Results 61 to 70 of about 17,882 (284)

Penfluridol Triggers GSDME‐Mediated Immunogenic Pyroptosis to Potentiate Antitumor Immunotherapy

open access: yesAdvanced Science, EarlyView.
A high‐throughput screen of FDA‐approved antipsychotics identifies penfluridol as a potent pyroptosis inducer acting via direct TTI1 inhibition. This triggers TNFA‐NFKB signaling and caspase‐8/‐3‐dependent GSDME cleavage. The compound stimulates antitumor immunity alone and synergizes with anti‐PD‐1 therapy, while low TTI1 expression emerges as a ...
Linfeng Li   +11 more
wiley   +1 more source

Ion Man: GSDMD Punches Pores to Knock Out cGAS [PDF]

open access: yesImmunity, 2018
The pore-forming protein GSDMD promotes cytokine release and induces pyroptotic cell death. In this issue of Immunity, Banerjee et al. (2018) document how GSDMD triggers potassium efflux to inhibit cGAS-STING and prevent damaging interferon production after bacterial infection.
Rebecca, Feltham, James E, Vince
openaire   +2 more sources

Compound loss of GSDMD and GSDME function is necessary to achieve maximal therapeutic effect in colitis [PDF]

open access: yes, 2022
Gasdermin D (GSDMD) and gasdermin E (GSDME) perpetuate inflammation by mediating the release of cytokines such as interleukin-1β (IL-1β) and IL-18. However, not only are the actions of GSDMD in colitis still controversial, but its interplay with GSDME in
Mbalaviele, Gabriel   +9 more
core   +1 more source

Targeted Degradation of STING by a Neutrophil Membrane‐Coated Nanoplatform Suppresses Microglial Pyroptosis After Subarachnoid Hemorrhage

open access: yesAdvanced Science, EarlyView.
MG1@NM‐Px serves as a microglia‐targeted STING‐degrading nanoplatform for subarachnoid hemorrhage. Following systemic administration, it crosses the blood–brain barrier and accumulates in activated microglia. STP1‐mediated STING ubiquitination and degradation suppress MAPK/inflammasome signaling, GSDME‐mediated pyroptosis, and IL‐1β release, revealing ...
Ruotian Zhang   +13 more
wiley   +1 more source

GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death [PDF]

open access: yes, 2016
Pyroptosis is a lytic type of cell death that is initiated by inflammatory caspases. These caspases are activated within multi-protein inflammasome complexes that assemble in response to pathogens and endogenous danger signals.
Stahlberg, Henning   +9 more
core   +2 more sources

Membrane‐Active Peptide Protects Against Inflammation by Targeting NLRP3 Activation at the Trans‐Golgi Network

open access: yesAdvanced Science, EarlyView.
The membrane‐active peptide Pep19‐2.5 reduces harmful inflammation by blocking activation of the NLRP3 inflammasome at trans‐Golgi network membranes. By targeting key membrane interactions, Pep19‐2.5 suppresses inflammatory IL‐1β production and alleviates allergic airway inflammation in mice, leading to reduced immune cell infiltration and improved ...
Jonas Engelhardt   +16 more
wiley   +1 more source

Rewiring Pyroptosis to Potentiate Cancer Immunotherapy via a Gasdermin D Agonist Bypassing Caspase‐3

open access: yesAdvanced Science, EarlyView.
This work introduces a small‐molecule agonist, DIBDO, that bypasses Casp‐3 to directly trigger GSDMD‐mediated pyroptosis in tumors. Activated by glutathione, DIBDO generates singlet oxygen and molecular iodine, blocking Casp‐3 pathways and inducing immunogenic cell death.
Dan Zhao   +6 more
wiley   +1 more source

Gasdermin D mediates endoplasmic reticulum stress via FAM134B to regulate cardiomyocyte autophagy and apoptosis in doxorubicin-induced cardiotoxicity

open access: yesCell Death and Disease, 2022
Cardiomyocyte pyroptosis and apoptosis play a vital role in the pathophysiology of several cardiovascular diseases. Our recent study revealed that gasdermin D (GSDMD) can promote myocardial I/R injury via the caspase-11/GSDMD pathway.
Ya’nan Qu   +12 more
doaj   +1 more source

Chemically induced dimerization of GSDMD C-terminal domain blocks GSDMD N-terminal domain-mediated pyroptosis

open access: yesCell Death Discovery
Abstract GSDMD is a pyroptosis executioner in which the C-terminal domain completely inhibits the pore-forming ability of the N-terminal domain. Caspase cleavage separates GSDMD into the free C-terminal fragment (GD-CT) and the free N-terminal fragment (GD-NT). Although GD-CT retains the ability to bind with GD-NT, it can no longer completely
Jixuan Xu   +13 more
openaire   +2 more sources

Data_Sheet_2_Ablation of GSDMD Attenuates Neurological Deficits and Neuropathological Alterations After Traumatic Brain Injury.CSV

open access: yes, 2022
Pyroptosis plays a significant role in neuroinflammation after traumatic brain injury (TBI). However, the role of pyroptosis executor Gasdermin D (GSDMD) in neurological deficits and neuropathological alterations after TBI have not been elucidated.
Hao Du (748002)   +4 more
core   +1 more source

Home - About - Disclaimer - Privacy