Evidence map›Paper›PMID 34789923›Full record

ReviewNature reviews. Endocrinology2022

The manifold roles of protein S-nitrosylation in the life of insulin.

Hua-Lin Zhou, Richard T Premont, Jonathan S Stamler

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Endocrinology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.0field-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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
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  8. Review
  9. Redox regulation of mNature cell biology · 2024
    Article
  10. Article
  11. Article
  12. Metabolic regulation of glucagon secretion.The Journal of endocrinology · 2023
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. 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

3 authors at 2 institutions in 1 country.

Hua-Lin ZhouDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
Richard T PremontDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH, USA.ORCID http://orcid.org/0000-0002-8053-5026
Jonathan S StamlerDepartment of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH, USA. jonathan.stamler@case.edu.ORCID http://orcid.org/0000-0002-6866-1572
University School · USUniversity Hospitals Cleveland Medical Center · US

Funding

S-nitrosylation signaling in asthmaP01HL158507 · NHLBI · INDIANA UNIVERSITY INDIANAPOLIS · PI LAHM, TIM · 2021 to 2025
$12.0M
Restoration and Function of S-Nitrosothiol in Stored BloodR01HL126900 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI JONATHAN S. STAMLER · 2016 to 2026
$5.0M
Novel Regulation of Renal Function by S-NitrosylationR01DK119506 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI JONATHAN S. STAMLER, Hualin Zhou · 2018 to 2026
$3.7M
Role of S-Nitrosylation on Beta-Adrenergic Signaling in Cardiac Injury and RepairR01HL157151 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI KOCH, WALTER J., STAMLER, JONATHAN S. · 2021 to 2024
$2.8M
Gut Microbe-Derived Nitric Oxide As A Signal To Host: Role In Normal Physiology And In DiseaseR01DK128347 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI SETH, PUNEET, STAMLER, JONATHAN S. · 2021 to 2024
$1.4M
NHLBI NIH HHS P01 HL158507NHLBI NIH HHS R01 HL126900NHLBI NIH HHS R01 HL157151NIDDK NIH HHS R01 DK119506NIDDK NIH HHS R01 DK128347
6 · The paper itself

Abstract

Insulin, which is released by pancreatic islet β-cells in response to elevated levels of glucose in the blood, is a critical regulator of metabolism. Insulin triggers the uptake of glucose and fatty acids into the liver, adipose tissue and muscle, and promotes the storage of these nutrients in the form of glycogen and lipids. Dysregulation of insulin synthesis, secretion, transport, degradation or signal transduction all cause failure to take up and store nutrients, resulting in type 1 diabetes mellitus, type 2 diabetes mellitus and metabolic dysfunction. In this Review, we make the case that insulin signalling is intimately coupled to protein S-nitrosylation, in which nitric oxide groups are conjugated to cysteine thiols to form S-nitrosothiols, within effectors of insulin action. We discuss the role of S-nitrosylation in the life cycle of insulin, from its synthesis and secretion in pancreatic β-cells, to its signalling and degradation in target tissues. Finally, we consider how aberrant S-nitrosylation contributes to metabolic diseases, including the roles of human genetic mutations and cellular events that alter S-nitrosylation of insulin-regulating proteins. Given the growing influence of S-nitrosylation in cellular metabolism, the field of metabolic signalling could benefit from renewed focus on S-nitrosylation in type 2 diabetes mellitus and insulin-related disorders.

Indexed as

Diabetes Mellitus, Type 2Insulin ResistanceInsulin-Secreting CellsHumansInsulinNitric OxideSulfhydryl CompoundsInsulinNitric OxideSulfhydryl Compounds

Identifiers

PMID34789923
PMCPMC8889587
OpenAlexW3211536474

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.