Evidence map›Paper›PMID 37034755›Full record

ArticlebioRxiv : the preprint server for biology2023

Mechanistic and evolutionary insights into isoform-specific 'supercharging' in DCLK family kinases.

Aarya Venkat, Grace Watterson, Dominic P Byrne, Brady O'Boyle, Safal Shrestha, Nathan Gravel, Emma E Fairweather, Leonard A Daly, Claire Bunn, Wayland Yeung and 5 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. 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, 6 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 2 institutions in 2 countries.

Aarya VenkatDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Grace WattersonDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Dominic P ByrneDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Brady O'BoyleDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Safal ShresthaInstitute of Bioinformatics, University of Georgia, Athens, GA 30602, USA.
Nathan GravelInstitute of Bioinformatics, University of Georgia, Athens, GA 30602, USA.
Emma E FairweatherDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Leonard A DalyDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Claire BunnDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Wayland YeungInstitute of Bioinformatics, University of Georgia, Athens, GA 30602, USA.
Ishan AggarwalDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Samiksha KatiyarDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Claire E EyersDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Patrick A EyersDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Natarajan KannanDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
University of Georgia · USUniversity of Liverpool · GB

Funding

Unlocking sequence-structure-function-disease relationships in large protein super-familiesR35GM139656 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN · 2021 to 2025
$2.2M
NIGMS NIH HHS R35 GM139656
6 · The paper itself

Abstract

Catalytic signaling outputs of protein kinases are dynamically regulated by an array of structural mechanisms, including allosteric interactions mediated by intrinsically disordered segments flanking the conserved catalytic domain. The Doublecortin Like Kinases (DCLKs) are a family of microtubule-associated proteins characterized by a flexible C-terminal autoregulatory 'tail' segment that varies in length across the various human DCLK isoforms. However, the mechanism whereby these isoform-specific variations contribute to unique modes of autoregulation is not well understood. Here, we employ a combination of statistical sequence analysis, molecular dynamics simulations and

Identifiers

PMID37034755
PMCPMC10081240
OpenAlexW4361227878

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.