Results 101 to 110 of about 448,472 (368)
Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins. [PDF]
PLoS ONE, 2015 Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have
Mihaly Varadi +3 more
doaj +1 more source
Is the intrinsic disorder of proteins the cause of the scale-free architecture of protein-protein interaction networks? [PDF]
arXiv, 2006 In protein-protein interaction networks certain topological properties appear to be recurrent: networks maps are considered scale-free. It is possible that this topology is reflected in the protein structure. In this paper we investigate the role of protein disorder in the network topology.
arxiv
Configurational Entropy of Folded Proteins and its Importance for Intrinsically Disordered Proteins [PDF]
arXiv, 2020 Many pairwise additive force fields are in active use for intrinsically disordered proteins (IDPs) and regions (IDRs), some of which modify energetic terms to improve description of IDPs/IDRs, but are largely in disagreement with solution experiments for the disordered states.
arxiv
International Journal of Molecular Sciences, 2019 Advances in genomics and proteomics have revealed eukaryotic proteomes to be highly abundant in intrinsically disordered proteins that are susceptible to diverse post-translational modifications.
Izzy Owen, F. Shewmaker
semanticscholar +1 more source
Cells, 2020 Protein aggregation is associated with an increasing number of human disorders and premature aging. Moreover, it is a central concern in the manufacturing of recombinant proteins for biotechnological and therapeutic applications. Nevertheless, the unique
Jaime Santos +6 more
semanticscholar +1 more source
Intrinsically Disordered Proteins in Neurodegeneration [PDF]
Biophysical Journal, 2016 Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention.
openaire +2 more sources
Targeting intrinsically disordered proteins involved in cancer [PDF]
Cellular and Molecular Life Sciences, 2019 Abstract Intrinsically disordered proteins (IDPs) do not have a well-defined structure under physiological conditions, but they have key roles in cell signaling and regulation, and they are frequently related to the development of diseases, such as cancer and other malignancies.
Adrián Velázquez-Campoy +8 more
openaire +6 more sources
FEM1B enhances TRAIL‐induced apoptosis in T lymphocytes and monocytes
FEBS Open Bio, EarlyView.FEM1B facilitates TRAIL‐induced apoptosis through distinct mechanisms in T lymphocytes and monocytes. In T lymphocytes, FEM1B engages with TRAF2, leading to a reduction in TRAF2 expression, which subsequently lessens TRAF2's inhibitory influence on caspase‐8.
Chenbo Yang +5 more
wiley +1 more source
On the abundance of intrinsically disordered proteins in the human proteome and its relation to diseases: there is no enrichment [PDF]
arXiv, 2014 Intrinsically disordered proteins are fascinating the community of protein science since the last decade, at least. There is a well-established line of research that intends to reveal the crucial role played by intrinsically disordered proteins (IDPs) in the development of human diseases.
arxiv
Pathway Analyses of Inherited Neuropathies Identify Putative Common Mechanisms of Axon Degeneration
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT Objective Inherited neuropathies (IN) are associated with over 100 different genetic mutations presenting with a variety of phenotypes. This complexity suggests multiple pathways may converge onto a limited number of downstream pathways to effect axonal injury.
Christopher R. Cashman +2 more
wiley +1 more source