Structural basis of RIP2 activation and signaling

10.1038/s41467-018-07447-9

Saved in:

Bibliographic Details
Main Authors:	Gong, Q, Long, Z, Zhong, F.L, Teo, D.E.T, Jin, Y, Yin, Z, Boo, Z.Z, Zhang, Y, Zhang, J, Yang, R, Bhushan, S, Reversade, B, Li, Z, Wu, B
Other Authors:	PAEDIATRICS
Format:	Article
Published:	Nature Publishing Group 2020
Subjects:	adaptor protein beta actin caspase recruitment domain protein 15 caspase recruitment domain protein 4 caspase recruitment domain signaling protein mitochondria antiviral signaling protein monomer nlrc4 protein oligomer receptor interacting protein serine threonine kinase 2 snap protein unclassified drug protein binding recombinant protein RIPK2 protein, human bacterial disease chemical binding infectivity molecular analysis pathogen protein ultrastructure Article caspase activation and recruitment domain cell organelle controlled study electron tomography enzyme activation enzyme activity human in vitro study oligomerization protein protein interaction riposome signal transduction site directed mutagenesis amino acid sequence chemistry cryoelectron microscopy HEK293 cell line metabolism molecular model protein domain protein multimerization structure activity relation Bacteria (microorganisms) Mammalia Amino Acid Sequence CARD Signaling Adaptor Proteins Cryoelectron Microscopy HEK293 Cells Humans Models, Molecular Protein Binding Protein Domains Protein Multimerization Receptor-Interacting Protein Serine-Threonine Kinase 2 Recombinant Proteins Signal Transduction Structure-Activity Relationship
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/178379
Tags:	Add Tag No Tags, Be the first to tag this record!
Institution:	National University of Singapore

id	sg-nus-scholar.10635-178379
record_format	dspace
spelling	sg-nus-scholar.10635-1783792024-04-24T06:52:41Z Structural basis of RIP2 activation and signaling Gong, Q Long, Z Zhong, F.L Teo, D.E.T Jin, Y Yin, Z Boo, Z.Z Zhang, Y Zhang, J Yang, R Bhushan, S Reversade, B Li, Z Wu, B PAEDIATRICS adaptor protein beta actin caspase recruitment domain protein 15 caspase recruitment domain protein 4 caspase recruitment domain signaling protein mitochondria antiviral signaling protein monomer nlrc4 protein oligomer receptor interacting protein serine threonine kinase 2 snap protein unclassified drug protein binding receptor interacting protein serine threonine kinase 2 recombinant protein RIPK2 protein, human bacterial disease chemical binding infectivity molecular analysis pathogen protein ultrastructure Article caspase activation and recruitment domain cell organelle controlled study electron tomography enzyme activation enzyme activity human in vitro study oligomerization protein protein interaction riposome signal transduction site directed mutagenesis amino acid sequence chemistry cryoelectron microscopy HEK293 cell line metabolism molecular model protein domain protein multimerization structure activity relation ultrastructure Bacteria (microorganisms) Mammalia Amino Acid Sequence CARD Signaling Adaptor Proteins Cryoelectron Microscopy HEK293 Cells Humans Models, Molecular Protein Binding Protein Domains Protein Multimerization Receptor-Interacting Protein Serine-Threonine Kinase 2 Recombinant Proteins Signal Transduction Structure-Activity Relationship 10.1038/s41467-018-07447-9 Nature Communications 9 1 4993 2020-10-20T09:37:22Z 2020-10-20T09:37:22Z 2018 Article Gong, Q, Long, Z, Zhong, F.L, Teo, D.E.T, Jin, Y, Yin, Z, Boo, Z.Z, Zhang, Y, Zhang, J, Yang, R, Bhushan, S, Reversade, B, Li, Z, Wu, B (2018). Structural basis of RIP2 activation and signaling. Nature Communications 9 (1) : 4993. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-018-07447-9 2041-1723 https://scholarbank.nus.edu.sg/handle/10635/178379 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Nature Publishing Group Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	adaptor protein beta actin caspase recruitment domain protein 15 caspase recruitment domain protein 4 caspase recruitment domain signaling protein mitochondria antiviral signaling protein monomer nlrc4 protein oligomer receptor interacting protein serine threonine kinase 2 snap protein unclassified drug protein binding receptor interacting protein serine threonine kinase 2 recombinant protein RIPK2 protein, human bacterial disease chemical binding infectivity molecular analysis pathogen protein ultrastructure Article caspase activation and recruitment domain cell organelle controlled study electron tomography enzyme activation enzyme activity human in vitro study oligomerization protein protein interaction riposome signal transduction site directed mutagenesis amino acid sequence chemistry cryoelectron microscopy HEK293 cell line metabolism molecular model protein domain protein multimerization structure activity relation ultrastructure Bacteria (microorganisms) Mammalia Amino Acid Sequence CARD Signaling Adaptor Proteins Cryoelectron Microscopy HEK293 Cells Humans Models, Molecular Protein Binding Protein Domains Protein Multimerization Receptor-Interacting Protein Serine-Threonine Kinase 2 Recombinant Proteins Signal Transduction Structure-Activity Relationship
spellingShingle	adaptor protein beta actin caspase recruitment domain protein 15 caspase recruitment domain protein 4 caspase recruitment domain signaling protein mitochondria antiviral signaling protein monomer nlrc4 protein oligomer receptor interacting protein serine threonine kinase 2 snap protein unclassified drug protein binding receptor interacting protein serine threonine kinase 2 recombinant protein RIPK2 protein, human bacterial disease chemical binding infectivity molecular analysis pathogen protein ultrastructure Article caspase activation and recruitment domain cell organelle controlled study electron tomography enzyme activation enzyme activity human in vitro study oligomerization protein protein interaction riposome signal transduction site directed mutagenesis amino acid sequence chemistry cryoelectron microscopy HEK293 cell line metabolism molecular model protein domain protein multimerization structure activity relation ultrastructure Bacteria (microorganisms) Mammalia Amino Acid Sequence CARD Signaling Adaptor Proteins Cryoelectron Microscopy HEK293 Cells Humans Models, Molecular Protein Binding Protein Domains Protein Multimerization Receptor-Interacting Protein Serine-Threonine Kinase 2 Recombinant Proteins Signal Transduction Structure-Activity Relationship Gong, Q Long, Z Zhong, F.L Teo, D.E.T Jin, Y Yin, Z Boo, Z.Z Zhang, Y Zhang, J Yang, R Bhushan, S Reversade, B Li, Z Wu, B Structural basis of RIP2 activation and signaling
description	10.1038/s41467-018-07447-9
author2	PAEDIATRICS
author_facet	PAEDIATRICS Gong, Q Long, Z Zhong, F.L Teo, D.E.T Jin, Y Yin, Z Boo, Z.Z Zhang, Y Zhang, J Yang, R Bhushan, S Reversade, B Li, Z Wu, B
format	Article
author	Gong, Q Long, Z Zhong, F.L Teo, D.E.T Jin, Y Yin, Z Boo, Z.Z Zhang, Y Zhang, J Yang, R Bhushan, S Reversade, B Li, Z Wu, B
author_sort	Gong, Q
title	Structural basis of RIP2 activation and signaling
title_short	Structural basis of RIP2 activation and signaling
title_full	Structural basis of RIP2 activation and signaling
title_fullStr	Structural basis of RIP2 activation and signaling
title_full_unstemmed	Structural basis of RIP2 activation and signaling
title_sort	structural basis of rip2 activation and signaling
publisher	Nature Publishing Group
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/178379
_version_	1800914494340202496

Structural basis of RIP2 activation and signaling

Similar Items