Results 71 to 80 of about 1,484 (101)
Complement in neurological disorders and emerging complement-targeted therapeutics. [PDF]
Nat Rev Neurol, 2020 Dalakas MC, Alexopoulos H, Spaeth PJ.
europepmc +1 more source
Essential Role of Complement in Pregnancy: From Implantation to Parturition and Beyond. [PDF]
Front Immunol, 2020 Girardi G +3 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
The Journal of Biochemistry, 1985
Limited proteolysis of C3b by C3b inactivator (factor I) consists of a two-step reaction; rapid cleavage of C3b to yield a nicked C3b derivative, iC3b, and followed by slow cleavage of iC3b to yield two antigenically distinct fragments, C3c and C3d,g.
Tsukasa Seya, Shigeharu Nagasawa
openaire +3 more sources
Limited proteolysis of C3b by C3b inactivator (factor I) consists of a two-step reaction; rapid cleavage of C3b to yield a nicked C3b derivative, iC3b, and followed by slow cleavage of iC3b to yield two antigenically distinct fragments, C3c and C3d,g.
Tsukasa Seya, Shigeharu Nagasawa
openaire +3 more sources
Molecular Immunology, 1998
Abstract Vaccinia virus complement control protein (VCP) is a virulence determinant of vaccinia virus that helps protect the virus from the complement attack of the host. To characterize the interaction of VCP with C3 and C4 and understand the mechanism by which VCP inactivates complement, we have expressed VCP in a yeast expression ...
Stuart N. Isaacs +3 more
openaire +3 more sources
Abstract Vaccinia virus complement control protein (VCP) is a virulence determinant of vaccinia virus that helps protect the virus from the complement attack of the host. To characterize the interaction of VCP with C3 and C4 and understand the mechanism by which VCP inactivates complement, we have expressed VCP in a yeast expression ...
Stuart N. Isaacs +3 more
openaire +3 more sources
Journal of Immunological Methods, 1984
Factor H, purified from mouse EDTA-plasma using a 4-step procedure, consists of a single polypeptide chain of Mr 150,000 on SDS-PAGE. Mouse H (Hmo) was required for the cleavage of fluid-phase mouse C3b by mouse I (Imo). The final product of degradation of fluid-phase mouse C3b was iC3b, consisting of fragments of the alpha'-chain (alpha'-70, alpha'-43)
Taroh Kinoshita, Victor Nussenzweig
openaire +3 more sources
Factor H, purified from mouse EDTA-plasma using a 4-step procedure, consists of a single polypeptide chain of Mr 150,000 on SDS-PAGE. Mouse H (Hmo) was required for the cleavage of fluid-phase mouse C3b by mouse I (Imo). The final product of degradation of fluid-phase mouse C3b was iC3b, consisting of fragments of the alpha'-chain (alpha'-70, alpha'-43)
Taroh Kinoshita, Victor Nussenzweig
openaire +3 more sources
The Journal of Immunology, 1978
Abstract Radioiodinated β1H was demonstrated to bind to sheep EAC4b, EAC4,2,3b and EC3b, but not to E, EA, EAC4,2 or to C3bINA and β1H treated EC3b. This binding was dependent upon the C3b concentration on the surface of the cells and could be inhibited by unlabeled β1H, free C3b or high concentrations of Factor B.
M. K. Pangburn +2 more
openaire +1 more source
Abstract Radioiodinated β1H was demonstrated to bind to sheep EAC4b, EAC4,2,3b and EC3b, but not to E, EA, EAC4,2 or to C3bINA and β1H treated EC3b. This binding was dependent upon the C3b concentration on the surface of the cells and could be inhibited by unlabeled β1H, free C3b or high concentrations of Factor B.
M. K. Pangburn +2 more
openaire +1 more source
The Journal of Biochemistry, 1992
Proteolytic inactivation of C4b is a crucial step for regulation of the classical complement pathway. A plasma protease factor I and membrane cofactors, C3b/C4b receptor (CR1) and membrane cofactor protein (MCP), participate in the regulation of cell-bound C4b although the physiological potency of these cofactors remains unknown.
Misako Matsumoto +4 more
openaire +3 more sources
Proteolytic inactivation of C4b is a crucial step for regulation of the classical complement pathway. A plasma protease factor I and membrane cofactors, C3b/C4b receptor (CR1) and membrane cofactor protein (MCP), participate in the regulation of cell-bound C4b although the physiological potency of these cofactors remains unknown.
Misako Matsumoto +4 more
openaire +3 more sources
The Journal of Immunology, 1982
Abstract We have shown previously that C4 treated with amines or chaotropes, although uncleaved, exhibits properties that are similar to C4b. Studies by other groups suggest that this C4b-like form of C4 is characterized by the lack of an internal thiolester bond that is present in native C4.
I, von Zabern +3 more
openaire +2 more sources
Abstract We have shown previously that C4 treated with amines or chaotropes, although uncleaved, exhibits properties that are similar to C4b. Studies by other groups suggest that this C4b-like form of C4 is characterized by the lack of an internal thiolester bond that is present in native C4.
I, von Zabern +3 more
openaire +2 more sources