Sentence examples for binding domain shared by from inspiring English sources

NBS regions contain several conserved motifs and are homologous to the NB-ARC (nucleotide binding domain shared by Apaf-1, some R genes and Ced-4) domain of some eukaryotic cell death effectors such as Apaf-1 and Ced-4 [ 33].

The genes taken into account were those encoding for proteins containing any of the following domains or domain-combination: LRR (Leucine-rich repeat), WRKY, LRR-kinase, NB-ARC (Nucleotide Binding domain shared by Apaf-1 R gene products, and CED-4 -LRR, CED-4 -LRRinterleukin-1 reCED-4 -LRR-ARC-LRR, LysM (Lysin moTIR)-kinase.

Propyl-pyrazole-triol (PPT), an ERα specific ligand, and diarylpropionitrile (DPN), an ERβ specific ligand were developed thanks to the weak sequence identity of the C-terminal ligand-binding domain shared by two ER molecules, [39], [40].

Using sensitive sequence and structure analysis, we show that the ALOG domains are a distinct version of the N-terminal DNA-binding domain shared by the XerC/D-like, protelomerase, topoisomerase-IA, and Flp tyrosine recombinases.

The largest class of R proteins contains NB-ARC (Nucleotide-binding domain shared by Apaf-1, R gene products, and CED-4) and LRR domains which can be accompanied by the presence of a TIR (Toll/interleukin-1 receptor) domain in their N-terminus.

** Domain shared by both instruments.

Their DNA binding domain shares some similarity with the CCT domain of the nuclear flowering time regulator CONSTANS COO) [ 26, 27].

Most of the cloned R genes share two common domains: the central domain, which encodes a nucleotide binding adaptor shared by APAF-1, ceRtain R proteins, and CED-4 (NB-ARC), plus a C-terminal region that encodes Leu-rich repeats (LRR).

The NB-ARC domain is a nucleotide-binding motif shared by plant resistant gene products involved in regulated cell death [ 37, 38].

They contained the conserved NB-ARC (nucleotide-binding adaptor shared by Apaf-1, R proteins and Ced-4) domain of known R genes [ 40- 42].

This domain is shared by all HOX genes and is required for the DNA-binding activities of HOX proteins functioning as transcription factors (Alexander et al., 2009).