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Heat shock proteins appear to serve a significant cardiovascular role.
Heat shock proteins also help the tolerance to both high and low temperatures.
It is required for increased translational efficiency during the heat shock response.
The hsp90 gene product is involved in the Drosophila heat shock response.
As a result, samples might experience heat shock until they are returned to their usual temperature by surface equipment.
This has been examined experimentally for the heat shock protein 86.
Therefore it is clear, that a formation of large aggregates takes place under heat shock.
This was what Fergus referred to as a 'heat shock' crack.
Spawning is usually induced by heat shock under laboratory conditions;.
This is effective because many spores are stimulated to grow by the heat shock.
Hsp17 is a cyanobacterial heat shock protein belonging to the Hsp20 family.
A heat shock afterwards then invokes the cell to repair itself.
This "heat shock" technology is supposed to kill bacteria and reduce redness.
For this reason, the term "heat shock protein" has historically been used to name these chaperones.
As temperatures rise, production of heat shock proteins increases.
Under heat shock conditions the hairpin structure melts and translation takes place.
A typical example is the heat shock factor of Drosophila melanogaster.
Many corals around the world are now at risk from heat shock, irrespective of local pollution or stresses.
In eukaryotic organisms chaperones are known as heat shock proteins.
Adults and juveniles are subject to moisture loss as well as heat shock.
In these experiments, he exposed Drosophila pupae to heat shock.
A number of heat shock proteins 40 (hsp40) have been predicted from the sequenced genome.
Heat shock protein 20 has been shown to have a critical role in sporozoite motility.
The protein encoded by this gene belongs to the Hsp90 family of heat shock proteins.