ArticleScientific reports2017
Nucleobindin 1 binds to multiple types of pre-fibrillar amyloid and inhibits fibrillization.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Cross-seeding of IAPP and Aβ42: A review of the molecular link between type 2 diabetes and Alzheimer's disease.Metabolic brain disease · 2025Review
- The FindMNDBiomarker Program: Protein Changes in Motor Neuron Disease/Amyotrophic Lateral Sclerosis Postmortem Tissue and Biofluids.Annals of neurology · 2025Article
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- Potential of molecular chaperones for treating Alzheimer's disease.Neural regeneration research · 2024Article
- Deciphering the dual nature of nesfatin-1: a tale of zinc ion's Janus-faced influence.Cell communication and signaling : CCS · 2024Article
- A reduced proteomic signature in critically ill Covid-19 patients determined with plasma antibody micro-array and machine learning.Clinical proteomics · 2024Article
- A pancreatic player in dementia: pathological role for islet amyloid polypeptide accumulation in the brain.Neural regeneration research · 2023Review
- Transcriptomic profiling of Parkinson's disease brains reveals disease stage specific gene expression changes.Acta neuropathologica · 2023Article
- Amyloid inhibition by molecular chaperonesRSC medicinal chemistry · 2023Review
- The RNA-Binding and RNA-Melting Activities of the Multifunctional Protein Nucleobindin 1.International journal of molecular sciences · 2023Article
- Neurodegeneration and humoral response proteins in cerebrospinal fluid associate with pediatric-onset multiple sclerosis and not monophasic demyelinating syndromes in childhood.Multiple sclerosis (Houndmills, Basingstoke, England) · 2023Article
- Human Islet Amyloid Polypeptide (hIAPP) Protofibril-Specific Antibodies for Detection and Treatment of Type 2 Diabetes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Does one plus one always equal two? Structural differences between nesfatin-1, -2, and nesfatin-1/2.Cell communication and signaling : CCS · 2022Article
- In situ detection of protein interactions for recombinant therapeutic enzymes.Biotechnology and bioengineering · 2021Article
- Nucleobindin-2 consists of two structural components: The ZnComputational and structural biotechnology journal · 2021Article
- Article
- Nucleobindin-1 regulates ECM degradation by promoting intra-Golgi trafficking of MMPs.The Journal of cell biology · 2020Article
- Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro.Communications biology · 2020Article
- Fine mapping and identification of serum urate loci in American Indians: The Strong Heart Family Study.Scientific reports · 2019Article
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4 authors.
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Abstract
During amyloid fibril formation, amyloidogenic polypeptides misfold and self assemble into soluble pre-fibrillar aggregates, i.e., protofibrils, which elongate and mature into insoluble fibrillar aggregates. An emerging class of chaperones, chaperone-like amyloid binding proteins (CLABPs), has been shown to interfere with aggregation of particular misfolded amyloid peptides or proteins. We have discovered that the calcium-binding protein nuclebindin-1 (NUCB1) is a novel CLABP. We show that NUCB1 inhibits aggregation of islet-amyloid polypeptide associated with type 2 diabetes mellitus, a-synuclein associated with Parkinson's disease, transthyretin V30M mutant associated with familial amyloid polyneuropathy, and Aβ42 associated with Alzheimer's disease by stabilizing their respective protofibril intermediates. Kinetic studies employing the modeling software AmyloFit show that NUCB1 affects both primary nucleation and secondary nucleation. We hypothesize that NUCB1 binds to the common cross-β-sheet structure of protofibril aggregates to "cap" and stabilize soluble macromolecular complexes. Transmission electron microscopy and atomic force microscopy were employed to characterize the size, shape and volume distribution of multiple sources of NUCB1-capped protofibrils. Interestingly, NUCB1 prevents Aβ42 protofibril toxicity in a cellular assay. NUCB1-stabilized amyloid protofibrils could be used as immunogens to prepare conformation-specific antibodies and as novel tools to develop screens for anti-protofibril diagnostics and therapeutics.
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