Evidence map›Paper›PMID 32302608›Full record

ArticleJournal of molecular biology2020

Bacterial Phytochrome as a Scaffold for Engineering of Receptor Tyrosine Kinases Controlled with Near-Infrared Light.

Anna V Leopold, Sergei Pletnev, Vladislav V Verkhusha

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Synthetic Toll-Like Receptors for Control of Innate Immunity With Far-Red Light.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Red Light Optogenetics in Neuroscience.Frontiers in cellular neuroscience · 2021
    Review
  14. Review
  15. 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 at 3 institutions in 2 countries.

Anna V LeopoldMedicum, Faculty of Medicine, University of Helsinki, Helsinki 00290, Finland.
Sergei PletnevMacromolecular Crystallography Laboratory, National Cancer Institute, Basic Science Program, Leidos Biomedical Research Inc., Argonne, IL 60439, USA.
Vladislav V VerkhushaMedicum, Faculty of Medicine, University of Helsinki, Helsinki 00290, Finland; Department of Anatomy and Structural Biology, and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA. Electronic address: vladislav.verkhusha@einsteinmed.org.
Albert Einstein College of Medicine · USLeidos (United States) · USUniversity of Helsinki · FI

Funding

Near-Infrared Fluorescent Proteins, Biosensors and Optogenetic ToolsR35GM122567 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI Vladislav Verkhusha · 2017 to 2026
$4.3M
Calcium biosensors for deep-tissue imaging and spectral multiplexingU01NS103573 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VERKHUSHA, VLADISLAV · 2017 to 2019
$1.8M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENIGMS NIH HHS R35 GM122567NINDS NIH HHS U01 NS103573
6 · The paper itself

Abstract

Optically controlled receptor tyrosine kinases (opto-RTKs) allow regulation of RTK signaling using light. Until recently, the majority of opto-RTKs were activated with blue-green light. Fusing a photosensory core module of Deinococcus radiodurans bacterial phytochrome (DrBphP-PCM) to the kinase domains of neurotrophin receptors resulted in opto-RTKs controlled with light above 650 nm. To expand this engineering approach to RTKs of other families, here we combined the DrBpP-PCM with the cytoplasmic domains of EGFR and FGFR1. The resultant Dr-EGFR and Dr-FGFR1 opto-RTKs are rapidly activated with near-infrared and inactivated with far-red light. The opto-RTKs efficiently trigger ERK1/2, PI3K/Akt, and PLCγ signaling. Absence of spectral crosstalk between the opto-RTKs and green fluorescent protein-based biosensors enables simultaneous Dr-FGFR1 activation and detection of calcium transients. Action mechanism of the DrBphP-PCM-based opto-RTKs is considered using the available RTK structures. DrBphP-PCM represents a versatile scaffold for engineering of opto-RTKs that are reversibly regulated with far-red and near-infrared light.

Indexed as

Biosensing TechniquesDeinococcusGreen Fluorescent ProteinsHeLa CellsHumansLightMAP Kinase Signaling SystemNerve Growth FactorsPhosphatidylinositol 3-KinasesPhytochromeProtein ConformationProto-Oncogene Proteins c-aktReceptor, Fibroblast Growth Factor, Type 1Receptor Protein-Tyrosine KinasesReceptors, Nerve Growth FactorSignal TransductionGreen Fluorescent ProteinsNerve Growth FactorsPhosphatidylinositol 3-KinasesPhytochromeProto-Oncogene Proteins c-aktReceptor, Fibroblast Growth Factor, Type 1Receptor Protein-Tyrosine KinasesReceptors, Nerve Growth FactorbacteriophytochromeDrBphPEGFRFGFR1opto-RTK

Identifiers

PMID32302608
PMCPMC7306426
OpenAlexW3016786681

What OpenQuestion holds

Textmetadata
LicenceTDM
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.