Results 161 to 170 of about 5,737 (217)

The role of complement in long COVID pathogenesis. [PDF]

open access: yesJCI Insight
Bayarri-Olmos R, Bain W, Iwasaki A.
europepmc   +1 more source

Paramyosin inhibits complement C1.

The Journal of Immunology, 1992
Abstract We report here the results of studies showing that inhibition of C is a property of several invertebrate paramyosins. Paramyosins from Taenia solium, Schistosoma mansoni, and the mussel Mytilus edulis bind polymeric collagen and can be isolated from crude extracts of tissues by collagen affinity.
J P, Laclette   +7 more
openaire   +2 more sources

Complement C1-inhibitor expression in Alzheimer's disease

Acta Neuropathologica, 1998
In situ and in vitro studies suggest that activation of locally produced complement factors may act as a mediator between amyloid deposits and neurodegenerative changes seen in Alzheimer's disease (AD). C1-esterase inhibitor (C1-Inh), which regulates activation of C1 of the complement classical pathway, can be detected immunohistochemically in its ...
Veerhuis, R.   +5 more
openaire   +3 more sources

Molecular Basis of Human Complement C1s Deficiency

The Journal of Immunology, 1999
Abstract This is the first report on the molecular basis of human complement C1s deficiency. Two abnormalities in the C1s gene were identified in a Japanese family, including one patient, by using exon-specific PCR, single-strand conformation polymorphism analysis, and nucleotide sequencing.
Y, Endo   +5 more
openaire   +2 more sources

Clionasterol: A Potent Inhibitor of Complement Component C1

Planta Medica, 2003
Clionasterol (1a), clionasterol monoacetate (1b) and 5alpha,8alpha-epidioxy-24alpha-ethylcholest-6-en-3-ol (2), isolated from the marine sponge Xestospongia exigua, and beta-sitosterol (3) were tested for their influence on the classical (CP) and alternative (AP) pathways of activation of the human complement system in vitro.
Fátima, Cerqueira   +8 more
openaire   +2 more sources

Functional model of subcomponent C1 of human complement

Journal of Molecular Biology, 1986
The domain organization of the zymogen subunits of the first component of human complement C1s, C1r2 and the complex C1s-C1r2-C1s was studied by electron microscopy. In the absence of Ca2+, monomeric C1s was visualized as a dumb-bell-shaped molecule consisting of two globular domains (center-to-center distance 11 nm) connected by a rod.
V, Weiss, C, Fauser, J, Engel
openaire   +2 more sources

Inhibition of bFGF activity by complement C1s: covalent binding of C1s with bFGF

Cell Biochemistry and Function, 1998
The first complement component C1s formed large aggregates with bFGF when bFGF and C1s were incubated at 37 degrees C overnight. Under non-reducing conditions, a part of the aggregates did not penetrate into 5% polyacrylamide gel in the presence of SDS, and the rest penetrated into 5% gel but not into 12% gel.
H, Sakiyama   +3 more
openaire   +2 more sources

C1, MBL–MASPs and C1-inhibitor: novel approaches for targeting complement-mediated inflammation

Trends in Molecular Medicine, 2008
Complement activation is initiated by the pattern-recognition molecules complement component C1q, mannose-binding lectin (MBL) and ficolins (H-, L-, M-ficolin), which typically recognize antibody-antigen complexes or foreign polysaccharides. The associated proteases (C1r, C1s, MASP-1 and MASP-2) then activate the complement system.
László, Beinrohr   +3 more
openaire   +2 more sources

Biphenylsulfonyl-thiophene-carboxamidine inhibitors of the complement component C1s

Bioorganic & Medicinal Chemistry Letters, 2008
Complement activation has been implicated in disease states such as hereditary angioedema, ischemia-reperfusion injury, acute respiratory distress syndrome, and acute transplant rejection. Even though the complement cascade provides several protein targets for potential therapeutic intervention only two complement inhibitors have been approved so far ...
Jeremy M, Travins   +20 more
openaire   +2 more sources

Purification and characterization of recombinant hamster tissue complement C1s

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
Hamster complement C1s cDNA was inserted into expression plasmid BCMGSNeo, and transfected to SEA7 cells, A31 mouse fibroblasts transformed by polyoma virus. The transfectant secreted a large amount of recombinant C1s that was activated in the serum free culture medium and hydrolyzed acetyl-Gly-L-Lys-naphthyl ester (AGLNE).
T, Toyoguchi   +9 more
openaire   +2 more sources

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