E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group

Schaschke, Norbert; AssfalgMachleidt, I; Machleidt, W; Turk, D; Moroder, L

E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group

Schaschke N, AssfalgMachleidt I, Machleidt W, Turk D, Moroder L (1997)
BIOORGANIC & MEDICINAL CHEMISTRY 5(9): 1789-1797.

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DOI

https://doi.org/10.1016/S0968-0896(97)00105-3

Autor*in

Schaschke, Norbert^UniBi; AssfalgMachleidt, I; Machleidt, W; Turk, D; Moroder, L

Einrichtung

Fakultät für Chemie > Organische Chemie III

Erscheinungsjahr

1997

Zeitschriftentitel

BIOORGANIC & MEDICINAL CHEMISTRY

Band

5

Ausgabe

9

Seite(n)

1789-1797

ISSN

0968-0896

Page URI

https://pub.uni-bielefeld.de/record/2403882

Zitieren

Schaschke N, AssfalgMachleidt I, Machleidt W, Turk D, Moroder L. E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group. BIOORGANIC & MEDICINAL CHEMISTRY. 1997;5(9):1789-1797.

Schaschke, N., AssfalgMachleidt, I., Machleidt, W., Turk, D., & Moroder, L. (1997). E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group. BIOORGANIC & MEDICINAL CHEMISTRY, 5(9), 1789-1797. https://doi.org/10.1016/S0968-0896(97)00105-3

Schaschke, Norbert, AssfalgMachleidt, I, Machleidt, W, Turk, D, and Moroder, L. 1997. “E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group”. BIOORGANIC & MEDICINAL CHEMISTRY 5 (9): 1789-1797.

Schaschke, N., AssfalgMachleidt, I., Machleidt, W., Turk, D., and Moroder, L. (1997). E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group. BIOORGANIC & MEDICINAL CHEMISTRY 5, 1789-1797.

Schaschke, N., et al., 1997. E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group. BIOORGANIC & MEDICINAL CHEMISTRY, 5(9), p 1789-1797.

N. Schaschke, et al., “E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group”, BIOORGANIC & MEDICINAL CHEMISTRY, vol. 5, 1997, pp. 1789-1797.

Schaschke, N., AssfalgMachleidt, I., Machleidt, W., Turk, D., Moroder, L.: E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group. BIOORGANIC & MEDICINAL CHEMISTRY. 5, 1789-1797 (1997).

Schaschke, Norbert, AssfalgMachleidt, I, Machleidt, W, Turk, D, and Moroder, L. “E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group”. BIOORGANIC & MEDICINAL CHEMISTRY 5.9 (1997): 1789-1797.

Daten bereitgestellt von European Bioinformatics Institute (EBI)

17 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Cathepsin B Inhibitors: Combining Dipeptide Nitriles with an Occluding Loop Recognition Element by Click Chemistry.
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E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.
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Dipeptide-derived nitriles containing additional electrophilic sites: potentially irreversible inhibitors of cysteine proteases.
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Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases.
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Quantitative evaluation of each catalytic subsite of cathepsin B for inhibitory activity based on inhibitory activity-binding mode relationship of epoxysuccinyl inhibitors by X-ray crystal structure analyses of complexes.
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Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases.
Verhelst SH, Bogyo M., Chembiochem 6(5), 2005
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Design and evaluation of inhibitors for dipeptidyl peptidase I (Cathepsin C).
Kam CM, Götz MG, Koot G, McGuire M, Thiele D, Hudig D, Powers JC., Arch Biochem Biophys 427(2), 2004
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Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.
Stern I, Schaschke N, Moroder L, Turk D., Biochem J 381(pt 2), 2004
PMID: 15084146

Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors: when reaction mechanism is more important than specificity.
Rozman-Pungercar J, Kopitar-Jerala N, Bogyo M, Turk D, Vasiljeva O, Stefe I, Vandenabeele P, Brömme D, Puizdar V, Fonović M, Trstenjak-Prebanda M, Dolenc I, Turk V, Turk B., Cell Death Differ 10(8), 2003
PMID: 12867995

Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases).
James KE, Götz MG, Caffrey CR, Hansell E, Carter W, Barrett AJ, McKerrow JH, Powers JC., Biol Chem 384(12), 2003
PMID: 14719804

pH Dependence of inhibitors targeting the occluding loop of cathepsin B.
Cathers BE, Barrett C, Palmer JT, Rydzewski RM., Bioorg Chem 30(4), 2002
PMID: 12392705

Small molecule affinity fingerprinting. A tool for enzyme family subclassification, target identification, and inhibitor design.
Greenbaum DC, Arnold WD, Lu F, Hayrapetian L, Baruch A, Krumrine J, Toba S, Chehade K, Brömme D, Kuntz ID, Bogyo M., Chem Biol 9(10), 2002
PMID: 12401493

Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
Guncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L, Turk D., Structure 8(3), 2000
PMID: 10745011

Aziridinyl peptides as inhibitors of cysteine proteases: effect of a free carboxylic acid function on inhibition.
Schirmeister T, Peric M., Bioorg Med Chem 8(6), 2000
PMID: 10896108

Epoxysuccinyl peptide-derived affinity labels for cathepsin B.
Schaschke N, Assfalg-Machleidt I, Lassleben T, Sommerhoff CP, Moroder L, Machleidt W., FEBS Lett 482(1-2), 2000
PMID: 11018529

Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors.
Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L., FEBS Lett 421(1), 1998
PMID: 9462845

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