117 research outputs found
Faithful chaperones
This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major structural viral protein, hexon, and (5) HYPK, the huntingtin-interacting protein. These various-sized proteins (102–1,190 amino acids long) are all involved in the folding of oligomeric polypeptides but are otherwise functionally unique, as they each assist only one particular client. This raises a question regarding the biosynthetic cost of the high-level production of such chaperones. As the clients of faithful chaperones are all abundant proteins that are essential cellular or viral components, it is conceivable that this necessary metabolic expenditure withstood evolutionary pressure to minimize biosynthetic costs. Nevertheless, the complexity of the folding pathways in which these chaperones are involved results in error-prone processes. Several human disorders associated with these chaperones are discussed
Studies on the Mechanism of Vaccinia Virus Cytopathic Effects: Effect of Inhibitors of RNA and Protein Synthesis on Early Virus-induced Cell Damage
Characterization of small nontranslated polyadenylylated RNAs in vaccinia virus-infected cells.
Discriminatory inhibition of protein synthesis in cell-free systems by vaccinia virus transcripts.
Inhibition of Protein Synthesis by Vaccinia Virus. II. Studies on the Role of Virus-induced RNA Synthesis
Inductive requirements for the generation of virus specific t lymphocytes. Iii. Production of target cells lysable by poxvirus-specific and allospecific cytotoxic tt lymphocytes with membrane fragments bearing viral and h-2 antigens.
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