Three genes encoding putative transcriptional regulators (Table 3) and three genes associated with transport (Table S2) were upregulated, while transcripts for the major surface protein [tde0405] and numerous subunits of the outer membrane-associated protease, Dentilisin [tde0761 and tde0762], were downregulated.
Secondly, numerous subunits of the proteasome were identified as enriched.
These included numerous subunits of the vacuolar H+−ATPase (such as VMA1, VMA2, VMA3, VMA4, VMA6, VMA7, VMA11, VMA13, VMA16, and STV1) and 2 subunits of the RAVE complex (RAV1 and RAV2) which promotes assembly of the V-ATPase holoenzyme.
Accordingly, the main input of the numerous protein subunits of human RNase P should be in other complex and versatile tasks of this ribonucleoprotein complex, e. g. transcription [11], [16], as will be further corroborated in this study.
Numerous subunit fractions from Brucella have been examined as recombinant proteins vaccines in mouse model, and some of these have shown protective efficacy [ 21, 39].
Numerous transcripts encoding specific subunits of collagens, laminins, integrins, and various other extracellular matrix structural components were differentially up- or down-modulated (P < 0.01).
They are composed of numerous identical subunits forming a symmetric, porous, lattice-like layer that completely covers the cell surface.
The revolution of molecular biology brought about the rapid development of anatomy aimed at the localization of the numerous receptor subunits, ion channels, transporters and other proteins at the regional, cellular and subcellular levels that are being cloned every day (e.g. see Nusser, 2000).
Numerous ligands interact with the intracellular domain of the GluN2A subunits of NMDAR [ 32].
We further identified numerous genes from the rod phototransduction pathway, including all three subunits of the G protein (GNAT1, GNB1, GNGT1), phosphodiesterase subunits (PDE6a, PDE6b, PDE6g), the sodium/calcium exchanger (NCKX1) and G protein kinase (GRK1).
By doing so, individual subunits of a protein complex can be preserved instead of specifying numerous species names, each of which would reflect a different combination of subunit states and bindings (recall the scaffold protein example in the background).
