Sentence examples for mutations causing human from inspiring English sources

Alternative Splicing (AS), which affects most of human genes and is altered in at least 15% of all point mutations causing human genetic disease [2], [3], is a potential critical mechanism for the regulation and fine-tuning of physiological immune responses [4], [5].

The HGMD (Stenson et al., 2009) documents known mutations causing human inherited disease, as well as disease-associated and/or functional polymorphisms reported in the literature.

To date, all mitochondrial ARSs bearing genetic mutations causing human diseases exhibit compromised aminoacylation activity, and effects on noncanonical functions unrelated to translation have not been demonstrated.

Interestingly, most mutations causing human genetic diseases in TRPV4-ARD are located away from the ATP-binding site, suggesting that additional regulatory interactions and mechanisms exist.

Studies of mutations causing human chronic granulomatous disease show that mutations in NCF1, CYBB, CYBA, or NCF2 lead to a complete lack of function of the NOX complex [ 65, 66].

To obtain insight into regulatory mechanisms of TRPV4, we focused on TRPV4-ARD, which can mediate channel regulation through binding of ligands to its concave surface and is the target of many mutations causing human diseases.

Taken together, we provide insight into the mechanisms by which KATNB1 mutations cause human cerebral cortical malformations, demonstrating its fundamental role during brain development.

The discovery that NDUFA4 mutations cause human COX deficiency indicates an important role of the NDUFA4 protein in COX function.

Resolution of this question is fundamental to full understanding of telomerase mechanism and how heterozygous TERT or telomerase RNA mutations cause human disease.

Both NDEL1 and NDE1 were identified via their interactions with lissencephaly 1 (LIS1), a gene in which mutations cause human lissencephaly (15– 15).

Hanna and colleagues now demonstrate that NDUFA4 mutations cause human COX deficiency, thus confirming NDUFA4 as a COX subunit that is essential for the enzyme's activity.