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- Currently displaying 1081 - 1100 of 2453 publications
Amyloid-like Fibrils from an α-Helical Transmembrane Protein.
Biochemistry
(2017)
56
3225
(doi: 10.1021/acs.biochem.7b00157)
Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates
Angew Chem Int Ed Engl
(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
Science Advances
(2017)
3
e1700488
(doi: 10.1126/sciadv.1700488)
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.
Biophysical Journal
(2017)
112
2540
(doi: 10.1016/j.bpj.2017.05.011)
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.
Proceedings of the National Academy of Sciences
(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)
Corrigendum: A brain-sparing diphtheria toxin for chemical genetic ablation of peripheral cell lineages.
Nat Commun
(2017)
8
15673
(doi: 10.1038/ncomms15673)
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 86
(2017)
86
27
Corrigendum: Structural basis of synaptic vesicle assembly promoted by α-synuclein
Nat Commun
(2017)
8
15667
(doi: 10.1038/ncomms15667)
Frontispiece: Site-Selective Modification of Proteins with Oxetanes
Chemistry - A European Journal
(2017)
23
chem.201782762
(doi: 10.1002/chem.201782762)
Structural Characterization of the Early Events in the Nucleation-Condensation Mechanism in a Protein Folding Process
Journal of the American Chemical Society
(2017)
139
6899
(doi: 10.1021/jacs.7b01540)
Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates
Angewandte Chemie
(2017)
129
7858
(doi: 10.1002/ange.201700966)
Protein modification via alkyne hydrosilylation using a substoichiometric amount of ruthenium(ii) catalyst.
Chemical science
(2017)
8
3871
(doi: 10.1039/c6sc05313k)
Site-Selective Modification of Proteins with Oxetanes.
Chemistry - A European Journal
(2017)
23
6483
(doi: 10.1002/chem.201700745)
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.
Chem Sci
(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
(2017)
114
e3935
(doi: 10.1073/pnas.1613854114)
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)
A brain-sparing diphtheria toxin for chemical genetic ablation of peripheral cell lineages.
Nat Commun
(2017)
8
14967
(doi: 10.1038/ncomms14967)