The role of ficolins in the lectin pathway of innate immunity (Q37840510)

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scientific article published on February 18, 2011

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English	The role of ficolins in the lectin pathway of innate immunity	scientific article published on February 18, 2011

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scholarly article

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Europe PubMed Central

PubMed publication ID

24 August 2017

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Europe PubMed Central

The role of ficolins in the lectin pathway of innate immunity (English)

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Europe PubMed Central

PubMed publication ID

24 August 2017

innate immune response

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21315829

24 November 2024

author name string

Yuichi Endo

1

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Europe PubMed Central

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24 August 2017

Misao Matsushita

2

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24 August 2017

Teizo Fujita

3

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24 August 2017

language of work or name

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National Center for Biotechnology Information

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=21315829

24 November 2024

publication date

18 February 2011

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24 August 2017

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https://api.elsevier.com/content/article/PII:S1357272511000434?httpAccept=text/xml

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10.1016/J.BIOCEL.2011.02.003

https://api.crossref.org/works/10.1016/J.BIOCEL.2011.02.003

24 November 2024

https://api.elsevier.com/content/article/PII:S1357272511000434?httpAccept=text/plain

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10.1016/J.BIOCEL.2011.02.003

https://api.crossref.org/works/10.1016/J.BIOCEL.2011.02.003

24 November 2024

International Journal of Biochemistry & Cell Biology

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Europe PubMed Central

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24 August 2017

43

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Europe PubMed Central

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24 August 2017

5

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Europe PubMed Central

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24 August 2017

705-712

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Europe PubMed Central

PubMed publication ID

24 August 2017

Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile

1

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Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci

2

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10.1016/J.BIOCEL.2011.02.003

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Expression and secretion of ficolin beta by porcine neutrophils

3

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Extremes of L-ficolin concentration in children with recurrent infections are associated with single nucleotide polymorphisms in the FCN2 gene

4

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L-ficolin (ficolin-2) insufficiency is associated with combined allergic and infectious respiratory disease in children

5

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Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2

6

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MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway

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MAp44, a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation

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

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Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins

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Mannose-binding lectin deficiency and respiratory tract infection

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Cloning and characterization of the human lectin P35 gene and its related gene

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Origin of mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 involved in the lectin complement pathway traced back to the invertebrate, amphioxus

14

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Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins

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10.1016/J.BIOCEL.2011.02.003

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Carbohydrate-binding specificities of mouse ficolin A, a splicing variant of ficolin A and ficolin B and their complex formation with MASP-2 and sMAP

16

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10.1016/J.BIOCEL.2011.02.003

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Structure and function of ficolins

17

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Role of ficolin in innate immunity and its molecular basis

18

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Interactions of ficolin and mannose-binding lectin with fibrinogen/fibrin augment the lectin complement pathway

20

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Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2

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Molecular cloning and characterization of mouse ficolin-A.

23

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Evolution of the lectin-complement pathway and its role in innate immunity

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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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Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch

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Carbohydrate recognition and complement activation by rat ficolin-B.

28

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

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The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin

30

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Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot

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The biological functions of MBL-associated serine proteases (MASPs)

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EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth factor-beta 1-binding proteins

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The innate pattern recognition molecule Ficolin-1 is secreted by monocytes/macrophages and is circulating in human plasma

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Polymorphisms in the FCN2 gene determine serum variation and function of Ficolin-2.

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Molecular organization of human Ficolin-2.

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Small mannose-binding lectin-associated protein plays a regulatory role in the lectin complement pathway.

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

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Ancient origin of the complement lectin pathway revealed by molecular cloning of mannan binding protein-associated serine protease from a urochordate, the Japanese ascidian, Halocynthia roretzi

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Molecular cloning and characterization of novel ficolins from Xenopus laevis

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Cloning and characterization of novel ficolins from the solitary ascidian, Halocynthia roretzi

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No strong relationship between mannan binding lectin or plasma ficolins and chemotherapy-related infections

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

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Expression of H-ficolin/Hakata antigen, mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 by human glioma cell line T98G.

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

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Human M-ficolin is a secretory protein that activates the lectin complement pathway

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Ficolin A and ficolin B are expressed in distinct ontogenic patterns and cell types in the mouse.

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Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9

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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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Human mannose-binding lectin and L-ficolin function as specific pattern recognition proteins in the lectin activation pathway of complement

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The lectin pathway

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Immunodeficiency associated with FCN3 mutation and ficolin-3 deficiency

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Mannose-binding lectin engagement with late apoptotic and necrotic cells

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Two oligomeric forms of plasma ficolin have differential lectin activity.

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The disulfide bonding pattern in ficolin multimers

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Local inflammation induces complement crosstalk which amplifies the antimicrobial response

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10.1016/J.BIOCEL.2011.02.003

1 reference

Europe PubMed Central

PubMed publication ID

24 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 August 2017

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