Evidence map›Paper›PMID 24876415›Full record

ArticleJournal of diabetes science and technology2014

Selective allosteric antibodies to the insulin receptor for the treatment of hyperglycemic and hypoglycemic disorders.

Hassan Issafras, Daniel H Bedinger, John A Corbin, Ira D Goldfine, Vinay Bhaskar, Mark L White, Paul Rubin, Patrick J Scannon

Abstract read
In one paragraph

Article in Journal of diabetes science and technology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Competitive Epitope Binning Using HT-SPR.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Lipid mediators of insulin signaling in diabetic kidney disease.American journal of physiology. Renal physiology · 2019
    Review
  8. Article
  9. Review
  10. 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

8 authors.

Hassan IssafrasPreclinical Research, XOMA Corporation, Berkeley, CA, USA issafras@xoma.com.
Daniel H BedingerPreclinical Research, XOMA Corporation, Berkeley, CA, USA.
John A CorbinPreclinical Research, XOMA Corporation, Berkeley, CA, USA.
Ira D GoldfinePreclinical Research, XOMA Corporation, Berkeley, CA, USA Department of Medicine, University of California, San Francisco, USA.
Vinay BhaskarPreclinical Research, XOMA Corporation, Berkeley, CA, USA.
Mark L WhitePreclinical Research, XOMA Corporation, Berkeley, CA, USA.
Paul RubinPreclinical Research, XOMA Corporation, Berkeley, CA, USA.
Patrick J ScannonPreclinical Research, XOMA Corporation, Berkeley, CA, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many therapeutic monoclonal antibodies act as antagonists to receptors by targeting and blocking the natural ligand binding site (orthosteric site). In contrast, the use of antibodies to target receptors at allosteric sites (distinct from the orthosteric site) has not been extensively studied. This approach is especially important in metabolic diseases in which endogenous ligand levels are dysregulated. Herein, we review our investigations of 3 categories of human monoclonal antibodies that bind allosterically to the insulin receptor (INSR) and affect its activity: XMetA, XMetS and XMetD. XMetA directly activates the INSR either alone or in combination with insulin. XMetS, in contrast, does not directly activate the INSR but markedly enhances the receptor's ability to bind insulin and potentiate insulin signaling. Both XMetA and XMetS are effective in controlling hyperglycemia in mouse models of diabetes. A third allosteric antibody, XMetD, is an inhibitor of INSR signaling. This antibody reverses insulin-induced hypoglycemia in a mouse model of hyperinsulinemia. These studies indicate, therefore, that allosteric antibodies to INSR can modulate its signaling and correct conditions of glucose dysregulation. These studies also raise the possibility that the use of allosteric antibodies can be expanded to other receptors for the treatment of metabolic disorders.

Indexed as

AnimalsAntibodies, MonoclonalCHO CellsCricetinaeCricetulusHumansHyperglycemiaHypoglycemiaHypoglycemic AgentsInsulinOncogene Protein v-aktPhosphorylationReceptor, InsulinAntibodies, MonoclonalHypoglycemic AgentsInsulinOncogene Protein v-aktReceptor, Insulinallostericblood glucosediabetesglycemic disordershyperinsulinemiamonoclonal antibody

Identifiers

PMID24876415
PMCPMC4764207

What OpenQuestion holds

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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.