In one paragraphArticle in Cells, 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
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
13 authors.
Andrea Lauer BetránDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0009-0003-5191-1015 Alessandro AgnarelliDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0003-3218-3836 Mark SamuelsDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.
Viviana VellaDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0003-1000-3443 Reza Shirazi NiaInternational Oncology Institute, The First Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou 310053, China.ORCID 0000-0003-4002-4712 Daniel De VegaInternational Oncology Institute, The First Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou 310053, China.
Niloufar PoudineInternational Oncology Institute, The First Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou 310053, China.
Daniela Carter-LopezDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0009-0006-6645-6125 Angeliki DitsiouDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0003-3743-8447 Murat EravciDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0003-4786-9179 Chrisostomos ProdromouDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0003-4320-1147 Erika J ManciniSussex Drug Discovery Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0001-9591-7898 Georgios GiamasDepartment of Biochemistry and Biomedicine, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.ORCID 0000-0002-4417-2707 Funding
action against cancer G1868
6 · The paper itselfAbstract
Lemur tail kinase 3 (LMTK3) is an oncogenic Ser/Thr kinase implicated in breast cancer (BC) progression, therapy resistance, and poor clinical outcomes, yet the molecular mechanisms governing its regulation remain poorly understood, particularly the role of its C-terminal intrinsically disordered region (IDR). Given that IDRs frequently harbour hidden structural motifs that control protein dynamics, we combined computational, biophysical, and biochemical approaches to systematically map regulatory elements within the LMTK3 C-terminus, identifying two regions (residues 688-1095 and 1181-1486) that interact with the LMTK3 kinase domain (LMTK3-KD). Characterisation of these interactions revealed that LMTK3
Indexed as
Breast NeoplasmsIntrinsically Disordered ProteinsProtein Serine-Threonine KinasesAmino Acid SequenceAnimalsCell Line, TumorCell ProliferationFemaleHumansMembrane ProteinsMicePhenotypePhosphorylationProtein BindingProtein DomainsIntrinsically Disordered ProteinsLMTK3 protein, humanMembrane ProteinsProtein Serine-Threonine Kinasesbreast cancerintrinsically disordered regionkinase regulationLMTK3phosphorylation
Identifiers
PMID42645201
PMCPMC13510533
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