Evidence map›Paper›PMID 30888575›Full record

ReviewBiophysical reviews2019

Unified theoretical description of the kinetics of protein aggregation.

Nami Hirota, Herman Edskes, Damien Hall

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Biophysical reviews · 2023
    Article
  7. Article
  8. Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Effect of DNA Origami Nanostructures on hIAPP Aggregation.Nanomaterials (Basel, Switzerland) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 2019-A year in Biophysical Reviews.Biophysical reviews · 2019
    Article
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Nami HirotaDo International Trading House, Koshienguchi-1-chome, Nishinomiya, Hyogo, 6113, Japan.
Herman EdskesLaboratory of Biochemistry and Genetics, NIDDK, NIH, Bld 8, Bethesda, MD, 20892-0830, USA.
Damien HallInstitute for Protein Research, Osaka University, 3-1- Yamada-oka, Suita, Osaka, 565-0871, Japan. damien.hall@protein.osaka-u.ac.jp.ORCID http://orcid.org/0000-0003-1538-7618

Funding

National Institute of Diabetes and Digestive and Kidney Diseases IntramuralOsaka University Institute for Protein Research (Funds in Aid)
6 · The paper itself

Abstract

Solution conditions chosen for the production of amyloid can also promote formation of significant extents of amorphous protein aggregate. In one interpretation, the amyloid and amorphous aggregation pathways are considered to be in competition with each other. An alternative conceptualization involves considering amorphous aggregation as an obligatory intermediate process of the amyloid formation pathway. Here, we review recently developed macroscopic-level theories of protein aggregation that unify these two competing models into a single paradigm. Key features of the unified model included (1) a description of the amorphous aggregate as a second liquid phase with the degree of liquid-like character determined by the mobility of the monomer within it, and (2) heterogeneous growth pathways based on nucleation, growth, and fragmentation of amyloid occurring within different phases and at their interfacial boundary. Limiting-case behaviors of the protein aggregation reaction, either singly involving amyloid or amorphous aggregate production, and mixed-case behaviors, involving competitive and/or facilitated growth of amorphous and amyloid species, are presented and reviewed in context. This review principally describes an approach developed by Hirota and Hall 2019 (Hirota, N. and Hall, D. 2019. Protein Aggregation Kinetics: A Unified Theoretical Description. Chapter 7 of 'Protein Solubility and Amorphous Aggregation: From Academic Research to Applications in Drug Discovery and Bioindustry' edited by Y. Kuroda and F. Arisaka. CMC Publishers). Sections of that work are translated from the original Japanese and republished here with the full permission of CMC Publishing Corporation.

Indexed as

AmyloidKineticsProtein aggregationUnited model

Identifiers

PMID30888575
PMCPMC6441446

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.