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Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function
The human tripartite motif (TRIM) family comprises 70 members, including HIV restriction factor TRIM5α and disease-associated proteins TRIM20 (pyrin) and TRIM21. TRIM proteins have conserved domainExpand
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Paths reunited: Initiation of the classical and lectin pathways of complement activation.
Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since itsExpand
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Mechanism and cleavage specificity of the H-N-H endonuclease colicin E9.
Colicin endonucleases and the H-N-H family of homing enzymes share a common active site structural motif that has similarities to the active sites of a variety of other nucleases such as theExpand
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TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved
The newly identified tripartite motif (TRIM) family of proteins mediate innate immunity and other critical cellular functions. Here we show that TRIM21, which mediates the autoimmune diseasesExpand
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Activation of Human γδ T Cells by Cytosolic Interactions of BTN3A1 with Soluble Phosphoantigens and the Cytoskeletal Adaptor Periplakin
The three butyrophilin BTN3A molecules, BTN3A1, BTN3A2, and BTN3A3, are members of the B7/butyrophilin-like group of Ig superfamily receptors, which modulate the function of T cells. BTN3A1 controlsExpand
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Cytokinergic IgE Action in Mast Cell Activation
Some 10 years ago it emerged that at sufficiently high concentrations certain monoclonal mouse IgEs exert previously unsuspected effects on mast cells. Thus they can both promote survival and induceExpand
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Evolving Accelerated Amidation by SpyTag/SpyCatcher to Analyze Membrane Dynamics
Abstract SpyTag is a peptide that forms a spontaneous amide bond with its protein partner SpyCatcher. This protein superglue is a broadly useful tool for molecular assembly, locking togetherExpand
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Analogous Interactions in Initiating Complexes of the Classical and Lectin Pathways of Complement1
The classical and lectin pathways of complement activation neutralize pathogens and stimulate key immunological processes. Both pathways are initiated by collagen-containing, soluble patternExpand
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Human immunoglobulin E flexes between acutely bent and extended conformations
Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cɛ2 domain pair folded back onto the Cɛ3-Cɛ4 domains, but is theExpand
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A Fluorescent Biosensor Reveals Conformational Changes in Human Immunoglobulin E Fc
Background: Immunoglobulin E (IgE) antibodies play a role in allergic disease. Results: IgE has a bent conformation in solution that becomes more bent upon binding to the FcϵRI receptor but less bentExpand
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