Disease relevance of PSMB4

• Gibberelic acid (GA) was used alone or in combination with cytostatics (Vincristine, Cyclophosphamide, HN3), surgical treatment or radiotherapy, in treatment of 65 patients with lung cancer [1].
• The cell lines, and the total number of expressed genes that were cloned from each were: HN3 (oral cancer), 263 genes; HN4 (oral cancer), 550 genes; HN5 (primary keratinocytes), 237 genes; HN6 (immortalized keratinocytes), 408 genes [2].

High impact information on PSMB4

• Using electron microscopy, the binding sites of a monoclonal antibody with specificity for subunit HsN3 have been located in the two juxtaposed inner rings of the human proteasome [3].
• Similar kinetics were not observed for alpha-277His MoFe-protein-catalyzed reduction of either HCN or HN3 with nonsaturating CO levels, indicating that these substrates are unlikely to share common binding sites with C2H2 [4].
• The 5'-azidonucleosides 3 and 4 were obtained by treating thymidine and 2'-deoxyuridine with TPP/DEAD/HN3 [5].
• Tax also enhanced binding of I kappa B alpha to the proteasome subunit HsN3, resulting in a Tax-enhanced, constitutive degradation of wild-type and mutated forms of I kappa B alpha in the absence of phosphorylation and ubiquitination [6].
• Both PSMB2 and PSMB4 mapped to a region of chromosome 1 that is proposed to be paralogous to other regions of the human genome where beta proteasome genes map: chromosome 6 containing the major histocompatibility complex (MHC) and chromosome 9 [7].

Biological context of PSMB4

• Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues [8].
• Here we report the nucleotide sequences of three human proteasomal subunits, HsN3, HsC7-I and HsC10-II, coding for proteins with 264, 201 and 205 amino acid residues with calculated molecular weights of 29,192, 22,836 and 22,931, respectively [8].
• Computationally, molecular structures, vibrational frequencies and adsorption energies of possible adsorbates including HN3 and its derivatives, N3, N2, NH, and H, have been predicted by first-principles calculations based on the density functional theory (DFT) and the pseudopotential method [9].

Anatomical context of PSMB4

• Reactions of the trifunctional nitrogen mustard tris(2-chloroethyl)-amine (HN3) with human erythrocyte membranes in vitro [10].
• Conversely, HN3 had no effect on L5178Y cell membrane proteins [11].

Associations of PSMB4 with chemical compounds

• Protonated molecules, obtained by CI(NH3) of azidofuranosyl derivatives, lose HN3 giving abundant furanosyl (S+) ions [12].
• Following arsenite treatment or irradiation, a significant increase compared with that of the control was observed for glutathione (GSH) transferase omega 1 and proteasome subunit beta type 4 precursor [13].
• Rat dosing experiments confirmed that EDEA, MDEA, and TEA could be detected in urine for at least 48 h after exposure to HN1, HN2, and HN3, respectively [14].
• It was also observed at ultrasonic intensities exceeding 3.5 W cm-2 that the decomposition of HN3 led to the accumulation of NH4+ in solution [15].
• The kinetics of N2H5+ decomposition and initial HN3 formation increase in a linear manner with the HNO3 concentration (from 1 to 6 M) and with the ultrasonic intensity (from 0.5 to 3.1 W cm-2) [15].

Physical interactions of PSMB4

• Smad1 forms a complex with a proteasome beta subunit HsN3 and the ornithine decarboxylase antizyme (Az) [16].

Analytical, diagnostic and therapeutic context of PSMB4

• Reactions of N3, the product of the reaction of HO with HN3, were studied in an environmental chamber using an FTIR spectrometer for end-product analysis [17].

References