Unrelenting exhaustion may be a sign of a condition or an effect of the drugs or therapies used to treat it, such as: Acute liver failure. Anemia. Anxiety disorders.
<span>Similarities and Differences
There are many similarities and differences between the three domains. Bacteria and Archaea differ in how they gain energy. Bacteria gain energy either by being phototrophs, lithotrophs or organotrophs. One similarity between domain Archaea and domain Bacteria is that they both contain only prokaryotes while domain Eukarya only contains eukaryotes. Domain Archaea is the only domain that is sensitive to antibiotics. Another similarity between domain Bacteria and domain Eukarya is that Methionine is the first amino acid seen during protein synthesis while in domain Archaea, the first amino acid is Formylmethionine. The last major similarity between domain Archaea and domain Bacteria is that they do not contain any organelles while domain Eukarya does. A difference between all three domains is what their cell walls contain. A cell wall in domain Archaea has peptidoglycan. The organisms that have a cell wall in domain Eukarya, will have a cell wall made up of polysaccharides.</span>
Sick could mean disgusting, horrible, brutal, awesome, amazing, etc. However it's commonly used in everyday talk to say "that's cool"There are four main types of disease: infectious diseases, deficiency diseases, hereditary diseases (including both genetic diseases and non-genetic hereditary diseases), and physiological diseases. Diseases can also be classified in other ways, such as communicable versus non-communicable diseases.
<span>Lafora disease is the most severe teenage-onset progressive epilepsy, a unique form of glycogenosis with perikaryal accumulation of an abnormal form of glycogen, and a neurodegenerative disorder exhibiting an unusual generalized organellar disintegration. The disease is caused by mutations of the EPM2A gene, which encodes two isoforms of the laforin protein tyrosine phosphatase, having alternate carboxyl termini, one localized in the cytoplasm (endoplasmic reticulum) and the other in the nucleus. To date, all documented disease mutations, including the knockout mouse model deletion, have been in the segment of the protein common to both isoforms. It is therefore not known whether dysfunction of the cytoplasmic, nuclear, or both isoforms leads to the disease. In the present work, we identify six novel mutations, one of which, c.950insT (Q319fs), is the first mutation specific to the cytoplasmic laforin isoform, implicating this isoform in disease pathogenesis. To confirm this mutation's deleterious effect on laforin, we studied the resultant protein's subcellular localization and function and show a drastic reduction in its phosphatase activity, despite maintenance of its location at the endoplasmic reticulum.
I got my information from </span>https://www.ncbi.nlm.nih.gov/pubmed/14722920
This answer to this question is c
