Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Sarah R Needham"'
Autor:
Christian Tiede, Robert Bedford, Sophie J Heseltine, Gina Smith, Imeshi Wijetunga, Rebecca Ross, Danah AlQallaf, Ashley PE Roberts, Alexander Balls, Alistair Curd, Ruth E Hughes, Heather Martin, Sarah R Needham, Laura C Zanetti-Domingues, Yashar Sadigh, Thomas P Peacock, Anna A Tang, Naomi Gibson, Hannah Kyle, Geoffrey W Platt, Nicola Ingram, Thomas Taylor, Louise P Coletta, Iain Manfield, Margaret Knowles, Sandra Bell, Filomena Esteves, Azhar Maqbool, Raj K Prasad, Mark Drinkhill, Robin S Bon, Vikesh Patel, Sarah A Goodchild, Marisa Martin-Fernandez, Ray J Owens, Joanne E Nettleship, Michael E Webb, Michael Harrison, Jonathan D Lippiat, Sreenivasan Ponnambalam, Michelle Peckham, Alastair Smith, Paul Ko Ferrigno, Matt Johnson, Michael J McPherson, Darren Charles Tomlinson
Publikováno v:
eLife, Vol 6 (2017)
Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many sh
Externí odkaz:
https://doaj.org/article/703d31dbc0f14e0190b7ae2c2e80be55
Autor:
R. Sumanth Iyer, Sarah R. Needham, Ioannis Galdadas, Benjamin M. Davis, Selene K. Roberts, Rico C. H. Man, Laura C. Zanetti-Domingues, David T. Clarke, Gilbert O. Fruhwirth, Peter J. Parker, Daniel J. Rolfe, Francesco L. Gervasio, Marisa L. Martin-Fernandez
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-21 (2024)
Abstract The Epidermal Growth Factor Receptor (EGFR) is frequently found to be mutated in non-small cell lung cancer. Oncogenic EGFR has been successfully targeted by tyrosine kinase inhibitors, but acquired drug resistance eventually overcomes the e
Externí odkaz:
https://doaj.org/article/85aaaaecf9114b44adb21e316e7276e8
Autor:
Holly. E. Smith, Alasdair M. Mackenzie, Chloe Seddon, Rhys Mould, Ifi Kalampouka, Partha Malakar, Sarah R. Needham, Konstantinos Beis, Jimmy D. Bell, Alistair Nunn, Stanley W. Botchway
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-14 (2024)
Abstract Life may be expressed as the flow of electrons, protons, and other ions, resulting in large potential difference. It is also highly photo-sensitive, as a large proportion of the redox capable molecules it relies on are chromophoric. It is th
Externí odkaz:
https://doaj.org/article/ca19fb62f5e542bfb5271897cdf078ce
Autor:
Sarah R Needham, Michael Hirsch, Daniel J Rolfe, David T Clarke, Laura C Zanetti-Domingues, Richard Wareham, Marisa L Martin-Fernandez
Publikováno v:
PLoS ONE, Vol 8, Iss 5, p e62331 (2013)
Detecting receptor dimerisation and other forms of clustering on the cell surface depends on methods capable of determining protein-protein separations with high resolution in the ~10-50 nm range. However, this distance range poses a significant chal
Externí odkaz:
https://doaj.org/article/65659914eed14992aed31154ac648a36
Autor:
Laura C Zanetti-Domingues, Marisa L Martin-Fernandez, Sarah R Needham, Daniel J Rolfe, David T Clarke
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e45655 (2012)
Single-molecule techniques are being increasingly applied to biomedical investigation, notwithstanding the numerous challenges they pose in terms of signal-to-noise ratio issues. Non-specific binding of probes to glass substrates, in particular, can
Externí odkaz:
https://doaj.org/article/081846f03e6b4b3abf132961d4777327
Autor:
Ellen Clancy, Siva Ramadurai, Sarah R. Needham, Karen Baker, Tara A. Eastwood, Julia A. Weinstein, Daniel P. Mulvihill, Stanley W. Botchway
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-15 (2023)
Abstract Cytoplasmic viscosity is a crucial parameter in determining rates of diffusion-limited reactions. Changes in viscosity are associated with several diseases, whilst nuclear viscosity determines gene integrity, regulation and expression. Yet h
Externí odkaz:
https://doaj.org/article/b8177410469a46f5968c335a1144f149
The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
Autor:
Laura C. Zanetti-Domingues, Dimitrios Korovesis, Sarah R. Needham, Christopher J. Tynan, Shiori Sagawa, Selene K. Roberts, Antonija Kuzmanic, Elena Ortiz-Zapater, Purvi Jain, Rob C. Roovers, Alireza Lajevardipour, Paul M. P. van Bergen en Henegouwen, George Santis, Andrew H. A. Clayton, David T. Clarke, Francesco L. Gervasio, Yibing Shan, David E. Shaw, Daniel J. Rolfe, Peter J. Parker, Marisa L. Martin-Fernandez
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
To prevent ligand-independent dimerisation the epidermal growth factor receptor (EGFR) is autoinhibited by an extracellular dimer interaction. Here, the authors use several imaging technologies and simulations to provide structural insights on the in
Externí odkaz:
https://doaj.org/article/d8f1227aa2394ee08a80e9812006d6b2
Autor:
Sarah R. Needham, Selene K. Roberts, Anton Arkhipov, Venkatesh P. Mysore, Christopher J. Tynan, Laura C. Zanetti-Domingues, Eric T. Kim, Valeria Losasso, Dimitrios Korovesis, Michael Hirsch, Daniel J. Rolfe, David T. Clarke, Martyn D. Winn, Alireza Lajevardipour, Andrew H. A. Clayton, Linda J. Pike, Michela Perani, Peter J. Parker, Yibing Shan, David E. Shaw, Marisa L. Martin-Fernandez
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Epidermal growth factor receptors have been shown to oligomerise upon binding to their cognate ligands. Here, the authors use biochemical, biophysical and cell biology techniques to analyse the structures of these oligomers, and argue that these form
Externí odkaz:
https://doaj.org/article/4106f1db16d64a39ab5d782e227f6e6e
Autor:
Benjamin M. Davis, Sarah R. Needham, Sumanth Iyer, Selene K. Roberts, Laura C. Zanetti Domingues, Marisa Martin-Fernandez, Daniel J. Rolfe
Publikováno v:
Biophysical Journal. 122:278a
Investigating the Structure of Epidermal Growth Factor Receptor (EGFR) Dimers and Oligomers in Cells
Autor:
Selene K. Roberts, Sarah R. Needham, Laura Zanetti Domingues, Benjamin M. Davis, Marisa L. Martin-Fernandez, Sumanth Iyer, Daniel R. Rolfe
Publikováno v:
Biophysical Journal. 120:326a-327a