ArticleThe Journal of biological chemistry2013
Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Understanding the structural dynamics of human islet amyloid polypeptide: Advancements in and applications of ion-mobility mass spectrometry.Biophysical chemistry · 2024Review
- On-Pathway Oligomer of Human Islet Amyloid Polypeptide Induced and Stabilized by Mechanical Rotation during Magic Angle Spinning Nuclear Magnetic Resonance.The journal of physical chemistry letters · 2023Article
- The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of β-microglobulin.Acta biochimica et biophysica Sinica · 2022Article
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- Quantitative interrogation of protein co-aggregation using multi-color fluorogenic protein aggregation sensors.Chemical science · 2021Article
- Extremely Amyloidogenic Single-Chain Analogues of Insulin's H-Fragment: Structural Adaptability of an Amyloid Stretch.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Article
- Extracellular matrix components modulate different stages in βThe Journal of biological chemistry · 2019Article
- Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein.Journal of molecular biology · 2018Article
- Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Nature communications · 2018Article
- Aggregation and Fibril Structure of AβBiochemistry · 2017Article
- Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Chemical science · 2017Article
- The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding.Scientific reports · 2016Article
- Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.The Journal of biological chemistry · 2016Article
- Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.The Analyst · 2015Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Distinguishing closely related amyloid precursors using an RNA aptamer.The Journal of biological chemistry · 2014Article
- Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Molecular cell · 2014Article
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Protein science : a publication of the Protein Society · 2014Article
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8 authors at 4 institutions in 2 countries.
Funding
Abstract
Amyloid fibrils can be generated from proteins with diverse sequences and folds. Although amyloid fibrils assembled in vitro commonly involve a single protein precursor, fibrils formed in vivo can contain more than one protein sequence. How fibril structure and stability differ in fibrils composed of single proteins (homopolymeric fibrils) from those generated by co-polymerization of more than one protein sequence (heteropolymeric fibrils) is poorly understood. Here we compare the structure and stability of homo and heteropolymeric fibrils formed from human β2-microglobulin and its truncated variant ΔN6. We use an array of approaches (limited proteolysis, magic angle spinning NMR, Fourier transform infrared spectroscopy, and fluorescence) combined with measurements of thermodynamic stability to characterize the different fibril types. The results reveal fibrils with different structural properties, different side-chain packing, and strikingly different stabilities. These findings demonstrate how co-polymerization of related precursor sequences can expand the repertoire of structural and thermodynamic polymorphism in amyloid fibrils to an extent that is greater than that obtained by polymerization of a single precursor alone.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.