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Collagen hydrogel confinement of Amyloid-β (Aβ) accelerates aggregation and reduces cytotoxic effects
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Protein folding in confined and crowded environments
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Elastic Moduli of Collagen Gels Can Be Predicted from Two-Dimensional Confocal Microscopy
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inferredcites →https://doi.org/10.1063/1.4941054openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.0409630102openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.0506723102openalex-snapshot
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inferredcites →https://doi.org/10.1073/pnas.1309175110openalex-snapshot
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inferredcites →https://doi.org/10.1074/jbc.m109.002832openalex-snapshot
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inferredcites →https://doi.org/10.1074/jbc.m110.181313openalex-snapshot
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inferredcites →https://doi.org/10.1074/jbc.m110429200openalex-snapshot
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inferredcites →https://doi.org/10.1074/jbc.r800016200openalex-snapshot
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inferredcites →https://doi.org/10.1080/13506129.2016.1257986openalex-snapshot
Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines
inferredcites →https://doi.org/10.1089/scd.2013.0511openalex-snapshot
Induced Pluripotent Stem Cells from Familial Alzheimer's Disease Patients Differentiate into Mature Neurons with Amyloidogenic Properties
inferredcites →https://doi.org/10.1089/ten.tea.2011.0221openalex-snapshot
Substrate Three-Dimensionality Induces Elemental Morphological Transformation of Sensory Neurons on a Physiologic Timescale
inferredcites →https://doi.org/10.1089/ten.tea.2016.0103openalex-snapshot
Three-Dimensional Environment Sustains Morphological Heterogeneity and Promotes Phenotypic Progression During Astrocyte Development
inferredcites →https://doi.org/10.1093/emboj/18.24.6927openalex-snapshot
Effects of macromolecular crowding on protein folding and aggregation
inferredcites →https://doi.org/10.1110/ps.062514807openalex-snapshot
Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway
inferredcites →https://doi.org/10.1110/ps.36201openalex-snapshot
Molecular confinement influences protein structure and enhances thermal protein stability
inferredcites →https://doi.org/10.1111/cas.13843openalex-snapshot
High‐throughput screening in colorectal cancer tissue‐originated spheroids
inferredcites →https://doi.org/10.1111/j.1471-4159.2006.04426.xopenalex-snapshot
Aβ Oligomers – a decade of discovery
inferredcites →https://doi.org/10.1111/j.1749-6632.1996.tb34406.xopenalex-snapshot
Amyloid Fibril Toxicity in Alzheimer's Disease and Diabetesa
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inferredcites →https://doi.org/10.1146/annurev.bb.22.060193.000331openalex-snapshot
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inferredcites →https://doi.org/10.1146/annurev.biophys.37.032807.125817openalex-snapshot
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inferredcites →https://doi.org/10.1155/2015/849017openalex-snapshot
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inferredcites →https://doi.org/10.1177/1087057117696795openalex-snapshot
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inferredcites →https://doi.org/10.1186/1754-1611-3-5openalex-snapshot
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Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
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inferredcites →https://doi.org/10.1371/journal.pone.0066101openalex-snapshot
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Phenol Red Interacts with the Protofibril-Like Oligomers of an Amyloidogenic Hexapeptide NFGAIL through Both Hydrophobic and Aromatic Contacts
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Molecular Structure of beta-Amyloid Fibrils in Alzheimer's Disease Brain Tissue.
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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