Serine protease mechanism and specificity.

By L. Hedstrom. Chemical Reviews, 2002

1,806 citations recorded by the source corpus.

Subfields: Biotechnology, Hematology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/36edb8308047207b04fe707ce5b03a4620d37b0b

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Citations in the corpus

Cleavage Entropy as Quantitative Measure of Protease Specificity (2013, background): “This canonical conformation usually includes residues in the P3-P39 substrate region, at most extended to P5, in serine protease elastase [10].”
Protein sectors: evolutionary units of three-dimensional structure (2009, methodology): “Consistent with prior work (Hedstrom, 2002), we find that mutations in the red sector have significant effect on catalytic activity (red circles, Figure 5A).”
Approaches to efficiently estimate solvation and explicit water energetics in ligand binding: the use of WaterMap (2013, methodology): “[89] applied the combined WaterMap--MM-GB/ SA analysis to explain the SARs established using traditional computational methods in the inhibitor binding in blood coagulation factor serine protease [90].”
Phenoloxidase: a key component of the insect immune system (2012, background): “Serine proteases cut the polypeptide chain in the carboxyl side of specific amino acids, resulting in peptide bond degradation (Hedstrom, 2002).”
Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases (2010, neutral): “(Hedstrom, 2002).”
Evolution-Based Functional Decomposition of Proteins (2015, positive): “The methods are implemented in an open-source python-based software package that is available to the scientific community, and illustrated in the main text using the small G protein family of nucleotidedependent switches [25, 26] and the S1A family of serine proteases [27, 28].”