Human ficolin-2 recognition versatility extended: an update on the binding of ficolin-2 to sulfated/phosphated carbohydrates (Q27696251)

6

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author name string

Emmanuelle Laffly

1

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Monique Lacroix

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Lydie Martin

3

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Emilie Vassal-Stermann

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Nicole M Thielens

A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin

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language of work or name

English

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publication date

20 December 2014

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published in

FEBS Letters

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volume

588

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issue

24

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page(s)

4694-700

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cites work

1 reference

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Carbohydrate Recognition Properties of Human Ficolins: GLYCAN ARRAY SCREENING REVEALS THE SIALIC ACID BINDING SPECIFICITY OF M-FICOLIN

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The lectin pathway of complement activation is a critical component of the innate immune response to pneumococcal infection

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Low invasiveness of pneumococcal serotype 11A is linked to ficolin-2 recognition of O-acetylated capsule epitopes and lectin complement pathway activation.

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Ficolin-2 recognizes DNA and participates in the clearance of dying host cells.

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Mitochondria and the lectin pathway of complement

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Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation

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The lectin-complement pathway--its role in innate immunity and evolution

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

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Ficolins in complement activation

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

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

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Ficolin-B marks apoptotic and necrotic cells

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The complement protein properdin binds apoptotic T cells and promotes complement activation and phagocytosis.

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

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Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein

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Functional characterization of the recombinant human C1 inhibitor serpin domain: insights into heparin binding.

21 January 2018

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Phasercrystallographic software

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REFMAC5 for the refinement of macromolecular crystal structures

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Features and development of Coot

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Correlating structure and function during the evolution of fibrinogen-related domains

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10.1016/J.FEBSLET.2014.10.042

21 January 2018

Identifiers

DOI

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Fatcat ID

release_rrzdo5izevgbrh7fj67uh5hpc4

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Fatcat

https://api.fatcat.wiki/v0/release/rrzdo5izevgbrh7fj67uh5hpc4