Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Konrad Winkels"'
Publikováno v:
Journal of Proteome Research. 21:2185-2196
Bottom-up proteomics (BUP)-based N-terminomics techniques have become standard to identify protein N-termini. While these methods rely on the identification of N-terminal peptides only, top-down proteomics (TDP) comes with the promise to provide addi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e66fc9b652959946b293249d56babf8
https://doi.org/10.1021/acs.jproteome.2c00277
https://doi.org/10.1021/acs.jproteome.2c00277
Autor:
Jan Leipert, Philipp T. Kaulich, Max K. Steinbach, Britta Steer, Konrad Winkels, Christine Blurton, Matthias Leippe, Andreas Tholey
Publikováno v:
Angewandte Chemie International Edition.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d72972d2c0f221aacc0f579dd0d4335c
https://doi.org/10.1002/anie.202301969
https://doi.org/10.1002/anie.202301969
Autor:
Jan Leipert, Philipp T. Kaulich, Max K. Steinbach, Britta Steer, Konrad Winkels, Christine Blurton, Matthias Leippe, Andreas Tholey
Publikováno v:
Angewandte Chemie.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b39a9f1af7e278c51493d9040721d900
https://doi.org/10.1002/ange.202301969
https://doi.org/10.1002/ange.202301969
Autor:
Andreas Tholey, Philipp T. Kaulich, Tobias B. Kaulich, Liam Cassidy, Konrad Winkels, Christian Treitz
Publikováno v:
Journal of Proteome Research. 21:20-29
Top-down proteomics analyzes intact proteoforms with all of their post-translational modifications and genetic and RNA splice variants. In addition, modifications introduced either deliberately or inadvertently during sample preparation, that is, via
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a76609ee21a16d5c87bb3a32b6622f12
https://doi.org/10.1021/acs.jproteome.1c00766
https://doi.org/10.1021/acs.jproteome.1c00766
Autor:
Sinas Furan, Stefan Mebs, Jens Beckmann, Enno Lork, Konrad Winkels, Emanuel Hupf, Martin Molkenthin
Publikováno v:
Organometallics. 40:3785-3796
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d8d5701e9a80f45592a73f1debccd4f
https://doi.org/10.1021/acs.organomet.1c00522
https://doi.org/10.1021/acs.organomet.1c00522
Autor:
Konrad Winkels, Jens Beckmann, Stefan Mebs, Sinas Furan, Matthias Vogt, Enno Lork, Emanuel Hupf
Publikováno v:
Organometallics. 40:1284-1295
The reaction of (5-Ph2P-Ace-6-)Li (I) with InCl3 provided (6-Ph2P-Ace-5-)3In (1), which proved to be a remarkably mild transmetalation reagent. The reaction of 1 with NiCl2, originally aimed to all...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::690946daaf9175dc3a9d064b1a571911
https://doi.org/10.1021/acs.organomet.1c00078
https://doi.org/10.1021/acs.organomet.1c00078
Publikováno v:
Analytical chemistry. 94(8)
In top-down (TD) proteomics, prefractionation prior to mass spectrometric (MS) analysis is a crucial step for both the high confidence identification of proteoforms and increased proteome coverage. In addition to liquid-phase separations, gas-phase f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1302de94af7fb2fead50407717f27ca
https://pubmed.ncbi.nlm.nih.gov/35172570
https://pubmed.ncbi.nlm.nih.gov/35172570
Publikováno v:
Journal of proteome research. 20(9)
While identification-centric (qualitative) top-down proteomics (TDP) has seen rapid progress in the recent past, the quantification of intact proteoforms within complex proteomes is still challenging. The by far mostly applied approach is label-free
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::138294913a9bd4857e116b1c548f2b5a
https://pubmed.ncbi.nlm.nih.gov/34338531
https://pubmed.ncbi.nlm.nih.gov/34338531
Publikováno v:
Biochimica et biophysica acta. Molecular cell research. 1869(1)
Though proteases were long regarded as nonspecific degradative enzymes, over time, it was recognized that they also hydrolyse peptide bonds very specifically with a limited substrate pool. This irreversible posttranslational modification modulates th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8c83bef8dcd4c290fd2f9673cd8d5fb
https://pubmed.ncbi.nlm.nih.gov/34626679
https://pubmed.ncbi.nlm.nih.gov/34626679