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Polyamines: mysterious modulators of cellular functions.
Polyamines were found to modulate protein synthesis at several different levels including stimulation of special kinds of protein synthesis, stimulation of the assembly of 30 S ribosomal subunits and stimulation of Ile-tRNA formation.
Modulation of cellular function by polyamines.
Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver.
Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins.
- Y. Endo, K. Tsurugi, T. Yutsudo, Y. Takeda, T. Ogasawara, K. Igarashi
- Biology, ChemistryEuropean journal of biochemistry
Results indicate that both VT2 and Shiga toxin inactivate 60S ribosomal subunits by cleaving the N-glycosidic bond at A-4324 in 28S ribOSomal RNA.
Channel blockers acting at N-methyl-D-aspartate receptors: differential effects of mutations in the vestibule and ion channel pore.
The effects of mutations in and around the membrane-spanning and pore-forming regions of NMDA receptor subunits were studied with three blockers, MK-801, memantine, and TB-3-4, using recombinant NMDA receptors expressed in Xenopus laevis oocytes.
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
It is demonstrated that immunodepletion of proteasomes from cell extracts causes almost complete loss of ATP-and antizyme-dependent degradation of ODC, suggesting that the 26S proteasome, widely viewed as specific for ubiquitin-conjugated proteins, is the main enzyme responsible for ODC degradation.
Excess of de novo deleterious mutations in genes associated with glutamatergic systems in nonsyndromic intellectual disability.
Physiological role of the chaA gene in sodium and calcium circulations at a high pH in Escherichia coli
The present study showed that the mutation of RS1 was compensated for by a cloned chaA gene, and it was suggested that ChaA plays a role in calcium ion circulation at alkaline pH.
Characteristics of cellular polyamine transport in prokaryotes and eukaryotes.
Protein kinase C zeta subspecies from rat brain: its structure, expression, and properties.
- Y. Ono, T. Fujii, K. Ogita, U. Kikkawa, K. Igarashi, Y. Nishizuka
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 May 1989
The structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from, other subspecies of protein kinase C, and perhaps belongs to another entity of the enzyme family.