Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors

Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L (1998)
FEBS LETTERS 421(1): 80-82.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Schaschke, NorbertUniBi; Assfalg-Machleidt, I; Machleidt, W; Moroder, L
Einrichtung
Fakultät für Chemie > Organische Chemie III
Erscheinungsjahr
1998
Zeitschriftentitel
FEBS LETTERS
Band
421
Ausgabe
1
Seite(n)
80-82
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/2403869

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Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 1998;421(1):80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., & Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), 80-82. https://doi.org/10.1016/S0014-5793(97)01538-X
Schaschke, Norbert, Assfalg-Machleidt, I, Machleidt, W, and Moroder, L. 1998. “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”. FEBS LETTERS 421 (1): 80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., and Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS 421, 80-82.
Schaschke, N., et al., 1998. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), p 80-82.
N. Schaschke, et al., “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”, FEBS LETTERS, vol. 421, 1998, pp. 80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., Moroder, L.: Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 421, 80-82 (1998).
Schaschke, Norbert, Assfalg-Machleidt, I, Machleidt, W, and Moroder, L. “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”. FEBS LETTERS 421.1 (1998): 80-82.

18 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
Cysteine cathepsins: cellular roadmap to different functions.
Brix K, Dunkhorst A, Mayer K, Jordans S., Biochimie 90(2), 2008
PMID: 17825974
Inhibition of cathepsin L by epoxysuccinyl peptides simultaneously addressing active-site and remote-site regions.
Schaschke N, Assfalg-Machleidt I, Machleidt W., Chembiochem 9(11), 2008
PMID: 18551692
(2S,3S)-Oxirane-2,3-dicarboxylic acid: a privileged platform for probing human cysteine cathepsins.
Schaschke N., J Biotechnol 129(2), 2007
PMID: 17339064
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
Cathepsin B is essential for regeneration of scratch-wounded normal human epidermal keratinocytes.
Büth H, Luigi Buttigieg P, Ostafe R, Rehders M, Dannenmann SR, Schaschke N, Stark HJ, Boukamp P, Brix K., Eur J Cell Biol 86(11-12), 2007
PMID: 17651862
Chemical tools for activity-based proteomics.
Hagenstein MC, Sewald N., J Biotechnol 124(1), 2006
PMID: 16442651
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
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
Epoxysuccinyl peptide-derived cathepsin B inhibitors: modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin.
Schaschke N, Deluca D, Assfalg-Machleidt I, Höhneke C, Sommerhoff CP, Machleidt W., Biol Chem 383(5), 2002
PMID: 12108551
Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation.
Balaji KN, Schaschke N, Machleidt W, Catalfamo M, Henkart PA., J Exp Med 196(4), 2002
PMID: 12186841
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
Beta-cyclodextrin/epoxysuccinyl peptide conjugates: a new drug targeting system for tumor cells.
Schaschke N, Assfalg-Machleidt I, Machleidt W, Lassleben T, Sommerhoff CP, Moroder L., Bioorg Med Chem Lett 10(7), 2000
PMID: 10762052
Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.
Brinker A, Weber E, Stoll D, Voigt J, Müller A, Sewald N, Jung G, Wiesmüller KH, Bohley P., Eur J Biochem 267(16), 2000
PMID: 10931191
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
The lysosomal cysteine proteases.
McGrath ME., Annu Rev Biophys Biomol Struct 28(), 1999
PMID: 10410800
Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
Czaplewski C, Grzonka Z, Jaskólski M, Kasprzykowski F, Kozak M, Politowska E, Ciarkowski J., Biochim Biophys Acta 1431(2), 1999
PMID: 10350606

25 References

Daten bereitgestellt von Europe PubMed Central.

Vacuolar/lysosomal proteolysis: proteases, substrates, mechanisms.
Knop M, Schiffer HH, Rupp S, Wolf DH., Curr. Opin. Cell Biol. 5(6), 1993
PMID: 8129953
Identification of proteases that process distinct epitopes on the same protein.
Takahashi H, Cease KB, Berzofsky JA., J. Immunol. 142(7), 1989
PMID: 2466893

Vaes, Clin. Orthop. 231(), 1988
Cysteine proteinases and metastasis.
Sloane BF, Honn KV., Cancer Metastasis Rev. 3(3), 1984
PMID: 6093995
Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis.
Esser RE, Angelo RA, Murphey MD, Watts LM, Thornburg LP, Palmer JT, Talhouk JW, Smith RE., Arthritis Rheum. 37(2), 1994
PMID: 8129779
Abnormal expression of lysosomal cysteine proteinases in muscle wasting diseases.
Katunuma N, Kominami E., Rev. Physiol. Biochem. Pharmacol. 108(), 1987
PMID: 3306875

AUTHOR UNKNOWN, 0
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
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 an actinidin-E-64 complex.
Varughese KI, Su Y, Cromwell D, Hasnain S, Xuong NH., Biochemistry 31(22), 1992
PMID: 1606141
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
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
Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex.
Yamamoto A, Hara T, Tomoo K, Ishida T, Fujii T, Hata Y, Murata M, Kitamura K., J. Biochem. 121(5), 1997
PMID: 9192742
E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group.
Schaschke N, Assfalg-Machleidt I, Machleidt W, Turk D, Moroder L., Bioorg. Med. Chem. 5(9), 1997
PMID: 9354234
Potent slow-binding inhibition of cathepsin B by its propeptide.
Fox T, de Miguel E, Mort JS, Storer AC., Biochemistry 31(50), 1992
PMID: 1472493
Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes.
Taylor MA, Baker KC, Briggs GS, Connerton IF, Cummings NJ, Pratt KA, Revell DF, Freedman RB, Goodenough PW., Protein Eng. 8(1), 1995
PMID: 7770454
Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion.
Cygler M, Sivaraman J, Grochulski P, Coulombe R, Storer AC, Mort JS., Structure 4(4), 1996
PMID: 8740363
Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide.
Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V., FEBS Lett. 384(3), 1996
PMID: 8617355
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

AUTHOR UNKNOWN, 0

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

AUTHOR UNKNOWN, 0

Korn, Tetrahedron 50(), 1994
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