Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. (Q42981725)

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scientific article published on April 1996

Language	Label	Description	Also known as
English	Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L.	scientific article published on April 1996

Statements

scholarly article

1 reference

Europe PubMed Central

12 November 2017

Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. (English)

1 reference

Europe PubMed Central

12 November 2017

author name string

Brömme D

1

1 reference

Europe PubMed Central

12 November 2017

Klaus JL

2

1 reference

Europe PubMed Central

12 November 2017

Okamoto K

3

1 reference

Europe PubMed Central

12 November 2017

Rasnick D

4

1 reference

Europe PubMed Central

12 November 2017

Palmer JT

5

1 reference

Europe PubMed Central

12 November 2017

language of work or name

0 references

publication date

1 April 1996

1 reference

Europe PubMed Central

12 November 2017

Biochemical Journal

1 reference

Europe PubMed Central

12 November 2017

315 ( Pt 1)

1 reference

Europe PubMed Central

12 November 2017

85-89

1 reference

Europe PubMed Central

12 November 2017

Hydrolysis of amyloid precursor protein-derived peptides by cysteine proteinases and extracts of rat brain clathrin-coated vesicles.

1 reference

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Protease inhibitors: role and potential therapeutic use in human cancer

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Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone

1 reference

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Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution

1 reference

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26 May 2018

Cathepsin B, Cathepsin H, and cathepsin L

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217200

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Principles that determine the structure of proteins

1 reference

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Synthesis of peptide fluoromethyl ketones and the inhibition of human cathepsin B.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217200

26 May 2018

A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen

1 reference

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Potent and selective inactivation of cysteine proteinases with N-peptidyl-O-acyl hydroxylamines

1 reference

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Reversible covalent binding of peptide nitriles to papain

1 reference

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Reversible binding of peptide aldehydes to papain. Structure-activity relationships

1 reference

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The specificity and elastinolytic activities of bovine cathepsins S and H

1 reference

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Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease

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N,O-diacyl hydroxamates as selective and irreversible inhibitors of cysteine proteinases

1 reference

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Peptidyl (acyloxy)methanes as quiescent affinity labels for cysteine proteinases

1 reference

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Vinyl sulfones as mechanism-based cysteine protease inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217200

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Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier.

1 reference

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Peptidyl fluoromethyl ketones as inhibitors of cathepsin B. Implication for treatment of rheumatoid arthritis

1 reference

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Functional expression of human cathepsin S in Saccharomyces cerevisiae. Purification and characterization of the recombinant enzyme

1 reference

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Epoxysuccinyl dipeptides as selective inhibitors of cathepsin B

1 reference

https://pubmed.ncbi.nlm.nih.gov/8670136

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based on heuristic

inferred from PubMed ID database lookup

Novel N-peptidyl-O-acyl hydroxamates: selective inhibitors of cysteine proteinases

1 reference

https://pubmed.ncbi.nlm.nih.gov/8670136

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The affinity-labelling of cathepsin S with peptidyl diazomethyl ketones. Comparison with the inhibition of cathepsin L and calpain

1 reference

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Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and an inhibitor of matrix metalloproteinases. Evidence for two converging pathways of chondrocyte-mediated proteoglycan degradation

1 reference

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Peptidyl diazomethanes as inhibitors of cysteine and serine proteinases

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Prognostic value of the cysteine proteases cathepsins B and cathepsin L in human breast cancer

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The Slow, Tight-Binding Inhibition of Cathepsin B by Leupeptin. A Hysteretic Effect

1 reference

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Peptidyl sulfonium salts. A new class of protease inhibitors

1 reference

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Novel epoxysuccinyl peptides. Selective inhibitors of cathepsin B, in vitro

1 reference

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Structure-activity relationships for inhibition of papain by peptide Michael acceptors

1 reference

https://pubmed.ncbi.nlm.nih.gov/8670136

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ3150085

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

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