Christian Siebold (0000-0002-6635-3621)

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I am a full Professor at the University of Oxford, UK. Research in my group is focused on the molecular mechanisms of morphogen signalling, using structural, biochemical and cellular methods. I completed my Diploma in Chemistry majoring in Biochemistry (BSc and MSc) at the Albert-Ludwigs-University Freiburg, Germany, and received a PhD from the University of Bern, Switzerland, in Structural Biology and Biochemistry. This was followed by postdoctoral training, a Wellcome Trust-funded Research Career Development Fellowship and a CRUK-funded Senior Research Fellowship focusing on the structural biology of human cell surface receptor and morphogen signalling at the University of Oxford.

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University of Oxford: Oxford, Oxfordshire, GB

2012-10-01 to present | Professor of Structural Biology, Cancer Research UK Research Fellow, ERC Consolidator Grant Holder (Division of Structural Biology, Wellcome Centre for Human Genetics)

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Christian Siebold

https://orcid.org/0000-0002-6635-3621

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Employment (3)

University of Oxford: Oxford, Oxfordshire, GB

University of Oxford: Oxford, Oxfordshire, GB

University of Oxford: Oxford, Oxfordshire, GB

Education and qualifications (2)

University of Bern: Bern, Bern, CH

Albert-Ludwigs-Universität Freiburg: Freiburg im Breisgau, Baden-Württemberg, DE

Works (50 of 55)

LipIDens: Simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins

Patched 1 regulates Smoothened by controlling sterol binding to its extracellular cysteine-rich domain.

Hedgehog-Interacting Protein is a multimodal antagonist of Hedgehog signalling.

Structure, mechanism, and inhibition of Hedgehog acyltransferase.

Patched 1 reduces the accessibility of cholesterol in the outer leaflet of membranes.

Relative Affinities of Protein-Cholesterol Interactions from Equilibrium Molecular Dynamics Simulations.

Structure and function of the ROR2 cysteine-rich domain in vertebrate noncanonical WNT5A signaling

Photochemical Probe Identification of a Small-Molecule Inhibitor Binding Site in Hedgehog Acyltransferase (HHAT)*.

Simultaneous binding of Guidance Cues NET1 and RGM blocks extracellular NEO1 signaling.

Cholesterol access in cellular membranes controls Hedgehog signaling.

Glypicans shield the Wnt lipid moiety to enable signalling at a distance.

Repulsive guidance molecules lock growth differentiation factor 5 in an inhibitory complex.

R-spondins engage heparan sulfate proteoglycans to potentiate WNT signaling.

Cholesterol accessibility at the ciliary membrane controls hedgehog signaling.

The morphogen Sonic hedgehog inhibits its receptor Patched by a pincer grasp mechanism.

Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning.

iASPP mediates p53 selectivity through a modular mechanism fine-tuning DNA recognition.

Acylation-coupled lipophilic induction of polarisation (Acyl-cLIP): a universal assay for lipid transferase and hydrolase enzymes.

Structures of vertebrate Patched and Smoothened reveal intimate links between cholesterol and Hedgehog signalling.

Robin Hood: non-fitting, non-smoothing image detrending for bleaching correction

Biochemical mechanisms of vertebrate hedgehog signaling.

A calcium-sensing receptor mutation causing hypocalcemia disrupts a transmembrane salt bridge to activate β-arrestin-biased signaling

Calcium-sensing receptor residues with loss- and gain-of-function mutations are located in regions of conformational change and cause signalling bias

Calibration-free in vitro quantification of protein homo-oligomerization using commercial instrumentation and free, open source brightness analysis software

Cilia-Associated Oxysterols Activate Smoothened

Cholesterol Interaction Sites on the Transmembrane Domain of the Hedgehog Signal Transducer and Class F G Protein-Coupled Receptor Smoothened.

Lentiviral transduction of mammalian cells for fast, scalable and high-level production of soluble and membrane proteins.

Multiple ligand binding sites regulate the Hedgehog signal transducer Smoothened in vertebrates.

RGMs: Structural Insights, Molecular Regulation, and Downstream Signaling.

Restoring p53 Function in Human Melanoma Cells by Inhibiting MDM2 and Cyclin B1/CDK1-Phosphorylated Nuclear iASPP.

Cholesterol activates the G-protein coupled receptor Smoothened to promote Hedgehog signaling.

Structural basis for integration of GluD receptors within synaptic organizer complexes.

Structural basis of Smoothened regulation by its extracellular domains.

Initiation of T cell signaling by CD45 segregation at 'close contacts'.

Lrig2 Negatively Regulates Ectodomain Shedding of Axon Guidance Receptors by ADAM Proteases.

Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein.

Secreted HHIP1 interacts with heparan sulfate and regulates Hedgehog ligand localization and function.

Structure and function of the Smoothened extracellular domain in vertebrate Hedgehog signaling

Structural insights into proteoglycan-shaped Hedgehog signaling.

Structure and function of the Smoothened extracellular domain in vertebrate Hedgehog signaling.

Structure of the repulsive guidance molecule (RGM)-neogenin signaling hub.

Restoring p53 function in human melanoma cells by inhibiting MDM2 and cyclin B1/CDK1-phosphorylated nuclear iASPP.

Structural insights into semaphorins and their receptors.

Neuropilins lock secreted semaphorins onto plexins in a ternary signaling complex.

Structural and functional studies of LRP6 ectodomain reveal a platform for Wnt signaling.

A dual binding mode for RhoGTPases in plexin signalling.

Automation of large scale transient protein expression in mammalian cells.

Recording information on protein complexes in an information management system.

Modular mechanism of Wnt signaling inhibition by Wnt inhibitory factor 1.

Structure of HLA-A*0301 in complex with a peptide of proteolipid protein: insights into the role of HLA-A alleles in susceptibility to multiple sclerosis.