Works matching AU Felli, Isabella C.
Results: 55
Frontispiz: Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
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- Angewandte Chemie, 2020, v. 132, n. 42, p. 1, doi. 10.1002/ange.202084262
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- Article
Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments.
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- Angewandte Chemie, 2020, v. 132, n. 42, p. 18696, doi. 10.1002/ange.202008079
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- Article
<sup>15</sup>N-detected TROSY for <sup>1</sup>H-<sup>15</sup>N heteronuclear correlation to study intrinsically disordered proteins: strategies to increase spectral quality.
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- Journal of Biomolecular NMR, 2025, v. 79, n. 1, p. 15, doi. 10.1007/s10858-024-00453-8
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- Article
Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water.
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- Journal of Biomolecular NMR, 2020, v. 74, n. 2/3, p. 161, doi. 10.1007/s10858-020-00301-5
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<sup>13</sup>C APSY-NMR for sequential assignment of intrinsically disordered proteins.
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- Journal of Biomolecular NMR, 2018, v. 70, n. 3, p. 167, doi. 10.1007/s10858-018-0167-4
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- Article
The Role of Disordered Regions in Orchestrating the Properties of Multidomain Proteins: The SARS-CoV-2 Nucleocapsid Protein and Its Interaction with Enoxaparin.
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- Biomolecules (2218-273X), 2022, v. 12, n. 9, p. 1302, doi. 10.3390/biom12091302
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NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering.
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- Biomolecules (2218-273X), 2022, v. 12, n. 7, p. N.PAG, doi. 10.3390/biom12070929
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- Article
Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins.
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- Biomolecules (2218-273X), 2020, v. 10, n. 11, p. 1541, doi. 10.3390/biom10111541
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- Article
Putting the Right Spin on It.
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- ChemPhysChem, 2013, v. 14, n. 13, p. 2998, doi. 10.1002/cphc.201300791
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- Article
<sup>13</sup>C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
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- ChemPhysChem, 2013, v. 14, n. 13, p. 3131, doi. 10.1002/cphc.201201097
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- Article
Combination of DQ and ZQ Coherences for Sensitive Through-Bond NMR Correlation Experiments in Biosolids under Ultra-Fast MAS.
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- ChemPhysChem, 2012, v. 13, n. 9, p. 2405, doi. 10.1002/cphc.201200099
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- Article
Exclusively Heteronuclear NMR Experiments to Obtain Structural and Dynamic Information on Proteins.
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- ChemPhysChem, 2010, v. 11, n. 3, p. 689, doi. 10.1002/cphc.200900772
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- Article
Recent Advances in Solution NMR: Fast Methods and Heteronuclear Direct Detection.
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- ChemPhysChem, 2009, v. 10, n. 9/10, p. 1356, doi. 10.1002/cphc.200900133
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- Article
NMR Characterization of Long‐Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in <sup>13</sup>C Direct‐Detection Experiments.
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- ChemBioChem, 2019, v. 20, n. 3, p. 335, doi. 10.1002/cbic.201800539
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- Article
Proline Fingerprint in Intrinsically Disordered Proteins.
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- ChemBioChem, 2018, v. 19, n. 15, p. 1625, doi. 10.1002/cbic.201800172
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High-dimensionality <sup>13</sup>C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
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- Journal of Biomolecular NMR, 2013, v. 57, n. 4, p. 353, doi. 10.1007/s10858-013-9793-z
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Mapping protein–protein interaction by <sup>13</sup>C′-detected heteronuclear NMR spectroscopy.
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- Journal of Biomolecular NMR, 2006, v. 36, n. 2, p. 111, doi. 10.1007/s10858-006-9068-z
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Side chain mobility as monitored by CH-CH cross correlation: The example of cytochrome b5.
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- Journal of Biomolecular NMR, 2001, v. 20, n. 1, p. 1, doi. 10.1023/A:1011245101351
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- Article
Lanthanide induced residual dipolar couplings for the conformational investigation of peripheral 15NH2 moieties.
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- Journal of Biomolecular NMR, 2000, v. 18, n. 4, p. 347, doi. 10.1023/A:1026785228634
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Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.
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- Magnetic Resonance, 2021, v. 2, n. 1, p. 511, doi. 10.5194/mr-2-511-2021
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- Article
Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-020-62069-w
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Optimal <sup>13</sup>C NMR investigation of intrinsically disordered proteins at 1.2 GHz.
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- Nature Protocols, 2024, v. 19, n. 2, p. 406, doi. 10.1038/s41596-023-00921-9
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- Article
Fast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High-Resolution Proton-Detected Solid-State MAS NMR Spectroscopy.
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- Angewandte Chemie International Edition, 2011, v. 50, n. 49, p. 11697, doi. 10.1002/anie.201106340
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- Article
13C Direct-Detection Biomoleculat NMR Spectroscopy in Living Cells.
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- Angewandte Chemie International Edition, 2011, v. 50, n. 10, p. 2339, doi. 10.1002/anie.201006636
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- Article
Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy.
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- ChemBioChem, 2015, v. 16, n. 2, p. 268, doi. 10.1002/cbic.201402534
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The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.
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- ChemBioChem, 2013, v. 14, n. 14, p. 1876, doi. 10.1002/cbic.201300172
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- Article
Inside Cover: Exclusively Heteronuclear <sup>13</sup>C-Detected Amino-Acid-Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs) (ChemBioChem 16/2012).
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- ChemBioChem, 2012, v. 13, n. 16, p. 2310, doi. 10.1002/cbic.201290067
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- Article
Exclusively Heteronuclear <sup>13</sup>C-Detected Amino-Acid-Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs).
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- ChemBioChem, 2012, v. 13, n. 16, p. 2425, doi. 10.1002/cbic.201200447
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- Article
High-Resolution Characterization of Intrinsic Disorder in Proteins: Expanding the Suite of <sup>13</sup>C-Detected NMR Spectroscopy Experiments to Determine Key Observables.
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- ChemBioChem, 2011, v. 12, n. 15, p. 2347, doi. 10.1002/cbic.201100406
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Towards a Protocol for Solution Structure Determination of Copper(II) Proteins: the Case of Cu<sup>II</sup>Zn<sup>II</sup> Superoxide Dismutase.
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- ChemBioChem, 2007, v. 8, n. 12, p. 1422, doi. 10.1002/cbic.200700006
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A further investigation of the cytochrome b <sub>5</sub>-cytochrome c complex.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 7, p. 777, doi. 10.1007/s00775-003-0479-y
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- Article
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.
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- Biomolecular NMR Assignments, 2021, v. 15, n. 1, p. 219, doi. 10.1007/s12104-021-10009-8
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- Article
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
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
The Solution Structure of Oxidized HiPIP I from Ectothiorhodospira halophila; Can NMR Spectroscopy Be Used to Probe Rearrangements Associated with Electron Transfer Processes?
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- Chemistry - A European Journal, 1995, v. 1, n. 9, p. 598, doi. 10.1002/chem.19950010906
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- Article
Recent progress in NMR spectroscopy: Toward the study of intrinsically disordered proteins of increasing size and complexity.
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- IUBMB Life, 2012, v. 64, n. 6, p. 473, doi. 10.1002/iub.1045
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- Article
<sup>13</sup>C Direct-detection biomolecular NMR.
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- Concepts in Magnetic Resonance. Part A: Bridging Education & Research, 2008, v. 32A, n. 3, p. 183, doi. 10.1002/cmr.a.20109
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- Article
A complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: Reduced HiPIP I from Ectothiorhodospira halophila.
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- Proteins, 1996, v. 24, n. 2, p. 158, doi. 10.1002/(SICI)1097-0134(199602)24:2<158::AID-PROT3>3.0.CO;2-F
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- Article
Fast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High-Resolution Proton-Detected Solid-State MAS NMR Spectroscopy.
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- Angewandte Chemie, 2011, v. 123, n. 49, p. 11901, doi. 10.1002/ange.201106340
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- Publication type:
- Article
13C Direct-Detection Biolmolecular NMR Spectroscopy in Living Cells.
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- Angewandte Chemie, 2011, v. 123, n. 10, p. 2387, doi. 10.1002/ange.201006636
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- Article
Complete Assignment of Heteronuclear Protein Resonances by Protonless NMR SpectroscopyThe authors are grateful to Dr. Alan Stern and Dr. Frank Delaglio for useful comments. L.D. was supported by the EC Marie Curie Fellowship (Contract HPMT-2000-000137). This work was supported in part by the EC Contracts HPRI-CT-2001-50026, HPRN-CT-2000-00092, and QLG2-CT-2002-00988. All NMR pulse sequences written for the Bruker Avance series spectrometers are available upon request.
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- Angewandte Chemie, 2005, v. 117, n. 20, p. 3149, doi. 10.1002/ange.200461794
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A Heteronuclear Direct-Detection NMR Spectroscopy Experiment for Protein-Backbone Assignment ( L.D. was supported by the EC Marie Curie Fellowship, Contract Number HPMT-2000000137. P.R.V. acknowledges the CROSSCORRELATION Research Training Network, Contract Number HPRN-CT-200000092. The authors thank Dr. Wolfgang Bermel for critical reading of the manuscript and Prof. Lyndon Emsley for stimulating discussions and useful comments. )
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- Angewandte Chemie, 2004, v. 116, n. 17, p. 2307, doi. 10.1002/ange.200453661
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Author Correction: Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor.
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- 2019
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- Correction Notice
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor.
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- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-11594-y
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Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.
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- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-09923-2
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In-cell <sup>13</sup>C NMR spectroscopy for the study of intrinsically disordered proteins.
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- Nature Protocols, 2014, v. 9, n. 9, p. 2005, doi. 10.1038/nprot.2014.124
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Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus.
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- Chemistry - A European Journal, 2016, v. 22, n. 37, p. 13010, doi. 10.1002/chem.201602510
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NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
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- Angewandte Chemie, 2013, v. 125, n. 45, p. 12024, doi. 10.1002/ange.201304272
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Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
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- Scientific Reports, 2020, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41598-020-76522-3
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pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins.
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- Nucleic Acids Research, 2014, v. 42, n. D1, p. D326, doi. 10.1093/nar/gkt960
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