Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using...
Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen–deuterium exchange mass spectrometry
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Publisher
Cham: Springer International Publishing
Journal title
Language
English
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Publisher
Cham: Springer International Publishing
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Scope and Contents
Contents
Tripartite motif (TRIM) E3 ligases target specific substrates, including viral proteins, for proteasomal degradation, and are thus essential regulators of the innate antiviral response. TRIM69 ubiquitinates the non-structural NS3 protein of Dengue virus for its degradation by the host machinery. This antiviral strategy abrogates the immunosuppressi...
Alternative Titles
Full title
Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen–deuterium exchange mass spectrometry
Authors, Artists and Contributors
Author / Creator
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Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11072344
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11072344
Other Identifiers
ISSN
1420-682X
E-ISSN
1420-9071
DOI
10.1007/s00018-022-04245-x
