Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Christian Dalhoff"'
Autor:
Christian Dalhoff, Joji Grace Villamor, Hubert Köster, Renier A. L. van der Hoorn, Farnusch Kaschani, Janina Lenger, Thomas Lenz, Norbert Sewald
Publikováno v:
Bioorganic & Medicinal Chemistry. 20:592-596
Matrix metalloproteases (MMPs) are secreted or membrane-bound zinc-containing proteases that play diverse roles in development and immunity in plants and in tissue remodeling in animals. We developed a photoreactive probe based on the MMP inhibitor m
Publikováno v:
Nature Protocols. 1:1879-1886
Here we describe a one-step synthetic procedure for the preparation of S-adenosyl-L-methionine (AdoMet) analogs with extended carbon chains replacing the methyl group. These AdoMet analogs function as efficient cofactors for DNA methyltransferases (M
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 13:3207-3211
Incorporation of sulfoximines as backbone modifying element results in two new pseudopeptide bonds which display enhanced (bond A) and strongly reduced reactivity (bond B) towards hydrolysis by Proteinase K.
Autor:
Mirko Glinski, Anna K. Schrey, Christian Dalhoff, Jenny J. Fischer, Hubert Koester, Michael Sefkow, Olivia Baessler, Kathrin Andrich, Mathias Dreger, Friedrich Kroll, Simon Michaelis
Publikováno v:
Journal of proteomics. 75(1)
Capture Compound Mass Spectrometry (CCMS) is a platform technology for the functional isolation of subproteomes. Here we report the synthesis of two new kinase Capture Compounds (CCs) based on the tyrosine-kinase specific inhibitors dasatinib and ima
Autor:
Peter Poot, Elmar Weinhold, Eckhard Nordhoff, Michael Hüben, Christian Dalhoff, Thomas Lenz, Hubert Köster
Publikováno v:
Chembiochem : a European journal of chemical biology. 11(2)
Understanding the interplay of different cellular proteins and their substrates is of major interest in the postgenomic era. For this purpose, selective isolation and identification of proteins from complex biological samples is necessary and targete
Autor:
Elmar Weinhold, Christian Dalhoff
Publikováno v:
Modified Nucleosides: in Biochemistry, Biotechnology and Medicine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90f2c9366a0387277bcbdd309604dbbd
https://doi.org/10.1002/9783527623112.ch9
https://doi.org/10.1002/9783527623112.ch9
Autor:
Vidmantas Lapienė, Christian Dalhoff, Gražvydas Lukinavičius, Elmar Weinhold, Zdislav Staševskij, Saulius Klimašauskas
Publikováno v:
Journal of the American Chemical Society
Methyltransferases catalyze highly specific transfers of methyl groups from the ubiquitous cofactor S-adenosyl-l-methionine (AdoMet) to various biopolymers like DNA, RNA, and proteins. Here we describe the first synthetic analogue of AdoMet with an a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86b137e45bbdab149f4f721af0152589
https://hdl.handle.net/21.11116/0000-0001-DFEE-921.11116/0000-0001-DFF0-521.11116/0000-0001-DFF1-4
https://hdl.handle.net/21.11116/0000-0001-DFEE-921.11116/0000-0001-DFF0-521.11116/0000-0001-DFF1-4
Publikováno v:
Nature Chemical Biology
S-Adenosyl-L-methionine (AdoMet) is the major methyl donor for biological methylation reactions catalyzed by methyltransferases. We report the first chemical synthesis of AdoMet analogs with extended carbon chains replacing the methyl group and their