Does Generic Cyclic Kinase Insert Domain of Receptor Tyrosine Kinase KIT Clone Its Native Homologue?

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Article in International journal of molecular sciences, 2022. 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

0.2field-weighted citation impact, top 53% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

2 authors at 1 institution in 1 country.

Julie LedouxCentre Borelli, ENS Paris-Saclay, CNRS, Université Paris-Saclay, 4 Avenue des Sciences, F-91190 Gif-sur-Yvette, France.ORCID 0000-0002-2945-735X

Luba TchertanovCentre Borelli, ENS Paris-Saclay, CNRS, Université Paris-Saclay, 4 Avenue des Sciences, F-91190 Gif-sur-Yvette, France.

Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor tyrosine kinases (RTKs) are modular membrane proteins possessing both well-folded and disordered domains acting together in ligand-induced activation and regulation of post-transduction processes that tightly couple extracellular and cytoplasmic events. They ensure the fine-turning control of signal transmission by signal transduction. Deregulation of RTK KIT, including overexpression and gain of function mutations, has been detected in several human cancers. In this paper, we analysed by in silico techniques the Kinase Insert Domain (KID), a key platform of KIT transduction processes, as a generic macrocycle (KID

Indexed as

PhosphotransferasesReceptor Protein-Tyrosine KinasesClone CellsHumansLigandsProto-Oncogene Proteins c-kitSignal TransductionLigandsPhosphotransferasesProto-Oncogene Proteins c-kitReceptor Protein-Tyrosine Kinasesconformational plasticityfree energy landscapegeneric cyclic KIDIDRintrinsically disordered regionKIDkinase insert domainKIT cytoplasmic regionmolecular dynamics and foldingreceptor tyrosine kinaseRTKtransient states

Identifiers

PMID36361689

DOI10.3390/ijms232112898

PMCPMC9656684

OpenAlexW4307551433

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.