7MZZ
| |
7MZW
| |
7MZX
| |
5JTL
| The structure of chaperone SecB in complex with unstructured proPhoA | 分子名称: | Alkaline phosphatase, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
5JTM
| The structure of chaperone SecB in complex with unstructured PhoA binding site a | 分子名称: | Alkaline phosphatase, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
5JTQ
| The structure of chaperone SecB in complex with unstructured MBP binding site d | 分子名称: | Maltose-binding periplasmic protein, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
5JTP
| The structure of chaperone SecB in complex with unstructured proPhoA binding site e | 分子名称: | Alkaline phosphatase, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-15 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
5JTO
| The structure of chaperone SecB in complex with unstructured proPhoA binding site d | 分子名称: | Alkaline phosphatase, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-15 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
5JTR
| The structure of chaperone SecB in complex with unstructured MBP binding site e | 分子名称: | Maltose-binding periplasmic protein, Protein-export protein SecB | 著者 | Huang, C, Saio, T, Rossi, P, Kalodimos, C.G. | 登録日 | 2016-05-09 | 公開日 | 2016-08-24 | 最終更新日 | 2024-05-15 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for the antifolding activity of a molecular chaperone. Nature, 537, 2016
|
|
6PQ2
| |
6PQM
| |
2M1N
| |
6PPT
| |
6PRJ
| |
6PRP
| |
6PQE
| |
6PRI
| |
2LQN
| |
2LQW
| |
2MS4
| Cyclophilin a complexed with a fragment of crk-ii | 分子名称: | Peptide, Peptidyl-prolyl cis-trans isomerase A | 著者 | Jankowski, W, Saleh, T, Rossi, P, Kalodimos, C. | 登録日 | 2014-07-22 | 公開日 | 2015-09-09 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway. Nat.Chem.Biol., 12, 2016
|
|
5KP0
| Recognition and targeting mechanisms by chaperones in flagella assembly and operation | 分子名称: | Flagellar protein FliT,Flagellum-specific ATP synthase | 著者 | Khanra, N.K, Rossi, P, Economou, A, Kalodimos, C.G. | 登録日 | 2016-07-01 | 公開日 | 2016-08-17 | 最終更新日 | 2024-05-15 | 実験手法 | SOLUTION NMR | 主引用文献 | Recognition and targeting mechanisms by chaperones in flagellum assembly and operation. Proc.Natl.Acad.Sci.USA, 113, 2016
|
|
5KS6
| |
5KRW
| Recognition and targeting mechanisms by chaperones in flagella assembly and operation | 分子名称: | Flagellar protein FliT,Flagellar hook-associated protein 2 fusion | 著者 | Khanra, N.K, Rossi, P, Economou, A, Kalodimos, C.G. | 登録日 | 2016-07-07 | 公開日 | 2016-08-17 | 最終更新日 | 2024-05-15 | 実験手法 | SOLUTION NMR | 主引用文献 | Recognition and targeting mechanisms by chaperones in flagellum assembly and operation. Proc.Natl.Acad.Sci.USA, 113, 2016
|
|
2LHK
| |
2MLX
| NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310 | 分子名称: | Alkaline phosphatase, Trigger factor | 著者 | Saio, T, Guan, X, Rossi, P, Economou, A, Kalodimos, C.G. | 登録日 | 2014-03-05 | 公開日 | 2014-05-21 | 最終更新日 | 2024-05-01 | 実験手法 | SOLUTION NMR | 主引用文献 | Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science, 344, 2014
|
|