Work

The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations

Year: 2019

Type: article

Source: Nature Structural & Molecular Biology

DOI: 10.1038/s41594-019-0238-6

Authors: Martin D. Gelenter, Katelyn J. Smith, Shu-Yu Liao, Venkata S. Mandala, Aurelio J. Dregni, Matthew S. Lamm, Yu Tian, Wei Xu, Darrin J. Pochan, Thomas J. Tucker, Yongchao Su, Mei Hong

Institutions: Massachusetts Institute of Technology, Merck & Co., Inc., Rahway, NJ, USA (United States), University of North Carolina Wilmington, University of Chicago, University of Delaware

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Institutes of Health, National Institute on Aging, National Institute of Allergy and Infectious Diseases

Awards: Molecular structures of tau aggregates studied by solid-state NMR, Solid-state NMR studies of the dynamic interactions of the influenza A M2 membrane protein with water, antiviral drugs, and the M1 protein, G9000202055, Tau structure and dynamics in Alzheimer's disease

OpenAlex ID: W2949010601

FWCI: 3.225

Cites: 63

Cited by: 90

Related to: 10