Evidence map›Paper›PMID 39809320›Full record

ReviewOpen biology2025

Stepwise order in protein complex assembly: approaches and emerging themes.

Michael T Brown, Michael A McMurray

Abstract readReview
In one paragraph

Review in Open biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

2 authors.

Michael T BrownDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus School of Medicine , Aurora, CO 80045, USA.
Michael A McMurrayDepartment of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus School of Medicine , Aurora, CO 80045, USA.ORCID 0000-0002-4615-4334

Funding

Step-wise order of assembly of histone proteins into nucleosomes in living cellsR35GM148198 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI MICHAEL A MCMURRAY · 2023 to 2026
$1.6M
NIGMS NIH HHS R35 GM148198
6 · The paper itself

Abstract

Protein-based nanomachines drive every cellular process. An explosion of high-resolution structures of multiprotein complexes has improved our understanding of what these machines look like and how they work, but we still know relatively little about how they assemble in living cells. For example, it has only recently been appreciated that many complexes assemble co-translationally, with at least one subunit still undergoing active translation while already interacting with other subunits. One aspect that is particularly understudied is assembly order, the idea that there is a stepwise order to the subunit-subunit associations that underlies the efficient assembly of the quaternary structure. Here, we integrate a review of the methodological approaches commonly used to query assembly order within a discussion of studies of the 20S proteasome core particle, septin protein complexes, and the histone octamer. We highlight shared and distinct properties of these complexes that illustrate general themes applicable to most other multisubunit assemblies.

Indexed as

Multiprotein ComplexesProteasome Endopeptidase ComplexAnimalsHistonesHumansModels, MolecularProtein BindingProtein MultimerizationProtein SubunitsSeptinsHistonesMultiprotein ComplexesProteasome Endopeptidase ComplexProtein SubunitsSeptinsassemblyoligomerizationorderprotein complexessubunits

Identifiers

PMID39809320
PMCPMC11732423

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.