Sandbox Reserved 1103: Difference between revisions

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Dyskeratosis congenita is a disorder which is characterised by bone marrow dysfunction, abnormality of the skin, mucocutaneous triad of oral leucoplakia, nail dystrophy, as well as a predisposition to cancer.  
Dyskeratosis congenita is a disorder which is characterised by bone marrow dysfunction, abnormality of the skin, mucocutaneous triad of oral leucoplakia, nail dystrophy, as well as a predisposition to cancer.  
TINF2 is one of the nine identified genes that when mutated are related to the Dyskeratosis congenita, the others being [https://en.wikipedia.org/wiki/Dyskerin DKC1],[https://en.wikipedia.org/wiki/Telomerase_RNA_component TERC],[https://en.wikipedia.org/wiki/Telomerase_reverse_transcriptase TERT], NOP10, NHP2, C16orf57, TCAB1 and [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN]. TIN2 mutation are imply in several different mechanims.  
TINF2 is one of the nine identified genes that when mutated are related to the Dyskeratosis congenita, the others being [https://en.wikipedia.org/wiki/Dyskerin DKC1],[https://en.wikipedia.org/wiki/Telomerase_RNA_component TERC],[https://en.wikipedia.org/wiki/Telomerase_reverse_transcriptase TERT], NOP10, NHP2, C16orf57, TCAB1 and [https://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease PARN]. TIN2 mutations are imply in several different mechanims.  


The majority of identified TIN2 dyskeratosis congenita mutations cluster is a highly conserved 30-amino-acid region near the ends of its TRF1 binding domain <ref>PMID: 15316005 </ref>, from position 270 to 300, located eight amino acids C-terminal to the FxLxP motif. A disrutpion of this domain causes a loss of TRF1 binding to TIN2, resulting in a telomeric instability<ref>PMID: 18252230 </ref>.  
The majority of identified TIN2 dyskeratosis congenita mutations cluster is a highly conserved 30-amino-acid region near the ends of its TRF1 binding domain <ref>PMID: 15316005 </ref>, from position 270 to 300, located eight amino acids C-terminal to the FxLxP motif. A disrutpion of this domain causes a loss of TRF1 binding to TIN2, resulting in a telomeric instability<ref>PMID: 18252230 </ref>.  
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