ArticleBiochemistry2018
Cooperative Assembly of Hsp70 Subdomain Clusters.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Microfluidics for protein interaction studies: current methods, challenges, and future perspectives.European biophysics journal : EBJ · 2026Review
- Microfluidic diffusional sizing in bioanalysis and biosensing.Lab on a chip · 2026Review
- Determining the Hydrodynamic Size of Lipid Nanoparticles by Fluorescent Universal Lipid Labeling for Microfluidic Diffusional Sizing (FULL-MDS).Methods in molecular biology (Clifton, N.J.) · 2026Article
- Single-molecule digital sizing of proteins in solution.Nature communications · 2024Article
- An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis.Protein science : a publication of the Protein Society · 2023Article
- The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends.Nature communications · 2021Article
- LAG3 is not expressed in human and murine neurons and does not modulate α-synucleinopathies.EMBO molecular medicine · 2021Article
- DL-3-n-butylphthalide protects H9c2 cardiomyoblasts from ischemia/reperfusion injury by regulating HSP70 expression via PI3K/AKT pathway activation.Experimental and therapeutic medicine · 2021Article
- Microfluidic approaches for the analysis of protein-protein interactions in solution.Biophysical reviews · 2020Review
- Kinetics of Transient Protein Complexes Determined via Diffusion-Independent Microfluidic Mixing and Fluorescence Stoichiometry.The journal of physical chemistry. B · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Many molecular chaperones exist as oligomeric complexes in their functional states, yet the physical determinants underlying such self-assembly behavior, as well as the role of oligomerization in the activity of molecular chaperones in inhibiting protein aggregation, have proven to be difficult to define. Here, we demonstrate direct measurements under native conditions of the changes in the average oligomer populations of a chaperone system as a function of concentration and time and thus determine the thermodynamic and kinetic parameters governing the self-assembly process. We access this self-assembly behavior in real time under native-like conditions by monitoring the changes in the micrometer-scale diffusion of the different complexes in time and space using a microfluidic platform. Using this approach, we find that the oligomerization mechanism of the Hsp70 subdomain occurs in a cooperative manner and involves structural constraints that limit the size of the species formed beyond the limits imposed by mass balance. These results illustrate the ability of microfluidic methods to probe polydisperse protein self-assembly in real time in solution and to shed light on the nature and dynamics of oligomerization processes.
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Registered trials
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