T
Thomas P. J. Garrett
Researcher at Walter and Eliza Hall Institute of Medical Research
Publications - 42
Citations - 6553
Thomas P. J. Garrett is an academic researcher from Walter and Eliza Hall Institute of Medical Research. The author has contributed to research in topics: Growth factor receptor & Ectodomain. The author has an hindex of 27, co-authored 42 publications receiving 6289 citations. Previous affiliations of Thomas P. J. Garrett include Cooperative Research Centre & Royal Melbourne Hospital.
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Journal ArticleDOI
Epidermal growth factor receptor: mechanisms of activation and signalling.
Robert N. Jorissen,Francesca Walker,Francesca Walker,Normand Pouliot,Thomas P. J. Garrett,Thomas P. J. Garrett,Colin W. Ward,Colin W. Ward,Antony W. Burgess,Antony W. Burgess +9 more
TL;DR: The structure and function of the EGFR is reviewed, from ligand binding to the initiation of intracellular signalling pathways that lead to changes in the biochemical state of the cell.
Journal ArticleDOI
An Open-and-Shut Case? Recent Insights into the Activation of EGF/ErbB Receptors
Antony W. Burgess,Hyun Soo Cho,Hyun Soo Cho,Charles Eigenbrot,Kathryn M. Ferguson,Thomas P. J. Garrett,Thomas P. J. Garrett,Daniel J. Leahy,Mark A. Lemmon,Mark X. Sliwkowski,Colin W. Ward,Colin W. Ward,Shigeyuki Yokoyama +12 more
TL;DR: A mechanistic view of ErbB receptor homo- and heterodimerization is outlined, which suggests new approaches for interfering with these processes when they are implicated in human cancers.
Journal ArticleDOI
Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor α
Thomas P. J. Garrett,Thomas P. J. Garrett,Neil M. McKern,Neil M. McKern,Meizhen Lou,Meizhen Lou,T. C. Elleman,Timothy E. Adams,Timothy E. Adams,George O. Lovrecz,George O. Lovrecz,Hong-Jian Zhu,Hong-Jian Zhu,Francesca Walker,Francesca Walker,Morry J. Frenkel,Morry J. Frenkel,Peter A. Hoyne,Peter A. Hoyne,Robert N. Jorissen,Robert N. Jorissen,Edouard C. Nice,Edouard C. Nice,Antony W. Burgess,Antony W. Burgess,Colin W. Ward,Colin W. Ward +26 more
TL;DR: The results indicate how EGFR family members can bind a family of highly variable ligands and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
Journal ArticleDOI
The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors.
Thomas P. J. Garrett,Thomas P. J. Garrett,Neil M. McKern,Meizhen Lou,Meizhen Lou,T. C. Elleman,Timothy E. Adams,Timothy E. Adams,George O. Lovrecz,George O. Lovrecz,Michael Kofler,Robert N. Jorissen,Robert N. Jorissen,Edouard C. Nice,Edouard C. Nice,Antony W. Burgess,Antony W. Burgess,Colin W. Ward,Colin W. Ward +18 more
TL;DR: The crystal structure of residues 1-509 of ErbB2 reveals an activated conformation similar to that of the EGFR when complexed with ligand and very different from that seen in the unactivated forms ofErbB3 or EGFR.
Journal ArticleDOI
A binding site for the T-cell co-receptor CD8 on the alpha 3 domain of HLA-A2.
Russell D. Salter,Richard J. Benjamin,Pamela K. Wesley,Sarah E. Buxton,Thomas P. J. Garrett,Carol Clayberger,Alan M. Krensky,Anne M. Norment,Dan R. Littman,Peter Parham +9 more
TL;DR: Adhesion measurements between CD8 and 48 point mutants of HLA-A2.1 have shown that the CD8 alpha-chain binds to the alpha 3 domain of the protein-protein interaction as mentioned in this paper.