(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins

Schaschke N (2007)
JOURNAL OF BIOTECHNOLOGY 129(2): 308-315.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Erscheinungsjahr
2007
Zeitschriftentitel
JOURNAL OF BIOTECHNOLOGY
Band
129
Ausgabe
2
Seite(n)
308-315
ISSN
0168-1656
Page URI
https://pub.uni-bielefeld.de/record/2403744

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Schaschke N. (2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins. JOURNAL OF BIOTECHNOLOGY. 2007;129(2):308-315.
Schaschke, N. (2007). (2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins. JOURNAL OF BIOTECHNOLOGY, 129(2), 308-315. https://doi.org/10.1016/j.jbiotec.2007.01.023
Schaschke, Norbert. 2007. “(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins”. JOURNAL OF BIOTECHNOLOGY 129 (2): 308-315.
Schaschke, N. (2007). (2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins. JOURNAL OF BIOTECHNOLOGY 129, 308-315.
Schaschke, N., 2007. (2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins. JOURNAL OF BIOTECHNOLOGY, 129(2), p 308-315.
N. Schaschke, “(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins”, JOURNAL OF BIOTECHNOLOGY, vol. 129, 2007, pp. 308-315.
Schaschke, N.: (2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins. JOURNAL OF BIOTECHNOLOGY. 129, 308-315 (2007).
Schaschke, Norbert. “(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins”. JOURNAL OF BIOTECHNOLOGY 129.2 (2007): 308-315.

2 Zitationen in Europe PMC

Daten bereitgestellt von 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

44 References

Daten bereitgestellt von Europe PubMed Central.

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
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

Barrett, 1998
HaCaT keratinocytes secrete lysosomal cysteine proteinases during migration.
Buth H, Wolters B, Hartwig B, Meier-Bornheim R, Veith H, Hansen M, Sommerhoff CP, Schaschke N, Machleidt W, Fusenig NE, Boukamp P, Brix K., Eur. J. Cell Biol. 83(11-12), 2004
PMID: 15679122
Developing photoactive affinity probes for proteomic profiling: hydroxamate-based probes for metalloproteases.
Chan EW, Chattopadhaya S, Panicker RC, Huang X, Yao SQ., J. Am. Chem. Soc. 126(44), 2004
PMID: 15521763
An affinity-based probe for the proteomic profiling of aspartic proteases
Chattopadhaya, Tetrahedron Lett. 46(), 2005
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
The crystal structure of human cathepsin L complexed with E-64.
Fujishima A, Imai Y, Nomura T, Fujisawa Y, Yamamoto Y, Sugawara T., FEBS Lett. 407(1), 1997
PMID: 9141479
Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.
Greenbaum D, Medzihradszky KF, Burlingame A, Bogyo M., Chem. Biol. 7(8), 2000
PMID: 11048948
Chemical approaches for functionally probing the proteome.
Greenbaum D, Baruch A, Hayrapetian L, Darula Z, Burlingame A, Medzihradszky KF, Bogyo M., Mol. Cell Proteomics 1(1), 2002
PMID: 12096141
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
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
Chemical tools for activity-based proteomics.
Hagenstein MC, Sewald N., J. Biotechnol. 124(1), 2006
PMID: 16442651
Isolation and characterization of E-64, a new thiol protease inhibitor
Hanada, Agric. Biol. Chem. 42(), 1978
Structure and synthesis of E-64, a new thiol protease inhibitor
Hanada, Agric. Biol. Chem. 42(), 1978

Hooper, 2002
TMC-52A to D, novel cysteine proteinase inhibitors, produced by Gliocladium sp.
Isshiki K, Nishio M, Sakurai N, Uchida T, Okuda T, Komatsubara S., J. Antibiot. 51(7), 1998
PMID: 9727388
Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8.
James KE, Asgian JL, Li ZZ, Ekici OD, Rubin JR, Mikolajczyk J, Salvesen GS, Powers JC., J. Med. Chem. 47(6), 2004
PMID: 14998341
Activity-based probes that target diverse cysteine protease families.
Kato D, Boatright KM, Berger AB, Nazif T, Blum G, Ryan C, Chehade KA, Salvesen GS, Bogyo M., Nat. Chem. Biol. 1(1), 2005
PMID: 16407991
Design and synthesis of an affinity probe that targets caspases in proteomic experiments
Liau, Tetrahedron Lett. 44(), 2003
Activity-based protein profiling: the serine hydrolases.
Liu Y, Patricelli MP, Cravatt BF., Proc. Natl. Acad. Sci. U.S.A. 96(26), 1999
PMID: 10611275
Protease degradomics: a new challenge for proteomics.
Lopez-Otin C, Overall CM., Nat. Rev. Mol. Cell Biol. 3(7), 2002
PMID: 12094217
Proteome Analysis: A Pathway to the Functional Analysis of Proteins.
Lottspeich F., Angew. Chem. Int. Ed. Engl. 38(17), 1999
PMID: 10508327
The lysosomal cysteine proteases.
McGrath ME., Annu Rev Biophys Biomol Struct 28(), 1999
PMID: 10410800
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
A classical enzyme active center motif lacks catalytic competence until modulated electrostatically.
Pinitglang S, Watts AB, Patel M, Reid JD, Noble MA, Gul S, Bokth A, Naeem A, Patel H, Thomas EW, Sreedharan SK, Verma C, Brocklehurst K., Biochemistry 36(33), 1997
PMID: 9254592
Irreversible inhibitors of serine, cysteine, and threonine proteases.
Powers JC, Asgian JL, Ekici OD, James KE., Chem. Rev. 102(12), 2002
PMID: 12475205
MEROPS: the protease database.
Rawlings ND, O'Brien E, Barrett AJ., Nucleic Acids Res. 30(1), 2002
PMID: 11752332
Activity-based probes for the proteomic profiling of metalloproteases.
Saghatelian A, Jessani N, Joseph A, Humphrey M, Cravatt BF., Proc. Natl. Acad. Sci. U.S.A. 101(27), 2004
PMID: 15220480
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
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., Biol. Chem. 383(5), 2002
PMID: 12108551
On the size of the active site in proteases. I. Papain.
Schechter I, Berger A., Biochem. Biophys. Res. Commun. 27(2), 1967
PMID: 6035483
Activity-based proteomics: enzymatic activity profiling in complex proteomes.
Schmidinger H, Hermetter A, Birner-Gruenberger R., Amino Acids 30(4), 2006
PMID: 16773240
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
Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets?
Turk, Biochem. Soc. Symp. 70(), 2003
Development of an isotope-coded activity-based probe for the quantitative profiling of cysteine proteases.
van Swieten PF, Maehr R, van den Nieuwendijk AM, Kessler BM, Reich M, Wong CS, Kalbacher H, Leeuwenburgh MA, Driessen C, van der Marel GA, Ploegh HL, Overkleeft HS., Bioorg. Med. Chem. Lett. 14(12), 2004
PMID: 15149659
Cysteine Protease Inhibitors Produced by the Industrial Koji Mold, Aspergillus oryzae O-1018.
Yamada T, Hiratake J, Aikawa M, Suizu T, Saito Y, Kawato A, Suginami K, Oda J., Biosci. Biotechnol. Biochem. 62(5), 1998
PMID: 27392587
Structural basis for development of cathepsin B-specific noncovalent-type inhibitor: crystal structure of cathepsin B-E64c complex.
Yamamoto A, Tomoo K, Matsugi K, Hara T, In Y, Murata M, Kitamura K, Ishida T., Biochim. Biophys. Acta 1597(2), 2002
PMID: 12044902
Crystal structure of human osteoclast cathepsin K complex with E-64.
Zhao B, Janson CA, Amegadzie BY, D'Alessio K, Griffin C, Hanning CR, Jones C, Kurdyla J, McQueney M, Qiu X, Smith WW, Abdel-Meguid SS., Nat. Struct. Biol. 4(2), 1997
PMID: 9033588
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