Results 111 to 120 of about 29,703 (304)
Sequence conservation of protein binding segments in intrinsically disordered regions
Intrinsically disordered proteins are proteins with intrinsically disordered regions (IDRs) that do not adopt a globular structure in their free state. IDRs have unique regions having protein-binding segments of which play pivotal roles in many biological processes.
Haruki, Ota, Satoshi, Fukuchi
openaire +2 more sources
Blood Biomarkers and Surface‐Enhanced Raman Spectroscopy for Gout: A Comprehensive Review
Schematic illustrating gout disease progression from asymptomatic hyperuricemia to chronic tophaceous disease, highlighting the limitations of conventional imaging and biochemical diagnostics and the potential of engineered SERS platforms for ultrasensitive blood‐based detection of urate‐related biomarkers across disease stages, with the color gradient
Isuri Perera +6 more
wiley +1 more source
A PagP fusion protein system for the expression of intrinsically disordered proteins in E. coli
PagP, a beta-barrel membrane protein found in Gram-negative bacteria, expresses robustly in inclusion bodies when its signal sequence is removed. We have developed a new fusion protein expression system based on PagP and demonstrated its utility in the ...
Pan, Jonathan S. +2 more
core +1 more source
Cells are inhomogeneously crowded, possessing a wide range of intracellular liquid droplets abundantly present in the cytoplasm of eukaryotic and bacterial cells, in the mitochondrial matrix and nucleoplasm of eukaryotes, and in the chloroplast’s ...
Vladimir N. Uversky
doaj +1 more source
A molecular shielding strategy to convert “protein‐sticky” and “non‐tumor specific” clinical ICG dye, into a “low protein binding” and “tumor‐targeting” dye with prolonged blood circulation and renal clearance is described. These shielded ICGs demonstrate strong tumor accumulation and optimal tissue clearance, resulting in high tumor‐to‐background ...
Li Xiang +9 more
wiley +1 more source
Intrinsically Disordered Proteins May Select Partners by Fold [PDF]
Intrinsically disordered proteins lack a rigid structure due to their simple amino acid sequence. Because of their multiple roles, disordered proteins often account for a majority of proteins known to be associated with various diseases.
Gonzalez, Kim 1988-
core
Molecular driving force of a small molecule-induced protein disorder-order transition
The selectivity and affinity of numerous protein–protein interactions depends upon the folding of intrinsically disordered regions (IDRs) that accompanies complexation.
Cesar Mendoza-Martinez +4 more
doaj +1 more source
A nanounit‐assembled hydrogel employing a “pull‐and‐push” strategy simultaneously scavenges pro‐inflammatory cell‐free DNA (cfDNA) and delivers regenerative therapeutics in response to burn‐induced hyperthermia. By repolarizing macrophages and promoting angiogenesis, this multifunctional platform accelerates burn wound healing, offering a blueprint for
Han‐Sem Kim +9 more
wiley +1 more source
Significance The cell is divided into compartments where specific biochemical functions are performed. These compartments can be delineated by membranes or through phase separation of proteins or protein and nucleic acids to form membraneless ...
Patrick J. Farber +10 more
core +1 more source
We present a novel proteolysis‐targeting chimera (PROTAC) system conjugated to lipoic acid gold nanoclusters (PLANC), designed to degrade pTau, regulate inflammatory signaling, and effectively traverse the blood‐brain barrier (BBB). PLANC degraded pTau at various phosphorylation sites, with mechanistic studies confirming proteasome‐mediated degradation
Sarah Nevins +9 more
wiley +1 more source

