IndraLab

Statements


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reach
"While ubiquitin inhibits USP2 with a K i of 2.8 muM, mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"USP2 is inhibited by ubiquitin with a K i of 2.8 mM, which is in the same range as the K i of 3 mM for the related enzyme USP5, also known as isopeptidase T (Dang et al., 1998) ."

sparser
"While ubiquitin inhibits USP2 with a K of 2.8 μM, mutants lacking residues or affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration."

sparser
"Figure 4: USP2 Inhibition by Full-Length Ubiquitin and the C-Terminally Truncated Mutants, Ubiquitin 1-74 and 1-73 Residual enzymatic activity was determined at 22°C with ubiquitin-AMC as substrate."

reach
"In summary, our data show that the ubiquitin core and the ubiquitin C terminus alone bind USP2 very weakly with affinities at best in the high micromolar range, while full-length ubiquitin inhibits US[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"In summary, our data show that the ubiquitin core and the ubiquitin C terminus alone bind USP2 very weakly with affinities at best in the high micromolar range, while full-length ubiquitin inhibits US[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

eidos
"While ubiquitin inhibits USP2 with a Ki of 2.8 muM , mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration ."

eidos
"Figure 4 : USP2 Inhibition by Full-Length Ubiquitin and the C-Terminally Truncated Mutants , Ubiquitin 1-74 and 1-73 Residual enzymatic activity was determined at 22degreesC with ubiquitin-AMC as substrate ."

reach
"USP2 is inhibited by ubiquitin with a K i of 2.8 muM, which is in the same range as the K i of 3 muM for the related enzyme USP5, also known as isopeptidase T (Dang et al., 1998)."

sparser
"In summary, our data show that the ubiquitin core and the ubiquitin C terminus alone bind USP2 very weakly with affinities at best in the high micromolar range, while full-length ubiquitin inhibits USP2 with a Ki of 2.8 μM."

sparser
"USP2 is inhibited by ubiquitin with a Ki of 2.8 μM, which is in the same range as the Ki of 3 μM for the related enzyme USP5, also known as isopeptidase T (Dang et al., 1998)."

sparser
"While ubiquitin inhibits USP2 with a K i of 2.8 mM, mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration."

reach
"While ubiquitin inhibits USP2 with a K i of 2.8 mM, mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration."

reach
"USP2 is inhibited by ubiquitin with a Ki of 2.8 μM, which is in the same range as the Ki of 3 μM for the related enzyme USP5, also known as isopeptidase T (Dang et al., 1998)."

reach
"While ubiquitin inhibits USP2 with a Ki of 2.8 μM, mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration."

sparser
"USP2 is inhibited by ubiquitin with a K i of 2.8 mM, which is in the same range as the K i of 3 mM for the related enzyme USP5, also known as isopeptidase T (Dang et al., 1998) ."

sparser
"While ubiquitin inhibits USP2 with a Ki of 2.8 μM, mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration."

sparser
"Substrate Binding Region of USP2 and USP7 USP2 Inhibition by Full-Length Ubiquitin and the C-Terminally Truncated Mutants, Ubiquitin 1-74 and 1-73 Steady-State Kinetic Parameters for the Hydrolysis of AMC Substrates by UCH-L3 and USP2 Inhibition of USP2 Crystallographic Data and Refinement Statistics Data Set Statistics"

sparser
"USP2 is inhibited by ubiquitin with a K of 2.8 μM, which is in the same range as the K of 3 μM for the related enzyme USP5, also known as isopeptidase T ()."

reach
"Only USP7 residues that differ from USP2 are labeled.Figure 4: USP2 Inhibition by Full-Length Ubiquitin and the C-Terminally Truncated Mutants, Ubiquitin 1-74 and 1-73 Residual enzymatic activity was determined at 22°C with ubiquitin-AMC as substrate."

eidos
"While ubiquitin inhibits USP2 with a K i of 2.8 mM , mutants lacking residues Arg74-Gly75-Gly76 or Leu73-Arg74-Gly75-Gly76 affect the proteolytic activity of USP2 only marginally even at the highest inhibitor concentration ."

sparser
"In summary, our data show that the ubiquitin core and the ubiquitin C terminus alone bind USP2 very weakly with affinities at best in the high micromolar range, while full-length ubiquitin inhibits USP2 with a K i of 2.8 mM."