- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
-
Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy ; volume:04 ; number:01 ; year:2017 ; pages:021-031
AIMS genetics ; 04, Heft 01 (2017), 021-031
- Contributor
-
Sultanov, Daniel
Gerasimova, Nadezhda
Kudryashova, Kseniya
Maluchenko, Natalya
Kotova, Elena
Langelier, Marie-France
Pascal, John
Kirpichnikov, Mikhail
Feofanov, Alexey
Studitsky, Vasily
- DOI
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10.3934/genet.2017.1.21
- URN
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urn:nbn:de:101:1-2021061708272491893799
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2023, 10:52 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
- Sultanov, Daniel
- Gerasimova, Nadezhda
- Kudryashova, Kseniya
- Maluchenko, Natalya
- Kotova, Elena
- Langelier, Marie-France
- Pascal, John
- Kirpichnikov, Mikhail
- Feofanov, Alexey
- Studitsky, Vasily
Other Objects (12)
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Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
Sarcomere dynamics revealed by a myofilament integrated FRET-based biosensor in live skeletal muscle fibers
Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies
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Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely moving C. elegans
Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry
Multiscale unfolding of real networks by geometric renormalization
The in vivo mechanics of the magnetotactic backbone as revealed by correlative FLIM-FRET and STED microscopy
Protein–Protein Affinity Determination by Quantitative FRET Quenching
Unfolding and compaction in chaperonin-assisted protein folding followed by single molecule and ensemble FRET
Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET
Quantitative single-molecule FRET and its application in experiments on DNA damage recognition by PARP-1
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
Sarcomere dynamics revealed by a myofilament integrated FRET-based biosensor in live skeletal muscle fibers
Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies
Monitoring protein unfolding transitions by NMR-spectroscopy
Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely moving C. elegans
Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry
Multiscale unfolding of real networks by geometric renormalization
The in vivo mechanics of the magnetotactic backbone as revealed by correlative FLIM-FRET and STED microscopy
Protein–Protein Affinity Determination by Quantitative FRET Quenching
Unfolding and compaction in chaperonin-assisted protein folding followed by single molecule and ensemble FRET
Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET
Quantitative single-molecule FRET and its application in experiments on DNA damage recognition by PARP-1
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
Sarcomere dynamics revealed by a myofilament integrated FRET-based biosensor in live skeletal muscle fibers
Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies
Monitoring protein unfolding transitions by NMR-spectroscopy
Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely moving C. elegans
Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry
Multiscale unfolding of real networks by geometric renormalization
The in vivo mechanics of the magnetotactic backbone as revealed by correlative FLIM-FRET and STED microscopy