| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 18933 |
2014-03-31 |
Chemical Shifts: 1 set
|
ASFV Pol X structure |
How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.
|
Chun-Wei Eric Wang, Frank HT Nelissen, Jian-Li Wu, Jurgen F Doreleijers, Liang-Hin Lim, Mei-I Su, Ming-Chuan Chad Chen, Ming-Daw Tsai, Sandeep Kumar, Sybren S Wijmenga, Wen-Jin Wu |
| 18934 |
2014-03-31 |
Chemical Shifts: 1 set
|
Binary complex of African Swine Fever Virus Pol X with MgdGTP |
How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.
|
Chun-Wei Eric Wang, Frank HT Nelissen, Jian-Li Wu, Jurgen F Doreleijers, Liang-Hin Lim, Mei-I Su, Ming-Chuan Chad Chen, Ming-Daw Tsai, Sandeep Kumar, Sybren S Wijmenga, Wen-Jin Wu |
| 18935 |
2014-03-31 |
Chemical Shifts: 1 set
|
African Swine Fever Virus Pol X in the ternary complex with MgdGTP and DNA |
How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.
|
Chun-Wei Eric Wang, Frank HT Nelissen, Jian-Li Wu, Jurgen F Doreleijers, Liang-Hin Lim, Mei-I Su, Ming-Chuan Chad Chen, Ming-Daw Tsai, Sandeep Kumar, Sybren S Wijmenga, Wen-Jin Wu |
| 6748 |
2007-01-29 |
Chemical Shifts: 1 set
|
NMR assignments of the Ki67FHA/hNIFK(226-269)3P complex |
Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.
|
Angela M Gronenborn, Haiyan Song, Hongyuan Li, In-Ja L Byeon, Ming-Daw Tsai |
| 5959 |
2004-09-30 |
Chemical Shifts: 1 set
|
Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions |
Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions
|
Hongyuan Li, In-Ja L Byeon, Ming-Daw Tsai |
| 5898 |
2004-10-25 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C and 15N resonance assignments for the 24.4 kDa human gankyrin protein |
Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure--function relationship.
|
A Mahajan, Chunhua Yuan, In-Ja L Byeon, Junan Li, Ming-Daw Tsai, Mingjye Poi |
| 4701 |
2000-05-09 |
Chemical Shifts: 1 set
|
Tumor suppressor INK4: refinement of p16/INK4A structure and determination of p15/INK4B structure by comparative modeling and NMR data |
Tumor suppressor INK4: refinement of p16/INK4A structure and determination of p15/INK4B structure by comparative modeling and NMR data
|
Chunhua Yuan, In-Ja L Byeon, Junan Li, Ming-Daw Tsai, Thomas L Selby |
| 4086 |
2002-07-17 |
Chemical Shifts: 1 set
|
Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism |
Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism
|
Anton Tevelev, Hee-Jung Kim, In-Ja L Byeon, Karen Ericson, Ming-Daw Tsai, Thomas Selby, Vadim Kraynov |
| 918 |
1999-06-14 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
| 919 |
1999-06-14 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
| 920 |
1999-06-14 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
