Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Thomas P. J. Garrett"'
Autor:
Thomas P. J. Garrett, Nicos A. Nicola, Priscilla Soo, Yibin Xu, Francesca Walker, Chin Wee Tan, Timothy E. Adams, Nicholas T. Redpath, Antony W. Burgess, Hui Hua Zhang, Jian-Guo Zhang
Publikováno v:
Journal of Molecular Biology. 427:1934-1948
We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6408a59a1629d1ec0f7db83262fa95d
https://doi.org/10.1016/j.jmb.2015.03.001
https://doi.org/10.1016/j.jmb.2015.03.001
Autor:
Thomas P. J. Garrett, Douglas J. Hilton, Priscilla Soo, Michael J. Pocock, Yibin Xu, Jian-Guo Zhang, Nicos A. Nicola, Nadia J. Kershaw, Cindy S. Luo, Peter E. Czabotar
Publikováno v:
Journal of Biological Chemistry. 285:21214-21218
gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines. Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba549bc590d4d0a506466fa6c2cef2d6
https://doi.org/10.1074/jbc.c110.129502
https://doi.org/10.1074/jbc.c110.129502
Autor:
Webster K. Cavenee, Dane Wittrup, Ginger Chao, Anthony W Burgess, Gerd Ritter, Andrew M. Scott, Timothy E. Adams, Mezhen Lou, Bruno Catimel, Elisabeth Stockert, Thomas P. J. Garrett, Peter A. Hoyne, Rodney B. Luwor, Shenggen Yao, Francesca Walker, Edouard C. Nice, Lloyd J. Old, Jennifer R. Cochran, Julie Rothacker, Suzanne G Orchard, Trevor Huyton, W. Douglas Fairlie, Glenn A Cartwright, Andrew H. A. Clayton, Cindy S. Luo, Yibin Xu, Terrance Grant Johns, Hui K Gan
Publikováno v:
Proceedings of the National Academy of Sciences. 106:5082-5087
Epidermal Growth Factor Receptor (EGFR) is involved in stimulating the growth of many human tumors, but the success of therapeutic agents has been limited in part by interference from the EGFR on normal tissues. Previously, we reported an antibody (m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ce01a0861ee98c2cd87a7c48ae03217
https://doi.org/10.1073/pnas.0811559106
https://doi.org/10.1073/pnas.0811559106
Autor:
Colin W. Ward, Robert N. Jorissen, Thomas P. J. Garrett, Vidanagamage Chandana Epa, Antony W. Burgess, Herbert R. Treutlein
Publikováno v:
Protein Science. 9:310-324
The Epidermal Growth Factor (EGF) receptor is a tyrosine kinase that mediates the biological effects of ligands such as EGF and transforming growth factor alpha. An understanding of the molecular basis of its action has been hindered by a lack of str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e1a06c0b53c32b1aabe75457300b529
https://doi.org/10.1110/ps.9.2.310
https://doi.org/10.1110/ps.9.2.310
Autor:
Colin W. Ward, Thomas P. J. Garrett, Timothy E. Adams, Victor A. Streltsov, Michael C. Lawrence, Meizhen Lou, Neil M. McKern, George O. Lovrecz
Publikováno v:
Acta Physiologica. 192:3-9
The current model for insulin binding to the insulin receptor proposes that there are two binding sites, referred to as sites 1 and 2, on each monomer in the receptor homodimer and two binding surfaces on insulin, one involving residues predominantly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::469bf7dc0f276bcf822543ebc93363a1
https://doi.org/10.1111/j.1748-1716.2007.01781.x
https://doi.org/10.1111/j.1748-1716.2007.01781.x
Autor:
Jennifer L. McKimm-Breschkin, Nikolaos E. Labrou, Cindy S. Luo, Trevor Huyton, Mei Zhen Lou, Thomas P. J. Garrett, Brian J. Smith, Jian-Guo Zhang, Robbie P. Joosten
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:947-952
The X-ray structure of influenza virus neuraminidase (NA) isolated from whale, subtype N9, has been determined at 2.2 A resolution and contains a tetrameric protein in the asymmetric unit. In structures of NA determined previously, a calcium ion is o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::701a14098691b0819714f11bb7ca265c
https://doi.org/10.1107/s0907444906020063
https://doi.org/10.1107/s0907444906020063
Autor:
Thomas P. J. Garrett, Peter A. Hoyne, Leah J. Cosgrove, Colin W. Ward, Neil M. McKern, M. J. Frenkel, George O. Lovrecz, John D. Bentley, Meizhen Lou, V. Chandana Epa
Publikováno v:
Proceedings of the National Academy of Sciences. 103:12429-12434
The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity. Here we report the crystal structure of the first three domains (L1–CR–
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f7319cfa62520b71edfbb6d82c78449
https://doi.org/10.1073/pnas.0605395103
https://doi.org/10.1073/pnas.0605395103
Autor:
Antony W. Burgess, Hyun Soo Cho, Charles Eigenbrot, Mark X. Sliwkowski, Kathryn M. Ferguson, Mark A. Lemmon, Colin W. Ward, Thomas P. J. Garrett, Shigeyuki Yokoyama, Daniel J. Leahy
Publikováno v:
Molecular Cell. 12:541-552
Recent crystallographic studies have provided significant new insight into how receptor tyrosine kinases from the EGF receptor or ErbB family are regulated by their growth factor ligands. EGF receptor dimerization is mediated by a unique dimerization
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25c01f1eee7030a5ea27d505ee7af3f0
https://doi.org/10.1016/s1097-2765(03)00350-2
https://doi.org/10.1016/s1097-2765(03)00350-2
Autor:
Normand Pouliot, Colin W. Ward, Thomas P. J. Garrett, Antony W. Burgess, Robert N. Jorissen, Francesca Walker
Publikováno v:
Experimental Cell Research. 284:31-53
The epidermal growth factor (EGF) receptor (EGFR) is one of four homologous transmembrane proteins that mediate the actions of a family of growth factors including EGF, transforming growth factor-alpha, and the neuregulins. We review the structure an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8410166fb8f33289f03f656d57c6a86
https://doi.org/10.1016/s0014-4827(02)00098-8
https://doi.org/10.1016/s0014-4827(02)00098-8
Autor:
Colin W. Ward, T. C. Elleman, Morry J. Frenkel, Francesca Walker, Hong-Jian Zhu, Edouard C. Nice, George O. Lovrecz, Antony W. Burgess, Robert N. Jorissen, Thomas P. J. Garrett, Neil M. McKern, Timothy E. Adams, Meizhen Lou, Peter A. Hoyne
Publikováno v:
Cell. 110:763-773
We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2bbb4000c9c4df0d767dcc0bffb5b19
https://doi.org/10.1016/s0092-8674(02)00940-6
https://doi.org/10.1016/s0092-8674(02)00940-6