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Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy

Biochemistry(2020)10.1021/acs.biochem.9b00892Source: DataRank Database

Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy is a research paper published in Biochemistry (2020). On theSindex it has a DataRank of 0. It has been cited 43 times.

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Open Access43 citations

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Enrichment:Funding (3 grants)Impact (FWCI 2.98)OA: greenTopics (87)IDs (PubMed, PMC, OpenAlex)Annotations (2)SDGs (1)

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Authors (2)

Robert Tycko ORCID,Dylan T. Murray ORCID

Live enrichment

PubMed:31895552 PMC:PMC7262780 OpenAlex:https://openalex.org/W2998272317

National Institute of Diabetes and Digestive and Kidney Diseases

Grant: Z-DK-075031-10

National Institute of General Medical Sciences

Grant: 1Fi2GM117604-01

Structure, Stability, and Function of the FUS Low Complexity Domain

Intramural NIH HHS

Grant: ZIA DK075031

FWCI

2.98

Citation Percentile

0.9%

Influential Citations

Citation Trend

2020

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2026

greenLicense: STM Policy #29

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7262780

GREENhttps://europepmc.org/articles/pmc7262780?pdf=render

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/7262780

publisherhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00892

journalhttps://doi.org/10.1021/acs.biochem.9b00892

Fields of Study

Advanced NMR Techniques and ApplicationsProtein Structure and DynamicsEnzyme Structure and FunctionChemistryMedicineBiology0301 basic medicine03 medical and health sciencesAmino Acid SequenceAmyloidAmyloid beta-PeptidesAmyloidogenic ProteinsHumansHydrogenHydrogen BondingHydrophobic and Hydrophilic InteractionsMagnetic Resonance SpectroscopyModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DomainsProtein Structure, SecondaryRNA-Binding Protein FUS

MeSH Terms

Protein DomainsAmino Acid SequenceAmyloidHumansHydrogenHydrogen BondingModels, MolecularMagnetic Resonance SpectroscopyProtein ConformationAmyloid beta-PeptidesProtein Structure, SecondaryNuclear Magnetic Resonance, BiomolecularRNA-Binding Protein FUSHydrophobic and Hydrophilic InteractionsAmyloidogenic Proteins

Keywords

FibrilChemistryHydrogen bondSide chainSolid-state nuclear magnetic resonanceResidue (chemistry)Nuclear magnetic resonance spectroscopyTyrosineCrystallographyAmyloid fibrilThreonineAmideSerineBiophysicsStereochemistryMoleculeBiochemistryOrganic chemistryAmyloid βNuclear magnetic resonancePhosphorylationPolymerModels, MolecularProtein StructureSecondaryBiochemistry & Molecular BiologyAmyloidMagnetic Resonance SpectroscopyProtein ConformationAmyloidogenic ProteinsMedical Biochemistry and MetabolomicsProtein Structure, SecondaryMedicinal and Biomolecular ChemistryProtein DomainsModelsHumansAmino Acid SequenceNuclear Magnetic Resonance, BiomolecularAmyloid beta-PeptidesMolecularHydrogen BondingBiological SciencesBrain DisordersBiochemistry and cell biologyChemical SciencesRNA-Binding Protein FUSHydrophobic and Hydrophilic InteractionsBiomolecularHydrogen

Sustainable Development Goals

SDG 0: Clean water and sanitation