Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin (Q24310140)

GOA release 2020-03-11

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Jesper B Moeller

3

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Søren Kragh Moestrup

object named as

Søren K Moestrup

7

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Uffe Holmskov

8

object named as

Uffe Holmskov

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author name string

Anders Schlosser

1

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Theresa Thomsen

2

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Ole Nielsen

4

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Ida Tornøe

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Jan Mollenhauer

A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives

6

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language of work or name

English

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publication date

15 September 2009

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published in

Journal of Immunology

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volume

183

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issue

6

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page(s)

3800-9

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cites work

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Chitin and chitosan: functional biopolymers from marine crustaceans

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Embryogenesis: anchors away!

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Scabrous complexes with Notch to mediate boundary formation

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Chitin induces accumulation in tissue of innate immune cells associated with allergy

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Toll-like receptors--taking an evolutionary approach

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An integrated model of the recognition of Candida albicans by the innate immune system.

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Structural insights into the innate immune recognition specificities of L- and H-ficolins

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Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor

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CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis

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The 2.0-A crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems

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Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen

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Identification of a novel acidic mammalian chitinase distinct from chitotriosidase

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L-ficolin is a pattern recognition molecule specific for acetyl groups

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Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2.

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Characterization of human phagocyte-derived chitotriosidase, a component of innate immunity.

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Fungal cell wall chitinases and glucanases

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The cell wall: a carbohydrate armour for the fungal cell

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M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement

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Microfibril-associated protein 4 binds to surfactant protein A (SP-A) and colocalizes with SP-A in the extracellular matrix of the lung.

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Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation

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Spacing differentiation in the developing Drosophila eye: a fibrinogen-related lateral inhibitor encoded by scabrous

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Alveolar macrophage priming by intravenous administration of chitin particles, polymers of N-acetyl-D-glucosamine, in mice.

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Expression and localization of lung surfactant protein A in human tissues

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Immune sensing of Candida albicans requires cooperative recognition of mannans and glucans by lectin and Toll-like receptors

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Cellular expression of gut chitinase mRNA in the gastrointestinal tract of mice and chickens

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Evolution of mammalian chitinase(-like) members of family 18 glycosyl hydrolases.

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Oral administration of chitin down-regulates serum IgE levels and lung eosinophilia in the allergic mouse.

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L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement

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TLR-2 and IL-17A in chitin-induced macrophage activation and acute inflammation.

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