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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Zeitschriftentitel
BIOORGANIC & MEDICINAL CHEMISTRY
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5
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9
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1789-1797
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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. doi:10.1016/S0968-0896(97)00105-3
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.

16 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Development of cell-active non-peptidyl inhibitors of cysteine cathepsins.
Dana D, Davalos AR, De S, Rathod P, Gamage RK, Huestis J, Afzal N, Zavlanov Y, Paroly SS, Rotenberg SA, Subramaniam G, Mark KJ, Chang EJ, Kumar S., Bioorg Med Chem 21(11), 2013
PMID: 23623677
E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.
Radzey H, Rethmeier M, Klimpel D, Grundhuber M, Sommerhoff CP, Schaschke N., ChemMedChem 8(8), 2013
PMID: 23780739
Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases.
Sadaghiani AM, Verhelst SH, Gocheva V, Hill K, Majerova E, Stinson S, Joyce JA, Bogyo M., Chem Biol 14(5), 2007
PMID: 17524981
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
PMID: 15196986
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
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

29 References

Daten bereitgestellt von Europe PubMed Central.

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PMID: 2713367
Kinetics of the pH-induced inactivation of human cathepsin L.
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Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.
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