Disease relevance of ACTGP10

• The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties [1].
• Presence of actin or actin-like proteins has also been reported in prokaryotic organisms belonging to the cyanobacteria [2].

High impact information on ACTGP10

• Thus, the ParM protein of plasmid R1 forms F actin-like filaments that separate and move plasmid DNA from mid-cell to the cell poles [3].
• The bacterial actin-like cytoskeleton [4].
• DNA sequence data from four representative and highly divergent clones, PAc2, PAc3, PAc4 and PAc7, demonstrate that these actin-like sequences are related to functional actin genes [5].
• Ultrastructurally, the stress fibers were found to be composed of thin actin-like filaments (5-8 nm) and thick myosin-like filaments (10-15 nm X 300 nm) [6].
• Actin-like sequences are present on human X and Y chromosomes [7].

Biological context of ACTGP10

• Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles [8].
• The presence of both actin-like and myosin-like proteins would be consistent with a role in gliding and other cell motility processes of this parasite [9].
• Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites [10].

Anatomical context of ACTGP10

• The molecules on the surface of neutrophils, which have actin-like antigenic epitopes and are recognized by these anti-actin antibodies, remain to be characterized [11].
• An actin-like material was extracted from human spermatozoa [12].
• By using the QF-DE method, dystrophin was localized just underneath the plasma membrane, and closely linked to actin-like filaments (8-10 nm in diameter), most of which were decorated with myosin subfragment 1 [13].
• Actin-like proteins have been detected in the ependymocytes of the cerebral ventricles, but the distribution of F-actin along the ventricular system has not been studied [14].
• Smooth-muscle-type focal densities amid fine actin-like filaments in typical epithelioid cells often containing prominent rER have been observed, as well as a structure in the form of a densely granular cytoplasmic body [15].

Associations of ACTGP10 with chemical compounds

• ACTP contains a radioiodinated phenylazide moiety which, upon activation, can cross-link the derivatized cysteine to an adjacent polypeptide domain [16].
• A sensitive, accurate and precise spectrophotometric method is described for the determination of Acetaminophen (paracetamol, ACTP) in pure form and in pharmaceutical formulations [17].
• The principle of the method is the reduction, of Fe(III) to Fe(II) by the ACTP in the presence of o-Phenanthroline (o-Phen), when the orange-red coloured chelate complex [Fe(II)-(o-Phen)3]2+ the ferroin complex was formed, and its absorbance was measured at lambda = 510 nm [17].

Analytical, diagnostic and therapeutic context of ACTGP10

• Structural evidence for actin-like filaments in Toxoplasma gondii using high-resolution low-voltage field emission scanning electron microscopy [18].

References