

G Tetz, V Tetz - Scientific reports, 2018 - nature.com
Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition
to the previously demonstrated pathogenic roles of prions during the development of …

RNA as the stone guest of protein aggregation

A Louka, E Zacco, PA Temussi… - Nucleic Acids …, 2020 - academic.oup.com
The study of prions as infectious aggregates dates several decades. From its original
formulation, the definition of a prion has progressively changed to the point that many …

From prions to stress granules: defining the compositional features of prion-like domains that promote different types of assemblies

A Fomicheva, ED Ross - International journal of molecular sciences, 2021 - mdpi.com
Stress granules are ribonucleoprotein assemblies that form in response to cellular stress.
Many of the RNA-binding proteins found in stress granule proteomes contain prion-like …

Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans

G Cereghetti, S Saad, R Dechant, M Peter - Cell Cycle, 2018 - Taylor & Francis
Protein aggregates, and in particular amyloids, are generally considered to be inherently
irreversible aberrant clumps, and are often associated with pathologies, such as Alzheimer's …