New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P(1) selected by combinatorial chemistry methods. (Q33291788)

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English	New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P(1) selected by combinatorial chemistry methods.	scientific article

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2 January 2020

New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P(1) selected by combinatorial chemistry methods (English)

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2 January 2020

Magdalena Wysocka

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2 January 2020

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2 January 2020

Krzysztof Rolka

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2 January 2020

Anna Łęgowska

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Anna Legowska

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2 January 2020

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Elzbieta Bulak

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2 January 2020

Anna Jaśkiewicz

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2 January 2020

Hanna Miecznikowska

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2 January 2020

publication date

1 May 2007

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2 January 2020

Molecular Diversity

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2 January 2020

11

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2 January 2020

2

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2 January 2020

93-99

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2 January 2020

Specificity of human cathepsin G.

1 reference

https://api.crossref.org/works/10.1007%2FS11030-007-9063-7

21 January 2018

Design, chemical synthesis and kinetic studies of trypsin chromogenic substrates based on the proteinase binding loop of Cucurbita maxima trypsin inhibitor (CMTI-III)

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Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity

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General method for rapid synthesis of multicomponent peptide mixtures

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Selection of low-molecular-mass trypsin and chymotrypsin inhibitors based on the binding loop of CMTI-III using combinatorial chemistry methods.

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Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with peptide 4-nitroanilide substrates and with peptide chloromethyl ketone and sulfonyl fluoride inhibitors

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Kinetic mechanism of the inhibition of cathepsin G by alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor

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Neutrophil elastase and cathepsin G: structure, function, and biological control.

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The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites.

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Cathepsin G enhances human natural killer cytotoxicity

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Human leukocyte cathepsin G. Subsite mapping with 4-nitroanilides, chemical modification, and effect of possible cofactors.

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Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Purification and properties

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Amino acids and peptides. XXXV. Facile preparation of p-nitroanilide analogs by the solid-phase method

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A simple method for selection of trypsin chromogenic substrates using combinatorial chemistry approach.

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Synthesis and physical characterization of a P1 arginine combinatorial library, and its application to the determination of the substrate specificity of serine peptidases

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Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions

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Selection of new chromogenic substrates of serine proteinases using combinatorial chemistry methods.

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The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities

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Identifiers

10.1007/S11030-007-9063-7

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17653609%20AND%20SRC:MED&resulttype=core&format=json

2 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17653609%20AND%20SRC:MED&resulttype=core&format=json

2 January 2020

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