Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways. [PDF]
PLoS Pathog, 2021 Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known
Parks SC +13 more
europepmc +3 more sources
Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection
eLife, 2014 Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified.
Mehabaw G Derebe +8 more
doaj +2 more sources
Structure-guided screening of FAR-1 antagonists with multi-stage anthelmintic activity. [PDF]
Antimicrob Agents ChemotherFatty acid and retinol binding proteins (FARs) are nematode-specific proteins that orchestrate lipid metabolism, development, and host immune response.
Wen J +9 more
europepmc +2 more sources
Possible Interacting Proteins for Retinol Binding Protein and Cellular Retinol Binding Protein [PDF]
, 2011 Retinol or vitamin A is crucial for many biological processes in the body such as proliferation, differentiation and reproduction. It is mainly stored in the liver and can be broken down to retinoic acid inside the cell. It travels in the circulatory system attached to Retinol Binding Protein (RBP) and its transport into the cell is mediated by the RBP
Cooney, David
core +5 more sources
The FAR protein family of parasitic nematodes.
PLoS Pathogens, 2022 Fatty acid-and retinol-binding proteins (FARs) belong to a unique family of excreted/secreted proteins (ESPs) found exclusively in nematodes. Much of our understanding of these proteins, however, is limited to their in vitro binding characteristics ...
Sophia C Parks +3 more
doaj +2 more sources
Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core +6 more sources
Identification of Transthyretin Tetramer Kinetic Stabilizers That Are Capable of Inhibiting the Retinol-Dependent Retinol Binding Protein 4-Transthyretin Interaction [PDF]
, 2021 Dissociation of transthyretin (TTR) tetramers may lead to misfolding and aggregation of pro-amyloidogenic monomers, which underlies TTR amyloidosis (ATTR) pathophysiology.
Arun, Raja +7 more
core +1 more source
DreamFold: A World Model to efficiently generate protein folding pathways in the latent space. [PDF]
Protein SciAbstract While there is an abundance of static data for the structure of biological macromolecules, the data regarding their folding mechanisms and dynamics is scarce, posing a challenge to the training of AI models. The World Model approach, which has been very successful in robotics, can come in handy in this regard. From limited data, it can build a
Ianeselli A +3 more
europepmc +2 more sources
Retinoid-binding proteins: similar protein architectures bind similar ligands via completely different ways. [PDF]
PLoS ONE, 2012 BACKGROUND: Retinoids are a class of compounds that are chemically related to vitamin A, which is an essential nutrient that plays a key role in vision, cell growth and differentiation. In vivo, retinoids must bind with specific proteins to perform their
Yu-Ru Zhang, Yu-Qi Zhao, Jing-Fei Huang
doaj +1 more source
Production of functional human vitamin A transporter/RBP receptor (STRA6) for structure determination. [PDF]
PLoS ONE, 2015 STRA6 is a plasma membrane protein that mediates the transport of vitamin A, or retinol, from plasma retinol binding protein (RBP) into the cell. Mutations in human STRA6 are associated with Matthew-Wood syndrome, which is characterized by severe ...
Conor J Breen +5 more
doaj +1 more source