Tips on using this search form
- All search terms are case-insensitive
- If you specify more than one search option (e.g. you search for both "Authors" and "Paper title") then the publications returned will be those that match all of your search terms
- To reset the search form, click here
- Currently displaying 341 - 360 of 2400 publications
Microscale Diffusiophoresis of Proteins.
The journal of physical chemistry. B
(2022)
126
8913
(doi: 10.1021/acs.jpcb.2c04029)
Multi-dimensional protein solubility optimization with an ultra-high-throughput microfluidic platform
(2022)
(doi: 10.1101/2022.10.21.513267)
Cysteine‐Assisted Click‐Chemistry for Proximity‐Driven, Site‐Specific Acetylation of Histones
Angew Chem Int Ed Engl
(2022)
61
e202208543
(doi: 10.1002/anie.202208543)
Characterization of full-length p53 aggregates and their kinetics of formation.
Biophys J
(2022)
121
4280
(doi: 10.1016/j.bpj.2022.10.013)
Intracellular FUS protein accumulation leads to cytoskeletal, organelle and cellular homeostasis perturbations
(2022)
(doi: 10.1101/2022.10.04.510756)
Hydrodynamics of Droplet Sorting in Asymmetric Acute Junctions.
Micromachines
(2022)
13
1640
(doi: 10.3390/mi13101640)
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.
Chem Sci
(2022)
13
13815
(doi: 10.1039/d2sc00066k)
Protein condensation diseases: therapeutic opportunities.
Nature Communications
(2022)
13
5550
(doi: 10.1038/s41467-022-32940-7)
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)
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.
Nature Communications
(2022)
13
5512
(doi: 10.1038/s41467-022-33252-6)
Effects of N-terminal Acetylation on the Aggregation of Disease-related a-synu- clein 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 Ca2+ 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
J Phys Chem Lett
(2022)
13
7853
(doi: 10.1021/acs.jpclett.2c01986)
Uncovering the universality of self-replication in protein aggregation and its link to disease.
Sci Adv
(2022)
8
eabn6831
(doi: 10.1126/sciadv.abn6831)
A conformational switch controlling the toxicity of the prion protein
Nat Struct Mol Biol
(2022)
29
831
(doi: 10.1038/s41594-022-00814-7)
The 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.
Journal of the American Chemical Society
(2022)
144
14404
(doi: 10.1021/jacs.2c00129)
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.
Sci Adv
(2022)
8
eabo0696
(doi: 10.1126/sciadv.abo0696)