U
Urmi Dhagat
Researcher at St. Vincent's Institute of Medical Research
Publications - 31
Citations - 783
Urmi Dhagat is an academic researcher from St. Vincent's Institute of Medical Research. The author has contributed to research in topics: Hydroxysteroid dehydrogenase & Reductase. The author has an hindex of 13, co-authored 31 publications receiving 632 citations. Previous affiliations of Urmi Dhagat include University of Melbourne & Monash University.
Papers
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Journal ArticleDOI
The GM–CSF/IL‐3/IL‐5 cytokine receptor family: from ligand recognition to initiation of signaling
Sophie E. Broughton,Urmi Dhagat,Timothy R. Hercus,Tracy L. Nero,Michele A. Grimbaldeston,Claudine S. Bonder,Angel F. Lopez,Michael W. Parker,Michael W. Parker +8 more
TL;DR: Crystal structures of the GM–CSF receptor ternary complex and the IL‐5 binary complex have revealed new paradigms of cytokine receptor activation and provide opportunities for structure‐based approaches for the discovery of novel and disease‐specific therapeutics.
Journal ArticleDOI
Signalling by the βc family of cytokines.
Timothy R. Hercus,Urmi Dhagat,Winnie L. Kan,Sophie E. Broughton,Tracy L. Nero,Michelle Perugini,Jarrod J. Sandow,Jarrod J. Sandow,Richard J D'Andrea,Paul G Ekert,Paul G Ekert,Timothy P. Hughes,Michael W. Parker,Michael W. Parker,Angel F. Lopez +14 more
TL;DR: Characterisation of the structural and dynamic requirements for the activation of the βc receptor family and the molecular definition of downstream signalling pathways are providing new insights into cytokine receptor signalling as well as new therapeutic opportunities.
Journal ArticleDOI
The βc receptor family – Structural insights and their functional implications
Sophie E. Broughton,Tracy L. Nero,Urmi Dhagat,Winnie L. Kan,Timothy R. Hercus,Denis Tvorogov,Angel F. Lopez,Michael W. Parker +7 more
TL;DR: The crystal structures of the GM-CSF ternary complex, the IL-5 binary complex and the very recent IL-3 receptor alpha subunit build upon decades of structure-function studies, giving new insights into cytokine-receptor specificity and signal transduction.
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Dual Mechanism of Interleukin-3 Receptor Blockade by an Anti-Cancer Antibody
Sophie E. Broughton,Timothy R. Hercus,Matthew P. Hardy,Barbara J. McClure,Tracy L. Nero,Mara Dottore,Huy Huynh,Hal Braley,Emma F Barry,Winnie L. Kan,Urmi Dhagat,Pierre Scotney,Dallas Hartman,Samantha J. Busfield,Catherine M. Owczarek,Andrew D. Nash,Nicholas J. Wilson,Michael W. Parker,Michael W. Parker,Angel F. Lopez +19 more
TL;DR: The crystal structure of the IL-3 receptor α chain in complex with the anti-leukemia antibody CSL362 is reported that reveals the N-terminal domain (NTD), a domain also present in the granulocyte-macrophage colony-stimulating factor (GM-CSF), IL-5, and IL-13 receptors, adopting unique "open" and classical "closed" conformations.
Journal ArticleDOI
CSL311, a novel, potent, therapeutic monoclonal antibody for the treatment of diseases mediated by the common β chain of the IL-3, GM-CSF and IL-5 receptors.
Con Panousis,Urmi Dhagat,Kirsten Edwards,Veronika Rayzman,Matthew P. Hardy,Hal Braley,Gail M. Gauvreau,Timothy R. Hercus,Steven G. Smith,Roma Sehmi,Laura McMillan,Mara Dottore,Barbara J. McClure,Louis Fabri,Gino Vairo,Angel F. Lopez,Michael W. Parker,Andrew D. Nash,Nicholas J. Wilson,Michael J. Wilson,Catherine M. Owczarek +20 more
TL;DR: CSL311 inhibited the survival of inflammatory cells present in induced sputum from human allergic asthmatic subjects undergoing allergen bronchoprovocation and may provide a new strategy for the treatment of chronic inflammatory diseases where the human βc receptor is central to pathogenesis.