Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Nadia Tournier"'
Autor:
Lasse Stach, Emily K. H. Dinley, Nadia Tournier, Ryan P. Bingham, Darren A. Gormley, Jo L. Bramhall, Adam Taylor, Jane E. Clarkson, Katherine A. Welbeck, Claire L. Harris, Maria Feeney, Jane P. Hughes, Armin Sepp, Thil D. Batuwangala, Semra J. Kitchen, Eva-Maria Nichols
Publikováno v:
Antibodies, Vol 10, Iss 4, p 39 (2021)
The terminal pathway of complement is implicated in the pathology of multiple diseases and its inhibition is, therefore, an attractive therapeutic proposition. The practicalities of inhibiting this pathway, however, are challenging, as highlighted by
Externí odkaz:
https://doaj.org/article/9c08d3afb4f34afc913b99f6d81d4c48
Autor:
Jane E Clarkson, Nadia Tournier, Ryan P. Bingham, Maria Feeney, Semra Kitchen, Jo L Bramhall, Darren A. Gormley, Lasse Stach, Eva-Maria Nichols, Jane P. Hughes, Katherine A Welbeck, Claire L. Harris, Adam Taylor, Armin Sepp, Thil D. Batuwangala, Emily K H Dinley
Publikováno v:
Antibodies, Vol 10, Iss 39, p 39 (2021)
Antibodies
Volume 10
Issue 4
Antibodies
Volume 10
Issue 4
The terminal pathway of complement is implicated in the pathology of multiple diseases and its inhibition is, therefore, an attractive therapeutic proposition. The practicalities of inhibiting this pathway, however, are challenging, as highlighted by
Publikováno v:
SLAS technology. 24(3)
The discovery of new medicines has become increasingly more challenging and requires significant collaboration between pharma, biotech, academia, and technology to be successful. These partnerships necessitate the streamlined exchange of samples whil
Autor:
Manish Burman, Chi-Man Tang, Gavin C. Jones, Chun-wa Chung, Thil Batuwangala, Michael J. Mullin, Vicky Chung, Nadia Tournier, Ian Richard Catchpole, Justyna Korczynska, Michael Steward, Margarete Neu, Adam K. Walker, Alan S. Lewis
Publikováno v:
The Journal of Biological Chemistry
A potent VEGF inhibitor with novel antibody architecture and antigen binding mode has been developed. The molecule, hereafter referred to as VEGF dual dAb (domain antibody), was evaluated in vitro for binding to VEGF and for potency in VEGF-driven mo