Results 161 to 170 of about 3,647 (206)

Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. [PDF]

J Biol Chem
Williams HM, Moeller JB, Burns I, Schlosser A, Sorensen GL, Greenhough TJ, Holmskov U, Shrive AK.   +7 more
europepmc   +1 more source

Evaluation of Mannose-Binding Lectin is a Useful Approach to Predict the Risk of Infectious Complications Following Autologous Hematopoietic Stem Cell Transplantation [PDF]

, 2017
Hársfalvi, Jolán, Illés, Árpád, Kiss, Attila, Papp, Mária, Pál, Ildikó, Radnay, Zita, Rejtő, László, Udvardy, Miklós   +7 more
core  

The ability of relapsing fever <i>Borrelia</i> species to survive in chicken serum <i>in vitro</i> and its correlation to interaction with serum components reactive to a polyclonal anti-complement regulator factor H antibody. [PDF]

Curr Res Parasitol Vector Borne Dis
Jakobsson T, Bergström S, Normark J.
europepmc   +1 more source

The Role of Complement Activation in Diabetic Nephropathy: Current Insights and Future Directions. [PDF]

J Clin Med
Kotsalas N, Fouza A, Daoudaki M.
europepmc   +1 more source

The inner fire: the shifting paradigm of complement system in aging. [PDF]

Front Immunol
Triggianese P, Della-Morte D.
europepmc   +1 more source

Endothelial Glycocalyx: The Missing Link Between Angiogenic Imbalance in Preeclampsia and Systemic Inflammation in HELLP Syndrome. [PDF]

Compr Physiol
Atallah A, Sarda MN, McCarey C, Massardier J, Huissoud C.   +4 more
europepmc   +1 more source

Structure of the Lipopolysaccharide from <i>Paenalcaligenes hominis</i>: A Chemical Perspective on Immune Recognition. [PDF]

JACS Au
Nieto-Fabregat F, Mercogliano M, Cangiano A, Vitiello G, Andretta E, Clifton LA, Vanacore A, Buono L, Campanero-Rhodes MA, Solís D, Di Carluccio C, Pecoraro G, Molinaro A, Smaldone G, Kim JK, Kim DH, Paduano L, Di Lorenzo F, Silipo A.   +18 more
europepmc   +1 more source

Emerging role of ficolins in autoimmune diseases

Pharmacological Research, 2021
Ficolins are pattern-recognition molecules (PRMs) that could form complexes with mannose-binding lectin-associated serine proteases (MASPs) to trigger complement activation via the lectin pathway, thereby mediating a series of immune responses including opsonization, phagocytosis and cytokine production.
Peng Wang, Qian Wu, Zongwen Shuai
exaly   +3 more sources

Ficolins and infectious diseases

Virologica Sinica, 2014
Ficolins are serum complement lectins, with a structure similar to mannose-binding lectin (MBL) and lung surfactant protein (SP)-A and SP-D. Ficolins activate the lectin complement system and play important roles in host innate immunity. Ficolins are members of the collectin family of proteins, which act as pattern recognition receptors (PRRs).
Yu-Shan Ren, Xiao-Lian Zhang
exaly   +4 more sources

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Ficolins in complement activation

Molecular Immunology, 2013
Ficolins are a group of multimeric lectins made up of single subunits each of which is composed of a collagen-like domain and a fibrinogen-like domain. Most of the ficolins identified to date bind to acetylated compounds such as N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc).
Misao Matsushita
exaly   +3 more sources