Fluorescence-quenched solid phase combinatorial libraries in the characterization of cysteine protease substrate specificity (Q30854464)

27 June 2017

title

Fluorescence-quenched solid phase combinatorial libraries in the characterization of cysteine protease substrate specificity (English)

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27 June 2017

5

Meldal M

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27 June 2017

St Hilaire PM

1

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27 June 2017

Willert M

series ordinal

2

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27 June 2017

Juliano MA

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3

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27 June 2017

Juliano L

series ordinal

4

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27 June 2017

publication date

1 November 1999

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ACS Combinatorial Science

27 June 2017

published in

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volume

1

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issue

6

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27 June 2017

page(s)

509-523

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New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain

27 June 2017

cites work

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Revised definition of substrate binding sites of papain-like cysteine proteases

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The specificity of the S1' subsite of cysteine proteases

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On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain

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A new, sensitive fluorogenic substrate for papain based on the sequence of the cystatin inhibitory site

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Evaluation of resins for on-bead screening: a study of papain and chymotrypsin specificity using PEGA-bound combinatorial peptide libraries

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

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Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching

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Use of papain as a model for the structure-based design of cathepsin K inhibitors: crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites

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Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors

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Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases

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Revisiting the S2 specificity of papain by structural analogs of Phe

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New coupling reagents in peptide chemistry

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Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsin

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Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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New substrates of papain, based on the conserved sequence of natural inhibitors of the cystatin family

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Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-amino acid inhibitors for cruzipain, cathepsin B and cathepsin L.

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Interaction between cystatin-derived peptides and papain

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Inactivation of dimeric D-amino acid transaminase by a normal substrate through formation of an unproductive coenzyme adduct in one subunit

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/CC990031U

Identifiers

DOI

10.1021/CC990031U

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27 June 2017

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