Results 41 to 50 of about 3,841,423 (288)
Intrinsic Structural Disorder in Cytoskeletal Proteins [PDF]
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and microtubules.
Guha Roy, Mainak +4 more
openaire +4 more sources
Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle [PDF]
The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi +4 more
core +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
Inferring function using patterns of native disorder in proteins [PDF]
Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB +14 more
core +2 more sources
Inherent structural disorder and dimerisation of murine norovirus NS1-2 protein [PDF]
Human noroviruses are highly infectious viruses that cause the majority of acute, non-bacterial epidemic gastroenteritis cases worldwide. The first open reading frame of the norovirus RNA genome encodes for a polyprotein that is cleaved by the viral ...
Krause Kurt L. +17 more
core +1 more source
Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are functional proteins and domains that devoid stable secondary and/or tertiary structure.
April L. Darling +2 more
doaj +1 more source
Intrinsically disordered proteins and protein regions (IDPs/IDPRs) are mainly involved in signaling pathways, where fast regulation, temporal interactions, promiscuous interactions, and assemblies of structurally diverse components including membranes ...
Hana Popelka, Vladimir N. Uversky
doaj +1 more source
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
Long-Range Entropic Effects on Protein Intrinsically Disordered Regions [PDF]
Entropy calculations represent one of the most challenging steps in obtaining the binding free energy in proteins and their complexes, which is a grand challenge in computational biology.
Agnieszka K., Bronowska +3 more
core +1 more source
From mice to humans—divergent strategies for intestinal homeostasis and regeneration
Recent advances such as organoid genome editing, xenotransplantation, imaging, and whole‐genome sequencing have enabled direct studies of human intestinal stem cells (ISCs). These studies reveal species‐specific features, including slower ISC proliferation, distinct injury responses, slower somatic mutation accumulation in humans, and an inverse ...
Keiko Ishikawa +2 more
wiley +1 more source

