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- Currently displaying 1161 - 1180 of 2524 publications
Single amyloid aggregates chemical and structural analysis by infrared nanospectroscopy
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
S370
Single α-synuclein oligomers are hydrophobically distinct from mature fibrils
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
S348
Mechanisms of Amyloid-β 42 oligomer formation from kinetic analysis
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
S240
Inverse electron demand Diels–Alder reactions in chemical biology
Chemical Society Reviews
(2017)
46
4895
(doi: 10.1039/c7cs00184c)
Amyloid-like Fibrils from an α‑Helical Transmembrane Protein
Biochemistry
(2017)
56
3225
(doi: 10.1021/acs.biochem.7b00157)
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)
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
Proc Natl Acad Sci U S A
(2017)
114
6444
(doi: 10.1073/pnas.1700407114)
The Amyloid Phenomenon and Its Links with Human Disease
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY
(2017)
9
a023648
(doi: 10.1101/cshperspect.a023648)
Self-assembled Protein Fibril-metal Oxide Nanocomposites
Israel Journal of Chemistry
(2017)
57
724
(doi: 10.1002/ijch.201600118)
Correction: Corrigendum: A brain-sparing diphtheria toxin for chemical genetic ablation of peripheral cell lineages
Nature Communications
(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
1
Frontispiece: Site-Selective Modification of Proteins with Oxetanes
Chemistry – A European Journal
(2017)
23
chem.201782762
(doi: 10.1002/chem.201782762)
Corrigendum: Structural basis of synaptic vesicle assembly promoted by α-synuclein
Nat Commun
(2017)
8
15667
(doi: 10.1038/ncomms15667)
Structural Characterization of the Early Events in the Nucleation-Condensation Mechanism in a Protein Folding Process
J Am Chem Soc
(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)
Site‐Selective Modification of Proteins with Oxetanes
Chemistry (Weinheim an der Bergstrasse, Germany)
(2017)
23
6483
(doi: 10.1002/chem.201700745)
Protein modification via alkyne hydrosilylation using a substoichiometric amount of ruthenium(ii) catalyst.
Chemical Science
(2017)
8
3871
(doi: 10.1039/c6sc05313k)
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)