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Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor

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Year: 2012
Type: article
Source: Nature Chemistry
DOI: 10.1038/nchem.1293
Authors: Chris T. Middleton, Peter Marek, Ping Cao, Chi-cheng Chiu, Sadanand Singh, Ann Marie Woys, Juan J. de Pablo, Daniel P. Raleigh, Martin T. Zanni
Institutions: University of Wisconsin–Madison, Stony Brook University
Language: English

Topic: Alzheimer's disease research and treatments
Subfield: Physiology
Field: Medicine
Domain: Health Sciences
SDG: Good health and well-being

Open Access status: green

Funders: National Science Foundation, National Institutes of Health, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases, Division of Chemistry
Awards: G1624356454, G2179468682, G2639221974, Biophysical Studies of Amyloid Formation by Polypeptide Hormones, G5513902213, Mechanism of membrane-catalyzed amyloid formation in diabetes, Structural mechanism of diabetic amyloid formation
OpenAlex ID: W2114335213
FWCI: 17.33
Cites: 55
Cited by: 169
Related to: 10
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