The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions ; volume:30 ; number:12 ; day:9 ; month:11 ; year:2023 ; pages:2009-2019 ; date:12.2023
Nature structural & molecular biology ; 30, Heft 12 (9.11.2023), 2009-2019, 12.2023
- Creator
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Braxton, Julian R.
Altobelli, Chad R.
Tucker, Maxwell R.
Tse, Eric
Thwin, Aye C.
Arkin, Michelle R.
Southworth, Daniel R.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41594-023-01126-0
- URN
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urn:nbn:de:101:1-2024022712531080667565
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:58 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Braxton, Julian R.
- Altobelli, Chad R.
- Tucker, Maxwell R.
- Tse, Eric
- Thwin, Aye C.
- Arkin, Michelle R.
- Southworth, Daniel R.
- SpringerLink (Online service)
Other Objects (12)
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Investigation of the interaction of FAT10 and VCP (p97)
VCP/p97 inhibitor CB-5083 modulates muscle pathology in a mouse model of VCP inclusion body myopathy
A systematic proteomic approach to the VCP/p97-cofactor interaction landscape reveals p97 functions in stress response signaling
The FAM104 proteins VCF1/2 promote the nuclear localization of p97/VCP
UBXD1 is a mitochondrial recruitment factor for p97/VCP and promotes mitophagy
ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97
Targeting the immunoproteasome and VCP/p97 in autoimmune disorders and viral infection
Molekulargenetische Analyse der Kandidatengene p97/VCP, Myotilin und Vimentin bei hereditären Myopathien
Molecular function of SEP domain adapters in VCP/p97 mediated protein unfolding
Akt enhances the vulnerability of cancer cells to VCP/p97 inhibition-mediated paraptosis
Strategic role of the ubiquitin-dependent segregase p97 (VCP or Cdc48) in DNA replication
VCF1 is a p97/VCP cofactor promoting recognition of ubiquitylated p97-UFD1-NPL4 substrates
Investigation of the interaction of FAT10 and VCP (p97)
VCP/p97 inhibitor CB-5083 modulates muscle pathology in a mouse model of VCP inclusion body myopathy
A systematic proteomic approach to the VCP/p97-cofactor interaction landscape reveals p97 functions in stress response signaling
The FAM104 proteins VCF1/2 promote the nuclear localization of p97/VCP
UBXD1 is a mitochondrial recruitment factor for p97/VCP and promotes mitophagy
ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97
Targeting the immunoproteasome and VCP/p97 in autoimmune disorders and viral infection
Molekulargenetische Analyse der Kandidatengene p97/VCP, Myotilin und Vimentin bei hereditären Myopathien
Molecular function of SEP domain adapters in VCP/p97 mediated protein unfolding
Akt enhances the vulnerability of cancer cells to VCP/p97 inhibition-mediated paraptosis
Strategic role of the ubiquitin-dependent segregase p97 (VCP or Cdc48) in DNA replication
VCF1 is a p97/VCP cofactor promoting recognition of ubiquitylated p97-UFD1-NPL4 substrates
Investigation of the interaction of FAT10 and VCP (p97)
VCP/p97 inhibitor CB-5083 modulates muscle pathology in a mouse model of VCP inclusion body myopathy
A systematic proteomic approach to the VCP/p97-cofactor interaction landscape reveals p97 functions in stress response signaling
The FAM104 proteins VCF1/2 promote the nuclear localization of p97/VCP
UBXD1 is a mitochondrial recruitment factor for p97/VCP and promotes mitophagy
ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97
Targeting the immunoproteasome and VCP/p97 in autoimmune disorders and viral infection
Molekulargenetische Analyse der Kandidatengene p97/VCP, Myotilin und Vimentin bei hereditären Myopathien
Molecular function of SEP domain adapters in VCP/p97 mediated protein unfolding
Akt enhances the vulnerability of cancer cells to VCP/p97 inhibition-mediated paraptosis