Insect-derived chitinases
Advances in Biochemical Engineering/Biotechnology, ISSN: 0724-6145, Vol: 136, Page: 19-50
2013
- 44Citations
- 21Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations44
- Citation Indexes44
- 44
- CrossRef16
- Captures21
- Readers21
- 21
Book Chapter Description
Insect chitinases belong to family 18 of the glycoside hydrolase superfamily (GH18) and comprise endo-splitting enzymes that retain the anomeric β-(1,4) configuration of the cleavage products. However, some of them have lost their catalytic activity but retained the chitin binding activity and/or possess imaginal disc growth factor activity. In all sequenced insect genomes, multiple genes encode chitinases, which are differentially expressed during development and in various insect tissues. Some of them have nonredundant functions and are essential for growth and development. A characteristic property is their multido- main architecture, which comprises varying numbers of catalytic and chitin- binding domains that are connected by glycosylated serine/threonine linker regions. Based on sequence similarities and domain organization, they have been classified into eight different groups. Insect chitinases have gained increasing interest for use in the biological control of parasites, fungi, and insect pests, and some enzymes have properties that make them highly attractive for biotechno- logical applications.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84902667403&origin=inward; http://dx.doi.org/10.1007/10_2013_207; http://www.ncbi.nlm.nih.gov/pubmed/23748348; http://link.springer.com/10.1007/10_2013_207; https://doi.org/10.1007%2F10_2013_207; https://dx.doi.org/10.1007/10_2013_207; https://link.springer.com/chapter/10.1007/10_2013_207
Springer Science and Business Media LLC
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