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, Hohneke C, Sommerhoff CP, Machleidt W (2002)
BIOLOGICAL CHEMISTRY 383(5): 849-852.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ;
Erscheinungsjahr
Zeitschriftentitel
BIOLOGICAL CHEMISTRY
Band
383
Zeitschriftennummer
5
Seite
849-852
ISSN
PUB-ID

Zitieren

Schaschke N, Deluca D, Assfalg-Machleidt I, Hohneke C, Sommerhoff CP, Machleidt W. Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY. 2002;383(5):849-852.
Schaschke, N., Deluca, D., Assfalg-Machleidt, I., Hohneke, C., Sommerhoff, C. P., & Machleidt, W. (2002). Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY, 383(5), 849-852. doi:10.1515/BC.2002.090
Schaschke, N., Deluca, D., Assfalg-Machleidt, I., Hohneke, C., Sommerhoff, C. P., and Machleidt, W. (2002). Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY 383, 849-852.
Schaschke, N., et al., 2002. Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY, 383(5), p 849-852.
N. Schaschke, et al., “Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin”, BIOLOGICAL CHEMISTRY, vol. 383, 2002, pp. 849-852.
Schaschke, N., Deluca, D., Assfalg-Machleidt, I., Hohneke, C., Sommerhoff, C.P., Machleidt, W.: Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. BIOLOGICAL CHEMISTRY. 383, 849-852 (2002).
Schaschke, Norbert, Deluca, D, Assfalg-Machleidt, I, Hohneke, C, Sommerhoff, CP, and Machleidt, W. “Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin”. BIOLOGICAL CHEMISTRY 383.5 (2002): 849-852.

7 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Selective targeting of tumor and stromal cells by a nanocarrier system displaying lipidated cathepsin B inhibitor.
Mikhaylov G, Klimpel D, Schaschke N, Mikac U, Vizovisek M, Fonovic M, Turk V, Turk B, Vasiljeva O., Angew Chem Int Ed Engl 53(38), 2014
PMID: 24975267
Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment.
Diederich S, Sauerhering L, Weis M, Altmeppen H, Schaschke N, Reinheckel T, Erbar S, Maisner A., J Virol 86(7), 2012
PMID: 22278224
A new cell-permeable calpain inhibitor.
Fiorino F, Gil-Parrado S, Assfalg-Machleidt I, Machleidt W, Moroder L., J Pept Sci 13(1), 2007
PMID: 17019744
Investigation of penetratin peptides. Part 2. In vitro uptake of penetratin and two of its derivatives.
Letoha T, Gaál S, Somlai C, Venkei Z, Glavinas H, Kusz E, Duda E, Czajlik A, Peták F, Penke B., J Pept Sci 11(12), 2005
PMID: 15942927
Delivery of bioactive molecules into the cell: the Trojan horse approach.
Dietz GP, Bähr M., Mol Cell Neurosci 27(2), 2004
PMID: 15485768
Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: enhancing cell permeability by conjugation with penetratin.
Gil-Parrado S, Assfalg-Machleidt I, Fiorino F, Deluca D, Pfeiler D, Schaschke N, Moroder L, Machleidt W., Biol Chem 384(3), 2003
PMID: 12715890

15 References

Daten bereitgestellt von Europe PubMed Central.

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

AUTHOR UNKNOWN, 0
Trojan peptides: the penetratin system for intracellular delivery.
Derossi D, Chassaing G, Prochiantz A., Trends Cell Biol. 8(2), 1998
PMID: 9695814

AUTHOR UNKNOWN, 0
Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin.
Fischer PM, Zhelev NZ, Wang S, Melville JE, Fahraeus R, Lane DP., J. Pept. Res. 55(2), 2000
PMID: 10784032
Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor.
Foghsgaard L, Wissing D, Mauch D, Lademann U, Bastholm L, Boes M, Elling F, Leist M, Jaattela M., J. Cell Biol. 153(5), 2001
PMID: 11381085
Molecular regulation, membrane association and secretion of tumor cathepsin B.
Frosch BA, Berquin I, Emmert-Buck MR, Moin K, Sloane BF., APMIS 107(1), 1999
PMID: 10190277
Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c.
Guicciardi ME, Deussing J, Miyoshi H, Bronk SF, Svingen PA, Peters C, Kaufmann SH, Gores GJ., J. Clin. Invest. 106(9), 2000
PMID: 11067865
Cell-penetrating peptides.
Lindgren M, Hallbrink M, Prochiantz A, Langel U., Trends Pharmacol. Sci. 21(3), 2000
PMID: 10689363
Cathepsin B.
Mort JS, Buttle DJ., Int. J. Biochem. Cell Biol. 29(5), 1997
PMID: 9251238
Cysteine Proteases and Their Inhibitors.
Otto HH, Schirmeister T., Chem. Rev. 97(1), 1997
PMID: 11848867
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
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
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

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 12108551
PubMed | Europe PMC

Suchen in

Google Scholar