Dr Peter Noy PhD, MSci

Dr Peter Noy

School of Biosciences
Postdoctoral Research Fellow

Contact details

School of Biosciences
University of Birmingham
B15 2TT

Dr Noy is a British Heart Foundation (BHF) funded post-doctoral fellow. He is a member of the vascular tetraspanin laboratory run by Dr Mike Tomlinson, and works with a small team of students characterising the role of tetraspanins in vascular diseases such as atherosclerosis and thrombosis. 


  • PhD Immunology
  • MSci Biochemistry and Biological Chemistry


Dr Noy studied his MSci in Biochemistry and Biological Chemistry at the University of Nottingham between 2003 and 2007. During this period he worked with Dr Eleni Stylianou on investigating the sub-nuclear localisation of the pleiotopic  transcription factor NF-kB. This work inspired Dr Noy to continue academic research.

Following the completion of his undergraduate degree he moved to the University of Birmingham to do his PhD in 2007. Here he joined the laboratory of Dr Padma-Sheela Jayaraman. This was a productive period, working on the transcription factor PRH and the regulation of the VEGF receptor axis. Dr Noy published 7 papers from his PhD work including 3 first author publications.

After the award of his doctorate in 2011, Dr Noy joined the molecular angiogenesis laboratory to work on novel tumour endothelial markers. His role was to characterise CLEC14A in normal and pathological angiogenesis. He has also undertaken some teaching roles whilst in this position.

In 2014 he moved to Biosciences to work on vascular expressed tetraspanins, such as Tspan 18, and the regulation of the molecular scissor ADAM10 by the TspanC8s. He has continued to work on angiogenesis and endothelial cell function and is now utilising CRISPR/Cas technology.


Postgraduate supervision

Dr Noy currently co-supervises one PhD student.


Vascular tetraspanins.

The Tomlinson laboratory is interested in characterising the function of poorly studied tetraspanins, primarily in endothelial cells and platelets. Tetraspanins have roles transporting, clustering and enhancing partner protein function. For example, the TspanC8 subgroup of tetraspanins facilitate surface expression of ADAM10, as well as determining ADAM10 substrate specificity.

Angiogenesis and Tumour angiogenesis targeting.

The Bicknell laboratory is interested in identifying novel genes that are elevated on tumour blood vessels. These genes are interrogated for their role in normal blood vessel function and validated as markers for tumour blood vessels. CLEC14A has been validated as one such marker.

Other activities

  • Co-organiser of the Vascular Inflammation, Thrombosis and Angiogenesis (VITA) meetings
  • STEM Ambassador
  • European Association of Cancer Research (EACR) Ambassador


Noy, P., Lodhia, P., Khan, K., Zhuang, X., Ward, D. G., Verissimo, A. R., Bacon, A., and Bicknell, R. (2015) Blocking CLEC14A-MMRN2 binding inhibits sprouting angiogenesis and tumour growth. Oncogene

Noy,P., Sawasdichai,A., Jayaraman,P.-S. and Gaston,K. (2012) Protein kinase CK2 inactivates PRH/Hhex using multiple mechanisms to de-repress VEGF-signalling genes and promote cell survival. Nucleic Acids Res, 40: 9008–9020.

Noy,P., Gaston,K. and Jayaraman,P.-S. (2012) Dasatinib inhibits leukaemic cell survival by decreasing PRH/Hhex phosphorylation resulting in increased repression of VEGF signalling genes. Leuk Res, 36: 1434–1437.

Noy,P., Williams,H., Sawasdichai,A., Gaston,K. and Jayaraman,P.-S. (2010) PRH/Hhex controls cell survival through coordinate transcriptional regulation of vascular endothelial growth factor signaling. Mol Cell Biol, 30: 2120–2134.

Wilson, E., Leszczynska, K., Poulter, N. S., Edelmann, F., Salisbury, V. A., Noy, P. J., Bacon, A., Rappoport, J. Z., Heath, J. K., Bicknell, R., and Heath, V. L. (2014) RhoJ interacts with the GIT-PIX complex and regulates focal adhesion disassembly. Journal of Cell Science 127, 3039–3051

Soufi,A., Noy,P., Buckle,M., Sawasdichai,A., Gaston,K. and Jayaraman,P.-S. (2009) CK2 phosphorylation of the PRH/Hex homeodomain functions as a reversible switch for DNA binding. Nucleic Acids Res, 37: 3288–3300.

Yusuf,D., Butland,S.L., Swanson,M.I., Bolotin,E., Ticoll,A., Cheung,W.A., Zhang,X.Y., Dickman,C.T., Fulton,D.L., Lim,J.S., et al. (2012) The Transcription Factor Encyclopedia. Genome Biol, 13: R24.