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- Currently displaying 1161 - 1180 of 2508 publications
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)
The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage
Elife
(2017)
6
e23872
(doi: 10.7554/eLife.23872)
Emergence and evolution of an interaction between intrinsically disordered proteins.
eLife
(2017)
6
e16059
(doi: 10.7554/eLife.16059)
Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS
Proceedings of the National Academy of Sciences of USA
(2017)
114
e3935
(doi: 10.1073/pnas.1613854114)
Intra-chain organisation of hydrophobic residues controls inter-chain aggregation rates of amphiphilic polymers
The Journal of chemical physics
(2017)
146
135102
(doi: 10.1063/1.4977932)
A brain-sparing diphtheria toxin for chemical genetic ablation of peripheral cell lineages
Nature Communications
(2017)
8
14967
(doi: 10.1038/ncomms14967)
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions
Journal of Biological Chemistry
(2017)
292
8269
(doi: 10.1074/jbc.M116.764886)
Simultaneous quantification of protein order and disorder.
Nat Chem Biol
(2017)
13
339
(doi: 10.1038/nchembio.2331)
Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation
Mol Cell
(2017)
65
1096
(doi: 10.1016/j.molcel.2017.02.022)
Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides
ChemistrySelect
(2017)
2
2476
(doi: 10.1002/slct.201601916)
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
Proceedings of the National Academy of Sciences of the United States of America
(2017)
114
E2543
(doi: 10.1073/pnas.1701964114)
Bayesian weighing of electron cryo-microscopy data for integrative structural modeling
(2017)
113951
(doi: 10.1101/113951)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans
Cell
(2017)
168
944
(doi: 10.1016/j.cell.2016.12.041)
Plagues and history: From the black death to alzheimer’s disease
(2017)
32
(doi: 10.1017/9781108147910.004)
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.
Proc Natl Acad Sci U S A
(2017)
114
E1009
(doi: 10.1073/pnas.1610586114)
Structural Investigation of an Immunoglobulin Domain on the Ribosome using NMR Spectroscopy
Biophysical Journal
(2017)
112
41A
(doi: 10.1016/j.bpj.2016.11.258)
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
Biophysical Journal
(2017)
112
494a
(doi: 10.1016/j.bpj.2016.11.2673)