LMB In The News


BBC: Daytime wounds ‘heal more quickly’

A new study led by John O’Neill and Ned Hoyle shows how bodyclocks in skin cells influence wound healing. More…

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Using cryo-EM to solve the structure of a protein complex critical for gene expression

Lori Passmore and her group have used electron cryo-microscopy to solve the structure of CPF, a protein complex critical for gene expression. Understanding the structure and function of intact CPF, and how it is assembled, has been a central question in the field of gene expression for decades. More…

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PINK1 caught on the brink of phosphorylation

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Scientists have caught a rare view of an unusual kinase poised to phosphorylate its substrate. Led by David Komander, MRC Laboratory of Molecular Biology in Cambridge, England, U.K., the researchers reported the crystal structure of the kinase PINK1 bound to ubiquitin in the October 30 Nature.  “We captured a pre-catalytic state, a snapshot of PINK1 holding ubiquitin before the phosphate group jumps on,” said first author Alexander Schubert. More…

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Fundamental rules for how the brain controls movements

Using the nematode as one test system, scientists at CCNR have spent the past several years understanding how a network controls itself—for instance, which individual neurons in the worm’s brain are in charge of a backward wiggle. In research published in Nature, they describe for the first time their ability to predict, test, and confirm with unprecedented detail how a nematode’s brain controls the way it moves.  Colleagues from Bill Schafer’s group at the LMB tested the predictions by killing individual neurons from the nematode brain with a laser.  They then measured the effects of these “microsurgeries” on behaviour. More…

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Researchers “drug the undruggable”

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A new approach to targeting key cancer-linked proteins, thought to be ‘undruggable’, has been discovered through an alliance between industry and academia created by Cancer Research UK.  David Komander’s group in the LMB is one of the groups involved in this unique collaboration, that shows that two novel and specific small-molecule inhibitors developed by the alliance can bind to and deactivate an enzyme that controls the stability of the p53 tumour suppressor protein. This deactivation allows p53 to be turned on, putting the brakes on cancer growth. More…

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The birth of the cool

Super cool microscopy wins the 2017 Nobel prize in chemistry: includes interview with LMB’s Richard Henderson. More…

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Electron cryo-microscopy wins chemistry Nobel

Jacques Dubochet, Joachim Frank and Richard Henderson were awarded the prize on 4 October for their work in developing electron cryo-microscopy (cryo-EM), a technique that fires beams of electrons at proteins that have been frozen in solution, to deduce the biomolecules’ structure. More…

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Richard Henderson shares 2017 Nobel Prize in Chemistry

The Nobel prize in chemistry has been awarded to three scientists, Jacques Dubochet, Joachim Frank and the LMB’s Richard Henderson, for developing a technique to produce images of the molecules of life frozen in time.  The technique, called cryo-electron microscopy, allowed biomolecules to be visualised in their natural configuration for the first time, triggering a “revolution in biochemistry”, according to the Nobel committee. The latest versions of the technology mean scientists can record biochemical processes as they unfold in film-like sequences. More…

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Leprosy turns the immune system against itself

An international team of scientists, including Lalita Ramakrishnan’s group in the University of Cambridge Molecular Immunity Unit, based at the LMB, have discovered that Leprosy hijacks our immune system, turning an important repair mechanism into one that causes potentially irreparable damage to our nerve cells. More…

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Protein localization inside cells

Ramanujan Hegde talks about protein localization inside cells and quality control of this process. More…

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