Evidence map›Paper›PMID 14529486›Full record

ReviewCurrent medicinal chemistry2003

Glucagon-like peptide-1 synthetic analogs: new therapeutic agents for use in the treatment of diabetes mellitus.

George G Holz, Oleg G Chepurny

Open access · greenAbstract readReview
In one paragraph

Review in Current medicinal chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
15.6field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.

  1. Pooled it
  2. Sitagliptin exerts an antinflammatory action.The Journal of clinical endocrinology and metabolism · 2012
    Trial
  3. Exenatide exerts a potent antiinflammatory effect.The Journal of clinical endocrinology and metabolism · 2012 · on this map
    Trial
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Regulation of glucose homeostasis by GLP-1.Progress in molecular biology and translational science · 2014
    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

2 authors at 1 institution in 1 country.

George G HolzDepartment of Physiology and Neuroscience, New York University School of Medicine, New York, 10016, USA. holzg01@popmail.med.nyu.edu
Oleg G Chepurny
New York University · US

Funding

Insulinotropin: A Modulator Of B-Cell Glucose SignalingR01DK045817 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI HOLZ, GEORGE G · 2001 to 2008
$3.0M
MOLECULAR BASIS OF ANTIDIABETOGENIC HORMONE ACTIONR01DK052166 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HOLZ, GEORGE G · 1997 to 2000
$205k
NIDDK NIH HHS R01 DK045817NIDDK NIH HHS R01-DK45817NIDDK NIH HHS R01-DK52166
6 · The paper itself

Abstract

Glucagon-like peptide-1-(7-36)-amide (GLP-1) is a potent blood glucose-lowering hormone now under investigation for use as a therapeutic agent in the treatment of type 2 (adult onset) diabetes mellitus. GLP-1 binds with high affinity to G protein-coupled receptors (GPCRs) located on pancreatic beta-cells, and it exerts insulinotropic actions that include the stimulation of insulin gene transcription, insulin biosynthesis, and insulin secretion. The beneficial therapeutic action of GLP-1 also includes its ability to act as a growth factor, stimulating formation of new pancreatic islets (neogenesis) while slowing beta-cell death (apoptosis). GLP-1 belongs to a large family of structurally-related hormones and neuropeptides that include glucagon, secretin, GIP, PACAP, and VIP. Biosynthesis of GLP-1 occurs in the enteroendocrine L-cells of the distal intestine, and the release of GLP-1 into the systemic circulation accompanies ingestion of a meal. Although GLP-1 is inactivated rapidly by dipeptidyl peptidase IV (DDP-IV), synthetic analogs of GLP-1 exist, and efforts have been directed at engineering these peptides so that they are resistant to enzymatic hydrolysis. Additional modifications of GLP-1 incorporate fatty acylation and drug affinity complex (DAC) technology to improve serum albumin binding, thereby slowing renal clearance of the peptides. NN2211, LY315902, LY307161, and CJC-1131 are GLP-1 synthetic analogs that reproduce many of the biological actions of GLP-1, but with a prolonged duration of action. AC2993 (Exendin-4) is a naturally occurring peptide isolated from the lizard Heloderma, and it acts as a high affinity agonist at the GLP-1 receptor. This review summarizes structural features and signal transduction properties of GLP-1 and its cognate beta-cell GPCR. The usefulness of synthetic GLP-1 analogs as blood glucose-lowering agents is discussed, and the applicability of GLP-1 as a therapeutic agent for treatment of type 2 diabetes is highlighted.

Indexed as

AnimalsBlood GlucoseDiabetes Mellitus, Type 2ExenatideGlucagonGlucagon-Like Peptide 1Glucagon-Like Peptide-1 ReceptorHumansInsulinInsulin SecretionPeptide FragmentsPeptidesProtein PrecursorsReceptors, GlucagonVenomsBlood GlucoseExenatideGLP1R protein, humanGlucagonGlucagon-Like Peptide 1Glucagon-Like Peptide-1 ReceptorInsulinPeptide FragmentsPeptidesProtein PrecursorsReceptors, GlucagonVenoms

Identifiers

PMID14529486
PMCPMC2911578
OpenAlexW2144546532

What OpenQuestion holds

Textmetadata
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.