Answer:
Microtubules
Explanation:
These filament-like structures are a major component of the cytoskeleton of the cell and help is maintain asymmetrical cell shape. They are composed of tubulin molecules arranged to form a 'hollow straw' attached to the cell membrane end to end . The contraction and lengthening of these microtubules are controlled by the addition of removal these of tubulin molecules to vary its length.
Answer:
nice.....................
Explanation:
yes
Answer:
a. retained in the pyruvate
Explanation:
Glycolysis is a cytoplasmic pathway that converts glucose into two pyruvate, releasing a modest amount of energy captured in two substrate-level phosphorylations and one oxidation reaction.
Following are the important enzymes in it :
- Hexokinase
- Phosphofructokinase
- Pyruvate kinase
Aerobic glycolysis yields 2ATP/glucose plus 2NADH/glucose but most of the energy is retained in pyruvate which is then converted into Acetyl-CoA and enters the kreb's cycle.
A volcanic winter is a reduction in global temperatures caused by volcanic ash and droplets of sulfuric acid and water obscuring the Sun and raising Earth's albedo (increasing the reflection of solar radiation) after a large, particularly explosive volcanic eruption.
<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
