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RING1- and YY1-binding protein (RYBP) belongs to the polycomb group (PcG). RYBP interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, which leads to stabilization of p53 and an increase in p53 activity. RYBP causes cell-cycle arrest and is involved in the p53 response to DNA damage. RYBP interacts with RING1, YY1, Caspase 10, E2F3, E2F2, Mdm2, Abl gene and CBX2. RYBP inhibits ubiquitination and subsequent degradation of TP53, and thus has a role in regulating transcription of TP53 target genes. RYBP may also be involved in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. RYBP may bind to DNA, and promote apoptosis.

Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

High Mobility Group AT-Hook 2 (HMGA2) is a member of the non-histone chromosomal high mobility group (HMG) family. HMG proteins perform as architectural factors and are necessary components of the enhancesome. Thisprotein contains structural DNA-binding domains and may function as a transcriptional regulating factor. In addition, identification ofthe deletion, amplification, and rearrangement of this gene that are associated with myxoid liposarcoma proposes arole in adipogenesis and mesenchymal differentiation. A gene knock out study of the mouse counterpartdemonstrated that this gene is implicated in diet-induced obesit.Among the Diseases associated with HMGA2 are diffuse lipomatosis, and 12q14 microdeletion syndrome.

Helicobacter pylori, a Gram-negative, microaerophilic bacterium that populates in the stomach, predominantly at the antrum. Helicobacter pylori causes a chronic inflammation of the mucoid lining of stomach and is highly related to the growth of duodenal and gastric ulcers and stomach cancer. Over 50% of the world's population harbor H. pylori in their upper gastrointestinal tract, infection is more prevalent in developing countries. Thus far, no ideal target H. pylori antigen has been developed for the diagnostic purpose. 23 kDa H. pylori outer membrane protein was identified with a good sensitivity and coverage in the diagnosis of H. pylori infection.

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

Tumor necrosis factor receptor superfamily member 16 (NGFR) BELONGS TO the tumor necrosis factor receptor superfamily with an extensive pattern of expression in tissues such as the brain, liver, lung, and muscle. NGFR has a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, possibly by regulating RAB31 activity, and thus contributes to the regulation of insulin-dependent glucose uptake. NGFRs are low affinity receptors which can bind to NGF, BDNF, NT-3, and NT-4. NGFR mediates cell survival as well as cell death of neural cells.

Neuregulin-4 (NRG4) is a part of the neuregulin family that owns 1 EGF-like domain and is a low affinity ligand for the ERBB4 tyrosine kinase receptor. NRG4 links ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors.

GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.

Secreted Frizzled-Related Protein 5, also known as SFRP5, belongs to the SFRP family which includes a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs perform like soluble modulators of Wnt signaling. SFRP5 & SFRP1 are implicated in determining the polarity of photoreceptor cells in the retina. SFRP5 is highly expressed in the retinal pigment epithelium, as well as moderately expressed in the pancreas.

NHP2 belongs to the H/ACA snoRNPs (small nucleolar ribonucleoproteins) gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been organized into 2 families: C/D and H/ACA. NHP2 (NOLA2) forms a small ribonucleoprotein particle with GAR1 (NOLA1), Nop10 for the isomerization of uridine to pseudouridine. NHP2 is involved in a variety of aspects of rRNA processing and modification. NHP2 localizes to the dense fibrillar component of the nucleolus and in nuclear Cajal bodies.

GPD1 enzyme catalyzes the reduction of dihydroxyacetone phosphate to sn-glycerol 3-phosphate. (sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH) previous names for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase and glycerolphosphate dehydrogenase. However, GPD1 differs from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a neurotrophic factor for spinal and sensory neurons.
Defects in the GPI gene cause the nonspherocytic hemolytic anemia and a severe enzyme deficiency can be linked to hydrops fetalis, immediate neonatal death and neurological impairment.

Regulator of G-protein signaling 21 (RGS21) belongs to the RGS family and regulatory molecules which act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. The RGS21 protein inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thus driving them into their inactive GDP-bound form.

Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.

GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.

Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.

SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

Sex-hormone-binding globulin (SHBG) is a beta-globulin which specifically binds steroid hormones; it is involved in the transport of sex steroids in plasma. The main site of SHBG synthesis is assumed to be the hepatocytes. The production of SHBG is regulated by androgen/estrogen balance, thyroid hormones, insulin and dietary factors, among others. The concentration of SHBG is a key factor regulating their distribution between protein-bound and free states. SHBG concentration determination is primarily significant in the evaluation of mild disorders of androgen metabolism and it allows detection of women with hirsutism who are likely to react to estrogen therapy. Testosterone/SHBG-ratios correlate well with both measured and calculated values for free testosterone thus aid to distinguish between subjects with excessive androgen activity and normal individuals. SHBG gene polymorphisms are linked with polycystic ovary syndrome and type 2 diabetes mellitus.

Liraglutide is a long-acting GLP1 analogue sharing 97% a.a. homology to human GLP1. Liraglutide differs from GLP1 by the substitution of arginine for lysine at position 34. While GLP1 is degraded swiftly by DPP4 resulting in short life of insulin, Liraglutide contains a fatty acid that binds to albumin and prolongs the half-life of the structure. liraglutide causes insulin to secret in the presence of increasing glucose levels. Due toits receptor site, liraglutide inhibits glucagon secretion and delays gastric emptying.

HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.