Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides. (Q36862577)

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scientific article published on April 1997

Language	Label	Description	Also known as
English	Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides.	scientific article published on April 1997

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scholarly article

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3 November 2019

Characterization of the substrate specificity of the major cysteine protease (cruzipain) from Trypanosoma cruzi using a portion-mixing combinatorial library and fluorogenic peptides (English)

1 reference

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3 November 2019

Trypanosoma cruzi

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Morten P. Meldal

3

object named as

M Meldal

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3 November 2019

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E D Nery

1

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3 November 2019

M A Juliano

2

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I Svendsen

4

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J Scharfstein

5

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A Walmsley

6

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L Juliano

7

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publication date

1 April 1997

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Biochemical Journal

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323 ( Pt 2)

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427-433

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Investigation of the substrate specificity of cruzipain, the major cysteine proteinase of Trypanosoma cruzi, through the use of cystatin-derived substrates and inhibitors

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Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity

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Benzyloxycarbonylphenylalanylcitrulline p-nitroanilide as a substrate for papain and other plant cysteine proteinases

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On the size of the active site in proteases. I. Papain

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The C-terminal extension of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi

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Conformation of angiotensin II in aqueous solution. Titration of several peptide analogs and homologs

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Subcellular localization of a cysteine proteinase from Trypanosoma cruzi

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Identifiers

10.1042/BJ3230427

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3 November 2019

1 reference

Europe PubMed Central

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3 November 2019

1 reference

Europe PubMed Central

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3 November 2019

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