Shuttle factor UBQLN Ubiquitin-associated adjacent domain Ubiquitin-associated domain Ubiquitin-proteasome pathway

Journal

Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371

Informations de publication

Date de publication:
06 2023
Historique:
received: 12 01 2023
accepted: 30 03 2023
medline: 2 6 2023
pubmed: 7 4 2023
entrez: 6 4 2023
Statut: ppublish

Résumé

UBQLN1 functions in autophagy and proteasome-mediated protein degradation. It contains an N-terminal ubiquitin-like domain (UBL), a C-terminal ubiquitin-associated domain (UBA), and a flexible central region which functions as a chaperone to prevent protein aggregation. Here, we report the

Identifiants

pubmed: 37022617
doi: 10.1007/s12104-023-10127-5
pii: 10.1007/s12104-023-10127-5
pmc: PMC10232632
doi:

Substances chimiques

Proteasome Endopeptidase Complex EC 3.4.25.1
Ubiquitin 0
Molecular Chaperones 0
Nitrogen N762921K75

Types de publication

Journal Article Research Support, N.I.H., Intramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

101-106

Subventions

Organisme : NCI NIH HHS
ID : 1 ZIA BC011490
Pays : United States

Informations de copyright

© 2023. This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply.

Références

Mol Cell. 2018 Mar 15;69(6):965-978.e6
pubmed: 29526694
J Mol Biol. 2019 Mar 1;431(5):939-955
pubmed: 30664872
Structure. 2023 Apr 6;31(4):395-410.e6
pubmed: 36827983
J Biomol NMR. 1995 Nov;6(3):277-93
pubmed: 8520220
Mol Cell. 2016 Jul 7;63(1):21-33
pubmed: 27345149
J Biomol NMR. 1995 Jul;6(1):1-10
pubmed: 22911575
Biochemistry. 2002 Feb 12;41(6):1767-77
pubmed: 11827521
Cell. 2016 Aug 11;166(4):935-949
pubmed: 27477512
J Mol Biol. 2008 Mar 14;377(1):162-80
pubmed: 18241885

Auteurs

Gwen R Buel (GR)

Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA.

Xiang Chen (X)

Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA.

Olumide Kayode (O)

Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA.

Anthony Cruz (A)

Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA.

Kylie J Walters (KJ)

Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA. kylie.walters@nih.gov.

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Classifications MeSH