ReviewJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology2015
Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology.
Review in Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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.
Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Integrated Microbiome, Transcriptome, and Physiology Analyses Reveal the Response Of Kuruma Shrimp (Penaeus japonicus) to Oxygen Nanobubble Exposure.Marine biotechnology (New York, N.Y.) · 2025Article
- Changes in Biochemical Properties and Activity of Trypsin-like Protease (Foods (Basel, Switzerland) · 2022Article
- Review
- Crustacean Proteases and Their Application in Debridement.Tropical life sciences research · 2020Article
- Article
- Identification and in silico structural and functional analysis of a trypsin-like protease from shrimpPeerJ · 2020Article
- Biochemical characterization of a native group III trypsin ZT from Atlantic cod (Gadus morhua).International journal of biological macromolecules · 2019Article
- Digestive enzyme activity in the intestine of Nile tilapia (Oreochromis niloticus L.) under pond and cage farming systems.Fish physiology and biochemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trypsin enzymes have been studied in a wide variety of animal taxa due to their central role in protein digestion as well as in other important physiological and biotechnological processes. Crustacean trypsins exhibit a high number of isoforms. However, while differences in properties of isoenzymes are known to play important roles in regulating different physiological processes, there is little information on this aspect for decapod trypsins. The aim of this review is to integrate recent findings at the molecular level on trypsin enzymes of the spiny lobster Panulirus argus, into higher levels of organization (biochemical, organism) and to interpret those findings in relation to the feeding ecology of these crustaceans. Trypsin in lobster is a polymorphic enzyme, showing isoforms that differ in their biochemical features and catalytic efficiencies. Molecular studies suggest that polymorphism in lobster trypsins may be non-neutral. Trypsin isoenzymes are differentially regulated by dietary proteins, and it seems that some isoenzymes have undergone adaptive evolution coupled with a divergence in expression rate to increase fitness. This review highlights important but poorly studied issues in crustaceans in general, such as the relation among trypsin polymorphism, phenotypic (digestive) flexibility, digestion efficiency, and feeding ecology.
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Registered trials
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.