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Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9547173

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

About this item

Full title

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

Publisher

New York: Portland Press Ltd The Biochemical Society

Journal title

Bioscience reports, 2022-10, Vol.42 (10), p.1

Language

English

Formats

Publication information

Publisher

New York: Portland Press Ltd The Biochemical Society

More information

Scope and Contents

Contents

There are 28 unique human members of the homologous to E6AP C-terminus (HECT) E3 ubiquitin ligase family. Each member of the HECT E3 ubiquitin ligases contains a conserved bilobal HECT domain of approximately 350 residues found near their C-termini that is responsible for their respective ubiquitylation activities. Recent studies have begun to eluc...

Alternative Titles

Full title

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9547173

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9547173

Other Identifiers

ISSN

0144-8463

E-ISSN

1573-4935

DOI

10.1042/BSR20221036

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