The conformations of protein chains at the interface of biomolecular condensates
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
1 Online-Ressource.
- Sprache
-
Englisch
- Erschienen in
-
The conformations of protein chains at the interface of biomolecular condensates ; volume:15 ; number:1 ; day:19 ; month:11 ; year:2024 ; pages:1-4 ; date:12.2024
Nature Communications ; 15, Heft 1 (19.11.2024), 1-4, 12.2024
- Urheber
-
Bauer, D. Janka
Nikoubashman, Arash
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s41467-024-53575-w
- URN
-
urn:nbn:de:101:1-2502052138281.744504696143
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
- 15.08.2025, 07:39 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Bauer, D. Janka
- Nikoubashman, Arash
- SpringerLink (Online service)
Ähnliche Objekte (12)
Reply to: The conformations of protein chains at the interface of biomolecular condensates
Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations
Dynamical control enables the formation of demixed biomolecular condensates
Decoding the genomic landscape of chromatin-associated biomolecular condensates
Technologies for studying phase-separated biomolecular condensates
Single-photon microscopy to study biomolecular condensates
Biomolecular condensates form spatially inhomogeneous network fluids
RNase E biomolecular condensates stimulate PNPase activity
Reversible Kinetic Trapping of FUS Biomolecular Condensates
Biomolecular condensates as arbiters of biochemical reactions inside the nucleus
Ultrasmall Gold Nanoparticles as Clients of Biomolecular Condensates
Photoswitchable Endocytosis of Biomolecular Condensates in Giant Vesicles
Reply to: The conformations of protein chains at the interface of biomolecular condensates
Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations
Dynamical control enables the formation of demixed biomolecular condensates
Decoding the genomic landscape of chromatin-associated biomolecular condensates
Technologies for studying phase-separated biomolecular condensates
Single-photon microscopy to study biomolecular condensates
Biomolecular condensates form spatially inhomogeneous network fluids
RNase E biomolecular condensates stimulate PNPase activity
Reversible Kinetic Trapping of FUS Biomolecular Condensates
Biomolecular condensates as arbiters of biochemical reactions inside the nucleus
Ultrasmall Gold Nanoparticles as Clients of Biomolecular Condensates
Photoswitchable Endocytosis of Biomolecular Condensates in Giant Vesicles
Reply to: The conformations of protein chains at the interface of biomolecular condensates
Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations
Dynamical control enables the formation of demixed biomolecular condensates
Decoding the genomic landscape of chromatin-associated biomolecular condensates
Technologies for studying phase-separated biomolecular condensates
Single-photon microscopy to study biomolecular condensates
Biomolecular condensates form spatially inhomogeneous network fluids
RNase E biomolecular condensates stimulate PNPase activity
Reversible Kinetic Trapping of FUS Biomolecular Condensates
Biomolecular condensates as arbiters of biochemical reactions inside the nucleus
Ultrasmall Gold Nanoparticles as Clients of Biomolecular Condensates