<sup>13</sup>C APSY-NMR for sequential assignment of intrinsically disordered proteins.
- Published in:
- Journal of Biomolecular NMR, 2018, v. 70, n. 3, p. 167, doi. 10.1007/s10858-018-0167-4
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- Publication type:
- Article
Works matching AU Schiavina, Marco
Results: 14
1
2
Optimal <sup>13</sup>C NMR investigation of intrinsically disordered proteins at 1.2 GHz.
- Published in:
- Nature Protocols, 2024, v. 19, n. 2, p. 406, doi. 10.1038/s41596-023-00921-9
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- Publication type:
- Article
3
Frontispiece: Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
- Published in:
- Angewandte Chemie International Edition, 2020, v. 59, n. 42, p. 1, doi. 10.1002/anie.202084262
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- Publication type:
- Article
4
Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
- Published in:
- Angewandte Chemie International Edition, 2020, v. 59, n. 42, p. 18537, doi. 10.1002/anie.202008079
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- Publication type:
- Article
5
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
- Published in:
- Scientific Reports, 2020, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41598-020-76522-3
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- Publication type:
- Article
6
The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR.
- Published in:
- Biomolecular NMR Assignments, 2021, v. 15, n. 1, p. 219, doi. 10.1007/s12104-021-10009-8
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- Publication type:
- Article
7
Revealing the Potential of a Chimaera: a Peptide‐Peptide Nucleic Acid Molecule Designed To Interact with the SARS‐CoV‐2 Nucleocapsid Protein.
- Published in:
- Angewandte Chemie International Edition, 2025, v. 64, n. 11, p. 1, doi. 10.1002/anie.202420134
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- Publication type:
- Article
8
Optimized 13 C Relaxation-Filtered Nuclear Magnetic Resonance: Harnessing Optimal Control Pulses and Ultra-High Magnetic Fields for Metalloprotein Structural Elucidation.
- Published in:
- International Journal of Molecular Sciences, 2025, v. 26, n. 8, p. 3870, doi. 10.3390/ijms26083870
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- Publication type:
- Article
9
Revealing the Potential of a Chimaera: a Peptide‐Peptide Nucleic Acid Molecule Designed To Interact with the SARS‐CoV‐2 Nucleocapsid Protein.
- Published in:
- Angewandte Chemie, 2025, v. 137, n. 11, p. 1, doi. 10.1002/ange.202420134
- By:
- Publication type:
- Article
10
Frontispiz: Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
- Published in:
- Angewandte Chemie, 2020, v. 132, n. 42, p. 1, doi. 10.1002/ange.202084262
- By:
- Publication type:
- Article
11
Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
- Published in:
- Angewandte Chemie, 2020, v. 132, n. 42, p. 18696, doi. 10.1002/ange.202008079
- By:
- Publication type:
- Article
12
Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity.
- Published in:
- Scientific Reports, 2019, v. 9, n. 1, p. 1, doi. 10.1038/s41598-019-39480-z
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- Publication type:
- Article
13
The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin.
- Published in:
- Biomolecules (2218-273X), 2022, v. 12, n. 9, p. 1302, doi. 10.3390/biom12091302
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- Publication type:
- Article
14
NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering.
- Published in:
- Biomolecules (2218-273X), 2022, v. 12, n. 7, p. N.PAG, doi. 10.3390/biom12070929
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- Publication type:
- Article