Evidence map›Paper›PMID 35350789›Full record

ArticleFrontiers in immunology2022

Antibody-Mediated Inhibition of Insulin-Degrading Enzyme Improves Insulin Activity in a Diabetic Mouse Model.

Ofir Fursht, Mirit Liran, Yuval Nash, Vijay Krishna Medala, Dor Ini, Tabitha Grace Royal, Guy Goldsmith, Limor Nahary, Itai Benhar, Dan Frenkel

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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

10 authors at 1 institution in 1 country.

Ofir FurshtDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Mirit LiranThe Shmunis School of Biomedicine and Cancer Research, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Yuval NashDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Vijay Krishna MedalaDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Dor IniThe Shmunis School of Biomedicine and Cancer Research, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Tabitha Grace RoyalDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Guy GoldsmithDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Limor NaharyThe Shmunis School of Biomedicine and Cancer Research, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Itai BenharThe Shmunis School of Biomedicine and Cancer Research, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Dan FrenkelDepartment of Neurobiology, School of Neurobiology, Biochemistry and Biophysics, the George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetes is a metabolic disease that may lead to different life-threatening complications. While insulin constitutes a beneficial treatment, its use may be limited due to increased degradation and an increase in side effects such as weight gain and hypoglycemia. Small molecule inhibitors to insulin-degrading enzyme (IDE) have been previously suggested as a potential treatment for diabetes through their ability to reduce insulin degradation and thus increase insulin activity. Nevertheless, their tendency to bind to the zinc ion in the catalytic site of IDE may affect other important metalloproteases and limit their clinical use. Here, we describe the isolation of an IDE-specific antibody that specifically inhibits insulin degradation by IDE. Using phage display, we generated a human IDE-specific antibody that binds human and mouse IDE with high affinity and specificity and can differentiate between active IDE to a mutated IDE with reduced catalytic activity in the range of 30 nM. We further assessed the ability of that IDE-inhibiting antibody to improve insulin activity

Indexed as

Diabetes Mellitus, ExperimentalInsulysinAnimalsAntibodiesCatalytic DomainDisease Models, AnimalInsulinMiceAntibodiesInsulinInsulysinantibodyantibody engineeringdiabetesinsulin-degrading enzyme (IDE)ScFv library

Identifiers

PMID35350789
PMCPMC8958001
OpenAlexW4221109485

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.