Found: 19
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Interprotein Electron Transfer between FeS-Protein Nanowires and Oxygen-Tolerant NiFe Hydrogenase.
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- Angewandte Chemie, 2017, v. 129, n. 27, p. 7882, doi. 10.1002/ange.201702042
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- Article
Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry.
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- Angewandte Chemie, 2016, v. 128, n. 7, p. 2386, doi. 10.1002/ange.201508995
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- Article
Frontispiz: Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry.
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- Angewandte Chemie, 2016, v. 128, n. 7, p. n/a, doi. 10.1002/ange.201680761
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- Article
Gd-nanoparticles functionalization with specific peptides for β-amyloid plaques targeting.
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- Journal of Nanobiotechnology, 2016, v. 14, p. 1, doi. 10.1186/s12951-016-0212-y
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- Article
Development of Conformational Antibodies to Detect Bcl-xL's Amyloid Aggregates in Metal-Induced Apoptotic Neuroblastoma Cells.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 20, p. 7625, doi. 10.3390/ijms21207625
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- Article
Interprotein Electron Transfer between FeS-Protein Nanowires and Oxygen-Tolerant NiFe Hydrogenase.
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- Angewandte Chemie International Edition, 2017, v. 56, n. 27, p. 7774, doi. 10.1002/anie.201702042
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- Article
Frontispiece: Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 7, p. n/a, doi. 10.1002/anie.201680761
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- Article
Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 7, p. 2340, doi. 10.1002/anie.201508995
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- Article
Interactions of apomyoglobin with membranes: Mechanisms and effects on heme uptake.
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- Protein Science: A Publication of the Protein Society, 2007, v. 16, n. 3, p. 391, doi. 10.1110/ps.062531207
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- Article
Cofactor effects on the protein folding reaction: Acceleration of α-lactalbumin refolding by metal ions.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 4, p. 659, doi. 10.1110/ps.051904206
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- Article
Solution structure and dynamics of bovine β-lactoglobulin A.
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- Protein Science: A Publication of the Protein Society, 1999, v. 8, n. 11, p. 2541, doi. 10.1110/ps.8.11.2541
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- Article
Does fusion of domains from unrelated proteins affect their folding pathways and the structural changes involved in their function? A case study with the diphtheria toxin T domain.
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- Protein Engineering, 2002, v. 15, n. 5, p. 383, doi. 10.1093/protein/15.5.383
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- Article
Hybrid Amyloid‐Based Redox Hydrogel for Bioelectrocatalytic H<sub>2</sub> Oxidation.
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- Angewandte Chemie International Edition, 2021, v. 60, n. 26, p. 14488, doi. 10.1002/anie.202101700
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- Article
Type III secretion system translocator has a molten globule conformation both in its free and chaperone-bound forms.
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- FEBS Journal, 2007, v. 274, n. 14, p. 3601, doi. 10.1111/j.1742-4658.2007.05893.x
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- Article
Hybrid Amyloid‐Based Redox Hydrogel for Bioelectrocatalytic H<sub>2</sub> Oxidation.
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- Angewandte Chemie, 2021, v. 133, n. 26, p. 14609, doi. 10.1002/ange.202101700
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- Article
Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy.
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- Nature Structural Biology, 2000, v. 7, n. 1, p. 78
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- Article
Magnetic Nanoparticles Applications for Amyloidosis Study and Detection: A Review.
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- Nanomaterials (2079-4991), 2018, v. 8, n. 9, p. 740, doi. 10.3390/nano8090740
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- Article
Solution and membrane-bound chaperone activity of the diphtheria toxin translocation domain towards the catalytic domain.
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- FEBS Journal, 2011, v. 278, n. 23, p. 4516, doi. 10.1111/j.1742-4658.2011.08053.x
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- Article
Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.
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- FEBS Journal, 2010, v. 277, n. 3, p. 653, doi. 10.1111/j.1742-4658.2009.07511.x
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- Article