يعرض 1 - 10 نتائج من 42 نتيجة بحث عن '"Dieter Willbold"', وقت الاستعلام: 1.21s تنقيح النتائج
  1. 1
    Structural determinants underlying the adduct lifetime in the LOV proteins of Pseudomonas putida

    المؤلفون: Vladimir Arinkin, Joachim Granzin, Karl-Erich Jaeger, Ulrich Krauss, Dieter Willbold, Renu Batra-Safferling

    المصدر: 'FEBS Journal ', vol: 288, pages: 4955-4972 (2021)
    The FEBS journal 288(16), 4955-4972 (2021). doi:10.1111/febs.15785

    مصطلحات موضوعية: 0301 basic medicine, Protein Conformation, Flavin group, Molecular Dynamics Simulation, Biochemistry, Adduct, 03 medical and health sciences, 0302 clinical medicine, Bacterial Proteins, PAS domain, ddc:610, Molecular Biology, chemistry.chemical_classification, biology, Pseudomonas putida, Cell Biology, Protein superfamily, Chromophore, Photochemical Processes, biology.organism_classification, Amino acid, Oxygen, 030104 developmental biology, chemistry, 030220 oncology & carcinogenesis, Helix, Biophysics

    وصف الملف: application/pdf

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5a0d0e1ea2406d85596917d4c78631bTest
    https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:58012Test


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  2. 2
    Correction: Freischem et al. Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria. Biomolecules 2021, 11, 1057

    المؤلفون: Stefan Freischem, Immanuel Grimm, Arancha López-Pérez, Dieter Willbold, Burkhard Klenke, Cuong Vuong, Andrew J. Dingley, Oliver H. Weiergräber

    المصدر: Biomolecules
    Biomolecules, Vol 12, Iss 5, p 5 (2022)
    Biomolecules 12(1), 5-(2022). doi:10.3390/biom12010005

    مصطلحات موضوعية: Models, Molecular, Magnetic Resonance Spectroscopy, Protein Conformation, Escherichia coli Proteins, Correction, Crystallography, X-Ray, Biochemistry, Microbiology, QR1-502, n/a, ddc:570, Pseudomonas aeruginosa, Penicillin-Binding Proteins, Molecular Biology, Monobactams

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daed67d5fbdd7fae321f73cabf8b8849Test
    http://europepmc.org/articles/PMC8774175Test


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  3. 3
    Amperometric Aptasensor for Amyloid-β Oligomer Detection by Optimized Stem-Loop Structures with an Adjustable Detection Range

    المؤلفون: Dirk Mayer, Yuting Zhang, Christian Zafiu, Dieter Willbold, Gabriela Figueroa-Miranda, Andreas Offenhäusser

    المصدر: ACS sensors 4(11), 3042-3050 (2019). doi:10.1021/acssensors.9b01630

    مصطلحات موضوعية: Conformational change, Protein Conformation, Surface Properties, Aptamer, Bioengineering, Biosensing Techniques, 02 engineering and technology, 01 natural sciences, Oligomer, chemistry.chemical_compound, Molecular recognition, Molecular beacon, ddc:570, Particle Size, Instrumentation, Voltammetry, Fluorescent Dyes, Fluid Flow and Transfer Processes, Detection limit, Amyloid beta-Peptides, Chemistry, Process Chemistry and Technology, 010401 analytical chemistry, Electrochemical Techniques, Aptamers, Nucleotide, 021001 nanoscience & nanotechnology, Amperometry, 0104 chemical sciences, Biophysics, 0210 nano-technology

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e34cbc5a56557f9523095f800c2f472eTest
    https://doi.org/10.1021/acssensors.9b01630Test


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  4. 4
    In vitro study of Hesperetin and Hesperidin as inhibitors of zika and chikungunya virus proteases

    المؤلفون: Marcos Serrou do Amaral, Raghuvir K. Arni, Raphael J. Eberle, Clarita M. S. Avilla, Danilo S. Olivier, Carolina Colombelli Pacca, Maurício Lacerda Nogueira, Dieter Willbold, Monika A. Coronado

    المساهمون: Universidade Estadual Paulista (Unesp), Forschungszentrum Jülich, Federal University of Tocantins, FACERES Medical School, Faculdade de Medicina de São José do Rio Preto-FAMERP, Federal University of Mato Grosso do Sul, Heinrich-Heine-Universität Düsseldorf, Forchungszentrum Jülich

    المصدر: PLoS ONE
    PLoS ONE, Vol 16, Iss 3, p e0246319 (2021)
    PLOS ONE 16(3), e0246319-(2021). doi:10.1371/journal.pone.0246319
    Scopus
    Repositório Institucional da UNESP
    Universidade Estadual Paulista (UNESP)
    instacron:UNESP

    مصطلحات موضوعية: 0301 basic medicine, RNA viruses, Models, Molecular, Viral Diseases, Citrus, Protein Conformation, viruses, Dengue virus, medicine.disease_cause, Pathology and Laboratory Medicine, Biochemistry, Zika virus, chemistry.chemical_compound, Medical Conditions, Spectrum Analysis Techniques, Chlorocebus aethiops, Medicine and Health Sciences, Biochemical Simulations, Enzyme assays, Chikungunya, Colorimetric assays, Bioassays and physiological analysis, Multidisciplinary, Chikungunya Virus, MTT assay, biology, Hesperetin, virus diseases, Proteases, Enzymes, Molecular Docking Simulation, Flavivirus, Infectious Diseases, Medical Microbiology, Viral Pathogens, Viruses, Medicine, Pathogens, Research Article, Neglected Tropical Diseases, Science, Alphaviruses, 030106 microbiology, Alphavirus, Research and Analysis Methods, Microbiology, Virus, Togaviruses, 03 medical and health sciences, Inhibitory Concentration 50, Viral Proteins, medicine, Animals, Humans, ddc:610, Microbial Pathogens, Vero Cells, Biology and life sciences, Flaviviruses, Plant Extracts, Hesperidin, Organisms, Proteins, Computational Biology, Chikungunya Infection, Fluorescence Spectroscopy, Zika Virus, biochemical phenomena, metabolism, and nutrition, Dengue Virus, biology.organism_classification, Tropical Diseases, Virology, 030104 developmental biology, chemistry, Biochemical analysis, Enzymology, Peptide Hydrolases

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0eed40a5d6ef186d7d0e3a53e400dd1Test
    http://europepmc.org/articles/PMC7932080Test


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  5. 5
    Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

    المؤلفون: Wolfgang Hoyer, Lothar Gremer, Luisa U. Schäfer, Dieter Willbold, Gunnar F. Schröder, Karunakar R. Pothula, Tatsiana Kupreichyk, Christine Röder, Raimond B. G. Ravelli

    المساهمون: Institute of Nanoscopy (IoN), RS: M4I - Nanoscopy

    المصدر: Nature Structural and Molecular Biology, 27(7), 660-667. Nature Publishing Group
    Nature structural & molecular biology 27(7), 660-667 (2020). doi:10.1038/s41594-020-0442-4
    Nature Structural & Molecular Biology

    مصطلحات موضوعية: DYNAMICS, MECHANISM, System, Models, Molecular, endocrine system, Amyloid β, Atomic-resolution structure, Cryo-electron microscopy, HUMAN AMYLIN, Protein Conformation, Molecular Dynamics Simulation, Fibril, Gene, 03 medical and health sciences, 0302 clinical medicine, Protein structure, Structural Biology, Alzheimer Disease, ddc:570, medicine, Humans, Molecular Biology, 030304 developmental biology, 0303 health sciences, geography, geography.geographical_feature_category, Crystallography, Amyloid beta-Peptides, Chemistry, C-terminus, Pancreatic islets, Cryoelectron Microscopy, S20g mutation, Hydrogen-Ion Concentration, Islet, In vitro, Islet Amyloid Polypeptide, ALZHEIMERS-DISEASE, medicine.anatomical_structure, Amino Acid Substitution, Diabetes Mellitus, Type 2, Iapp, Biophysics, 030217 neurology & neurosurgery

    وصف الملف: application/pdf

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02dff321ad64be4d2613fc91f964157fTest
    https://pubmed.ncbi.nlm.nih.gov/32541895Test


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  6. 6
    Viral rhodopsins 1 are an unique family of light-gated cation channels

    المؤلفون: R. Astashkin, G. A. Armeev, Natalia Yutin, Andreas Offenhäusser, Ekaterina Savelyeva, Kirill Kovalev, Igor Chizhov, Dmitrii Zabelskii, Francisco Rodriguez-Valera, Ernst Bamberg, Alexander Popov, Vladan Rankovic, Maksim Rulev, Dmitry Bratanov, Valentin Gordeliy, Alexey Alekseev, Michel Vivaudou, D V Soloviov, Riccardo Rosselli, Taras Balandin, Tatiana I. Rokitskaya, Eugene V. Koonin, Georg Büldt, Svetlana Vaganova, Ana-Sofia Eria-Oliveira, Yuri N. Antonenko, Tobias Moser, Mikhail P. Kirpichnikov, A. V. Rogachev, Thomas Mager, Dieter Willbold, Elizaveta Podolyak, Dmytro Volkov, Konstantin V. Shaitan

    المساهمون: Institute of Biological Information Processing [Jülich] (IBI-7), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institute for Auditory Neuroscience and InnerEarLab, Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow, Hannover Medical School [Hannover] (MHH), National Center for Biotechnology Information (NCBI), European Synchrotron Radiation Facility (ESRF), Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University (MSU), Max-Planck-Institut für Biophysik - Max Planck Institute of Biophysics (MPIBP), Max-Planck-Gesellschaft, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández [Elche] (UMH), Lomonosov Moscow State University, Biological Faculty, N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences [Moscow] (RAS), InnerEarLab, Department of Otolaryngology and Center for Molecular Physiology of the Brain-Georg-August-University = Georg-August-Universität Göttingen, National Center for Biotechnology Information, National Institutes of Health, Department of Health and Human Services, Bethesda, Md, National Institutes of Health [Bethesda] (NIH), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), ANR-19-CE11-0026,Viral_Rhodopsins,Rhodopsines virales: Structure, Fonction, et Nouveaux Outils pour l'Optogénétique(2019), Department of Otolaryngology and Center for Molecular Physiology of the Brain-University of Göttingen - Georg-August-Universität Göttingen

    المصدر: Nature Communications
    Nature Communications, 2020, 11 (1), ⟨10.1038/s41467-020-19457-7⟩
    Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
    Nature Communications, Nature Publishing Group, 2020, 11 (1), ⟨10.1038/s41467-020-19457-7⟩
    Nature Communications 11(1), 5707 (2020). doi:10.1038/s41467-020-19457-7
    'Nature Communications ', vol: 11, pages: 5707-1-5707-16 (2020)

    مصطلحات موضوعية: 0301 basic medicine, genetic structures, Light, Protein Conformation, General Physics and Astronomy, Channelrhodopsin, 0302 clinical medicine, Protein structure, X-Ray Diffraction, Phototaxis, lcsh:Science, Cells, Cultured, Phylogeny, Neurons, Multidisciplinary, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Cell biology, Rhodopsin, ddc:500, Ion Channel Gating, Science, Optogenetics, Nucleocytoplasmic large DNA viruses, Virus-host interactions, Article, General Biochemistry, Genetics and Molecular Biology, Structure-Activity Relationship, Viral Proteins, 03 medical and health sciences, Channelrhodopsins, Phylogenetics, Cations, Animals, Humans, 14. Life underwater, Rats, Wistar, Ion transport, HEK 293 cells, fungi, General Chemistry, biology.organism_classification, HEK293 Cells, 030104 developmental biology, Phytoplankton, biology.protein, lcsh:Q, Calcium, sense organs, 030217 neurology & neurosurgery

    وصف الملف: application/pdf

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d834a22c1d45d62d39ff739a6a38a72eTest


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  7. 7
    Mechanistic Basis of the Fast Dark Recovery of the Short LOV Protein DsLOV from Dinoroseobacter shibae

    المؤلفون: Ulrich Krauss, Katrin Röllen, Thomas Drepper, Joachim Granzin, Timo Fettweiss, Stephan Endres, Oliver Reiners, Dieter Willbold, Karl-Erich Jaeger, Renu Batra-Safferling

    المصدر: Biochemistry. 57:4833-4847

    مصطلحات موضوعية: 0301 basic medicine, Light, genetic structures, Protein Conformation, Optogenetics, Crystallography, X-Ray, Photoreceptors, Microbial, 010402 general chemistry, medicine.disease_cause, 01 natural sciences, Biochemistry, 03 medical and health sciences, Protein structure, Bacterial Proteins, medicine, Rhodobacteraceae, Phototropism, Mutation, Pseudomonas putida, Chemistry, Circular Dichroism, Mutagenesis, Dinoroseobacter shibae, 0104 chemical sciences, Oxygen, Kinetics, 030104 developmental biology, Dark state, Mutagenesis, Site-Directed, Biophysics, sense organs, Function (biology), Transcription Factors

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::102a8b3c8601993a3ae36218e4d18784Test
    https://doi.org/10.1021/acs.biochem.8b00645Test


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  8. 8
    Structural Studies of Autophagy-Related Proteins

    المؤلفون: Melanie, Schwarten, Oliver H, Weiergräber, Dušan, Petrović, Birgit, Strodel, Dieter, Willbold

    المصدر: Methods in molecular biology (Clifton, N.J.). 1880

    مصطلحات موضوعية: Cryopreservation, Cryoprotective Agents, Protein Conformation, Vesicular Transport Proteins, Animals, Autophagy-Related Proteins, Humans, Molecular Dynamics Simulation, Crystallization, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Software

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=pmid________::894ba1df73e0614487465dbde87c2fa3Test
    https://pubmed.ncbi.nlm.nih.gov/30610688Test


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  9. 9
    Proline Restricts Loop I Conformation of the High Affinity WW Domain from Human Nedd4-1 to a Ligand Binding-Competent Type I β-Turn

    المؤلفون: Dieter Willbold, Andrew J. Dingley, Marianne Schulte, Stefan Freischem, Vineet Panwalkar

    المصدر: The journal of physical chemistry. B. 122(15)

    مصطلحات موضوعية: chemistry.chemical_classification, Binding Sites, biology, Proline, Stereochemistry, Protein Conformation, Nedd4 Ubiquitin Protein Ligases, NEDD4, Sequence alignment, Peptide, Molecular Dynamics Simulation, Ligand (biochemistry), Ligands, Surfaces, Coatings and Films, WW domain, Protein structure, chemistry, Materials Chemistry, biology.protein, Humans, Physical and Theoretical Chemistry, Binding site

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9ca971fd298dccabbcc776e55ea3878Test
    https://pubmed.ncbi.nlm.nih.gov/29595969Test


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  10. 10
    Structural insights into ion conduction by channelrhodopsin 2

    المؤلفون: Alexander Popov, Valentin Borshchevskiy, Oleksandr Volkov, Christian Bamann, Egor Marin, Georg Büldt, Vitaly Polovinkin, Kirill Kovalev, Dieter Willbold, Valentin Gordeliy, Ernst Bamberg, R. Astashkin, Taras Balandin

    المساهمون: Institute of Complex Systems (ICS), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association, Moscow Institute of Physics and Technology [Moscow] (MIPT), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institute of Crystallography [Aachen], Rheinisch-Westfälische Technische Hochschule Aachen (RWTH), Czech Academy of Sciences [Prague] (CAS), Max-Planck-Institut für Biophysik - Max Planck Institute of Biophysics (MPIBP), Max-Planck-Gesellschaft, European Synchrotron Radiation Facility (ESRF), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], ANR-15-CE11-0029,NEWOPTOGENETICSTOOLS,Nouveaux canaux et transporteurs régulés par la lumière pour l'optogénétique(2015), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Rheinisch-Westfälische Technische Hochschule Aachen University (RWTH)

    المصدر: Science
    Science, American Association for the Advancement of Science, 2017, 358 (6366), pp.eaan8862. ⟨10.1126/science.aan8862⟩
    Science, 2017, 358 (6366), pp.eaan8862. ⟨10.1126/science.aan8862⟩

    مصطلحات موضوعية: 0301 basic medicine, Membrane potential, Ion Transport, Multidisciplinary, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Conformation, Stereochemistry, Chemistry, Channelrhodopsin, Gating, Crystallography, X-Ray, Organelle membrane, Optogenetics, 03 medical and health sciences, 030104 developmental biology, Protein structure, Channelrhodopsins, Helix, Amino Acid Sequence, Sequence Alignment, Integral membrane protein, Chlamydomonas reinhardtii, Ion channel

    الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c267c8aee4932fde46b729457cc5fa01Test
    https://hal.archives-ouvertes.fr/hal-01685056Test


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