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المؤلفون: Stephen P. Muench, Merete Storflor, Saranya Subramani, J. Preben Morth, David P. Klebl, Julia Weikum, Jeroen Van Dyck, Frank Sobott, Sören Abel
مصطلحات موضوعية: biology, Chemistry, Magnesium transporter, ATPase, chemistry.chemical_compound, Ion homeostasis, Membrane protein, Biochemistry, Cytoplasm, biology.protein, Cardiolipin, lipids (amino acids, peptides, and proteins), Binding site, Lipid bilayer
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::6925dd5c9188fbd167311cfbd74fec68
https://doi.org/10.1101/2021.09.27.462033 -
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المؤلفون: Marie Skepö, Julia Weikum, Alina Kulakova, Jack C. Leo, Shogo Yoshimoto, J. Preben Morth, Katsutoshi Hori, Giulio Tesei, Pernille Harris, Line Vejby Jægerum, Monika Schütz
المصدر: Weikum, J, Kulakova, A, Tesei, G, Yoshimoto, S, Jægerum, L V, Schütz, M, Hori, K, Skepö, M, Harris, P, Leo, J C & Morth, J P 2020, ' The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action ', Scientific Reports, vol. 10, 21249 . https://doi.org/10.1038/s41598-020-77706-7
Scientific Reports
Weikum, J, Vitaliyivna Kulakova, A, Tesei, G, Yoshimoto, S, Jægerum, L V, Schütz, M, Hori, K, Skepö, M, Harris, P, Leo, J C & Morth, J P 2020, ' The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action ', Scientific Reports, vol. 10, no. 1, 21249 . https://doi.org/10.1038/s41598-020-77706-7
Scientific reports 10(1), 21249 (2020). doi:10.1038/s41598-020-77706-7مصطلحات موضوعية: 0301 basic medicine, Virulence Factors, Mathematics and computing, 030106 microbiology, Biophysics, Biochemistry, Protein Structure, Secondary, Article, Virulence factor, Atomic force microscopy, 03 medical and health sciences, Extracellular, Enteropathogenic Escherichia coli, Adhesins, Bacterial, Biological sciences, X-ray crystallography, Juncture, Intimin, Bacterial structural biology, Multidisciplinary, Chemistry, Escherichia coli Proteins, SAXS, Cell biology, 030104 developmental biology, Mitochondrial Membranes, Molecular modelling, Pathogens, Structural biology, ddc:600, Bacterial Outer Membrane Proteins, Autotransporters
وصف الملف: application/pdf
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::023c209e29fde8baa2495ee27655d3c8
https://curis.ku.dk/portal/da/publications/the-extracellular-juncture-domains-in-the-intimin-passenger-adopt-a-constitutively-extended-conformation-inducing-restraints-to-its-sphere-of-action(e47b40d1-c894-4780-a8ae-3aaf17436d9c).html -
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المؤلفون: Niklas Ritzmann, Fabian Grein, Michaele Josten, Anna Klöckner, Sebastian Herkersdorf, Nils Jelden, Hans-Georg Sahl, Julia Weikum
المصدر: Antimicrobial Agents and Chemotherapy. 62
مصطلحات موضوعية: 0301 basic medicine, Staphylococcus aureus, Sulfide, medicine.drug_class, Antibiotics, Respiratory chain, Microbial Sensitivity Tests, Sulfides, medicine.disease_cause, Microbiology, 03 medical and health sciences, Mechanisms of Resistance, Drug Resistance, Bacterial, medicine, Pharmacology (medical), Inhibitory effect, Pharmacology, chemistry.chemical_classification, biology, Chemistry, Mechanism (biology), Aminoglycoside, biology.organism_classification, Anti-Bacterial Agents, Aminoglycosides, 030104 developmental biology, Infectious Diseases, Bacteria
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19405534d7b0214bb3b2e76673abb8c2
https://doi.org/10.1128/aac.00602-18 -
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المؤلفون: Rebecca Keller, Nicole Schleppi, Dirk Schneider, Julia Weikum
المصدر: FEBS Letters. 589:842-848
مصطلحات موضوعية: Protein family, DNA Mutational Analysis, Biophysics, Virulence, lac operon, medicine.disease_cause, Biochemistry, Protein Structure, Secondary, Tvp38, Structural Biology, Escherichia coli, Genetics, medicine, Oligomerization, Function, Molecular Biology, Alanine, Chemistry, Escherichia coli Proteins, Cell Membrane, Mutagenesis, Membrane Proteins, Gene Expression Regulation, Bacterial, Cell Biology, Alanine scanning, Transmembrane domain, Membrane protein, DedA, Mutation, Protein Multimerization
