Molecular cloning and characterization of novel ficolins from Xenopus laevis. (Q48252038)

10 February 2018

title

Molecular cloning and characterization of novel ficolins from Xenopus laevis. (English)

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10 February 2018

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Yuji Kakinuma

1

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10 February 2018

Yuichi Endo

2

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10 February 2018

Minoru Takahashi

3

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Munehiro Nakata

4

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Misao Matsushita

5

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Seiichi Takenoshita

6

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10 February 2018

Teizo Fujita

7

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language of work or name

English

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publication date

5 April 2003

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10 February 2018

published in

Immunogenetics

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10 February 2018

volume

55

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issue

1

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page(s)

29-37

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10 February 2018

https://scigraph.springernature.com/pub.10.1007/s00251-003-0552-2

exact match

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cites work

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Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease

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Oligomeric structure and tissue distribution of ficolins from mouse, pig and human.

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The antihemorrhagic factor, erinacin, from the European hedgehog (Erinaceus europaeus), a metalloprotease inhibitor of large molecular size possessing ficolin/opsonin P35 lectin domains

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Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family

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Purification of transforming growth factor-beta 1 binding proteins from porcine uterus membranes.

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

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Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain

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A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway.

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

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A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement

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Molecular cloning and characterization of mouse ficolin-A.

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Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease

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12 December 2020

Biosynthesis of human ficolin, an Escherichia coli-binding protein, by monocytes: comparison with the synthesis of two macrophage-specific proteins, C1q and the mannose receptor

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Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein

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M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli

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Activation of the lectin complement pathway by H-ficolin (Hakata antigen)

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

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Mannose-binding lectin: the pluripotent molecule of the innate immune system

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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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Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

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Isolation and characterization of a thermolabile β-2 macroglycoprotein (‘thermolabile substance’ or ‘Hakata antigen’) detected by precipitating (auto) antibody in sera of patients with systemic lupus erythematosus

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates.

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12 December 2020

Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains.

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12 December 2020

10.1007/S00251-003-0552-2

Identifiers

DOI

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PubMed ID

12679857

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10 February 2018