Evidence map›Paper›PMID 40358525›Full record

ReviewBiochemical Society transactions2025

Cdk activation by phosphorylation: linking growth signals to cell cycle control.

Heidi M Blank, Eun-Gyu No, Michael Polymenis

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 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

3 authors.

Heidi M BlankDepartment of Biochemistry and Biophysics, Texas A&M University, 300 Olsen Blvd., College Station, Texas 77843, U.S.A.ORCID 0000-0002-2251-5246
Eun-Gyu NoDepartment of Biochemistry and Biophysics, Texas A&M University, 300 Olsen Blvd., College Station, Texas 77843, U.S.A.
Michael PolymenisDepartment of Biochemistry and Biophysics, Texas A&M University, 300 Olsen Blvd., College Station, Texas 77843, U.S.A.ORCID 0000-0003-1507-0936

Funding

Coupling Of Protein Synthesis With Cell DivisionR01GM123139 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI POLYMENIS, MICHAEL S · 2017 to 2024
$2.9M
NIGMS NIH HHS R01 GM123139
6 · The paper itself

Abstract

Cells adjust their proliferation in response to extrinsic factors and nutrients. Such inputs must reach the cell cycle machinery to ensure proper cell proliferation. This minireview focuses on evidence suggesting that phosphorylating the T-loop domain of cyclin-dependent kinases may be a critical and conserved conduit for these external signals. Understanding this regulatory mechanism could provide crucial insights into how all eukaryotic cells integrate external information to decide whether or not to divide.

Indexed as

Cell CycleCell Cycle CheckpointsCyclin-Dependent KinasesSignal TransductionAnimalsCell ProliferationEnzyme ActivationHumansPhosphorylationCyclin-Dependent KinasesCAKCak1pCdc28pcell cyclephosphorylationT-loop

Identifiers

PMID40358525
PMCPMC12203924

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.