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- Currently displaying 801 - 820 of 1256 publications
Ultrasensitive Measurement of Ca
Angewandte Chemie (International ed. in English)
(2017)
56
7750
(doi: 10.1002/anie.201700966)
Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.
Sci Adv
(2017)
3
e1700488
(doi: 10.1126/sciadv.1700488)
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication
Proc Natl Acad Sci U S A
(2017)
114
6444
(doi: 10.1073/pnas.1700407114)
Self-assembled Protein Fibril-metal Oxide Nanocomposites
Israel Journal of Chemistry
(2017)
57
724
(doi: 10.1002/ijch.201600118)
Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates
Angewandte Chemie
(2017)
129
7858
(doi: 10.1002/ange.201700966)
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.
Chemical science
(2017)
8
4352
(doi: 10.1039/c7sc00215g)
Three-Dimensional Super-Resolution in Eukaryotic Cells Using the Double-Helix Point Spread Function.
Biophysical Journal
(2017)
112
1444
(doi: 10.1016/j.bpj.2017.02.023)
Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers.
Journal of Chemical Physics
(2017)
146
135102
(doi: 10.1063/1.4977932)
PEGylated liposomes associate with Wnt3A protein and expand putative stem cells in human bone marrow populations
Nanomedicine (Lond)
(2017)
12
845
(doi: 10.2217/nnm-2016-0386)
Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides
ChemistrySelect
(2017)
2
2476
(doi: 10.1002/slct.201601916)
3D structure of individual mammalian genomes studied by single cell Hi-C
Nature
(2017)
544
59
(doi: 10.1038/nature21429)
Physical principles of filamentous protein self-assembly kinetics
Journal of Physics: Condensed Matter
(2017)
29
153002
(doi: 10.1088/1361-648X/aa5f10)
Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.
Biochemistry
(2017)
56
1177
(doi: 10.1021/acs.biochem.6b01178)
Correction for Perni et al., A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.
Proc Natl Acad Sci U S A
(2017)
114
E2543
(doi: 10.1073/pnas.1701964114)
The stoichiometric ‘signature’ of Rhodopsin-family G protein-coupled receptors
(2017)
(doi: 10.1101/112466)
A cell-topography based mechanism for ligand discrimination by the T-cell receptor
(2017)
(doi: 10.1101/109785)
A natural product inhibits the initiation of α-synuclein aggregation & suppresses its toxicity
Proceedings of the National Academy of Sciences of the United States of America
(2017)
114
e1009
(doi: 10.1073/pnas.1610586114)
Direct Modulation of the Mitochondrial Permeability Transition Pore by Oligomeric Alpha-Synuclein Causes Toxicity in PD
Biophysical Journal
(2017)
112
440a
(doi: 10.1016/j.bpj.2016.11.2351)
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
Biophysical Journal
(2017)
112
494A
(doi: 10.1016/j.bpj.2016.11.2673)