Biomolecular Structure To Mechanism Division
Design and evaluation of tadpole-like conformational antimicrobial peptides
Antimicrobial peptides are promising alternatives to conventional antibiotics. Herein, we report a class of “tadpole-like” peptides consisting of an amphipathic α-helical head and an aromatic tail.
ReadElucidating the Effect of Polyethylene Terephthalate Chain Structure on Its Enzymatic Degradation Behavior
KEYWORDS: Polyethylene terephthalate chemical modification crystallinity structural characterization thermal properties enzymatic degradation
ReadDisrupting the Dok3–Card9 Interaction with Synthetic Peptides Enhances Antifungal Effector Functions of Human Neutrophils
neutrophils; antifungal immunity; Dok3; Card9; interference peptide
ReadDisrupted chromatin architecture in olfactory sensory neurons: looking for the link from COVID-19 infection to anosmia
The COVID-19 pandemic, caused by the SARS-CoV-2 coronavirus, has placed significant strain on medical resources worldwide, and early detection and isolation has been the primary strategy by which, research establishments and governments worked to contain the disease spread.
ReadSequence-dependent model of allosteric communication
The omnipresence and diversity of allosteric regulation in proteins and protein associations complemented by the potential for the design of allosterically acting biologics and drugs call for the development of a new generation of computational models for the analysis of allostery and rational engineering/design of desired signaling and effector molecules determining it.
ReadDOK3 promotes atopic dermatitis by enabling the phosphatase PP4C to inhibit the T cell signaling mediator CARD11
Atopic dermatitis (a type of eczema) is an itchy and painful inflammatory skin disorder of unknown cause, which is associated with decreased function of T cell signaling mediator CARD11 in some patients. Loh et al. found that a scaffolding protein may contribute to CARD11 repression and increased severity of atopic dermatitis symptoms in mice. The scaffolding protein DOK3, which was abundant in patient blood cells and bound strongly to patient-derived CARD11 variants, recruited the phosphatase PP4C to CARD11, functionally inactivating it and impairing T cell regulation. Reducing DOK3 abundance alleviated the symptoms in a mouse model of atopic dermatitis. Thus, the strength of the DOK3-CARD11 interaction may predict symptom severity in atopic dermatitis patients.
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