Conformational Substates of Amyloidogenic hIAPP Revealed by High Pressure NMR Spectroscopy-Reference-Cited by-同舟云学术

Conformational Substates of Amyloidogenic hIAPP Revealed by High Pressure NMR Spectroscopy

Published:2016-08-01 Issue:12 Volume:1 Page:3239-3243
ISSN:2365-6549
Container-title:ChemistrySelect
language:en
Short-container-title:ChemistrySelect

Author:

Erlach Markus Beck¹,Kalbitzer Hans Robert¹,Winter Roland²,Kremer Werner¹

Affiliation:

1. Institut für Biophysik und Physikalische Biochemie und Zentrum für Magnetische Resonanz in Chemie und Biomedizin; Universität Regensburg; Universitätsstr. 31 93053 Regensburg Germany, Fax: (+49-941-9432479

2. Physikalische Chemie I- Biophysikalische Chemie; Technische Universität Dortmund; Otto-Hahn-Str. 4a 44227 Dortmund Germany

Publisher

Wiley

Subject

General Chemistry

Reference44 articles.

1. Conformational Substates in Proteins

2. Proteins and pressure

3. Pressure provides new insights into protein folding, dynamics and structure

4. On the Temperature-Pressure Free-Energy Landscape of Proteins

5. High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins

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1. The thermodynamic and kinetic mechanisms of a Ganoderma lucidum proteoglycan inhibiting hIAPP amyloidosis;Biophysical Chemistry;2022-01

2. Exploring the polymorphism, conformational dynamics and function of amyloidogenic peptides and proteins by temperature and pressure modulation;Biophysical Chemistry;2021-01

3. High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease;Chemical Communications;2020

4. The pressure and temperature perturbation approach reveals a whole variety of conformational substates of amyloidogenic hIAPP monitored by 2D NMR spectroscopy;Biophysical Chemistry;2019-11

5. Characterization of low-lying excited states of proteins by high-pressure NMR;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2019-03