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Updated: Jan 22, 2026

A β-glucuronidase GUS Based Cell Death Assay
07:35

A β-glucuronidase GUS Based Cell Death Assay

Published on: May 6, 2011

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Keeping the Death Protein in Check

Longfei Wang1, Hao Wu1

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.

Immunity
|July 18, 2019
PubMed

Insights

Researchers reveal the crystal structures of human and mouse Gasdermin D, an inflammatory cell death executor. These findings clarify Gasdermin D

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Gasdermin D (GSDMD) is a key protein mediating programmed inflammatory cell death, a critical process in immunity and disease.
  • Understanding the structural basis of GSDMD regulation is essential for developing targeted therapies.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying Gasdermin D autoinhibition and activation.
  • To provide atomic-level insights into the full-length human and mouse Gasdermin D structures.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structures of full-length human and mouse Gasdermin D.

Main Results:

  • The crystal structures reveal the molecular details of Gasdermin D in its auto-inhibited conformation.
  • These structures provide a framework for understanding how Gasdermin D is activated to permeabilize membranes.

Conclusions:

  • The reported structures offer unprecedented insights into Gasdermin D's regulatory mechanisms.
  • This structural information will be invaluable for the rational design of novel therapeutics targeting Gasdermin D in inflammatory diseases.

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