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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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.
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.
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9 Citations in Europe PMC

Data provided by Europe PubMed Central.

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

29 References

Data provided by Europe PubMed Central.

Binding of chloromethyl ketone substrate analogues to crystalline papain.
Drenth J, Kalk KH, Swen HM., Biochemistry 15(17), 1976
PMID: 952885
Crystal structure of a papain-E-64 complex.
Varughese KI, Ahmed FR, Carey PR, Hasnain S, Huber CP, Storer AC., Biochemistry 28(3), 1989
PMID: 2713367
Kinetics of the pH-induced inactivation of human cathepsin L.
Turk B, Dolenc I, Turk V, Bieth JG., Biochemistry 32(1), 1993
PMID: 7678196
Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.
Turk D, Podobnik M, Popovic T, Katunuma N, Bode W, Huber R, Turk V., Biochemistry 34(14), 1995
PMID: 7718586

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