E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP

10.1038/ncomms15865

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Main Authors:	Bist P., Cheong W.S., Ng A., Dikshit N., Kim B.-H., Pulloor N.K., Khameneh H.J., Hedl M., Shenoy A.R., Balamuralidhar V., Malik N.B.A., Hong M., Neutzner A., Chin K.-C., Kobayashi K.S., Bertoletti A., Mortellaro A., Abraham C., MacMicking J.D., Xavier R.J., Sukumaran B.
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	Nature Publishing Group 2020
Subjects:	caspase recruitment domain protein 15 immunoglobulin enhancer binding protein muramyl dipeptide protein protein rip2 protein znrf4 transcription factor RelA ubiquitin protein ligase E3 unclassified drug DNA binding protein n acetylmuramylalanyl dextro isoglutamine NOD2 protein, human receptor interacting protein serine threonine kinase 2 RIPK2 protein, human ZNRF4 protein, human Znrf4 protein, mouse bacterial disease biodegradation cell organelle cells and cell components enzyme enzyme activity immune response immunity peptide rodent animal experiment Article caspase activation and recruitment domain controlled study cytokine release cytokine response endoplasmic reticulum human human cell in vitro study in vivo study monocyte mouse nonhuman protein degradation protein localization protein protein interaction regulatory mechanism signal transduction ubiquitination animal C57BL mouse drug effect genetics HEK293 cell line immunological tolerance immunology Listeria monocytogenes listeriosis metabolism mutant mouse strain pathogenicity physiology Bacteria (microorganisms) Mus Acetylmuramyl-Alanyl-Isoglutamine Animals DNA-Binding Proteins HEK293 Cells Humans Immune Tolerance Listeriosis Mice, Inbred C57BL Mice, Mutant Strains Monocytes NF-kappa B Nod2 Signaling Adaptor Protein Receptor-Interacting Protein Serine-Threonine Kinase 2 Signal Transduction Ubiquitination
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/174491
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1744912023-11-01T07:48:15Z E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP Bist P. Cheong W.S. Ng A. Dikshit N. Kim B.-H. Pulloor N.K. Khameneh H.J. Hedl M. Shenoy A.R. Balamuralidhar V. Malik N.B.A. Hong M. Neutzner A. Chin K.-C. Kobayashi K.S. Bertoletti A. Mortellaro A. Abraham C. MacMicking J.D. Xavier R.J. Sukumaran B. DUKE-NUS MEDICAL SCHOOL caspase recruitment domain protein 15 immunoglobulin enhancer binding protein muramyl dipeptide protein protein rip2 protein znrf4 transcription factor RelA ubiquitin protein ligase E3 unclassified drug caspase recruitment domain protein 15 DNA binding protein immunoglobulin enhancer binding protein n acetylmuramylalanyl dextro isoglutamine NOD2 protein, human receptor interacting protein serine threonine kinase 2 RIPK2 protein, human ZNRF4 protein, human Znrf4 protein, mouse bacterial disease biodegradation cell organelle cells and cell components enzyme enzyme activity immune response immunity peptide protein rodent animal experiment Article caspase activation and recruitment domain controlled study cytokine release cytokine response endoplasmic reticulum human human cell immunity in vitro study in vivo study monocyte mouse nonhuman protein degradation protein localization protein protein interaction regulatory mechanism signal transduction ubiquitination animal C57BL mouse drug effect genetics HEK293 cell line immunological tolerance immunology Listeria monocytogenes listeriosis metabolism mutant mouse strain pathogenicity physiology signal transduction Bacteria (microorganisms) Listeria monocytogenes Mus Acetylmuramyl-Alanyl-Isoglutamine Animals DNA-Binding Proteins HEK293 Cells Humans Immune Tolerance Listeria monocytogenes Listeriosis Mice, Inbred C57BL Mice, Mutant Strains Monocytes NF-kappa B Nod2 Signaling Adaptor Protein Receptor-Interacting Protein Serine-Threonine Kinase 2 Signal Transduction Ubiquitination 10.1038/ncomms15865 Nature Communications 8 15865 2020-09-06T16:04:57Z 2020-09-06T16:04:57Z 2017 Article Bist P., Cheong W.S., Ng A., Dikshit N., Kim B.-H., Pulloor N.K., Khameneh H.J., Hedl M., Shenoy A.R., Balamuralidhar V., Malik N.B.A., Hong M., Neutzner A., Chin K.-C., Kobayashi K.S., Bertoletti A., Mortellaro A., Abraham C., MacMicking J.D., Xavier R.J., Sukumaran B. (2017). E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP. Nature Communications 8 : 15865. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms15865 2041-1723 https://scholarbank.nus.edu.sg/handle/10635/174491 Nature Publishing Group Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	caspase recruitment domain protein 15 immunoglobulin enhancer binding protein muramyl dipeptide protein protein rip2 protein znrf4 transcription factor RelA ubiquitin protein ligase E3 unclassified drug caspase recruitment domain protein 15 DNA binding protein immunoglobulin enhancer binding protein n acetylmuramylalanyl dextro isoglutamine NOD2 protein, human receptor interacting protein serine threonine kinase 2 RIPK2 protein, human ZNRF4 protein, human Znrf4 protein, mouse bacterial disease biodegradation cell organelle cells and cell components enzyme enzyme activity immune response immunity peptide protein rodent animal experiment Article caspase activation and recruitment domain controlled study cytokine release cytokine response endoplasmic reticulum human human cell immunity in vitro study in vivo study monocyte mouse nonhuman protein degradation protein localization protein protein interaction regulatory mechanism signal transduction ubiquitination animal C57BL mouse drug effect genetics HEK293 cell line immunological tolerance immunology Listeria monocytogenes listeriosis metabolism mutant mouse strain pathogenicity physiology signal transduction Bacteria (microorganisms) Listeria monocytogenes Mus Acetylmuramyl-Alanyl-Isoglutamine Animals DNA-Binding Proteins HEK293 Cells Humans Immune Tolerance Listeria monocytogenes Listeriosis Mice, Inbred C57BL Mice, Mutant Strains Monocytes NF-kappa B Nod2 Signaling Adaptor Protein Receptor-Interacting Protein Serine-Threonine Kinase 2 Signal Transduction Ubiquitination
spellingShingle	caspase recruitment domain protein 15 immunoglobulin enhancer binding protein muramyl dipeptide protein protein rip2 protein znrf4 transcription factor RelA ubiquitin protein ligase E3 unclassified drug caspase recruitment domain protein 15 DNA binding protein immunoglobulin enhancer binding protein n acetylmuramylalanyl dextro isoglutamine NOD2 protein, human receptor interacting protein serine threonine kinase 2 RIPK2 protein, human ZNRF4 protein, human Znrf4 protein, mouse bacterial disease biodegradation cell organelle cells and cell components enzyme enzyme activity immune response immunity peptide protein rodent animal experiment Article caspase activation and recruitment domain controlled study cytokine release cytokine response endoplasmic reticulum human human cell immunity in vitro study in vivo study monocyte mouse nonhuman protein degradation protein localization protein protein interaction regulatory mechanism signal transduction ubiquitination animal C57BL mouse drug effect genetics HEK293 cell line immunological tolerance immunology Listeria monocytogenes listeriosis metabolism mutant mouse strain pathogenicity physiology signal transduction Bacteria (microorganisms) Listeria monocytogenes Mus Acetylmuramyl-Alanyl-Isoglutamine Animals DNA-Binding Proteins HEK293 Cells Humans Immune Tolerance Listeria monocytogenes Listeriosis Mice, Inbred C57BL Mice, Mutant Strains Monocytes NF-kappa B Nod2 Signaling Adaptor Protein Receptor-Interacting Protein Serine-Threonine Kinase 2 Signal Transduction Ubiquitination Bist P. Cheong W.S. Ng A. Dikshit N. Kim B.-H. Pulloor N.K. Khameneh H.J. Hedl M. Shenoy A.R. Balamuralidhar V. Malik N.B.A. Hong M. Neutzner A. Chin K.-C. Kobayashi K.S. Bertoletti A. Mortellaro A. Abraham C. MacMicking J.D. Xavier R.J. Sukumaran B. E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
description	10.1038/ncomms15865
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL Bist P. Cheong W.S. Ng A. Dikshit N. Kim B.-H. Pulloor N.K. Khameneh H.J. Hedl M. Shenoy A.R. Balamuralidhar V. Malik N.B.A. Hong M. Neutzner A. Chin K.-C. Kobayashi K.S. Bertoletti A. Mortellaro A. Abraham C. MacMicking J.D. Xavier R.J. Sukumaran B.
format	Article
author	Bist P. Cheong W.S. Ng A. Dikshit N. Kim B.-H. Pulloor N.K. Khameneh H.J. Hedl M. Shenoy A.R. Balamuralidhar V. Malik N.B.A. Hong M. Neutzner A. Chin K.-C. Kobayashi K.S. Bertoletti A. Mortellaro A. Abraham C. MacMicking J.D. Xavier R.J. Sukumaran B.
author_sort	Bist P.
title	E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
title_short	E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
title_full	E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
title_fullStr	E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
title_full_unstemmed	E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP
title_sort	e3 ubiquitin ligase znrf4 negatively regulates nod2 signalling and induces tolerance to mdp
publisher	Nature Publishing Group
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/174491
_version_	1781792196883644416

E3 Ubiquitin ligase ZNRF4 negatively regulates NOD2 signalling and induces tolerance to MDP

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