Related Experiment Video
Updated: Jul 12, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Multifaceted roles and regulation of nucleotide-binding oligomerization domain containing proteins
Charneal L Dixon1, Amy Wu2, Gregory D Fairn1,2,3
1Department of Pathology, Dalhousie University, Halifax, NS, Canada.
Abstract:
Nucleotide-binding oligomerization domain-containing proteins, NOD1 and NOD2, are cytosolic receptors that recognize dipeptides and tripeptides derived from the bacterial cell wall component peptidoglycan (PGN). During the past two decades, studies have revealed several roles for NODs beyond detecting PGN fragments, including activation of an innate immune anti-viral response, NOD-mediated autophagy, and ER stress induced inflammation. Recent studies have also clarified the dynamic regulation of NODs at cellular membranes to generate specific and balanced immune responses. This review will describe how NOD1 and NOD2 detect microbes and cellular stress and detail the molecular mechanisms that regulate activation and signaling while highlighting new evidence and the impact on inflammatory disease pathogenesis.
More Related Videos
Related Concept Videos
Regulation of Nuclear Protein Sorting
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Cooperative Binding of Transcription Regulators
Regulation of Expression at Multiple Steps

