The LMB is responsible for many pioneering techniques, such as methods for determining the three-dimensional structures of proteins and other macromolecules, the sequencing of DNA and the development of monoclonal antibodies.
Our scientists tackle difficult, long-term research problems. At the same time they are encouraged to exploit their discoveries – through patents, licensing and business start-ups – helping to advance medical research and improve the UK’s economic competitiveness.
A research team from the LMB’s Cell Biology division, working with colleagues from the Structural Studies division, has revealed how cells are able to find and tag for degradation the partially synthesised proteins generated when ribosomes occasionally stall. Cells make more than a hundred thousand new proteins every minute. Once in a while, one of…
When a bacterial cell divides, the cell membrane and cell envelope have to pinch together in the middle of the cell to separate it into two daughter cells. A ring of proteins called the divisome constricts, cleaving the cell in two. The protein FtsZ is a crucial component of this ring and many FtsZ subunits…
- LMB science portrayed in art: ‘Lens on Life’ exhibition in London
Works of art that resulted from unique collaborations between artists and scientists, including LMB group […]
- Melina Schuh awarded the EMBL Alumni John Kendrew Award 2015
Melina Schuh, from the LMB’s Cell Biology Division, has been awarded the EMBL Alumni John […]
- Michel Goedert awarded the 2014 European Grand Prix for Research
Michel Goedert, Joint Head of the LMB’s Neurobiology Division, has been awarded the European Grand […]
- LMB raises over £1,200 for “Mind in Cambridgeshire”
Staff at the LMB have raised over £1,200 from their annual charity fundraiser for Mind […]
- Genome3D: exploiting structure to help users understand their sequences.
Lewis, TE., et al.
Nucleic Acids Res. 43(Database issue): D382-6. (28th January 2015)
- Mechanosensory molecules and circuits in C. elegans.
Pflugers Arch. 467(1): 39-48. (23rd January 2015)
- Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface.
Aibara, S., Valkov, E., Lamers, M., Stewart, M.
Nucleic Acids Res. [Epub ahead of print]. (23rd January 2015)
- Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis.
Renard, HF., et al.
Nature 517(7535): 493-6. (22nd January 2015)
- Endophilin marks and controls a clathrin-independent endocytic pathway.
Boucrot, E., et al.
Nature 517(7535): 460-5. (22nd January 2015)
See more Publications