Epistasis and adaptation on fitness landscapes
C Bank - Annual Review of Ecology, Evolution, and Systematics, 2022 - annualreviews.org
Epistasis occurs when the effect of a mutation depends on its carrier's genetic background.
Despite increasing evidence that epistasis for fitness is common, its role during evolution is …
Despite increasing evidence that epistasis for fitness is common, its role during evolution is …
Towards evolutionary predictions: Current promises and challenges
Evolution has traditionally been a historical and descriptive science, and predicting future
evolutionary processes has long been considered impossible. However, evolutionary …
evolutionary processes has long been considered impossible. However, evolutionary …
Insights into Hsp90 mechanism and in vivo functions learned from studies in the yeast, Saccharomyces cerevisiae
EI Rios, IL Hunsberger, JL Johnson - Frontiers in Molecular …, 2024 - frontiersin.org
The molecular chaperone Hsp90 (Heat shock protein, 90 kDa) is an abundant and essential
cytosolic protein required for the stability and/or folding of hundreds of client proteins …
cytosolic protein required for the stability and/or folding of hundreds of client proteins …
Conformational dynamics and mechanisms of client protein integration into the hsp90 chaperone controlled by allosteric interactions of regulatory switches …
GM Verkhivker - The Journal of Physical Chemistry B, 2022 - ACS Publications
Understanding the allosteric mechanisms of the Hsp90 chaperone interactions with
cochaperones and client protein clientele is fundamental to dissect activation and regulation …
cochaperones and client protein clientele is fundamental to dissect activation and regulation …
Direct observation of chemo-mechanical coupling in DnaK by single-molecule force experiments
A Singh, M Rief, G Žoldák - Biophysical Journal, 2022 - cell.com
Protein allostery requires a communication channel for functional regulation between distal
sites within a protein. In the molecular chaperone Hsp70, a two-domain enzyme, the …
sites within a protein. In the molecular chaperone Hsp70, a two-domain enzyme, the …
Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions
Hsp90 is an abundant and essential molecular chaperone that mediates the folding and
activation of client proteins in a nucleotide-dependent cycle. Hsp90 inhibition directly or …
activation of client proteins in a nucleotide-dependent cycle. Hsp90 inhibition directly or …
gUMI-BEAR, a modular, unsupervised population barcoding method to track variants and evolution at high resolution
S Rezenman, M Knafo, I Tsigalnitski, S Barad, G Jona… - Plos one, 2023 - journals.plos.org
Cellular lineage tracking provides a means to observe population makeup at the clonal
level, allowing exploration of heterogeneity, evolutionary and developmental processes and …
level, allowing exploration of heterogeneity, evolutionary and developmental processes and …
Distribution and molecular evolution of the anti-CRISPR family AcrIF7
Anti-clustered regularly interspaced short palindromic repeats (CRISPRs) are proteins
capable of blocking CRISPR-Cas systems and typically their genes are located on mobile …
capable of blocking CRISPR-Cas systems and typically their genes are located on mobile …
Using deep mutational scanning to study protein function and disease
V Nguyen - 2023 - search.proquest.com
Hsp90 is a crucial molecular chaperone that regulates proteostasis by facilitating the
refolding and activation of various signaling proteins. Its importance in protein folding and …
refolding and activation of various signaling proteins. Its importance in protein folding and …
[PDF][PDF] Molecular evolution of the anti-CRISPR family AcrIF7 reveals conservation despite mutation tolerance
W Figueroa, A Cazares, D Cazares, A de la Cruz… - …, 2021 - scholar.archive.org
Anti-CRISPRs are molecules typically encoded in mobile elements and capable of blocking
CRISPR-Cas systems. Since their discovery, numerous anti-CRISPR families have been …
CRISPR-Cas systems. Since their discovery, numerous anti-CRISPR families have been …