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The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
Southern blot analysis indicates that a single gene in the haploid genome encodes both protein forms, and the inferred amino-acid sequence reveals the presence of a signal peptide, a long tandem repeat that matches the actin-binding domains of gelsolin, a tetrapeptide present in actin and extended regions of identical sequence with rabbit macrophages.
Purification and partial sequence of human osteoclast-activating factor: identity with interleukin 1 beta.
It is concluded that interleukin 1 beta is the major protein with OAF activity produced by lectin-stimulated peripheral blood mononuclear cells and that the m.w., isoelectric point, amino-terminal sequence, and specific activity in the thymocyte proliferation assay are the same for homogeneous OAF and interleucin 1beta.
A single receptor binds both insulin-like growth factor II and mannose-6-phosphate.
Results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.
Isolation and properties of two actin-binding domains in gelsolin.
Presentation of a structurally diverse and commercially available drug data set for correlation and benchmarking studies.
It is anticipated that this data set can serve as a benchmark set for validation of new experimental techniques or in silico models and can also be used as a diverse starting data set for the development of new computational models.
Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin.
Regulation of macrophage Fc receptor expression and phagocytosis by histidine-rich glycoprotein.
Results indicate that HRG is capable of modulating Fc gamma R expression in a biphasic fashion, which directly affects the overall efficiency of phagocytosis, and suggest thatHRG regulates macrophage function via a novel pathway different from that of heparin or IFN-gamma.
Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses.
The primary structure of the J chain from a human Waldenströms IgM protein has been determined using a combination of automated and conventional Edman degradative procedures. Eighty-five percent of…
Regulation of complement functional efficiency by histidine-rich glycoprotein.
In functional tests, HRG inhibited C8 hemolytic activity, probably by preventing C8 binding to EAC1-7 cells, and was further shown to inhibit factor D-mediated cleavage of factor B when bound by cobra venom factor.