ReviewCurrent Alzheimer research2008
Amyloidogenesis of natively unfolded proteins.
Review in Current Alzheimer research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
72 citing papers in PubMed, 189 citations in OpenAlex.
- Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers.Analytical chemistry · 2026Article
- Disease-disease interactions: molecular links of neurodegenerative diseases with cancer, viral infections, and type 2 diabetes.Translational neurodegeneration · 2025Review
- Inhibition of cytotoxic fibril formation of α-synuclein and human insulin by Silymarin from the Silybum marianum.PloS one · 2025Article
- Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024Article
- Anion Binding to Ammonium and Guanidinium Hosts: Implications for the Reverse Hofmeister Effects Induced by Lysine and Arginine Residues.The Journal of organic chemistry · 2024Article
- Efficient inhibition of amyloid fibrillation and cytotoxicity of α-synuclein and human insulin using biosynthesized silver nanoparticles decorated by green tea polyphenols.Scientific reports · 2024Article
- Leave-one-out-analysis (LOOA): web-based tool to predict influential proteins and interactions in aggregate-crosslinking proteomic data.Bioinformation · 2024Article
- Chaotic aging: intrinsically disordered proteins in aging-related processes.Cellular and molecular life sciences : CMLS · 2023Article
- The Sherpa hypothesis: Phenotype-Preserving Disordered Proteins stabilize the phenotypes of neurons and oligodendrocytes.NPJ systems biology and applications · 2023Article
- Alpha-Synuclein mRNA Level Found Dependent on L444P Variant in Carriers and Gaucher Disease Patients on Enzyme Replacement Therapy.Biomolecules · 2023Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Insights on Aggregation of Hen Egg-White Lysozyme from Raman Spectroscopy and MD Simulations.Molecules (Basel, Switzerland) · 2022Article
- Arrow of Time, Entropy, and Protein Folding: Holistic View on Biochirality.International journal of molecular sciences · 2022Review
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics.Chemical science · 2021Article
- The Amyloid Forming Peptides Islet Amyloid Polypeptide and Amyloid β Interact at the Molecular Level.International journal of molecular sciences · 2021Article
- Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases.European biophysics journal : EBJ · 2021Review
- Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects.Communications biology · 2021Article
- Isolation and Characterization of Human Colon Adenocarcinoma Stem-Like Cells Based on the Endogenous Expression of the Stem Markers.International journal of molecular sciences · 2021Article
- IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell.Cellular and molecular life sciences : CMLS · 2021Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Aggregation and subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. The accumulated data support the model where protein fibrillogenesis proceeds via the formation of a relatively unfolded amyloidogenic conformation, which shares many structural properties with the pre-molten globule state, a partially folded intermediate first found during the equilibrium and kinetic (un)folding studies of several globular proteins and later described as one of the structural forms of natively unfolded proteins. The flexibility of this structural form is essential for the conformational rearrangements driving the formation of the core cross-beta structure of the amyloid fibril. Obviously, molecular mechanisms describing amyloidogenesis of ordered and natively unfolded proteins are different. For ordered protein to fibrillate, its unique and rigid structure has to be destabilized and partially unfolded. On the other hand, fibrillogenesis of a natively unfolded protein involves the formation of partially folded conformation; i.e., partial folding rather than unfolding. In this review recent findings are surveyed to illustrate some unique features of the natively unfolded proteins amyloidogenesis.
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Registered trials
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.