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Interaction between the labile binding site of human C4 and methylamine

Human complement component C4 was irreversibly inactivated by low concentrations of methylamine at slightly alkaline pH. The inactivated C4 molecules lost the ability to bind to EAC1 cells but retained th capacity to participate in the formation of classical pathway C3 convertase in the fluid phase. 14C-methylamine was incorporated into the alpha-chain at a ratio of 1 mol methylamine per mol C4.

3-Substituted 1-Naphthamidomethyl-C-galactosyls Interact with Two Unique Sub-Sites for High-Affinity and High-Selectivity Inhibition of Galectin-3

The galectins are a family of galactose-binding proteins playing key roles in inflammatory processes and cancer. However, they are structurally very closely related, and discovery of highly selective inhibitors is challenging. In this work, we report the design of novel inhibitors binding to a subsite unique to galectin-3, which confers both high selectivity and affinity towards galectin-3. Olefin

Synthesis and SAR Studies of Antibacterial Peptidyl Derivatives Based upon the Binding Site of Human Cystatin C

BACKGROUND: Antibacterial peptidyl derivative - Cystapep 1, was previously found to be active both against antibiotic-resistant staphylococci and streptococci as well as antibiotic-susceptible strains of these species. Therefore, it is a promising lead compound to search for new antimicrobial peptidomimetics.OBJECTIVES: We focused on identifying structural elements that are responsible for the bio

Site of action of antinociceptive acupuncture like nerve stimulation in the spinal rat as visualized by the 14C-2-deoxyglucose method

Aim: It has been claimed that supraspinal structures are necessary forthe depression of nocifensive behaviour elicited by acupuncture or acupuncturelike (AL) stimulation. However, nocifensive reflexes in the spinal catwere inhibited for long periods by a mechanism releasing opieids on AL conditioning stimulation of groups II-III muscle afferents (Sj~lund and Eriksson, Neurosci.Lett. S3:264:1979).