| P50 | author | Ivano Bertini | Q3804830 |
| | Lucia Banci | Q21264278 |
| | Francesca Cantini | Q28316949 |
| | Letizia Barbieri | Q47316526 |
| | Enrico Luchinat | Q47316533 |
| P2860 | cites work | Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin. | Q54618890 |
| | SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds | Q57896548 |
| | In-cell NMR spectroscopy | Q57903761 |
| | The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 |
| | Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants | Q27654799 |
| | Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? | Q27765168 |
| | Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation | Q27860508 |
| | A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. | Q27936872 |
| | Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors | Q28203407 |
| | Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis | Q29615199 |
| | Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS | Q33742742 |
| | FlgM gains structure in living cells | Q34189211 |
| | Roles of thiol-redox pathways in bacteria | Q34360754 |
| | Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state | Q34429205 |
| | Mechanisms for copper acquisition, distribution and regulation | Q34750485 |
| | Escherichia coli mechanisms of copper homeostasis in a changing environment. | Q35164018 |
| | Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS | Q35854965 |
| | pH of the cytoplasm and periplasm of Escherichia coli: rapid measurement by green fluorescent protein fluorimetry | Q35949254 |
| | Looking into live cells with in-cell NMR spectroscopy | Q36821672 |
| | The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix | Q36944848 |
| | Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space | Q37724235 |
| | Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity | Q39864397 |
| | Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis | Q39972533 |
| | Affinity gradients drive copper to cellular destinations | Q42171712 |
| | Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. | Q45251257 |
| | Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form | Q46807674 |
| | Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy | Q48796099 |
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 8 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| P304 | page(s) | e23561 | |
| P577 | publication date | 2011-08-24 | |
| P1433 | published in | PLOS One | Q564954 |
| P1476 | title | In-cell NMR in E. coli to monitor maturation steps of hSOD1. | |
| P478 | volume | 6 | |