This mutation leads to an extra-long tract of glutamines within the HTT that causes the huntingtin protein to aggregate [3].
In cell culture studies, this mutation leads to inefficient F3 secretion and higher intracellular steady state levels, likely due to F3 disulfide bonding and/or protein folding problems.
Although it is unclear how this mutation leads to TGMS, the following observations in other species suggest a logical pathway by which the RNZ m mutation could result in TGMS.
Many patients with ileal Crohn's disease, a chronic intestinal inflammation, carry mutations in the gene encoding NOD2 (CARD15), but the mechanistic details of how this mutation leads to disease are not fully understood.
Structural studies of Abl wild-type and T315I mutant have provided better understanding of how this mutation leads to resistance and have been used to support the drug design process for the development of inhibitors able to target the T315I substitution.
This mutation leads to the replacement of R1607 by a stop codon.
This mutation leads to a wider distribution of cell lengths but not to altered growth rates.
Over time, this mutation leads to the development of cataracts and DRM [12].
This mutation leads to an abnormal polyglutamine expansion in the N-terminal part of the huntingtin (Htt) protein.
This mutation leads to constitutive activation of BRAF by bypassing the need for activation by NRAS and ATP.
The model prediction that this mutation leads to a constriction of the channel pore accords with experimental data obtained by various techniques [17].
