Výsledky vyhledávání - "Martin E. Boehm"

Akademický článek

Model Based Targeting of IL-6-Induced Inflammatory Responses in Cultured Primary Hepatocytes to Improve Application of the JAK Inhibitor Ruxolitinib

Publikováno v: Frontiers in Physiology, Vol 8 (2017)

IL-6 is a central mediator of the immediate induction of hepatic acute phase proteins (APP) in the liver during infection and after injury, but increased IL-6 activity has been associated with multiple pathological conditions. In hepatocytes, IL-6 ac

Externí odkaz: https://doaj.org/article/03da31470aeb4d8daea3fee3c7d95293

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Erythropoietin-driven dynamic proteome adaptations during erythropoiesis prevent iron overload in the developing embryo

Autor: Sajib Chakraborty, Geoffroy Andrieux, Philipp Kastl, Lorenz Adlung, Sandro Altamura, Martin E. Boehm, Luisa E. Schwarzmüller, Yomn Abdullah, Marie-Christine Wagner, Barbara Helm, Hermann-Josef Gröne, Wolf D. Lehmann, Melanie Boerries, Hauke Busch, Martina U. Muckenthaler, Marcel Schilling, Ursula Klingmüller

Publikováno v: Cell Reports. 40:111360

Erythropoietin (Epo) ensures survival and proliferation of colony-forming unit erythroid (CFU-E) progenitor cells and their differentiation to hemoglobin-containing mature erythrocytes. A lack of Epo-induced responses causes embryonic lethality, but

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acd2082cda9a2f29ebd58fc7a489a36c
https://doi.org/10.1016/j.celrep.2022.111360

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Immunosuppression and Aberrant T Cell Development in the Absence of N-Myristoylation

Autor: Zoran B. Popović, Mahnaz Bonrouhi, Wolf D. Lehmann, Hermann Josef Gröne, Giuseppina Federico, Francesca Rampoldi, Sylvia Kaden, Stefan Porubsky, Fabian Brunk, Martin E. Boehm

Publikováno v: The Journal of Immunology. 195:4228-4243

N-myristoylation refers to the attachment of myristic acid to the N-terminal glycine of proteins and substantially affects their intracellular targeting and functions. The thymus represents an organ with a prominent N-myristoylation activity. To eluc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac64108c892586288e31a6c03adc139a
https://doi.org/10.4049/jimmunol.1500622

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Site-specific degree of phosphorylation in proteins measured by liquid chromatography-electrospray mass spectrometry

Autor: Martin E. Boehm, Wolf D. Lehmann, Joerg Seidler, Bettina Hahn

Publikováno v: PROTEOMICS. 12:2167-2178

This review focuses on quantitative protein phosphorylation analysis based on coverage of both the phosphorylated and nonphosphorylated forms. In this way, site-specific data on the degree of phosphorylation can be measured, generating the most detai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a66b1286ed7841dbc645c501ebdc3c80
https://doi.org/10.1002/pmic.201100561

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Improving the precision of quantitative bottom-up proteomics based on stable isotope-labeled proteins

Autor: Marion Rohmer, Wolf D. Lehmann, Dominic Baeumlisberger, Martin E. Boehm, Michael Karas, Anna Konopka

Publikováno v: Analytical and Bioanalytical Chemistry. 404:1079-1087

Stable isotope dilution-based quantitative proteomics with intact labeled proteins as internal standards in combination with a bottom-up approach, i.e., with quantification on the peptide level, is an established method. To explore the technical prec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93d7040d9d1a2a2f54893929087a60a9
https://doi.org/10.1007/s00216-012-6007-6

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Metal ion-mobilizing additives for comprehensive detection of femtomole amounts of phosphopeptides by reversed phase LC-MS

Autor: Erik Haaf, Wolf D. Lehmann, Joerg Seidler, Andreas Schlosser, Dominic Winter, Martin E. Boehm, Nico Zinn

Publikováno v: Amino Acids. 41:311-320

It is hypothesized that metal ion-mediated adsorption of phosphorylated peptides on stationary phases of LC-columns is the major cause for their frequently observed poor detection efficiency in LC-MS. To study this phenomenon in more detail, sample s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a49313ce58b9760fc220402294408390
https://doi.org/10.1007/s00726-010-0647-7

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Resolving the Combinatorial Complexity of Smad Protein Complex Formation and Its Link to Gene Expression

Publikováno v: Cell Systems. United States (2017).

Upon stimulation of cells with transforming growth factor beta (TGF-beta), Smad proteins form trimeric complexes and activate a broad spectrum of target genes. It remains unresolved which of the possible Smad complexes are formed in cellular contexts

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac6954a23a6d6994b6d66b53397fae48
https://doi.org/10.1016/j.cels.2017.11.010

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Identification of isoform-specific dynamics in phosphorylation-dependent STAT5 dimerization by quantitative mass spectrometry and mathematical modeling

Autor: Wolf D. Lehmann, Ursula Klingmüller, Marcel Schilling, Martin E. Boehm, Susanne Roth, Lorenz Adlung

Publikováno v: Journal of proteome research. 13(12)

STAT5A and STAT5B are important transcription factors that dimerize and transduce activation signals of cytokine receptors directly to the nucleus. A typical cytokine that mediates STAT5 activation is erythropoietin (Epo). Differential functions of S

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62439934a6e892f90bfc51d270211def
https://pubmed.ncbi.nlm.nih.gov/25333863

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One-source peptide/phosphopeptide ratio standards for accurate and site-specific determination of the degree of phosphorylation

Autor: Martin E, Boehm, Bettina, Hahn, Wolf D, Lehmann

Publikováno v: Methods in molecular biology (Clifton, N.J.). 1156

Reversible protein phosphorylation is a key mediator for intracellular signal transduction. Here we describe an innovative method for the production of pairs of peptide standards designed for quantitative mass spectrometry. These standard pairs can b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0cea688ecee58b8fec18a70c4b1624e8
https://pubmed.ncbi.nlm.nih.gov/24792001

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Proteomics Standards with Controllable Trueness—Absolute Quantification of Peptides, Phosphopeptides and Proteins Using ICP- and ESI-MS

Autor: Wolf D. Lehmann, Anna Konopka, Christina Wild, Martin E. Boehm

Publikováno v: Quantitative Proteomics ISBN: 9781849738088

Novel methods for the generation of peptide, phosphopeptide and protein standards are described. Inductively coupled plasma mass spectrometry (ICP-MS) is used for quantitative detection, and electrospray ionization mass spectrometry (ESI-MS) is used

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0720f50df30c13a8a96da6390e242420
https://doi.org/10.1039/9781782626985-00110

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