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.

Zeitschriftenaufsatz | Veröffentlicht | Englisch

Download

Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!

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.

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.
Schmitz J, Li T, Bartz U, Gütschow M., ACS Med Chem Lett 7(3), 2016
PMID: 26985300

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

Dipeptide-derived nitriles containing additional electrophilic sites: potentially irreversible inhibitors of cysteine proteases.
Löser R, Gütschow M., J Enzyme Inhib Med Chem 24(6), 2009
PMID: 19912058

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

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.
Watanabe D, Yamamoto A, Tomoo K, Matsumoto K, Murata M, Kitamura K, Ishida T., J Mol Biol 362(5), 2006
PMID: 16950396

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
PMID: 15776409

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

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

29 References

Daten bereitgestellt von Europe PubMed Central.

Hanada, Agric. Biol. Chem. 42(), 1978

L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.
Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, Hanada K., Biochem. J. 201(1), 1982
PMID: 7044372

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

Refined x-ray structure of papain.E-64-c complex at 2.1-A resolution.
Yamamoto D, Matsumoto K, Ohishi H, Ishida T, Inoue M, Kitamura K, Mizuno H., J. Biol. Chem. 266(22), 1991
PMID: 1860874

Crystal structure of papain-E64-c complex. Binding diversity of E64-c to papain S2 and S3 subsites.
Kim MJ, Yamamoto D, Matsumoto K, Inoue M, Ishida T, Mizuno H, Sumiya S, Kitamura K., Biochem. J. 287 ( Pt 3)(), 1992
PMID: 1445241

Rich, 1986

Binding of chloromethyl ketone substrate analogues to crystalline papain.
Drenth J, Kalk KH, Swen HM., Biochemistry 15(17), 1976
PMID: 952885

Yabe, J. Am. Chem. Soc. 110(), 1988

Novel epoxysuccinyl peptides. Selective inhibitors of cathepsin B, in vitro.
Murata M, Miyashita S, Yokoo C, Tamai M, Hanada K, Hatayama K, Towatari T, Nikawa T, Katunuma N., FEBS Lett. 280(2), 1991
PMID: 2013328

Novel epoxysuccinyl peptides. A selective inhibitor of cathepsin B, in vivo.
Towatari T, Nikawa T, Murata M, Yokoo C, Tamai M, Hanada K, Katunuma N., FEBS Lett. 280(2), 1991
PMID: 2013329

CA074 methyl ester: a proinhibitor for intracellular cathepsin B.
Buttle DJ, Murata M, Knight CG, Barrett AJ., Arch. Biochem. Biophys. 299(2), 1992
PMID: 1444478

Epoxysuccinyl dipeptides as selective inhibitors of cathepsin B.
Gour-Salin BJ, Lachance P, Plouffe C, Storer AC, Menard R., J. Med. Chem. 36(6), 1993
PMID: 8459399

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

Efficient synthetic method for ethyl (+)-(2S,3S)-3-[(S)-3-methyl- 1-(3-methylbutylcarbamoyl)butylcarbamoyl]-2-oxiranecarb oxylate (EST), a new inhibitor of cysteine proteinases.
Tamai M, Yokoo C, Murata M, Oguma K, Sota K, Sato E, Kanaoka Y., Chem. Pharm. Bull. 35(3), 1987
PMID: 3301019

Giordano, Eur. J. Med. Chem. 28(), 1993

The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
Musil D, Zucic D, Turk D, Engh RA, Mayr I, Huber R, Popovic T, Turk V, Towatari T, Katunuma N., EMBO J. 10(9), 1991
PMID: 1868826

E64 [trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane] analogues as inhibitors of cysteine proteinases: investigation of S2 subsite interactions.
Gour-Salin BJ, Lachance P, Magny MC, Plouffe C, Menard R, Storer AC., Biochem. J. 299 ( Pt 2)(), 1994
PMID: 8172599

Mori, Tetrahedron 36(), 1980

Korn, Tetrahedron 50(), 1994

Gour-Salin, Bioorg. Chem. 22(), 1994

A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses.
Khouri HE, Plouffe C, Hasnain S, Hirama T, Storer AC, Menard R., Biochem. J. 275 ( Pt 3)(), 1991
PMID: 2039451

Investigation of structure function relationships in cathepsin B.
Hasnain S, Huber CP, Muir A, Rowan AD, Mort JS., Biol. Chem. Hoppe-Seyler 373(7), 1992
PMID: 1515068

Kinetics of the pH-induced inactivation of human cathepsin L.
Turk B, Dolenc I, Turk V, Bieth JG., Biochemistry 32(1), 1993
PMID: 7678196

Temporary inhibition of papain by hairpin loop mutants of chicken cystatin. Distorted binding of the loops results in cleavage of the Gly(9)-Ala10 bond.
Machleidt W, Nagler DK, Assfalg-Machleidt I, Stubbs MT, Fritz H, Auerswald EA., FEBS Lett. 361(2-3), 1995
PMID: 7698320

Moroder, Biol. Chem. Hoppe-Seyler 357(), 1976

Machleidt, 1993

Morrison, Trends Biochem. Sci. 7(), 1982

Knight, 1986

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB