Evidence map›Paper›PMID 41648226›Full record

ArticlebioRxiv : the preprint server for biology2026

Identification and inhibition of the Cyclin D Rb-docking interface that drives cell division.

Benjamin R Topacio, Cecelia Brown Fleming, Michael C Lanz, Shuyuan Zhang, Shicong Xie, Jurgen Tuvikene, Aiden Weaver, Ioannis Sanidas, Julien Sage, Seth M Rubin and 2 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Benjamin R TopacioDepartment of Biology, Stanford University, Stanford CA, USA.
Cecelia Brown FlemingDepartment of Biology, Stanford University, Stanford CA, USA.
Michael C LanzDepartment of Biology, Stanford University, Stanford CA, USA.ORCID 0000-0001-8175-7627
Shuyuan ZhangDepartment of Biology, Stanford University, Stanford CA, USA.ORCID 0000-0002-6220-5998
Shicong XieDepartment of Biology, Stanford University, Stanford CA, USA.ORCID 0000-0002-3283-3248
Jurgen TuvikeneLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, 37 Convent Dr., Bethesda, MD 20892, USA.
Aiden WeaverLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, 37 Convent Dr., Bethesda, MD 20892, USA.
Ioannis SanidasMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown MA, USA.
Julien SageDepartments of Pediatrics and Genetics, Stanford University, Stanford, CA, USA.
Seth M RubinDepartment of Chemistry and Biochemistry, University of California Santa Cruz, Santa Cruz CA, USA.
Mardo KõivomägiDepartment of Biology, Stanford University, Stanford CA, USA.
Jan M SkotheimDepartment of Biology, Stanford University, Stanford CA, USA.

Funding

Project 3: Defining and targeting mechanisms of E2F transcription factor regulationP01CA254867 · NCI · STANFORD UNIVERSITY · PI Seth Michael Rubin, Jan M Skotheim · 2022 to 2026
$8.9M
Biochemical mechanisms cyclin-dependent kinases use to control cell divisionZIABC012133 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KOIVOMAGI, MARDO · 2023 to 2025
$4.3M
Intramural NIH HHS ZIA BC012133NCI NIH HHS P01 CA254867
6 · The paper itself

Abstract

The animal cell division cycle is initiated by the cyclin-dependent kinases CDK4 and CDK6 in complex with D-type cyclins. Cyclin D-CDK4/6 complex formation is promoted by the assembly factors p21 and p27, which bind both subunits. p27 binds the hydrophobic patch on cyclin D that is similar to the patch used by other cell cycle cyclins to dock their substrates. This raised the question as to how cyclin D could find its substrates if its hydrophobic patch were already occupied? Here, we show that D-type cyclins use their A2' helix to dock the retinoblastoma protein Rb, a key substrate regulating cell cycle progression. The specific interface of cyclin D's A2' helix is unique among cyclins and its mutation slows proliferation. Taken together, our work identifies a cyclin D-substrate docking mechanism that can be targeted by novel cancer therapeutics.

Identifiers

PMID41648226
PMCPMC12871278

What OpenQuestion holds

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Registered trials

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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.