Results 11 to 20 of about 710,495 (352)

Membrane cofactor protein (MCP; CD46) expression in transgenic mice [PDF]

open access: bronzeClinical and Experimental Immunology, 2001
SUMMARYHuman membrane cofactor protein (MCP; CD46) is a widely distributed complement regulator. In the mouse, expression of MCP is largely restricted to the testis while a related, widely expressed protein (Crry) appears to perform MCP's (CD46) regulatory activity.
Claudia Kemper   +6 more
openalex   +5 more sources

Human oligodendroglial cells express low levels of C1 inhibitor and membrane cofactor protein mRNAs [PDF]

open access: goldJournal of Neuroinflammation, 2004
Background Oligodendrocytes, neurons, astrocytes, microglia, and endothelial cells are capable of synthesizing complement inhibitor proteins. Oligodendrocytes are vulnerable to complement attack, which is particularly observed in multiple sclerosis. This
McGeer Patrick L   +2 more
doaj   +2 more sources

Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46). [PDF]

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1995
The human complement regulatory protein membrane cofactor protein (CD46) is the cellular receptor for measles virus (MV), whereas decay accelerating factor (DAF; CD55), a structurally similar complement regulatory protein, does not bind MV.
Marianne Manchester   +7 more
openalex   +2 more sources

Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus [PDF]

open access: yesJournal of Virology, 1993
A monoclonal antibody (MCI20.6) which inhibited measles virus (MV) binding to host cells was previously used to characterize a 57- to 67-kDa cell surface glycoprotein as a potential MV receptor. In the present work, this glycoprotein (gp57/67) was immunopurified, and N-terminal amino acid sequencing identified it as human membrane cofactor protein ...
Naniche, D   +6 more
openaire   +6 more sources

Membrane Cofactor Protein (CD46) Is a Basolateral Protein That Is Not Endocytosed [PDF]

open access: hybridJournal of Biological Chemistry, 1997
Membrane cofactor protein (MCP) is a widely distributed complement regulatory protein that is expressed on the basolateral surface of polarized epithelial cells. The basolateral targeting of the BC1 isoform of MCP was analyzed by generating deletion mutants and point mutants within the cytoplasmic tail of 16 amino acids. A sequence of four amino acids,
Andrea Maisner   +5 more
openalex   +5 more sources

Membrane Cofactor Protein Is a Receptor for Adenoviruses Associated with Epidemic Keratoconjunctivitis [PDF]

open access: yesJournal of Virology, 2004
ABSTRACTSubgroup D adenovirus (Ad) types 8, 19, and 37 (Ad8, -19, and -37, respectively) are causative agents of epidemic keratoconjunctivitis and genital tract infections. Previous studies showed that Ad37 binds to a 50-kDa membrane glycoprotein expressed on human ocular (conjunctival) cells.
Lars Pache   +6 more
openaire   +4 more sources

A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins [PDF]

open access: bronzeCell, 1998
We report the identification of the proteins encoded by the mttABC operon (formerly yigTUW), which mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine" leader motif.
Joël H. Weiner   +7 more
openalex   +4 more sources

Cooperation of decay-accelerating factor and membrane cofactor protein in regulating survival of human cervical cancer cells

open access: yesBMC Cancer, 2009
Background Decay-accelerating factor (DAF) and membrane cofactor protein (MCP) are the key molecules involved in cell protection against autologus complement, which restricts the action of complement at critical stages of the cascade reaction.
Gong Hui   +7 more
doaj   +2 more sources

Membrane targeting of a folded and cofactor-containing protein [PDF]

open access: bronzeEuropean Journal of Biochemistry, 2003
Targeting of proteins to and translocation across the membranes is a fundamental biological process in all organisms. In bacteria, the twin arginine translocation (Tat) system can transport folded proteins. Here, we demonstrate in vivo that the high potential iron‐sulfur protein (HiPIP) from Allochromatium vinosum is translocated into the periplasmic ...
Thomas Brüser   +3 more
openalex   +4 more sources

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