Disease relevance of PSMD1

• We have identified eight recombinant human single-chain variable region fragments (scFvs) against the S1 domain of spike (S) protein of the SARS-CoV from two nonimmune human antibody libraries [1].
• Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association [1].
• This interaction is isosteric with the adenosine N1-2'-OH interaction in the related mRNA from beet western yellows virus (BWYV); however, the ScYLV and BWYV mRNA structures differ in their detailed L2-S1 hydrogen bonding and L2 stacking interactions [2].
• Sulfhydryl-alkylating reagents are known to inactivate the NAD glycohydrolase and ADP-ribosyltransferase activities of the S1 subunit of pertussis toxin, a protein which contains two cysteines at positions 41 and 200 [3].
• Lupus autoantibodies to double-stranded DNA cross-react with ribosomal protein S1 [4].

Psychiatry related information on PSMD1

• Maximal GH peak coincided 9 times (50%) with SWS, 3 times (17%) with S2, 3 times with W, twice (11%) with S1, and once (6%) with rapid eye movement sleep [5].
• Specific labeling of this site was achieved by first attaching the desired chromophore to an "antipeptide" that by means of its charge complementarity specifically binds to this segment of S1 [Chaussepied & Morales (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7471] and then cross-linking the fluorescent peptide to the protein [6].
• No differences across NREM sleep stages were found for CAP cycle and phase B mean duration; on the contrary, phase A showed longer duration during SWS than in S1 and S2 [7].
• Also, epochs from sleep stage 1 (S1), REM and wakefulness preceding sleep were recorded [8].
• Sleep stage 1 (S1) was reduced and the slow wave sleep increased [9].

High impact information on PSMD1

• Their ability to bind S1 ribosomal protein suggests that poly(A) tracts may also play a role in mRNA translation [10].
• After demembranation with Triton X-100 and incubation with S-1, "arrowhead" formation was observed along the filaments of the stereocilia and their rootlets and also along filaments in the cuticular plate inside the receptor cell [11].
• A strategy employing a combination of peptide nucleic acid (PNA) probes, an optically amplifying conjugated polymer (CP), and S1 nuclease enzyme is capable of detecting SNPs in a simple, rapid, and sensitive manner [12].
• This technique allows definition of S1 orientation with respect to the myofilament axis [13].
• The x-ray crystal structure of the uPA B-chain complexed with this inhibitor revealed a surprising binding mode consisting of the expected insertion of the phenylguanidine moiety into the S1 pocket, but with the adamantyl residue protruding toward the hydrophobic S1' enzyme subsite, thus exposing the ureido group to hydrogen-bonding interactions [14].

Chemical compound and disease context of PSMD1

• Alkylation of cysteine 41, but not cysteine 200, decreases the ADP-ribosyltransferase activity of the S1 subunit of pertussis toxin [3].
• Factor C-derived Sushi peptides (S1 and S3) have been shown to bind lipopolysaccharide (LPS) and inhibit the growth of Gram-negative bacteria but do not affect mammalian cells [15].
• The combination of ATP, CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propane-sulfonate), and DTT (dithiothreitol) is known to promote the expression of the NAD glycohydrolase activity of pertussis toxin, which resides in the toxin's S1 subunit [16].
• The bone resorption marker urinary FDPD under basal conditions was significantly lower during S3 (dexamethasone) than during either hydrocortisone schedules, S1 or S2 [17].
• The S1 segment of the kidney proximal tubule (PT) is a major target of chronic Cd(2+) toxicity [18].

Biological context of PSMD1

• CONCLUSION: PSMC2 and PSMD1 genes may play an important role in the apoptosis and partial differentiation of NB(4) cells [19].
• For this study we determined the nucleotide sequences of the T2W S1, S2, S3 and S4 genome segments to allow molecular comparison with other reoviruses [20].
• For S1- to S7-proteins, five different N-terminal amino acid sequences sharing the YFQFTQQY sequence were determined [21].
• We conclude that the acto-S-1 complex is not dissociated by ATP during each cycle of ATP hydrolysis; in fact, the rate of the initial Pi burst appears to be even faster when S-1.ATP is bound to actin than when it is dissociated [22].
• This makes the -deltaG degrees of binding of F-actin to S-1 similar to the -deltaG degrees of binding of ATP to S-1, and the possible physiological relevance of the similarity to muscle contraction is discussed [23].

Anatomical context of PSMD1

• The S1 genes encode protein sigma 1, the protein against which serotype-specific neutralizing antibodies are directed; it is also the reovirus hemagglutinin and cell-attachment protein and is a major determinant of host range/tissue specificity and of the nature of the interaction of reovirus with cells of the immune system [24].
• The transcription start site was mapped by primer extension and S1 nuclease protection analyses of RNA from human brain, skeletal muscle, and heart [25].
• The actin-activated ATPase activities of subfragment 1 (S1) produced from gizzard myosin by papain or Staphylococcus aureus protease are different [26].
• Human cardiac ventricular myosin subfragment-1 (S-1) was prepared by chymotryptic digestion of myosin purified from adult and fetal hearts [27].
• S. typhi containing the S1 subunit gene of pertussis toxin cloned under the control of these promoters, selectively expressed the S1 subunit following infection of different phagocytic and non-phagocytic cell lines of human or murine origin [28].

Associations of PSMD1 with chemical compounds

• This region composed of 520 amino-acid residues which span the connecting segment between subfragment-1 (S-1) and S-2 to the NH2-terminal portion of light meromyosin (LMM) [29].
• Rotational correlation time (tau2) were determined for a spin label analog of iodoacetamide bound to the subfragment-1 (S-1) region of myosin under a variety of conditions likely to shed light on the molecular mechanism of muscle contraction [30].
• Recent experimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments in the presence and in the absence of Ca(2+) are analyzed by using a linear Ising model [31].
• In the present study, we tested this prediction by using either unmodified S-1 or S-1 chemically modified with N,N'-p-phenylenedimaleimide (pPDM X S-1) so that functionally it acts like S-1.ATP, although it does not hydrolyze ATP [32].
• These results suggest that the region near cysteine 41 contributes to features of the S1 subunit important for ADP-ribosyltransferase activity [3].

Physical interactions of PSMD1

• S10b bound to S6' and bound much more weakly to S1 and p50, another component of the dynactin complex [33].

Other interactions of PSMD1

• The HMM was not produced when digested at 10 degrees C. A further digestion of the 135 kD HMM isolated in the absence of calcium ion generated uniquely short subfragment-2 (S-2) with a size of 40 kDa (40 kDa S-2) together with subfragment-1 (S-1) [34].

Analytical, diagnostic and therapeutic context of PSMD1

• We have constructed mutant derivatives of the S1 protein from Papaver rhoeas by using site-directed mutagenesis and have tested their biological activity [35].
• Electron microscopy of acto-S1 frozen 10 ms after mixing revealed disordered binding [36].
• The cross-linked actin X S-1 preparation, which was composed of [14C]iodoacetamide-modified S-1 and [3H]N-ethylmaleimide-modified actin, was passed through several cycles of actin depolymerization and centrifugation [37].
• Sequence analysis indicated that the 3'-proximal ORF present on the NBV S1 genome segment also encodes a final sigmaC homolog, as evidenced by the presence of an extended N-terminal heptad repeat characteristic of the coiled-coil region common to the cell attachment proteins of reoviruses [38].
• Nevertheless, freeze-etched acto-S1 does not display the "arrowheads" that are seen after negative staining [39].

References