Evidence map›Paper›PMID 32708676›Full record

ArticleBiomolecules2020

Probing Structure and Function of Alkali Sensor IRR with Monoclonal Antibodies.

Alexander S Goryashchenko, Andrey A Mozhaev, Oxana V Serova, Tatiana N Erokhina, Alexander N Orsa, Igor E Deyev, Alexander G Petrenko

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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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

7 authors at 2 institutions in 1 country.

Alexander S GoryashchenkoLaboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.ORCID 0000-0001-9297-9284
Andrey A MozhaevLaboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.ORCID 0000-0001-5790-9926
Oxana V SerovaLaboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.ORCID 0000-0002-4941-8913
Tatiana N ErokhinaLaboratory of Molecular Diagnostics, Department of Plant Molecular Biology and Biotechnology, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.
Alexander N OrsaLaboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.
Igor E DeyevGroup of Molecular Physiology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.ORCID 0000-0002-2041-808X
Alexander G PetrenkoLaboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia.
Institute of Bioorganic Chemistry · RURussian Academy of Sciences · RU

Funding

Russian Foundation for Basic Research 17-00-00486
6 · The paper itself

Abstract

To study the structure and function of the pH-regulated receptor tyrosine kinase insulin receptor-related receptor (IRR), а member of the insulin receptor family, we obtained six mouse monoclonal antibodies against the recombinant IRR ectodomain. These antibodies were characterized in experiments with exogenously expressed full-length IRR by Western blotting, immunoprecipitation, and immunocytochemistry analyses. Utilizing a previously obtained set of IRR/IR chimeras with swapped small structural domains and point amino acid substitutions, we mapped the binding sites of the obtained antibodies in IRR. Five of them showed specific binding to different IRR domains in the extracellular region, while one failed to react with the full-length receptor. Unexpectedly, we found that 4D5 antibody can activate IRR at neutral pH, and 4C2 antibody can inhibit activation of IRR by alkali. Our study is the first description of the instruments of protein nature that can regulate activity of the orphan receptor IRR and confirms that alkali-induced activation is an intrinsic property of this receptor tyrosine kinase.

Indexed as

AlkaliesAnimalsAntibodies, MonoclonalBlotting, WesternHEK293 CellsHumansImmunohistochemistryImmunoprecipitationMiceModels, MolecularProtein ConformationProtein DomainsReceptor, InsulinAlkaliesAntibodies, Monoclonalinsulin receptor-related receptorReceptor, Insulinactivatoralkali sensorinhibitorIRRmonoclonal antibodyreceptor tyrosine kinase

Identifiers

PMID32708676
PMCPMC7408431
OpenAlexW3042284251

What OpenQuestion holds

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LicenceCC BY
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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.