Difference between revisions of "Prion"
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Originally an infection vector caused by a misfolded protein that can cause that same misfolding wherever it goes. Can also be used in computer system were a data element is changed in such a way as to cause a failure of the program the depends on a correct value for that data element. | Originally an infection vector caused by a misfolded protein that can cause that same misfolding wherever it goes. Can also be used in computer system were a data element is changed in such a way as to cause a failure of the program the depends on a correct value for that data element. | ||
==Context== | ==Context== | ||
| − | + | * In medicine [[Prion]]s are a type of intrinsically disordered protein that continuously changes conformation unless bound to a specific partner, such as another protein. Once a prion binds to another in the same conformation, it stabilizes and can form a fibril, leading to abnormal protein aggregates called amyloids. These amyloids accumulate in infected tissue, causing damage and cell death.[13] The structural stability of prions makes them resistant to denaturation by chemical or physical agents, complicating disposal and containment, and raising concerns about iatrogenic spread through medical instruments. | |
| + | *In computer systems major system failure was caused when CrowdStrike issued an update to their | ||
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==References== | ==References== | ||
[[Category: Attack]] | [[Category: Attack]] | ||
Revision as of 11:04, 2 October 2024
Full Title or Meme
Originally an infection vector caused by a misfolded protein that can cause that same misfolding wherever it goes. Can also be used in computer system were a data element is changed in such a way as to cause a failure of the program the depends on a correct value for that data element.
Context
- In medicine Prions are a type of intrinsically disordered protein that continuously changes conformation unless bound to a specific partner, such as another protein. Once a prion binds to another in the same conformation, it stabilizes and can form a fibril, leading to abnormal protein aggregates called amyloids. These amyloids accumulate in infected tissue, causing damage and cell death.[13] The structural stability of prions makes them resistant to denaturation by chemical or physical agents, complicating disposal and containment, and raising concerns about iatrogenic spread through medical instruments.
- In computer systems major system failure was caused when CrowdStrike issued an update to their
