Creutzfeldt-Jakob disease causes: Difference between revisions
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{{CMG}} {{AE}} {{MMJ}} | {{CMG}} {{AE}} {{MMJ}} | ||
==Overview== | ==Overview== | ||
Creutzfeldt-Jakob disease (CJD) is caused by the presence of a [[prion]] [[protein]], an abnormal isoform of a [[cellular]] [[glycoprotein]]. [[Prion]]s are transmissible particles that are devoid of [[nucleic acid]] and seem to be composed exclusively of a modified protein ( | Creutzfeldt-Jakob disease (CJD) is caused by the presence of a [[prion]] [[protein]], an abnormal isoform of a [[cellular]] [[glycoprotein]]. [[Prion]]s are transmissible particles that are devoid of [[nucleic acid]] and seem to be composed exclusively of a modified protein (PrPSc). The normal, [[cellular]] PrP ([[PrPC]]) is converted into [[PrPSc]] through a posttranslational process during which it acquires a high beta-sheet content. | ||
==Causes== | ==Causes== |
Revision as of 00:45, 2 November 2018
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1] Associate Editor(s)-in-Chief: Mohamadmostafa Jahansouz M.D.[2]
Overview
Creutzfeldt-Jakob disease (CJD) is caused by the presence of a prion protein, an abnormal isoform of a cellular glycoprotein. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular PrP (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta-sheet content.
Causes
- Creutzfeldt-Jakob disease (CJD) is caused by the presence of a prion protein, an abnormal isoform of a cellular glycoprotein.[1]
- Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrPSc). The normal, cellular PrP (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high beta-sheet content.[2]