- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2041-1723
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR ; volume:9 ; number:1 ; day:29 ; month:5 ; year:2018 ; pages:1-12 ; date:12.2018
Nature Communications ; 9, Heft 1 (29.5.2018), 1-12, 12.2018
- Classification
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Geschichte Europas
- Creator
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Dai, Yaxin
- Contributor
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Zhang, Aili
Shan, Shan
Gong, Zihua
Zhou, Zheng
SpringerLink (Online service)
- DOI
-
10.1038/s41467-018-04557-2
- URN
-
urn:nbn:de:101:1-2018080323014652981801
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:28 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
- Dai, Yaxin
- Zhang, Aili
- Shan, Shan
- Gong, Zihua
- Zhou, Zheng
- SpringerLink (Online service)
Other Objects (12)
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain
Discovery of small molecules targeting the tandem tudor domain of the epigenetic factor UHRF1 using fragment-based ligand discovery
Structural pattern recognition
Recognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins
The effect of posttranslational modifications on biochemical and structural characteristics of prion protein variants and the SMN Tudor domain
The effect of posttranslational modifications on biochemical and structural characteristics of Prion Protein variants and the SMN Tudor domain
Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1
Refined read‐out : the hUHRF1 Tandem‐Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3
Maria Tudor
Tudor Beverley
"Maria Tudor"
Arghezi, Tudor
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain
Discovery of small molecules targeting the tandem tudor domain of the epigenetic factor UHRF1 using fragment-based ligand discovery
Structural pattern recognition
Recognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins
The effect of posttranslational modifications on biochemical and structural characteristics of prion protein variants and the SMN Tudor domain
The effect of posttranslational modifications on biochemical and structural characteristics of Prion Protein variants and the SMN Tudor domain
Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1
Refined read‐out : the hUHRF1 Tandem‐Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3
Maria Tudor
Tudor Beverley
"Maria Tudor"
Arghezi, Tudor
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain
Discovery of small molecules targeting the tandem tudor domain of the epigenetic factor UHRF1 using fragment-based ligand discovery
Structural pattern recognition
Recognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins
The effect of posttranslational modifications on biochemical and structural characteristics of prion protein variants and the SMN Tudor domain
The effect of posttranslational modifications on biochemical and structural characteristics of Prion Protein variants and the SMN Tudor domain
Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1
Refined read‐out : the hUHRF1 Tandem‐Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3
Maria Tudor
Tudor Beverley
"Maria Tudor"