Phenomena and Processes

Kringles

Triple-looped protein domains linked by disulfide bonds. These common structural domains, so-named for their resemblance to Danish pastries known as kringlers, play a role in binding membranes, proteins, and phospholipids as well as in regulating proteolysis. Kringles are also present in coagulation-related and fibrinolytic proteins and other plasma proteinases.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

Triple-looped protein domains linked by disulfide bonds. These common structural domains, so-named for their resemblance to Danish pastries known as kringlers, play a role in binding membranes, proteins, and phospholipids as well as in regulating proteolysis. Kringles are also present in coagulation-related and fibrinolytic proteins and other plasma proteinases.

MeSH Record

Classification

Broader headings

Related Concepts

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MeSH Record

Synonyms

5 entry terms
  • Kringle Domains
  • Domain, Kringle
  • Domains, Kringle
  • Kringle
  • Kringle Domain

MeSH Record

Aspects Covered

5 allowable subheadings

Indexed with the subheadings drug effects, genetics, immunology, physiology, radiation effects.

MeSH Record

History Note

94; was KRINGLES (NM) 1980-93

MeSH Record

Previous Indexing

  • Amino Acid Sequence (1981-1993)
  • Peptide Fragments (1980-1993)

MeSH Hierarchy

Tree Number

  1. G02.111.570.820w.709.275.750w.375w

AMA Style

References

  1. National Library of Medicine. Kringles. Medical Subject Headings (MeSH). 2026. Unique ID D018082. http://id.nlm.nih.gov/mesh/2026/D018082
  2. Kringles. In: Wikipedia. https://en.wikipedia.org/wiki/Kringle_domain
  3. Kringles. In: Wikidata. https://www.wikidata.org/wiki/Q24726526