Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2399-3642
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates ; volume:1 ; number:1 ; day:18 ; month:10 ; year:2018 ; pages:1-11 ; date:12.2018
Communications biology ; 1, Heft 1 (18.10.2018), 1-11, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Shenkman, Marina
- Contributor
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Ron, Efrat
Yehuda, Rivka
Benyair, Ron
Khalaila, Isam
Lederkremer, Gerardo Z.
SpringerLink (Online service)
- DOI
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10.1038/s42003-018-0174-8
- URN
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urn:nbn:de:101:1-2018111922030106818839
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:44 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Shenkman, Marina
- Ron, Efrat
- Yehuda, Rivka
- Benyair, Ron
- Khalaila, Isam
- Lederkremer, Gerardo Z.
- SpringerLink (Online service)
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Transition between protein-like and polymer-like dynamic behavior: Internal friction in unfolded apomyoglobin depends on denaturing conditions
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HIV-1 integrase inhibitors are substrates for the multidrug transporter MDR1-P-glycoprotein
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