Results 271 to 280 of about 126,085 (349)

Structural and functional characterization of the newly identified Photorhabdus laumondii tumor necrosis factor‐like lectin

open access: yesThe FEBS Journal, EarlyView.
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

Intestinal REG3 Lectins Protect against Alcoholic Steatohepatitis by Reducing Mucosa-Associated Microbiota and Preventing Bacterial Translocation. [PDF]

open access: yesCell Host Microbe
Wang L   +11 more
europepmc   +1 more source

A guide to the types, structures, and multifaceted functions of matrix metalloproteinases in cancer

open access: yesThe FEBS Journal, EarlyView.
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

Odoribacter splanchnicus lipooligosaccharide: an uncommon structure with weak immunostimulatory activity. [PDF]

open access: yesChem Sci
Tiemblo-Martin M   +12 more
europepmc   +1 more source

Behind the scenes: how the EMILIN/Multimerin family shapes the cancer landscape

open access: yesThe FEBS Journal, EarlyView.
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

The fc fragment of IgMs binds C1q to activate the first step of the classical complement pathway, while inhibiting complement‐dependent cytotoxicity

open access: yesThe FEBS Journal, EarlyView.
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

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