Cytoplasmic casein kinase 2 and its substrate proteins in the brain in Alzheimer's disease]

The absence of casein kinase 2 on blots of temporal cortex extracts from Alzheimer's disease patients (ADP) was shown using antiserum to casein kinase 2. Casein kinase 2 activity towards endogenous substrates and casein is 2-5 times less in ADP brain in comparison to normal controls. The fractions of heparin-binding proteins, containing protein substrates for phosphorylation, were isolated from temporal cortex of ADP and normal controls. The total amount of heparin-binding proteins from ADP brains is less than from control brains, and the polypeptide composition of these fractions is much more poop.     

Increasing the effectiveness of antibiotic therapy by correcting immunologic disorders with vitamin A in patients with brucellosis

Experimental studies and clinical trials were performed on possible increase of antibiotic therapy efficacy in brucellosis patients by correction of the immunity disorders with vitamin A. It was experimentally shown that vitamin A increased cellular immunity and accelerated sanation of guinea pigs sensitized with Brucella abortus 19 BA. The clinical trials demonstrated that the use of vitamin A in a dose of 33,000 IU thrice a day for 10 to 12 days during the complex treatment of patients with acute (36 persons) and subacute (57 persons) brucellosis lowered the average period of manifestation of the disease clinical signs and formation of the antibodies, increased the skin allergic sensitivity, the lymphocyte blast cell transformation, the total number and subpopulations of the active T-cells, theophylline-resistant lymphocytes, phagocytic and metabolic activity of neutrophils, showed 1.5- and 2-fold increased in the frequency of the infection transformation into a chronic process in patients with acute or subacute brucellosis, respectively.     

Involvement of Boiling Stable Antioxidant Enzymes in Adaptation of Invasive Alien Plant Lantana to Abiotic Stress under Natural Conditions

Russian Journal of Plant Physiology - Lantana camara L. is noxious weed affecting ecosystem and biodiversity worldwide. However, the biochemical basis of invasiveness and adaptation to abiotic...     

Molecular Modeling of Disease Causing Mutations in Domain C1 of cMyBP-C

Cardiac myosin binding protein-C (cMyBP-C) is a multi-domain (C0–C10) protein that regulates heart muscle contraction through interaction with myosin, actin and other sarcomeric proteins. Several mutations of this protein cause familial hypertrophic cardiomyopathy (HCM). Domain C1 of cMyBP-C plays a central role in protein interactions with actin and myosin. Here, we studied structure-function relationship of three disease causing mutations, Arg177His, Ala216Thr and Glu258Lys of the domain C1 using computational biology techniques with its available X-ray crystal structure. The results suggest that each mutation could affect structural properties of the domain C1, and hence it’s structural integrity through modifying intra-molecular arrangements in a distinct mode. The mutations also change surface charge distributions, which could impact the binding of C1 with other sarcomeric proteins thereby affecting contractile function. These structural consequences of the C1 mutants could be valuable to understand the molecular mechanisms for the disease.