Výsledky vyhledávání - "Tobias Gräwert"

Akademický článek

Structural basis of CDNF interaction with the UPR regulator GRP78

Autor: Melissa A. Graewert, Maria Volkova, Klara Jonasson, Juha A. E. Määttä, Tobias Gräwert, Samara Mamidi, Natalia Kulesskaya, Johan Evenäs, Richard E. Johnsson, Dmitri Svergun, Arnab Bhattacharjee, Henri J. Huttunen

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)

Abstract Cerebral dopamine neurotrophic factor (CDNF) is an unconventional neurotrophic factor that is a disease-modifying drug candidate for Parkinson’s disease. CDNF has pleiotropic protective effects on stressed cells, but its mechanism of actio

Externí odkaz: https://doaj.org/article/96e49cedbeaa44d2becdda52aada34c8

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Structural Modeling Using Solution Small-Angle X-ray Scattering (SAXS)

Autor: Dmitri I. Svergun, Tobias Gräwert

Publikováno v: Journal of Molecular Biology. 432:3078-3092

Small-angle X-ray scattering (SAXS) offers a way to examine the overall shape and oligomerization state of biological macromolecules under quasi native conditions in solution. In the past decades, SAXS has become a standard tool for structure biologi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f2ef8ec06560634abe610d0e5798ac1
https://doi.org/10.1016/j.jmb.2020.01.030

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Adding Size Exclusion Chromatography (SEC) and Light Scattering (LS) Devices to Obtain High-Quality Small Angle X-Ray Scattering (SAXS) Data

Autor: Tobias Gräwert, Dmitri I. Svergun, Clement E. Blanchet, Cy M. Jeffries, Dmitry S. Molodenskiy, Melissa A. Graewert, Stefano Da Vela

Publikováno v: Crystals
Volume 10
Issue 11
Crystals, Vol 10, Iss 975, p 975 (2020)
Crystals 10(11), 975 (1-18) (2020). doi:10.3390/cryst10110975

Crystals 10(11), 975 (1-18) (2020). doi:10.3390/cryst10110975
We describe the updated size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) set-up used at the P12 bioSAXS beam line of the European Molecular Biology Laboratory (EM

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1be66682c811f57f345d275c073e82e

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Aryl bis-sulfonamides bind to the active site of a homotrimeric isoprenoid biosynthesis enzyme IspF and extract the essential divalent metal cation cofactor

Autor: Jonas Thelemann, Tobias Gräwert, Markus Fischer, Renato Zenobi, Anatol Schwab, Boris Illarionov, Julie G. Geist, Katharina Root, Adelbert Bacher, Konstantin Barylyuk, François Diederich

Publikováno v: Chemical Science, 9
Chemical Science

Native ESI-MS delivers unprecedented insight into unknown homomeric protein binding mechanisms involving complex, multistage binding equilibria with cofactors and ligands.
Characterizing the mode of action of non-covalent inhibitors in multisubu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0821cd16febef64de78f6cce278e8c6
https://doi.org/10.1039/c8sc00814k

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Structure of GTP cyclohydrolase I from Listeria monocytogenes, a potential anti-infective drug target

Autor: Markus Fischer, Tobias Gräwert, Alexandra Siemens, Sonja Schüssler, Ilka Haase, Adelbert Bacher, Markus Perbandt, Boris Illarionov, Klaus Richter

Publikováno v: Acta Crystallographica. Section F, Structural Biology Communications
Acta crystallographica / F Structural biology communications Section F 75(9), 586-592 (2019). doi:10.1107/S2053230X19010902

GTP cyclohydrolase I from Listeria monocytogenes, a putative anti-infective drug target, has been crystallized and the crystal structure was solved at 2.4 Å resolution.
A putative open reading frame encoding GTP cyclohydrolase I from Listeria m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec89e3fc3caae88f0256a8937f639f93
https://pubmed.ncbi.nlm.nih.gov/31475925

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Prodrugs of Reverse Fosmidomycin Analogues

Autor: Tobias Gräwert, Boris Illarionov, Markus Fischer, Thomas Kurz, Sergio Wittlin, Claudia Lienau, Benjamin Mordmüller, Adelbert Bacher, Louis Maes, Christoph T. Behrendt, Jana Held, Karin Brücher, Sarah Konzuch

Publikováno v: Journal of medicinal chemistry

Fosmidomycin inhibits IspC (Dxr, 1-deoxy-D-xylulose 5-phosphate reductoisomerase), a key enzyme in nonmevalonate isoprenoid biosynthesis that is essential in Plasmodium falciparum. The drug has been used successfully to treat malaria patients in clin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56d428904427c873d6447f76da1ff1e3
https://doi.org/10.1021/jm5019719

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The complex isotopologue space of glucose as a framework for the study of human intermediary metabolism

Autor: Silke Marsch, Markus Fischer, Michael Vogeser, Tobias Gräwert, Dietrich Seidel, Adelbert Bacher, Ulrike Bacher, Harald Mückter, Christian Ettenhuber, Ralf Laupitz, Wolfgang Eisenreich

Publikováno v: Isotopes in Environmental and Health Studies. 51:11-23

The positional distributions of stable isotopes in metabolites provide specific fingerprints of the pathways and fluxes that have occurred in the organisms under study. In particular, modern nuclear magnetic resonance (NMR) spectroscopy enables the d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0340dec138cb2d0c90ecdf050eed4d88
https://doi.org/10.1080/10256016.2014.1001845

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Novel reverse thia-analogs of fosmidomycin: Synthesis and antiplasmodial activity

Autor: Beate Lungerich, Lasse van Geelen, Leandro A. Alves Avelar, Claudia Lienau, Rainer Kalscheuer, Benjamin Mordmüller, Mirko Buchholz, Ulrich Riederer, Holger Cynis, Tobias Gräwert, Markus Fischer, Dieter Meier, Boris Illarionov, Tanja C. Knaab, Stefanie Geissler, Jana Held, Thomas Kurz, Adelbert Bacher

Publikováno v: European Journal of Medicinal Chemistry. 181:111555

Thia analogs of fosmidomycin are potent inhibitors of the non-mevalonate isoprenoid biosynthesis enzyme 1-deoxy- d -xylulose 5-phosphate reductoisomerase (IspC, Dxr) of Plasmodium falciparum. Several new thioethers displayed antiplasmodial in vitro a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba6ace739ec3d82720492527907c6654
https://doi.org/10.1016/j.ejmech.2019.07.058

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