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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 |
|---|---|---|---|---|
| 26533 | Heteronuclear NOE Values: 1 set T2 Relaxation Values: 1 set |
Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space |
Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space
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Charalambos Pozidis, Chiara Cefaro, Emmanouela Kallergi, Ivano Bertini, Karolina Gajda, Kostas Tokatlidis, Lucia Banci, Maria Andreadaki, Nitsa Katrakili, Paraskevi Kritsiligkou, Riccardo Peruzzini, Simone Ciofi-Baffoni |
| 26515 | Heteronuclear NOE Values: 1 set T2 Relaxation Values: 1 set |
Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space |
Targeting and Maturation of Erv1/ALR in the Mitochondrial Intermembrane Space
|
Charalambos Pozidis, Chiara Cefaro, Emmanouela Kallergi, Ivano Bertini, Karolina Gajda, Kostas Tokatlidis, Lucia Banci, Maria Andreadaki, Nitsa Katrakili, Paraskevi Kritsiligkou, Riccardo Peruzzini, Simone Ciofi-Baffoni |
| 18630 | Chemical Shifts: 1 set |
Backbone Chemical Shifts for N-terminal domain of sulfhydryl oxidase ALR |
An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control.
|
Angelo Gallo, Anna Pavelkova, Charalambos Pozidis, Chiara Cefaro, Emmanouela Kallergi, Isabella C Felli, Ivano Bertini, Karolina Gajda, Kostas Tokatlidis, Lucia Banci, Maria Andreadaki, Nitsa Katrakili, Simone Ciofi-Baffoni |
| 18631 | Chemical Shifts: 1 set |
N-terminal of Sulfydryl Oxidase of ALR reduced |
An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control.
|
Angelo Gallo, Anna Pavelkova, Charalambos Pozidis, Chiara Cefaro, Emmanouela Kallergi, Isabella C Felli, Ivano Bertini, Karolina Gajda, Kostas Tokatlidis, Lucia Banci, Maria Andreadaki, Nitsa Katrakili, Simone Ciofi-Baffoni |
| 18029 | Chemical Shifts: 1 set |
1H, 13C, and 15N Chemical Shift Assignments for sf-ALR |
Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.
|
Angelo Gallo, Charalambos Pozidis, Chiara Cefaro, Eirini Lionaki, Emmanouela Kallergi, Ivano Bertini, Kostas Tokatlidis, Lucia Banci, Simone Ciofi-Baffoni, Vito Calderone |
| 17821 | Chemical Shifts: 1 set |
Human C30S/C59S-Cox17 mutant |
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.
|
Angelo Gallo, Chiara Cefaro, Ivano Bertini, Lucia Banci, Simone Ciofi-Baffoni |
| 17067 | Chemical Shifts: 1 set |
Complex hMia40-hCox17 |
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.
|
Angelo Gallo, Chiara Cefaro, Dionisia Sideris, Enrico Luchinat, Isabella Caterina Felli, Ivano Bertini, Kostas Tokatlidis, Leonardo Gonnelli, Lucia Banci, Lucia Cenacchi, Simone Ciofi-Baffoni |
| 15763 | Chemical Shifts: 1 set |
The solution structure of human Mia40 |
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria
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Angelo Gallo, Chiara Cefaro, Ivano Bertini, Katrakili Nitsa, Kostas Tokatlidis, Lucia Banci, Manuele Martinelli, Sideris P Dionisia, Simone Ciofi-Baffoni |