Prion - Revision history

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Tom: Created page with "==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 w..."

2024-10-02T19:02:43Z

Created page with "==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 w..."

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==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==
A major system failure was caused when CrowdStrike issued an update to their
==References==

[[Category: Attack]]

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 * 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. 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. It was first isolated in "Mad Cow" disease.
 *In computer systems major system failure was caused when CrowdStrike issued an update to their
 ==References==
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 ==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. 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 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. 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. It was first isolated in "Mad Cow" disease.
 *In computer systems major system failure was caused when CrowdStrike issued an update to their

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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.
 ==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 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. 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