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Author Details
Full Name
Samuel A Kotler
Affiliation
ORCID
Career Start Year
2012
Papers
16
H Index
13
Expertise
CM4AI Collaborator
PMID
Paper Title
Journal Title
Published Year
33644966
Probing the Interaction of Huntingtin Exon-1 Polypeptides with the Chaperonin Nanomachine GroEL.
ChemBioChem
2021
31958230
Molecular Details of a Salt Bridge and Its Role in Insulin Fibrillation by NMR and Raman Spectroscopic Analysis.
Journal of Physical Chemistry B
2020
30855940
Lipopolysaccharide from Gut Microbiota Modulates α-Synuclein Aggregation and Alters Its Biological Function.
ACS Chemical Neuroscience
2019
30917192
Probing transient non-native states in amyloid beta fiber elongation by NMR.
Chem Commun (Camb)
2019
30808748
Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR.
Proc Natl Acad Sci U S A
2019
29727175
Interaction of Huntingtin Exon-1 Peptides with Lipid-Based Micellar Nanoparticles Probed by Solution NMR and Q-Band Pulsed EPR.
J Am Chem Soc
2018
29555190
A blend of two resveratrol derivatives abolishes hIAPP amyloid growth and membrane damage.
Biochimica et Biophysica Acta - Biomembranes
2018
29744846
Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods.
Methods in Molecular Biology
2018
26138908
High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification.
Scientific Reports
2015
25715195
Detergent-type membrane fragmentation by MSI-78, MSI-367, MSI-594, and MSI-843 antimicrobial peptides and inhibition by cholesterol: a solid-state nuclear magnetic resonance study.
Biochemistry
2015
24464312
Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.
Chemical Society Reviews
2014
23493863
Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments.
Physical Chemistry Chemical Physics
2013
22217000
Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology.
J Phys Chem B
2012
22242635
Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.
Biochemistry
2012
22947931
Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formation.
Biophysical Journal
2012
22423218
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
J Chem Theory Comput
2012
1 - 16 of 16
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