Evidence map›Paper›PMID 35765818›Full record

ArticleOpen biology2022

Cell cycle-dependent binding between Cyclin B1 and Cdk1 revealed by time-resolved fluorescence correlation spectroscopy.

Martina Barbiero, Luca Cirillo, Sapthaswaran Veerapathiran, Catherine Coates, Camilla Ruffilli, Jonathon Pines

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2022. 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
17.7field-weighted citation impact, top 1% of its field
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, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Tumor necrosis factor α-induced endoplasmic reticulum stress promotes airway smooth muscle cell proliferation.American journal of physiology. Lung cellular and molecular physiology · 2026
    Article
  4. Article
  5. Article
  6. Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Regulatory role of the miR-142-3p/Translational lung cancer research · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

6 authors at 1 institution in 1 country.

Martina BarbieroCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.
Luca CirilloCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.
Sapthaswaran VeerapathiranCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.
Catherine CoatesCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.
Camilla RuffilliCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.
Jonathon PinesCancer Biology, The Institute of Cancer Research Chester Beatty Laboratories, 237 Fulham Road, London, London SW3 6JB, UK.ORCID 0000-0002-5227-6004
Institute of Cancer Research · GB

Funding

Wellcome Trust 209470/Z/17/Z
6 · The paper itself

Abstract

Measuring the dynamics with which the regulatory complexes assemble and disassemble is a crucial barrier to our understanding of how the cell cycle is controlled that until now has been difficult to address. This considerable gap in our understanding is due to the difficulty of reconciling biochemical assays with single cell-based techniques, but recent advances in microscopy and gene editing techniques now enable the measurement of the kinetics of protein-protein interaction in living cells. Here, we apply fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy to study the dynamics of the cell cycle machinery, beginning with Cyclin B1 and its binding to its partner kinase Cdk1 that together form the major mitotic kinase. Although Cyclin B1 and Cdk1 are known to bind with high affinity, our results reveal that in living cells there is a pool of Cyclin B1 that is not bound to Cdk1. Furthermore, we provide evidence that the affinity of Cyclin B1 for Cdk1 increases during the cell cycle, indicating that the assembly of the complex is a regulated step. Our work lays the groundwork for studying the kinetics of protein complex assembly and disassembly during the cell cycle in living cells.

Indexed as

Gene EditingCell CycleCell DivisionCyclin B1Spectrum AnalysisCyclin B1Cdk1cell cyclecomplex assemblycyclinFCS

Identifiers

PMID35765818
PMCPMC9240681
OpenAlexW4283712037

What OpenQuestion 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 OpenQuestion graph.