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Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
- Published in:
- Angewandte Chemie, 2016, v. 128, n. 26, p. 7544, doi. 10.1002/ange.201601850
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Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.
- Published in:
- Angewandte Chemie International Edition, 2016, v. 55, n. 26, p. 7418, doi. 10.1002/anie.201601850
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- Article
F2‐06‐01: MAJOR DIFFERENCES BETWEEN THE SELF‐ASSEMBLY, SEEDING BEHAVIOR, AND INTERACTION WITH MODULATORS OF HEPARIN‐INDUCED VERSUS IN‐VITRO PHOSPHORYLATED TAU.
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- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2019, v. 15, p. P524, doi. 10.1016/j.jalz.2019.06.4436
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- Article
Modification by SUMOylation Controls Both the Transcriptional Activity and the Stability of Delta-Lactoferrin.
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- PLoS ONE, 2015, v. 10, n. 6, p. 1, doi. 10.1371/journal.pone.0129965
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SILAC-Based Proteomic Profiling of the Human MDA-MB-231 Metastatic Breast Cancer Cell Line in Response to the Two Antitumoral Lactoferrin Isoforms: The Secreted Lactoferrin and the Intracellular Delta-Lactoferrin.
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- PLoS ONE, 2014, v. 9, n. 8, p. 1, doi. 10.1371/journal.pone.0104563
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Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.
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- Proteins, 2012, v. 80, n. 2, p. 454, doi. 10.1002/prot.23210
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- Article
NMR Meets Tau: Insights into Its Function and Pathology.
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- Biomolecules (2218-273X), 2016, v. 6, n. 2, p. 28, doi. 10.3390/biom6020028
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- Article
The FK506-binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion-like behavior.
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- FASEB Journal, 2015, v. 29, n. 8, p. 3171, doi. 10.1096/fj.14-268243
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- Article
A Step‐by‐Step Guide for the Production of Recombinant Fluorescent TAT‐HA‐Tagged Proteins and their Transduction into Mammalian Cells.
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- Current Protocols, 2024, v. 4, n. 3, p. 1, doi. 10.1002/cpz1.1016
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- Article
Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.
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- Scientific Reports, 2018, v. 8, n. 1, p. 1, doi. 10.1038/s41598-018-32096-9
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- Article
Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor<sup>1</sup>.
- Published in:
- Biochemistry & Cell Biology, 2012, v. 90, n. 3, p. 307, doi. 10.1139/o11-070
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- Article