Results 191 to 200 of about 33,574 (255)
Injury to tissue caused by device penetration of the skin triggers formation of extracellular traps. [PDF]
Wood KA +6 more
europepmc +1 more source
Neutrophil elastase-activatable ratiometric photoacoustic nanoprobes for imaging atherosclerotic plaque vulnerability. [PDF]
Cao H +14 more
europepmc +1 more source
Endothelial cell injury: a crucial link in microcirculatory dysfunction associated with sepsis. [PDF]
Pan Y, Ma Y, Wan K, Xu Y, Wang G, Xie M.
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Proteolytic inactivation of human leukocyte elastase
Experientia, 1985Human leukocyte elastase can be proteolytically inactivated by bovine pancreatic trypsin. Neither porcine pancreatic elastase nor bovine pancreatic chymotrypsin causes inactivation of leukocyte elastase, nor are trypsin, pancreatic elastase, or chymotrypsin themselves susceptible to proteolysis.
R L, Stein, J C, Williams
openaire +2 more sources
Enantioselective inhibition of human leukocyte elastase
Archives of Biochemistry and Biophysics, 1992(RS)-Diethyl-2-benzyl-succinate was resolved using alpha-chymotrypsin. The two enantiomers were then elaborated to yield (S)-(+) and (R)-(-)-3-benzyl-N-[(methyl-sulfonyl)oxy]succinimide and the inhibitory activity of the two enantiomers toward human leukocyte elastase was subsequently determined.
Groutas, William C. +3 more
openaire +2 more sources
Annals of the New York Academy of Sciences, 2009
Poly(ADP‐ribose) polymerase‐1 (PARP‐1) uses NAD+ as a substrate to form ADP‐ribose. During apoptosis, caspases cleave PARP‐1 to avoid excessive NAD consumption. Because PARP‐1 is a key regulator of the activity of DNases involved in caspase‐dependent apoptosis, its cleavage is required to promote DNA degradation.
Chloé, Leprêtre +3 more
openaire +2 more sources
Poly(ADP‐ribose) polymerase‐1 (PARP‐1) uses NAD+ as a substrate to form ADP‐ribose. During apoptosis, caspases cleave PARP‐1 to avoid excessive NAD consumption. Because PARP‐1 is a key regulator of the activity of DNases involved in caspase‐dependent apoptosis, its cleavage is required to promote DNA degradation.
Chloé, Leprêtre +3 more
openaire +2 more sources

