Polymorphisms of OCT1 and metformin effects in Iraqi women with polycystic ovary syndrome in Karbala city.

Objectives: The current study aimed to correlate OCT1 (organic cation transporter 1) polymorphisms with metformin response variability in Iraqi women with PCOS (polycystic ovarian syndrome) and determine the impact of OCT1 polymorphism. PCOS, an endocrine metabolic disorder, can seriously impact female health including infertility. Although its cause is unclear, it is usually known to be associated with hormonal imbalances.

Immunoinformatics design of a structural proteins driven multi-epitope candidate vaccine against different SARS-CoV-2 variants based on fynomer.

The ideal vaccines for combating diseases that may emerge in the future require more than simply inactivating a few pathogenic strains. This study aims to provide a peptide-based multi-epitope vaccine effective against various severe acute respiratory syndrome coronavirus 2 strains. To design the vaccine, a library of peptides from the spike, nucleocapsid, membrane, and envelope structural proteins of various strains was prepared.

Effects of structural polymorphism on the risk of polycystic ovary syndrome and reproductive hormones in Iraqi women who take metformin.

Objective: To identify the effects of metformin and kisspeptin structural polymorphism on the risk of polycystic ovary syndrome (PCOS) in Iraqi women.

Methods: Samples were collected at the family planning center of Al-Hassan Teaching Hospital (infertility clinic), Iraq. Hormonal and hematological parameters were measured.

The production of the first functional antibody mimetic in higher plants: the chloroplast makes the DARPin G3 for HER2 imaging in oncology.

Background: Designed mimetic molecules are attractive tools in biopharmaceuticals and synthetic biology. They require mass and functional production for the assessment of upcoming challenges in the near future. The DARPin family is considered a mimetic pharmaceutical peptide group with high affinity binding to specific targets.

Pectin methylesterase activity of plant DUF538 protein superfamily.

DUF538 (domain of unknown function 538) proteins are known as a group of putative hypothetical proteins in a wide range of plant species. They have been identified from some plants challenged with various environmental stresses. However, a little is known about their functional properties.

Purification of a ribosome-inactivating protein with antioxidation and root developer potencies from .

Considering as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on . By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS-PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of . at vegetative growth stage.

DUF538 protein superfamily is predicted to be chlorophyll hydrolyzing enzymes in plants.

The possible hydrolytic activity towards chlorophyll molecules was predicted for DUF538 protein superfamily in plants. It was examined by using computational as well as experimental tools including in vitro chlorophyll degradation, antioxidant compounds production and in vivo real-time gene expression tests. Comparison of the computational data with the experimental results indicated that DUF538 proteins might be chlorophyll hydrolyzing enzyme (most probably carboxyesterase) which degrade chlorophyll molecules (66 % per 12 hrs) to produce new compounds (1.

Molecular analysis of maize cystatin expression as fusion product in Escherichia coli.

Nowadays, plant cysteine proteinase inhibitors "namely phytocystatins" have attracted researchers towards the identification of their molecular structures and novel physiological functions. Their important roles in plant developmental processes and different stress responses have been well known. In spite of advances in the understanding of phytocystatins, we lack enough data concerning their heterologous expression especially in the forms of fusion products that are most important whether for biochemical, pharmacological or clinical studies.

DUF538 protein super family is predicted to be the potential homologue of bactericidal/permeability-increasing protein in plant system.

DUF538 protein super family includes a number of plant proteins that their role is not yet clear. These proteins have been frequently reported to be expressed in plants under various stressful stimuli such as bacteria and elicitors. In order to further understand about this protein family we utilized bioinformatics tools to analyze its structure in details.

Functional fusion expression of sunflower multicystatin in E. coli and its comparison with a single domain cystatin.

Identification of the molecular structure and novel biophysiological functions of plant cystatins or phytocystatins is of great interest in the field of molecular biology. The important requirements for these are the efficient production, purification and correctly folded forms of these proteins. We report here the cloning, easy expression and characterization of a sunflower multicystatin (SMC) as a functional fusion protein in E.

Heterologous expression of stress-responsive DUF538 domain containing protein and its morpho-biochemical consequences.

As a usual response, plants induce/activate various proteins which are thought to be involved in defense mechanisms against the biotic and abiotic stresses they may be confronted with. The novel DUF538 domain containing proteins with unknown functions have been found to be induced/activated in response to different environmental stress stimuli in plants. In order to perform biochemical studies with these new plant stress-responsive proteins, a cDNA containing DUF538 domain was amplified from Celosia cristata full-length leaf expression library using a specific primer set.

Carborundum-dependent entrance of EcoRI restriction enzyme into plant cells and specific cleavage of genomic DNA.

In a basic research to determine the morpho-molecular interactions of plant tissues with EcoRI DNA restriction enzyme, it was demonstrated that this protein is capable of entering the sunflower and maize leaf cells using a plant tissue-abrading material and cleaving the genomic DNA at specific sites. This was inferred from the analysis of morphological patterns of EcoRI-treated leaf areas as well as using some molecular tests, including the cleavage pattern analysis of genomic DNA isolated from treated locations followed by ligation of cleaved fragments into EcoRI site of a DNA cloning vector system. The overall results indicated that the specific restriction of genomic DNA may happen following the entrance of EcoRI protein most likely into the nucleus of plant cells.

Cystatins may confer viral resistance in plants by inhibition of a virus-induced cell death phenomenon in which cysteine proteinases are active: cloning and molecular characterization of a cDNA encoding cysteine-proteinase inhibitor (celostatin) from Celosia cristata (crested cock's comb).

Cystatins (cysteine proteinase inhibitors) have been recently used in plants as antiviral strategy against those viruses whose replication involves cysteine proteinase activity. We proposed an idea that cystatins may confer resistance by inhibition of a virus-induced cell-death phenomenon in which cysteine proteinases are active. To test this idea, a full-length cDNA library was constructed from the preflowering stage of Celosia cristata (crested cock's comb) leaves, and a cDNA clone with cystatin domain was isolated using an oligonucleotide probe designed on the basis of the conserved peptide of plant cystatins.

Modifications in the purification protocol of Celosia cristata antiviral proteins lead to protein that can be N-terminally sequenced.

Plants antiviral proteins are being used as anticancer agents and inhibit other viral diseases in humans. We modified the purification protocol of the two N-terminally blocked antiviral glycoproteins, CCP-25 and CCP-27, purified from the leaves of Celosia cristata. This not only gave rise to single pure samples with few steps of purification but also resulted in N-terminally free proteins.