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Chitin

About: Chitin is a research topic. Over the lifetime, 6590 publications have been published within this topic receiving 253993 citations.


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Journal ArticleDOI
TL;DR: This review will focus on the preparative methods and applications of carboxymethyl and succinyl derivatives of chitin and chitosan with particular emphasis on their uses as materials for biomedical applications.

445 citations

Journal ArticleDOI
29 Sep 2004-Polymer
TL;DR: In this paper, an electrospinning method was used to fabricate chitin nanofibous matrix for wound dressings, which was depolymerized by gamma irradiation to improve its solubility.

438 citations

Journal ArticleDOI
TL;DR: This review article is mainly focused on the contemporary research on chitin and chitosan towards their applications in numerous biomedical fields namely tissue engineering, artificial kidney, skin, bone, cartilage, liver, nerve, tendon, wound-healing, burn treatment and some other useful purposes.
Abstract: Chitin and its deacetylated derivative chitosan are natural polymers composed of randomly distributed β-(1-4)-linked d-glucosamine (deacetylated unit) and N-acetyl-d-glucosamine (acetylated unit). Biopolymers like chitin and chitosan exhibit diverse properties that open up a wide-ranging of applications in various sectors especially in biomedical science. The latest advances in the biomedical research are important emerging trends that hold a great promise in wound-healing management products. Chitin and chitosan are considered as useful biocompatible materials to be used in a medical device to treat, augment or replace any tissue, organ, or function of the body. A body of recent studies suggests that chitosan and its derivatives are promising candidates for supporting materials in tissue engineering applications. This review article is mainly focused on the contemporary research on chitin and chitosan towards their applications in numerous biomedical fields namely tissue engineering, artificial kidney, skin, bone, cartilage, liver, nerve, tendon, wound-healing, burn treatment and some other useful purposes.

437 citations

Journal ArticleDOI
TL;DR: It is proposed that Slp1 sequesters chitin oligosaccharides to prevent PAMP-triggered immunity in rice, thereby facilitating rapid spread of the fungus within host tissue.
Abstract: Plants use pattern recognition receptors to defend themselves from microbial pathogens. These receptors recognize pathogen-associated molecular patterns (PAMPs) and activate signaling pathways that lead to immunity. In rice (Oryza sativa), the chitin elicitor binding protein (CEBiP) recognizes chitin oligosaccharides released from the cell walls of fungal pathogens. Here, we show that the rice blast fungus Magnaporthe oryzae overcomes this first line of plant defense by secreting an effector protein, Secreted LysM Protein1 (Slp1), during invasion of new rice cells. We demonstrate that Slp1 accumulates at the interface between the fungal cell wall and the rice plasma membrane, can bind to chitin, and is able to suppress chitin-induced plant immune responses, including generation of reactive oxygen species and plant defense gene expression. Furthermore, we show that Slp1 competes with CEBiP for binding of chitin oligosaccharides. Slp1 is required by M. oryzae for full virulence and exerts a significant effect on tissue invasion and disease lesion expansion. By contrast, gene silencing of CEBiP in rice allows M. oryzae to cause rice blast disease in the absence of Slp1. We propose that Slp1 sequesters chitin oligosaccharides to prevent PAMP-triggered immunity in rice, thereby facilitating rapid spread of the fungus within host tissue.

437 citations

Journal ArticleDOI
23 Oct 2014-eLife
TL;DR: The data suggest that AtLYK5 is the primary receptor for chitin, forming a chitIn inducible complex with AtCERK1 to induce plant immunity.
Abstract: Chitin is a fungal microbe-associated molecular pattern recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor and mediates chitin-induced signaling through homodimerization and phosphorylation. However, the reported chitin binding affinity of AtCERK1 is quite low, suggesting another receptor with high chitin binding affinity might be present. Here, we propose that AtLYK5 is the primary chitin receptor in Arabidopsis. Mutations in AtLYK5 resulted in a significant reduction in chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, Atlyk4/Atlyk5-2 double mutants show a complete loss of chitin response. AtLYK5 interacts with AtCERK1 in a chitin-dependent manner. Chitin binding to AtLYK5 is indispensable for chitin-induced AtCERK1 phosphorylation. AtLYK5 binds chitin at a much higher affinity than AtCERK1. The data suggest that AtLYK5 is the primary receptor for chitin, forming a chitin inducible complex with AtCERK1 to induce plant immunity.

433 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023434
2022868
2021271
2020354
2019333
2018271