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Alexander V. Shkumatov
Researcher at Vrije Universiteit Brussel
Publications - 35
Citations - 2593
Alexander V. Shkumatov is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Protein structure & Ligand (biochemistry). The author has an hindex of 19, co-authored 31 publications receiving 2324 citations. Previous affiliations of Alexander V. Shkumatov include Harvard University & University of York.
Papers
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Journal ArticleDOI
New developments in the ATSAS program package for small-angle scattering data analysis
Maxim V. Petoukhov,Daniel Franke,Alexander V. Shkumatov,Giancarlo Tria,Alexey Kikhney,Michal J. Gajda,Christian Gorba,Haydyn D. T. Mertens,Petr V. Konarev,Dmitri I. Svergun +9 more
TL;DR: The paper presents new developments and amendments to the ATSAS package (version 2.4) for processing and analysis of isotropic small-angle scattering data.
Journal ArticleDOI
Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
Kenneth Verstraete,Gonzalez Vandriessche,Mariska Januar,Jonathan Elegheert,Alexander V. Shkumatov,Ambroise Desfosses,Kathleen Van Craenenbroeck,Dmitri I. Svergun,Irina Gutsche,Bjorn Vergauwen,Savvas N. Savvides +10 more
TL;DR: The structural basis for the Flt3 ligand-receptor complex is reported and an unanticipated extracellular assembly unlike any other RTKIII/V complex characterized to date is unveiled, suggesting that the high-affinity Flt:FL complex is driven in part by a single preformed binding epitope on FL reminiscent of a "lock-and-key" binding mode, thereby setting the stage for antagonist design.
Journal ArticleDOI
Ligand-Binding Properties and Conformational Dynamics of Autolysin Repeat Domains in Staphylococcal Cell Wall Recognition
Sebastian Zoll,Martin Schlag,Alexander V. Shkumatov,Maren Rautenberg,Dmitri I. Svergun,Friedrich Götz,Thilo Stehle,Thilo Stehle +7 more
TL;DR: The crystal structure of R2 is determined, which reveals that each repeat folds into two half-open β-barrel subunits, which supports a model in which the repeats direct the catalytic AM domain to the septum, where it can optimally perform the final step of cell division.
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Human IL-34 and CSF-1 Establish Structurally Similar Extracellular Assemblies with Their Common Hematopoietic Receptor
Jan Felix,Jonathan Elegheert,Irina Gutsche,Alexander V. Shkumatov,Yurong Wen,Nathalie Bracke,Erwin Pannecoucke,Isabel Vandenberghe,Bart Devreese,Dmitri I. Svergun,Ewald Pauwels,Bjorn Vergauwen,Savvas N. Savvides +12 more
TL;DR: It is revealed that bivalent binding of human IL-34 to CSF-1R leads to an extracellular assembly hallmarked by striking similarities to the CSF -1:CSF- 1R complex, including homotypic receptor-receptor interactions.
Journal ArticleDOI
Tardigrade workbench: comparing stress-related proteins, sequence-similar and functional protein clusters as well as RNA elements in tardigrades.
Frank Förster,Chunguang Liang,Alexander V. Shkumatov,Daniela Beisser,Julia C. Engelmann,Martina Schnölzer,Marcus Frohme,Tobias Müller,Ralph O. Schill,Thomas Dandekar +9 more
TL;DR: Different protein clusters and regulatory elements implicated in tardigrade stress adaptations are analysed including unpublished tardigade sequences.