<p>A. NMR structure of mouse Bid (PDB 1DDB) with the two natural cysteines spin labeled in this study (C126 in p15 and C30 in p7) and the cleavage site in ball and stick models. B. Superposition of mouse Bid (colored) and human Bax (black, PDB 1F16). Color code for alpha helices in mouse Bid: 1, light yellow; 1/2, dark yellow; 2, orange; 3, gold; 4, pink; 5, red; 6, brown; 7, violet.</p
Y41 and H353 in mouse ACE2 are labeled in yellow, and D501 of S protein is in green. The salt bridge...
<p>The paired domain of wild-type Pax2 domain DNA are represented by red and white ribbons, respecti...
<p><b>A</b>, Model structure of mOSM (amino acids 25–205 of NP_001013383.1, orange) and rOSM (amino ...
<p>Secondary structure prediction of the Ring1B IRES of human and mouse origin, showing a striking s...
<p>(a) Superposition of the CNPase/RICH structures. Colouring: mouse, light blue; human, green; rat,...
<p>(<b>A</b>) Predicted domain structures of NOXO1 and NOXA1 in comparison to p47<sup>phox</sup> and...
<p>Different secondary structure elements are drawn in different colours (purple: α-helix, yellow: β...
<p>(<b>A</b>) Lid loops of mouse and human SMP30/GNL in the substrate free form are shown in purple ...
<p>(<b>A</b>) Pairwise sequence alignment between ODC and AZI in the putative AZ-binding element. (<...
<p>Six canonical hotspots for isoAsp formation are indicated with carets (∧). Color-coding indicates...
<p>(A) Sequence alignment of five vertebrate FAAP20-UBZs (human, mouse, rat, chicken and puffy fish)...
<p>Panels A–E are cartoon-format models with spiral ribbons representing alpha helices and thinner c...
<p>Black shading indicates identical residues. Red box represents residues from mouse and rat Aβ tha...
A multiple PIP alignment of mouse and tammar sequence against human (B). Conserved regions (red) and...
<p><b>(A)</b> Amino acid sequences of residues 2–21 in human αS, βS and γS and mouse αS. <b>(B)</b> ...
Y41 and H353 in mouse ACE2 are labeled in yellow, and D501 of S protein is in green. The salt bridge...
<p>The paired domain of wild-type Pax2 domain DNA are represented by red and white ribbons, respecti...
<p><b>A</b>, Model structure of mOSM (amino acids 25–205 of NP_001013383.1, orange) and rOSM (amino ...
<p>Secondary structure prediction of the Ring1B IRES of human and mouse origin, showing a striking s...
<p>(a) Superposition of the CNPase/RICH structures. Colouring: mouse, light blue; human, green; rat,...
<p>(<b>A</b>) Predicted domain structures of NOXO1 and NOXA1 in comparison to p47<sup>phox</sup> and...
<p>Different secondary structure elements are drawn in different colours (purple: α-helix, yellow: β...
<p>(<b>A</b>) Lid loops of mouse and human SMP30/GNL in the substrate free form are shown in purple ...
<p>(<b>A</b>) Pairwise sequence alignment between ODC and AZI in the putative AZ-binding element. (<...
<p>Six canonical hotspots for isoAsp formation are indicated with carets (∧). Color-coding indicates...
<p>(A) Sequence alignment of five vertebrate FAAP20-UBZs (human, mouse, rat, chicken and puffy fish)...
<p>Panels A–E are cartoon-format models with spiral ribbons representing alpha helices and thinner c...
<p>Black shading indicates identical residues. Red box represents residues from mouse and rat Aβ tha...
A multiple PIP alignment of mouse and tammar sequence against human (B). Conserved regions (red) and...
<p><b>(A)</b> Amino acid sequences of residues 2–21 in human αS, βS and γS and mouse αS. <b>(B)</b> ...
Y41 and H353 in mouse ACE2 are labeled in yellow, and D501 of S protein is in green. The salt bridge...
<p>The paired domain of wild-type Pax2 domain DNA are represented by red and white ribbons, respecti...
<p><b>A</b>, Model structure of mOSM (amino acids 25–205 of NP_001013383.1, orange) and rOSM (amino ...