Results 121 to 130 of about 1,811,289 (287)
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Molecular Oncology, EarlyView.Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Classification of Intrinsically Disordered Regions and Proteins
Chemical Reviews, 2014 1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Van Der Lee R. +17 more
openaire +3 more sources
Intrinsic Disorder in Proteins Involved in Amyotrophic Lateral Sclerosis
, 2017 Five structurally and functionally different proteins, an enzyme superoxide dismutase 1 (SOD1), a TAR-DNA binding protein-43 (TDP-43), an RNA-binding protein FUS, a cofilin-binding protein C9orf72, and polypeptides generated as a result of its intronic ...
Santamaria, Nikolas +4 more
core +1 more source
Molecular Oncology, EarlyView.Taxanes are widely used chemotherapeutics whose effects on cellular mechanics remain poorly understood. We show that paclitaxel induces rapid cellular contraction by promoting GEF‐H1 dissociation from microtubules and non‐muscle myosin II activation through RhoA/ROCK.
Gloria Asensio‐Juárez +5 more
wiley +1 more source
The role of disorder in interaction networks: a structural analysis
Molecular Systems Biology, 2008 Recent studies have emphasized the value of including structural information into the topological analysis of protein networks. Here, we utilized structural information to investigate the role of intrinsic disorder in these networks. Hub proteins tend to
Philip M Kim +3 more
doaj +1 more source
Evolutionary Conservation of Intrinsic Protein Disorder.
, 2016 A) Disorder conservation prediction of Twist1 proteins. The disorder feature found in the N-terminus region of Twist1 is evolutionary conserved. B) Disorder conservation prediction of Twist2 proteins.
Carmen L. Cadilla (160681) +2 more
core +1 more source
Molecular Oncology, EarlyView.The kinase SRPK1 directly interacts with the protein TOPBP1 and regulates the pre‐mRNA splicing of WIZ thereby contributing to the activation of the ATR/CHK1 replicative checkpoint in response to replicative stress. This allows cancer cells' genomic stability and survival.
Amani Shreim +17 more
wiley +1 more source
Analysis of a Nuclear Intrinsically Disordered Proteome
, 2020 Intrinsically disordered proteins (IDPs) play crucial roles in cell functioning, although they do not possess defined three-dimensional architecture. They are highly abundant in the cell nucleus, and the vast majority of transcription factors (TFs) contain extended regions of intrinsic disorder.
Skupień-Rabian, Bożena +2 more
openaire +3 more sources
Frontiers in Pharmacology, 2015 Phosphorylation events that occur in response to the second messenger cAMP are controlled spatially and temporally by protein kinase A (PKA) interacting with A-kinase anchoring proteins (AKAPs).
Patrick J Nygren +3 more
doaj +1 more source
SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning
, 2019 Intrinsically disordered or unstructured proteins (or regions in proteins) have been found to be important in a wide range of biological functions and implicated in many diseases.
Thomas Litfin +7 more
core +1 more source