ReviewAngewandte Chemie (International ed. in English)2019
Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering.
Review in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
The trial behind it
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
26 citing papers in PubMed, 52 citations in OpenAlex.
- A pharmacological modality to sequester homomeric proteins.Nature chemical biology · 2026Article
- A histidine switch controls the pH-responsive self-assembly of a helical protein filament.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of secreted acid phosphatase polymerization in the Leishmania parasite.Protein science : a publication of the Protein Society · 2026Article
- Bromodomain dimers: A case study of BRD4 and family-wide AlphaFold predictions.Structural dynamics (Melville, N.Y.) · 2026Article
- Association of Hemoglobin and Myoglobin into Supramolecular Complexes: Significance for Life and Practice.International journal of molecular sciences · 2025Review
- Surface-modified protein crowders influence mutant huntingtin exon 1 aggregation via crowding effects, crowder association, and crowder solution stability.Protein science : a publication of the Protein Society · 2025Article
- Mutation-induced filaments of folded proteins are inert and non-toxic in a cellular system.Molecular systems biology · 2025Article
- Protein aggregate or agglomerate: similar punctate structure with distinct biological profiles.Molecular systems biology · 2025Article
- Filamentation-driven peripheral clustering of the inducible lysine decarboxylase is crucial for E. coli acid stress response.Communications biology · 2025Article
- Polymerization of ZBTB transcription factors regulates chromatin occupancy.Molecular cell · 2024Article
- CryoEM structures reveal how the bacterial flagellum rotates and switches direction.Nature microbiology · 2024Article
- Agglomeration: when folded proteins clump together.Biophysical reviews · 2023Review
- Biocorona on Iron Oxide Nanoparticles in a Complex Biotechnological Environment: Analysis of Proteins, Lipids, and Carbohydrates.Small science · 2023Article
- Greater than the sum of parts: Mechanisms of metabolic regulation by enzyme filaments.Current opinion in structural biology · 2023Review
- Mutant libraries reveal negative design shielding proteins from supramolecular self-assembly and relocalization in cells.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Noncanonical protein kinase A activation by oligomerization of regulatory subunits as revealed by inherited Carney complex mutations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Abundance Imparts Evolutionary Constraints of Similar Magnitude on the Buried, Surface, and Disordered Regions of Proteins.Frontiers in molecular biosciences · 2021Article
- Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules.Journal of the American Chemical Society · 2020Article
- Filament formation by metabolic enzymes-A new twist on regulation.Current opinion in cell biology · 2020Review
- Designer protein assemblies with tunable phase diagrams in living cells.Nature chemical biology · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mutations and changes in a protein's environment are well known for their potential to induce misfolding and aggregation, including amyloid formation. Alternatively, such perturbations can trigger new interactions that lead to the polymerization of folded proteins. In contrast to aggregation, this process does not require misfolding and, to highlight this difference, we refer to it as agglomeration. This term encompasses the amorphous assembly of folded proteins as well as the polymerization in one, two, or three dimensions. We stress the remarkable potential of symmetric homo-oligomers to agglomerate even by single surface point mutations, and we review the double-edged nature of this potential: how aberrant assemblies resulting from agglomeration can lead to disease, but also how agglomeration can serve in cellular adaptation and be exploited for the rational design of novel biomaterials.
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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.