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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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| Entry ID | Data summary | Entry Title | Citation Title | Authors |
|---|---|---|---|---|
| 30576 | Chemical Shifts: 1 set |
Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate. |
Histone chaperone exploits intrinsic disorder to switch acetylation specificity
|
Frank Gabel, John Kirkpatrick, Luca Codutti, Lukas Lercher, Nataliya Danilenko, Teresa Carlomagno |
| 34201 | Chemical Shifts: 2 sets |
Rtt109 peptide bound to Asf1 |
Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation
|
John Kirkpatrick, Lukas Lercher, Nataliya Danilenko, Teresa Carlomagno |