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S W Dahl

Showing results (1-10 of 9) with videos related to

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Biochemistry|October 4, 2000
The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzymeB Cigić, S W Dahl, R H Pain
The Journal of Biological Chemistry|October 11, 1996
Heterologous expression of three plant serpins with distinct inhibitory specificitiesS W Dahl, S K Rasmussen, J Hejgaard
Plant Molecular Biology|February 1, 1996
A recombinant wheat serpin with inhibitory activityS K Rasmussen, S W Dahl, A Norgård, et al.
FEBS Letters|September 30, 1996
Inhibition of coagulation factors by recombinant barley serpin BSZxS W Dahl, S K Rasmussen, L C Petersen, et al.
FEBS Letters|October 17, 2001
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domainJ G Olsen, A Kadziola, C Lauritzen, et al.
Protein Expression and Purification|October 19, 2000
Carica papaya glutamine cyclotransferase belongs to a novel plant enzyme subfamily: cloning and characterization of the recombinant enzymeS W Dahl, C Slaughter, C Lauritzen, et al.
Biochemistry|May 1, 2001
Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processingS W Dahl, T Halkier, C Lauritzen, et al.
Protein Expression and Purification|January 12, 1999
Active recombinant rat dipeptidyl aminopeptidase I (cathepsin C) produced using the baculovirus expression systemC Lauritzen, J Pedersen, M T Madsen, et al.
The EMBO Journal|December 1, 2001
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteasesD Turk, V Janjić, I Stern, et al.
Pageof 1

Showing results (1-10 of 9) with videos related to

Sort By:
Pageof 1
Biochemistry|October 4, 2000
The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzymeB Cigić, S W Dahl, R H Pain
The Journal of Biological Chemistry|October 11, 1996
Heterologous expression of three plant serpins with distinct inhibitory specificitiesS W Dahl, S K Rasmussen, J Hejgaard
Plant Molecular Biology|February 1, 1996
A recombinant wheat serpin with inhibitory activityS K Rasmussen, S W Dahl, A Norgård, et al.
FEBS Letters|September 30, 1996
Inhibition of coagulation factors by recombinant barley serpin BSZxS W Dahl, S K Rasmussen, L C Petersen, et al.
FEBS Letters|October 17, 2001
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domainJ G Olsen, A Kadziola, C Lauritzen, et al.
Protein Expression and Purification|October 19, 2000
Carica papaya glutamine cyclotransferase belongs to a novel plant enzyme subfamily: cloning and characterization of the recombinant enzymeS W Dahl, C Slaughter, C Lauritzen, et al.
Biochemistry|May 1, 2001
Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processingS W Dahl, T Halkier, C Lauritzen, et al.
Protein Expression and Purification|January 12, 1999
Active recombinant rat dipeptidyl aminopeptidase I (cathepsin C) produced using the baculovirus expression systemC Lauritzen, J Pedersen, M T Madsen, et al.
The EMBO Journal|December 1, 2001
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteasesD Turk, V Janjić, I Stern, et al.
Pageof 1