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- Currently displaying 1181 - 1200 of 2399 publications
A kinetic model of the aggregation of α-synuclein provides insights into prion-like spreading
PRION
(2016)
10
S63
Determination of statistical ensembles of intrinsically disordered proteins using NMR measurements
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2016)
252
Microfluidic devices fabricated using soft lithography for the study of protein structures using synchrotron radiation circular dichroism
20th International Conference on Miniaturized Systems for Chemistry and Life Sciences Microtas 2016
(2016)
1079
Structural Insights into the Calcium-Mediated Allosteric Transition in the C-Terminal Domain of Calmodulin from Nuclear Magnetic Resonance Measurements.
Biochemistry
(2015)
55
19
(doi: 10.1021/acs.biochem.5b00961)
Microfluidic diffusion analysis of the sizes and interactions of proteins under native solution conditions
ACS nano
(2015)
10
333
(doi: 10.1021/acsnano.5b04713)
Using Pseudocontact Shifts and Residual Dipolar Couplings as Exact NMR Restraints for the Determination of Protein Structural Ensembles
Biochemistry
(2015)
54
7470
(doi: 10.1021/acs.biochem.5b01138)
Enhancing Methotrexate Tolerance with Folate Tagged Liposomes in Arthritic Mice
Journal of biomedical nanotechnology
(2015)
11
2243
(doi: 10.1166/jbn.2015.2170)
Site-selective protein-modification chemistry for basic biology and drug development.
Nat Chem
(2015)
8
102
(doi: 10.1038/nchem.2393)
Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation
(2015)
(doi: 10.48550/arxiv.1511.06590)
Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants
Scientific reports
(2015)
5
16696
(doi: 10.1038/srep16696)
N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42
J Am Chem Soc
(2015)
137
14673
(doi: 10.1021/jacs.5b07849)
Parmbsc1: a refined force field for DNA simulations
Nature methods
(2015)
13
55
(doi: 10.1038/nmeth.3658)
Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins.
Biochemistry
(2015)
54
6876
(doi: 10.1021/acs.biochem.5b00670)
Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide.
Biochemical and biophysical research communications
(2015)
468
696
(doi: 10.1016/j.bbrc.2015.11.018)
SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation
Molecular neurodegeneration
(2015)
10
57
(doi: 10.1186/s13024-015-0053-4)
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.
Neuron
(2015)
88
678
(doi: 10.1016/j.neuron.2015.10.030)
Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations.
PLoS computational biology
(2015)
11
e1004435
(doi: 10.1371/journal.pcbi.1004435)
The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.
Scientific Reports
(2015)
5
15449
(doi: 10.1038/srep15449)
The length distribution of frangible biofilaments.
The Journal of chemical physics
(2015)
143
164901
(doi: 10.1063/1.4933230)
ChemInform Abstract: Biophysical Approaches for the Study of Interactions Between Molecular Chaperones and Protein Aggregates
ChemInform
(2015)
46
no
(doi: 10.1002/chin.201545294)