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Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
Microtubules are cytoskeletal polymers of tubulin involved in many cellular functions. Their dynamic instability is controlled by numerous compounds and proteins, including colchicine and stathminExpand
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Fusion mutants of the influenza virus hemagglutinin glycoprotein
The influenza virus hemagglutinin (HA) mediates viral entry into cells by a low pH induced membrane-fusion event in endosomal vesicles. Mutant viruses with altered pH dependence for both hemolysisExpand
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Structural basis for the regulation of tubulin by vinblastine
Vinblastine is one of several tubulin-targeting Vinca alkaloids that have been responsible for many chemotherapeutic successes since their introduction in the clinic as antitumour drugs. In contrastExpand
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Structure of a kinesin–tubulin complex and implications for kinesin motility
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of theExpand
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Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
HAEMAGGLUTININ (HA) is the influenza surface glycoprotein that interacts with infectivity-neutralizing antibodies. As a consequence of this immune pressure, it is the variable virus component, whichExpand
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Variations in the colchicine-binding domain provide insight into the structural switch of tubulin
Structural changes occur in the αβ-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to aExpand
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A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody.
A single amino acid substitution, Asp-63 to Asn-63, was detected in the hemagglutinin of an antigenic variant of the 1968 Hong Kong (H3) influenza virus that was selected by growth of the wild-typeExpand
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The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin.
Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to αβ-tubulin is required for microtubule assembly, but whether this triggers conversionExpand
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The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement.
Kinesin-1 is a dimeric ATP-dependent motor protein that moves towards microtubules (+) ends. This movement is driven by two conformations (docked and undocked) of the two motor domainsExpand
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The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex
Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with theExpand
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