<p>Panel A shows the regions flanking the activating sites in natural substrates of thrombin. The amino acid sequences flanking both N-terminally and C-terminally of the cleavage sites for thrombin in FV, FVIII, PAR1,3 and 4, α & β fibrinogen and Protein C are depicted. Sequences are shown in a one-letter code and cleavage site numbering is based on the mature protein without signal peptide. The negatively charged amino acids are marked in red and thrombin cleavage sites are shown by arrows. Panels B-E shows schematic figures of FVIII, FV, fibrinogen and protein C showing the cleavage sites for thrombin (depicted by scissors with numbered residue).</p
<p>(A) The primary structure of pallilysin was manually analyzed for the presence of potential throm...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...
<p>Panels A to D shows the cleavage of a number of substrates by thrombin, where individual amino ac...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis. In t...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis of th...
<p>Panel A shows the result with 1 U of thrombin, panel B the result with 0.2 U of thrombin and pane...
<p>The name and sequence of the substrates are indicated above the gel pictures. The time of cleavag...
<p>This figure illustrates the differences in structure of the thrombin active site cleft upon the i...
<p>This figure illustrates a close up view of modeled holoenzyme complexes for the A) Arg<sup>391</s...
<p>Amino acids shown in bold and larger font are deviations from the preferred thrombin consensus se...
AbstractNative or denatured protein substrates which are hardly digested by thrombin can become much...
<p>Panel A shows a space-filling model with the alpha chain peptide in purple. Panel B shows the int...
<p>Panel A shows a schematic 3D structure of human thrombin with the charge density illustrated with...
<p>where N and C represent the N- and C-terminus of the 22-residue peptide, respectively, with the c...
<p>(A) The primary structure of pallilysin was manually analyzed for the presence of potential throm...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...
<p>Panels A to D shows the cleavage of a number of substrates by thrombin, where individual amino ac...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis. In t...
<p>Panel A shows the overall structure of the recombinant protein substrates used for analysis of th...
<p>Panel A shows the result with 1 U of thrombin, panel B the result with 0.2 U of thrombin and pane...
<p>The name and sequence of the substrates are indicated above the gel pictures. The time of cleavag...
<p>This figure illustrates the differences in structure of the thrombin active site cleft upon the i...
<p>This figure illustrates a close up view of modeled holoenzyme complexes for the A) Arg<sup>391</s...
<p>Amino acids shown in bold and larger font are deviations from the preferred thrombin consensus se...
AbstractNative or denatured protein substrates which are hardly digested by thrombin can become much...
<p>Panel A shows a space-filling model with the alpha chain peptide in purple. Panel B shows the int...
<p>Panel A shows a schematic 3D structure of human thrombin with the charge density illustrated with...
<p>where N and C represent the N- and C-terminus of the 22-residue peptide, respectively, with the c...
<p>(A) The primary structure of pallilysin was manually analyzed for the presence of potential throm...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...
Thrombin is a serine protease of the chymotrypsin family that acts both as a procoagulant and as an ...