Frank Gabel
Gabel, Frank, 1974-...., auteur(e) en biophysique
Gabel, Frank 1974-...
VIAF ID: 217205183 (Personal)
Permalink: http://viaf.org/viaf/217205183
Preferred Forms
4xx's: Alternate Name Forms (2)
Works
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Activity and molecular dynamics relationship within the family of human cholinesterases |
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Amphipols from A to Z. |
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Applications of SANS to Study Membrane Protein Systems. |
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Assembly and maturation of the bacteriophage T5 capsid : analysis of the expansion and decoration processes. |
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Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA. |
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Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway |
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Characterization of the elongasome core PBP2 : MreC complex of Helicobacter pylori |
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Chemical Shift Backbone Assignments of TAP-N, the 31 kDa Cargo-binding Region of the Protein TAP |
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Conformational states of a bacterial α2-macroglobulin resemble those of human complement C3. |
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Dynamic Flexibility of Double-stranded RNA Activated PKR in Solution |
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Dynamics of hydration water in deuterated purple membranes explored by neutron scattering |
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The effect of solvent composition, inhibition, and structure on cholinesterase molecular dynamics : a neutron scattering study. |
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Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii. |
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Elucidating the activation mechanism of the transcription factor DntR using X-ray crystallography and small angle X- ray scattering |
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Etude de la structure et du mécanisme d'action du complexe unfoldase PAN, un activateur du protéasome 20S |
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Étude du mécanisme d'action du protéasome PAN-20S par diffusion de neutrons aux petits angles résolue en temps |
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From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity. |
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity |
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Intrinsic disorder in measles virus nucleocapsids. |
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Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains |
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Low-resolution structure of vaccinia virus DNA replication machinery |
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The low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations. |
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Medical contrast media as possible tools for SAXS contrast variation |
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Modulation of structure and dynamics by disulfide bond formation in unfolded states. |
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Molecular adaptation and salt stress response of Halobacterium salinarum cells revealed by neutron spectroscopy |
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Molecular recognition of ubiquitin and Lysine 63 linked diubiquitin by STAM2 : the effect of the linkers length and flexibility |
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Neutron scattering: a tool to detect in vivo thermal stress effects at the molecular dynamics level in micro-organisms. |
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Neutron scattering in the biological sciences: progress and prospects |
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Neutron scattering reveals extremely slow cell water in a Dead Sea organism |
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Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure. |
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On the quest for the elusive mechanism of action of daptomycin: Binding, fusion, and oligomerization |
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Phénomènes dynamiques d'auto-assemblage et de désassemblage dans des virus icosaédriques. |
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Probing the conformation of FhaC with small-angle neutron scattering and molecular modeling. |
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Protein dynamics in solution and powder measured by incoherent elastic neutron scattering: the influence of Q-range and energy resolution |
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La reconnaissance de l'ubiquitine et de la diubiquitine Lysine 63 par la protéine STAM2 : l'effet de la longueur et de la flexibilité des linkers. |
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SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell |
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Self-assembly and disassembly dynamical phenomena in icosahedral viruses. |
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Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data |
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A simple procedure to evaluate the efficiency of bio-macromolecular rigid-body refinement by small-angle scattering. |
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Small-Angle Neutron Scattering for Structural Biology of Protein-RNA Complexes. |
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Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase. |
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The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic Archaea |
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Structural basis for the assembly of the Sxl-Unr translation regulatory complex |
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Structural, dynamical and functional study of the proteasome activating complex (PAN). |
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Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN+ Proteases. |
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The structure of the box C/D enzyme reveals regulation of RNA methylation |
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Structure of the K-turn U4 RNA: a combined NMR and SANS study |
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A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints |
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Study of large proteolytic assembly of the TET family : oligomerization process and associated functional regulation. |
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Study of the proteasome PAN-20S mechanism of action by time resolved small angle neutron scattering. |
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TET peptidases: A family of tetrahedral complexes conserved in prokaryotes. |
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Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase |
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Transient Electrostatic Interactions Dominate the Conformational Equilibrium Sampled by Multidomain Splicing Factor U2AF65: A Combined NMR and SAXS Study |
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Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins |
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Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints. |
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