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Bleomycin hydrolase (BLMH) is a neutral cysteine aminopeptidase that has been ascribed roles in many physiological and pathological processes, yet its primary biological function remains enigmatic.
Its exact function remains enigmatic.
However, despite intense efforts of many groups, H2A.Z function remains enigmatic.
Similarly, its function remains enigmatic and its role during spermiogenesis is open to speculation.
Due to the absence of experimental data for most of the chlamydial lipoproteins, their function remains enigmatic.
It has been known for more than four decades [ 6] that during mammalian ovulation, the ovaries exhibit a transitory (i.e. a few hours) rise in the enzyme ornithine decarboxylase (ODC) and its product putrescine and yet its physiological function remains enigmatic.
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However, the relationship between primary sequences and three-dimensional structures and functions remains enigmatic.
That's necessary not only because the brain's functioning remains enigmatic, but because it is difficult to study neurons in living animals, limiting scientific progress.
To date, the precise function of the middle part remains enigmatic, yet this part contains most of the conserved structural elements of class-A GPCRs, including a major hydrogen-bond network (MHN) formed by the hydrophilic "2.50-cavity" and hydrophobic "middle-cavity" (Fig. 1) (Zhang et al., 2013; Katritch et al., 2013; Angel et al., 2009).
Taperin function, however, remains enigmatic.
Nse3 is part of the Smc5-6 complex, which is structurally similar to cohesin, but whose precise function still remains enigmatic (Bustard et al. 2012).
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