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When the B-block binding subunits of human and S. cerevisiae are aligned using the early Clustal program, they show little sequence similarity [ 16].
However, the PSI-BLAST searches using the B-block binding subunits of human and S. pombe, and Arabidopsis homolog (GI 25402830) as queries, did not significantly hit any of the plant sequences except the Arabidopsis proteins shown in this study.
Here, I reported the results of PSI-BLAST searches using the B-block binding subunits of human and Shizosacchromyces pombe as queries, showing that the same Arabidopsis proteins were hit with low E-values in both searches.
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The B-block binding subunits of rat and human also were hit in this search, but with E-values of 5e-5 and 0.20, respectively (data not shown); the N-terminal 350 amino acid sequences of the rat and human subunits showed similarities to the N-terminal region of S. pombe Sfc3p protein.
In human and rat, the B-block binding subunits of TFIIICs are 243 kDa and 220 kDa respectively [ 14, 15], and there is great similarity between them at the amino acid sequence level [ 15].
Thus, understanding the relationship of the B-block binding subunits from human and yeast TFIIICs is important for understanding the evolution of the RNAP III transcription machinery.
(A) Schematic diagram showing the domain organization of each subunits of human coatomer.
Additionally, a molecular docking of the most active compounds of each series into the ligand binding pocket of one subunit of human 11β-HSD1 was performed.
Furthermore, low-mass molecular dynamics simulations (Pang, 2014) suggest that the cationic CP2 molecule competes with flavin mononucleotide (FMN) for binding to the redox subunit of human mitochondrial complex I (Fig. 5E, F).
SPOPisa substrate-binding subunit of the SPOP-CUL3-RBX1 E3 ligase complex.
Troponin T is the tropomyosin-binding subunit of troponin.
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