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- Currently displaying 321 - 340 of 2373 publications
Protein condensation diseases: therapeutic opportunities.
Nature Communications
(2022)
13
5550
(doi: 10.1038/s41467-022-32940-7)
Influence of denaturants on amyloid β42 aggregation kinetics
Frontiers in Neuroscience
(2022)
16
943355
(doi: 10.3389/fnins.2022.943355)
Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease
Nat Commun
(2022)
13
5512
(doi: 10.1038/s41467-022-33252-6)
Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease
Nature Communications
(2022)
13
5512
(doi: 10.1038/s41467-022-33252-6)
Effects of N-terminal acetylation on the aggregation of disease-related α-synuclein variants
J Mol Biol
(2022)
435
167825
(doi: 10.1016/j.jmb.2022.167825)
A chip-based supersonic microfluidic nebulizer for efficient sample introduction into inductively coupled plasma- Mass spectrometry
Analytica chimica acta
(2022)
1229
340342
(doi: 10.1016/j.aca.2022.340342)
Misfolded protein oligomers induce an increase of intracellular Ca 2+ causing an escalation of reactive oxidative species
Cellular and molecular life sciences : CMLS
(2022)
79
500
(doi: 10.1007/s00018-022-04513-w)
Analytical Solution to the Flory-Huggins Model
Journal of Physical Chemistry Letters
(2022)
13
7853
(doi: 10.1021/acs.jpclett.2c01986)
Uncovering the universality of self-replication in protein aggregation and its link to disease
Science advances
(2022)
8
eabn6831
(doi: 10.1126/sciadv.abn6831)
A conformational switch controlling the toxicity of the prion protein
Nature Structural and Molecular Biology
(2022)
29
831
(doi: 10.1038/s41594-022-00814-7)
N‑Terminal Acetylation of α‑Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates
Biochemistry
(2022)
61
1743
(doi: 10.1021/acs.biochem.2c00104)
Chemical and Enzymatic Methods for Post-Translational Protein-Protein Conjugation.
J Am Chem Soc
(2022)
144
14404
(doi: 10.1021/jacs.2c00129)
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy
Science Advances
(2022)
8
eabo0696
(doi: 10.1126/sciadv.abo0696)
Adsorption free energy predicts amyloid protein nucleation rates
Proc Natl Acad Sci U S A
(2022)
119
e2109718119
(doi: 10.1073/pnas.2109718119)
Are casein micelles extracellular condensates formed by liquid-liquid phase separation?
FEBS Letters
(2022)
596
2072
(doi: 10.1002/1873-3468.14449)
DNA-Liposome Hybrid Carriers for Triggered Cargo Release
ACS Appl Bio Mater
(2022)
5
3713
(doi: 10.1021/acsabm.2c00225)
Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes
Proc Natl Acad Sci U S A
(2022)
119
e2205412119
(doi: 10.1073/pnas.2205412119)
π-Clamp-Mediated Homo- and Heterodimerization of Single-Domain Antibodies via Site-Specific Homobifunctional Conjugation.
J Am Chem Soc
(2022)
144
13026
(doi: 10.1021/jacs.2c04747)
Structure-specific amyloid precipitation in biofluids.
Nat Chem
(2022)
14
1045
(doi: 10.1038/s41557-022-00976-3)
Editorial: Intrinsically Disordered Proteins and Regions: The Challenge to the Structure-Function Relationship.
Frontiers in Molecular Biosciences
(2022)
9
962643
(doi: 10.17863/CAM.87921)