Results 231 to 240 of about 39,289 (292)
Decreased sialic acid increases the adhesion of RBC membranes to immunoglobulins leading to an increased erythrocyte sedimentation rate (ESR). The increase in reactive oxygen species (ROS) damages the sialic acid glycosyl chains on the surface of RBC membrane proteins, causing the membrane proteins to be overexposed to the plasma environment due to the
Sicheng Bian +16 more
wiley +1 more source
A novel assay evaluates plant biostimulants targeting the brassinosteroid receptor BRI1, a central component in plant growth and development. By expressing BRI1 in fission yeast, functional activation by brassinolide (BL) was enabled. Transcriptomic profiling identified BL‐responsive genes, leading to a GFP‐based reporter system. This platform offers a
Maribel Marquina +9 more
wiley +1 more source
CLEC18A is a previously poorly characterized C‐type lectin. We mapped the expression of CLEC18A to the proximal tubule of the kidney and found CLEC18A to interact with sulfated glycosaminoglycans on proteoglycans. Furthermore, we found that CLEC18A plays an important role in hindering the progression of clear cell renal cell carcinomas in humans and in
Gustav Jonsson +10 more
wiley +1 more source
Heteromeric cis‐prenyltransferases (CPT) are indispensable for dolichol synthesis and protein N‐glycosylation in most eukaryotes. The catalytic subunits are strongly conserved throughout evolution, in contrast to the evolutionarily variable accessory subunits. The POC1 protein from Paramecium tetraurelia is the smallest identified CPT‐accessory subunit
Agnieszka Onysk +8 more
wiley +1 more source
We characterize the PLTL lectin from Photorhabdus laumondii, which adopts a unique TNF‐like fold. Binding assays reveal a preference for branched histo‐blood group oligosaccharides. Protein crystallography uncovers a novel hexameric assembly and identifies key residues involved in carbohydrate recognition.
Filip Melicher +7 more
wiley +1 more source
A guide to the types, structures, and multifaceted functions of matrix metalloproteinases in cancer
Matrix metalloproteinases (MMPs) orchestrate cancer progression and metastasis through proteolytic and non‐proteolytic actions. By remodeling the tumor microenvironment, enhancing growth factor availability, and modulating cell behavior, MMPs promote proliferation, migration or invasion, and epithelial‐to‐mesenchymal transition. Alongside extracellular
Zoi Piperigkou +4 more
wiley +1 more source
Behind the scenes: how the EMILIN/Multimerin family shapes the cancer landscape
The EMILIN/Multimerin family members regulate key hallmarks of cancer—including apoptosis, angiogenesis, metastasis, and tumor microenvironment remodeling. As indicated, their function in immune evasion, drug resistance, and metabolic reprogramming remains largely unexplored.
Evelina Poletto +9 more
wiley +1 more source
Multimeric IgM‐fragment crystallizable region (Fc) fragments retain the ability to bind C1q and initiate the classical complement pathway, leading to C4 activation and deposition in vitro. However, the Fc cores can also inhibit complement‐dependent cytotoxicity by competing with surface‐bound antibodies for C1q engagement.
Andrea J. Pinto +9 more
wiley +1 more source
The authors investigated the effects of various glycan ligands for CLEC10A, a lectin receptor expressed on dendritic cells (DCs). Monocyte‐derived DCs were stimulated with glycan‐conjugated dendrimers in combination with the TLR1/2 ligand Pam3CysK4, and responses were investigated at the mRNA and protein level.
Nadia L. van der Meijs +7 more
wiley +1 more source

