ArticleThe protein journal2025
Molecular, Structural and Functional Characterization of Antheraea mylitta Expressed Cocoonase: An Integrative Approach.
Article in The protein journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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, a vital naturally secreted protease, enables moth emergence by specifically degumming sericin from cocoons, leaving fibroin intact. This unique characteristic makes it highly promising for protein-based silk degumming. Present study comprehensively characterizes molecular, structural, and functional attributes of Antheraea mylitta cocoonase. Here 786 bp full-length cocoonase gene from A. mylitta pupae head RNA has been successfully cloned and expressed in E. coli and sequence obtained deposited in NCBI (Accession ID: ON261685). Extensive in-silico analyses including 3D structure prediction, motif analysis, phylogenetic relationships, TMHMM, InterProScan, STRING-based protein interactions, and flexibility predictions provided deeper structural insights. Gene ontology classified cocoonase as a serine-type endopeptidase. A. mylitta cocoonase protein of 261-amino acid exhibited a theoretical molecular weight of 27,663.35 Da and an isoelectric point of 9.10 while molecular weight of ~ 28 kDa by SDS-PAGE. Its presumed extracellular localization was supported by the absence of signal peptides and transmembrane helices. STRING analysis revealed functional interacting networks, while ProtScale elucidated protein flexibility. Optical Coherence Tomography based study demonstrated distinct morphological changes in cocoon sheets treated with recombinant cocoonase. This study represents the first successful cloning, expression, and comprehensive in-silico characterization of the A. mylitta cocoonase gene.
Indexed as
Identifiers
41125980What 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.