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Proteasome‐mediated cleavage of the Y‐box‐binding protein 1 is linked to DNA‐damage stress response
It is reported that YB‐1 undergoes a specific proteolytic cleavage by the 20S proteasome, which splits off the C‐terminal 105‐amino‐acid‐long YB•1 fragment containing a cytoplasmic retention signal, and found that genotoxic stress triggers a proteasomesome‐mediated cleavage of YB-1 in vivo and leads to accumulation of the truncated protein in nuclei of stressed cells.
A protein residing at the subunit interface of the bacterial ribosome.
The N-terminal sequence of the protein Y was determined and its gene was identified as yfia, an ORF located upstream the phe operon of E. coli and the protein was shown to stabilize ribosomes against dissociation.
The Domain Organization and Properties of Individual Domains of DNA Topoisomerase V, a Type 1B Topoisomerase with DNA Repair Activities*
Topo V has at least two active sites capable of processing AP DNA, and it is demonstrated that Topo78 and Topo34 possess AP lyase activities that are important in base excision DNA repair.
Hemoglobin as a source of endogenous bioactive peptides: the concept of tissue-specific peptide pool.
The general conclusion is reached that hemoglobin fragments must have a profound physiological function and the concept of a "tissue-specific peptide pool" is formulated, describing a novel system of peptidergic regulation complementary to the conventional hormonal and neuromodulatory systems.
Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Primary structure of the enzyme.
Compared with the other known primary structures of mammalian serine proteinases, the duodenase identity to granzymes from human and mice, human cathepsin G and mast cell chymases from rat, gives an overall sequence identity of 47-55% with the mentioned enzymes.