Results 41 to 50 of about 351,018 (238)

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

G-Protein Coupled Receptors Targeted by Analgesic Venom Peptides

open access: yesToxins, 2017
Chronic pain is a complex and debilitating condition associated with a large personal and socioeconomic burden. Current pharmacological approaches to treating chronic pain such as opioids, antidepressants and anticonvulsants exhibit limited efficacy in ...
James T. Daniel, Richard J. Clark
doaj   +1 more source

By dawn or dusk—how circadian timing rewrites bacterial infection outcomes

open access: yesFEBS Letters, EarlyView.
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo   +2 more
wiley   +1 more source

Fusion protein strategies for cryo-EM study of G protein-coupled receptors

open access: yesNature Communications, 2022
Here, Zhang et al. explore fusion protein strategies to facilitate cryo-EM structural studies of GPCRs alone- without signal transducers- in ligand bound or unliganded form.
Kaihua Zhang   +4 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Allostery of atypical modulators at oligomeric G protein-coupled receptors

open access: yesScientific Reports, 2021
Many G protein-coupled receptors (GPCRs) are therapeutic targets, with most drugs acting at the orthosteric site. Some GPCRs also possess allosteric sites, which have become a focus of drug discovery.
Rabindra V. Shivnaraine   +7 more
doaj   +1 more source

Agonist and antagonist TRUPATH assays for G protein-coupled receptors

open access: yesSTAR Protocols, 2022
Summary: TRUPATH is a bioluminescence resonance energy transfer-based platform for quantifying G protein-coupled receptor activity via dissociation of heterotrimeric G protein biosensors.
Jeffrey F. DiBerto   +3 more
doaj   +1 more source

Molecular bases of circadian magnesium rhythms across eukaryotes

open access: yesFEBS Letters, EarlyView.
Circadian rhythms in intracellular [Mg2+] exist across eukaryotic kingdoms. Central roles for Mg2+ in metabolism suggest that Mg2+ rhythms could regulate daily cellular energy and metabolism. In this Perspective paper, we propose that ancestral prokaryotic transport proteins could be responsible for mediating Mg2+ rhythms and posit a feedback model ...
Helen K. Feord, Gerben van Ooijen
wiley   +1 more source

Stabilization of G protein-coupled receptors by point mutations

open access: yesFrontiers in Pharmacology, 2015
G protein-coupled receptors (GPCRs) are flexible integral membrane proteins involved in transmembrane signaling. Their involvement in many physiological processes makes them interesting targets for drug development.
Franziska eHeydenreich   +7 more
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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