نتایج جستجو برای: ficolin

تعداد نتایج: 299  

Journal: :Journal of immunology 2005
Nicholas J Lynch Saeed-ul-Hassan Khan Cordula M Stover Sara M Sandrini Denise Marston Julia S Presanis Wilhelm J Schwaeble

The lectin pathway of complement is activated by multimolecular complexes that recognize and bind to microbial polysaccharides. These complexes comprise a multimeric carbohydrate recognition subunit (either mannan-binding lectin (MBL) or a ficolin), three MBL-associated serine proteases (MASP-1, -2, and -3), and MAp19 (a truncated product of the MASP-2 gene). In this study we report the cloning...

2014
Marcia Holsbach Beltrame Sandra Jeremias Catarino Isabela Goeldner Angelica Beate Winter Boldt Iara José de Messias-Reason

The innate immune system is the first line of host defense against infection and is comprised of humoral and cellular mechanisms that recognize potential pathogens within minutes or hours of entry. The effector components of innate immunity include epithelial barriers, phagocytes, and natural killer cells, as well as cytokines and the complement system. Complement plays an important role in the...

Journal: :Immunobiology 2010
Russell Wallis Daniel A Mitchell Ralf Schmid Wilhelm J Schwaeble Anthony H Keeble

Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since its isolation almost 50 years ago. Nevertheless, knowledge is still incomplete, especially with regard to the interactions between its subcomponents C1q, C1r and C1s that trigger activation upon binding ...

Journal: :The Journal of biological chemistry 2001
A Kenjo M Takahashi M Matsushita Y Endo M Nakata T Mizuochi T Fujita

Ficolins are animal lectins with collagen-like and fibrinogen-like domains. They are involved in the first line of host defense against pathogens. Human ficolin/P35 as well as mannose-binding lectin (MBL) activates the complement lectin pathway in association with MBL-associated serine proteases. To elucidate the origin and evolution of ficolins, we separated approximately 40 kDa (p40) and appr...

Journal: :Journal of innate immunity 2010
Misao Matsushita

Ficolins are a group of oligomeric lectins with subunits consisting of both collagen-like and fibrinogen-like domains. The majority of ficolins identified in vertebrates and invertebrates to date recognize N-acetylglucosamine (GlcNAc). X-ray crystallographic analysis of human ficolins has shown that the fibrinogen-like domain binds to the N-acetylated moiety. Ficolins in serum are associated wi...

Journal: :PLoS Pathogens 2009
Jing Zhang Jingyun Koh Jinhua Lu Steffen Thiel Benjamin S. H. Leong Sunil Sethi Cynthia Y. X. He Bow Ho Jeak L. Ding

By eliciting inflammatory responses, the human immunosurveillance system notably combats invading pathogens, during which acute phase proteins (CRP and cytokines) are elevated markedly. However, the Pseudomonas aeruginosa is a persistent opportunistic pathogen prevalent at the site of local inflammation, and its acquisition of multiple antibiotic-resistance factors poses grave challenges to pat...

Journal: :The Journal of biological chemistry 2004
Tomoo Ohashi Harold P Erickson

Ficolin is a plasma lectin, consisting of a short N-terminal multimerization domain, a middle collagen domain, and a C-terminal fibrinogen-like domain. The collagen domains assemble the subunits into trimers, and the N-terminal domain assembles four trimers into 12-mers. Two cysteine residues in the N-terminal domain are thought to mediate multimerization by disulfide bonding. We have generated...

Journal: :Nippon Saikingaku Zasshi 2008

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