Results 41 to 50 of about 4,409,964 (303)
Intrinsically Disordered Synthetic Polymers in Biomedical Applications [PDF]
In biology and medicine, intrinsically disordered synthetic polymers bio-mimicking intrinsically disordered proteins, which lack stable three-dimensional structures, possess high structural/conformational flexibility.
Uversky, Vladimir N. +10 more
core +1 more source
The serine/threonine phosphatase calcineurin acts as a crucial connection between calcium signaling the phosphorylation states of numerous important substrates.
Trevor P. Creamer
doaj +1 more source
Benchmarking of force fields to characterize the intrinsically disordered R2-FUS-LC region
Intrinsically Disordered Proteins (IDPs) play crucial roles in numerous diseases like Alzheimer's and ALS by forming irreversible amyloid fibrils. The effectiveness of force fields (FFs) developed for globular proteins and their modified versions for ...
Maud Chan-Yao-Chong +2 more
doaj +1 more source
Entropy and Information within Intrinsically Disordered Protein Regions [PDF]
Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution. This prevents application of the canonical sequence-structure-function paradigm to IDRs and motivates the development of new methods to extract information from ...
Iva Pritisanac +3 more
openaire +5 more sources
Many proteins contain intrinsically disordered regions (IDRs) which carry out important functions without relying on a single well-defined conformation.
Bálint Mészáros +3 more
doaj +1 more source
Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]
Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Jones, DT +7 more
core +1 more source
Functions of Intrinsically Disordered Regions
Intrinsically disordered regions (IDRs), defined as protein segments lacking stable tertiary structures, are ubiquitously present in the human proteome and enriched with disease-associated mutations. IDRs harbor molecular recognition features (MoRFs) and post-translational modification sites (e.g., phosphorylation), enabling dynamic intermolecular ...
Linhu Xiao, Kun Xia
openaire +3 more sources
As high fetal hemoglobin levels ameliorate the underlying pathophysiological defects in sickle cell anemia and beta (β)-thalassemia, understanding the mechanisms that enforce silencing of fetal hemoglobin postnatally offers the promise of effective ...
Xiaofei Yu +8 more
doaj +1 more source
Many-to-one binding by intrinsically disordered protein regions
Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions. DBR-protein complexes were collected from the Protein Data Bank for which two or more DBRs having different amino acid sequences bind to the same (100% sequence ...
Alterovitz, Wei-Lun +9 more
openaire +4 more sources
Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions [PDF]
Kap121 interacts with an intrinsically disordered region of Nup53 to allosterically modulate Nup53 binding to partner nucleoporins.
Bartlomiej Jan Blus +5 more
openaire +2 more sources

