Intrinsically disordered proteins in cellular signalling and regulation
PE Wright, HJ Dyson - Nature reviews Molecular cell biology, 2015 - nature.com
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling
machinery, allowing the same polypeptide to undertake different interactions with different …
machinery, allowing the same polypeptide to undertake different interactions with different …
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
G Wei, W ** a molecular dynamics force field for both folded and disordered protein states
Molecular dynamics (MD) simulation is a valuable tool for characterizing the structural
dynamics of folded proteins and should be similarly applicable to disordered proteins and …
dynamics of folded proteins and should be similarly applicable to disordered proteins and …
Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS, and single-molecule FRET
GNW Gomes, M Krzeminski, A Namini… - Journal of the …, 2020 - ACS Publications
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which
makes their structural characterization challenging. Although challenging, characterization …
makes their structural characterization challenging. Although challenging, characterization …
[HTML][HTML] How GPCR phosphorylation patterns orchestrate arrestin-mediated signaling
Binding of arrestin to phosphorylated G-protein-coupled receptors (GPCRs) controls many
aspects of cell signaling. The number and arrangement of phosphates may vary …
aspects of cell signaling. The number and arrangement of phosphates may vary …
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)
It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …
Intrinsically disordered proteins: a 10-year recap
P Tompa - Trends in biochemical sciences, 2012 - cell.com
The suggestion that the native state of many proteins is intrinsically disordered (or, as
originally termed, unstructured) is now integral to our general view of protein structure and …
originally termed, unstructured) is now integral to our general view of protein structure and …
Structure, dynamics, assembly, and evolution of protein complexes
The assembly of individual proteins into functional complexes is fundamental to nearly all
biological processes. In recent decades, many thousands of homomeric and heteromeric …
biological processes. In recent decades, many thousands of homomeric and heteromeric …
How phosphorylation impacts intrinsically disordered proteins and their function
EA Newcombe, E Delaforge… - Essays in …, 2022 - portlandpress.com
Phosphorylation is the most common post-translational modification (PTM) in eukaryotes,
occurring particularly frequently in intrinsically disordered proteins (IDPs). These proteins …
occurring particularly frequently in intrinsically disordered proteins (IDPs). These proteins …