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Subtilisin

Known as: Subtilisin [Chemical/Ingredient] 
A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large… 
National Institutes of Health

Related topics

Related topics

9 relations
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Broader (2)

Serine ProteasesSubtilisins

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2003
Highly Cited
2003
A green fluorescent chemosensor for amino acids provides a versatile high-throughput screening (HTS) assay for proteases.
Highly Cited
1993
Highly Cited
1993
Folding of subtilisin BPN': role of the pro-sequence.
Subtilisin BPN' is an extracellular serine protease from Bacillus amyloliquefaciens that requires an N-terminal 77 amino acid pro… 
Highly Cited
1993
Highly Cited
1993
Characterization and application of strong ion-exchange membrane adsorbers as stationary phases in high-performance liquid chromatography of proteins.
Highly Cited
1991
Highly Cited
1991
Stabilization of functional proteins by introduction of multiple disulfide bonds.
Highly Cited
1989
Highly Cited
1989
Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content.
Highly Cited
1988
Highly Cited
1988
The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case.
A weak Ca2+ binding site in the bacterial serine protease subtilisin BPN' (EC 3.4.21.14) was chosen as a model to explore the… 
Highly Cited
1979
Highly Cited
1979
Multiple molecular forms of glia maturation factor.
Highly Cited
1974
Highly Cited
1974
Studies on the amphipathic nature of the membrane proteins in Semliki Forest virus.
Highly Cited
1973
Highly Cited
1973
Characteristics and isolation of the phagocytosis-stimulating peptide, tuftsin.
Highly Cited
1962
Highly Cited
1962
A reinvestigation of the sequence of residues 11 to 18 in bovine pancreatic ribonuclease.
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