ReviewThe protein journal2025
Impression of Insect's Proteolytic Enzyme Cocoonase and Its Application: A Comprehensive Review.
Review in The protein journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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
1 citing paper in PubMed.
- Molecular, Structural and Functional Characterization of Antheraea mylitta Expressed Cocoonase: An Integrative Approach.The protein journal · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Cocoonase is a naturally secreted protease responsible for facilitating moth emergence from inside of cocoon. This protease is considered as of prime importance for all the cocooning lepidopteron. It specifically degrades sericin, the glue protein of the cocoon without damaging the fibroin and makes an escape hatch for adult emergence. Owing to this property cocoonase was characterized and explored for its prospective utilization in eco-friendly enzyme-based silk degumming. However, the applicability of cocoonase has not been explored much other than in silk degumming. Moreover, being a serine protease, and because of its similarity to trypsin, there is, tremendous potential for this enzyme to have biomedical applications, as well as numerous other uses that need to be investigated. This review article presents the comprehensive physicochemical properties of the cocoonase and its possible scope of applications in the near future.
Indexed as
Identifiers
39904822What OpenQuestion holds
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.