08-31-2021-2207 -
FOR: Allergy and Provirus Endogenous Vir Hay Fever etc..
USA DOM: Vaccina Poxiviridae Smith Petersen Molluscum Contagium 1900s USA NAC America.
Endogenous Provirus; Activation Endogenous Virus; Retrograde genetic expression ?
Allergy, hyperimmune/immune response
deltaproteo bacteria, dust mite, shellfish allergy, aspergillus.
infectious cancer, fibrosis.
immune system
immune system dysfunction
immunosuppression - drug methroxetrate
autoimmune disorder-disease
hyperimmunity
immunodeficiency, immunosuppression
compensatory immunity
immunodeficiency, immunosuppression
immunodeficiency
immunosuppression - biological course
allergy, proteobacteria.
Infectious cancer or cancerous spore or etc.
Fibromatosis or Fibroma or Fibrosis or etc.
pyrogenous necrosis endogenous virus endogenous gene activation expression ; endogenous toxin ; endogenous cytokine/pyo/pyr/sepsis/fever/etc. ; endogenous, etc..
A syncytium or symplasm (/sɪnˈsɪʃiəm/; plural syncytia; from Greek: σύν syn "together" and κύτος kytos "box, i.e. cell") is a multinucleate cell which can result from multiple cell fusions of uninuclear cells (i.e., cells with a single nucleus), in contrast to a coenocyte, which can result from multiple nuclear divisions without accompanying cytokinesis.[1] The muscle cell that makes up animal skeletal muscle is a classic example of a syncytium cell. The term may also refer to cells interconnected by specialized membranes with gap junctions, as seen in the heart muscle cells and certain smooth muscle cells, which are synchronized electrically in an action potential.
The field of embryogenesis uses the word syncytium to refer to the coenocytic blastoderm embryos of invertebrates, such as Drosophila melanogaster.[2]
https://en.wikipedia.org/wiki/Syncytium
Chromosome 7 is one of the 23 pairs of chromosomes in humans, who normally have two copies of this chromosome. Chromosome 7 spans about 159 million[5] base pairs (the building material of DNA) and represents between 5 and 5.5 percent of the total DNA in cells.
https://en.wikipedia.org/wiki/Chromosome_7
Exaptation and the related term co-option describe a shift in the function of a trait during evolution. For example, a trait can evolve because it served one particular function, but subsequently it may come to serve another. Exaptations are common in both anatomy and behaviour. Bird feathers are a classic example: initially they may have evolved for temperature regulation, but later were adapted for flight. Note here that when feathers were initially used to aid in flight they were doing so exaptively; however, since they have since been shaped by natural selection to improve flight, in their current state they are now best regarded as adaptations for flight. So it is with many structures that initially took on a function as exaptations, once molded for that new function they become adapted for that function. Interest in exaptation relates to both the process and products of evolution: the process that creates complex traits and the products (functions, anatomical structures, biochemicals, etc.) that may be imperfectly developed.[1][2] Exaptation was proposed by Stephen Jay Gould and Elisabeth Vrba, as a replacement for 'pre-adaptation', which they considered to be a teleologically loaded term.[3]
https://en.wikipedia.org/wiki/Exaptation
The molecular clock is a figurative term for a technique that uses the mutation rate of biomolecules to deduce the time in prehistory when two or more life forms diverged. The biomolecular data used for such calculations are usually nucleotide sequences for DNA, RNA, or amino acid sequences for proteins. The benchmarks for determining the mutation rate are often fossil or archaeological dates. The molecular clock was first tested in 1962 on the hemoglobin protein variants of various animals, and is commonly used in molecular evolution to estimate times of speciation or radiation. It is sometimes called a gene clock or an evolutionary clock.
https://en.wikipedia.org/wiki/Molecular_clock
Endogenous retroviruses (ERVs) are endogenous viral elements in the genome that closely resemble and can be derived from retroviruses. They are abundant in the genomes of jawed vertebrates, and they comprise up to 5–8% of the human genome (lower estimates of ~1%).[1][2] ERVs are a vertically inherited proviral sequence and a subclass of a type of gene called a transposon, which can normally be packaged and moved within the genome to serve a vital role in gene expression and in regulation.[3][4] ERVs however lack most transposon function, are typically not infectious and are often defective genomic remnants of the retroviral replication cycle.[5][6] They are distinguished as germline provirus retroelementsdue to their integration and reverse-transcription into the nuclear genome of the host cell. Researchers have suggested that retroviruses evolved from a type of transposon called a retrotransposon, a Class I element;[7] these genes can mutate and instead of moving to another location in the genome they can become exogenous or pathogenic. This means that not all ERVs may have originated as an insertion by a retrovirus but that some may have been the source for the genetic information in the retroviruses they resemble.[8] When integration of viral DNA occurs in the germ-line, it can give rise to an ERV, which can later become fixed in the gene pool of the host population.[1][9]
https://en.wikipedia.org/wiki/Endogenous_retrovirus
RecombinantAntigenProteinPoxviridaeSmallpox VaccineSmallpoxHuman Immunodeficiency VirusVaccinia Virus
Vaccinia
Vaccinia induced actin polymerization is dependent on Src and Abl family kinase mediated phosphorylation of the IEV protein A36 (Frischknecht et al., 1999;
From: Virus Research, 2015
https://www.sciencedirect.com/topics/medicine-and-dentistry/vaccinia
The typical size of simulants (1–5 µm) enables it to enter buildings with closed windows and doors and penetrate deep into the lungs. This bears a significant health risk, even if the biological agent is normally not pathogenic.
Bacillus globigii (historically named Bacillus subtilis in the context of bio-agent simulants) (BG, BS, or U)
Serratia marcescens (SM or P)
Aspergillus fumigatus mutant C-2 (AF)
https://en.wikipedia.org/wiki/Biological_agent
Phosphatidylethanolamine (PE) is a class of phospholipids found in biological membranes.[1] They are synthesized by the addition of cytidine diphosphate-ethanolamine to diglycerides, releasing cytidine monophosphate. S-Adenosyl methionine can subsequently methylate the amine of phosphatidylethanolamines to yield phosphatidylcholines. It can mainly be found in the inner (cytoplasmic) leaflet of the lipid bilayer.[2]
Phosphatidylethanolamines are found in all living cells, composing 25% of all phospholipids. In human physiology, they are found particularly in nervous tissue such as the white matter of brain, nerves, neural tissue, and in spinal cord, where they make up 45% of all phospholipids.[3]
Phosphatidylethanolamines play a role in membrane fusion and in disassembly of the contractile ring during cytokinesis in cell division.[4] Additionally, it is thought that phosphatidylethanolamine regulates membrane curvature. Phosphatidylethanolamine is an important precursor, substrate, or donor in several biological pathways.[3]
As a polar head group, phosphatidylethanolamine creates a more viscous lipid membrane compared to phosphatidylcholine. For example, the melting temperature of di-oleoyl-phosphatidylethanolamine is -16 °C while the melting temperature of di-oleoyl-phosphatidylcholine is -20 °C. If the lipids had two palmitoyl chains, phosphatidylethanolamine would melt at 63 °C while phosphatidylcholine would melt already at 41 °C.[5]Lower melting temperatures correspond, in a simplistic view, to more fluid membranes.
https://en.wikipedia.org/wiki/Phosphatidylethanolamine
https://nikiyaantonbettey.blogspot.com/2021/08/08-29-2021-214-vacuolar-type-atpase-v.html
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