Sentence examples for conserved card from inspiring English sources

Finally, HMMerThread identified a remotely conserved CARD domain in the Death Receptor 6 (DR6, aka TNFRSF21), the presence of which was also shown by structural analysis (pdb-code 2dbh, Inoue M, Koshiba S, Kigawa T, Yokoyama S, unpublished).

We have added this observation to the manuscript (in the subsection "Role of a conserved CarD Trp residue in CarD function").

We confirm that our structures correspond to functional activation complexes, and extend our understanding of the role of a conserved CarD Trp residue that serves as a minor groove wedge, preventing collapse of the transcription bubble to stabilize the transcription initiation complex.

c) We have added a sentence explaining the use of Mtb AP3 for Figure 3B (in the subsection "Role of a conserved CarD Trp residue in CarD function"): "We used Mtb AP3 for this analysis since Tth EσA was much more active on this promoter than on Tth 23S, allowing us to analyze the much weaker activity of the mutant promoters".

The CarD contacts with the DNA occur mostly through the backbone phosphates, except for highly conserved CarD-W86, which wedges between the splayed DNA strands at the upstream edge of the transcription bubble and may form a hydrogen bond with T−12 t) O2 presented in the highly distorted minor groove.

Based on these findings, we examined whether these residues, which are necessary for homophilic CARD-CARD interactions, are conserved among NLR CARDs and the CARDs of their effector proteins, respectively, by means of multiple sequence alignment (Figure 5A and 5B).

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It's kind of a hassle, but it's not for arbitrary reasons and rather is how the battery life in the card is conserved — it's not activated until flicked.

Notably, the first and last residues of the acidic as well as the basic patch are highly conserved among the analyzed CARD domains, suggesting a pattern of interaction similar to the one described for Apaf-1/C9 or NOD1/RICK.

To test if MAVS polymerization is required for its binding to TRAF proteins, we mutated several conserved charged residues within MAVS CARD, including E26A, R64A, and R65A.

W86 is conserved among greater than 95% of CarD proteins and was shown to be important for CarD function as an activator (Srivastava et al., 2013).