0000-0002-8307-2450 About
Dr Justin E. Molloy
Professor of Biophysics
Centre for Mechanochemical Cell Biology (L1.01)
Warwick Medical School
Coventry CV4 7AL
M: +44 (0) 7986143550
E: [email protected]
W: mechanochemistry.org/Molloy/
and
Dr Justin E. Molloy
Visiting Scientist
The Francis Crick Institute
1 Midland Road
London NW1 1AT
M: +44 (0) 7986 143 550
E: [email protected]
W: https://www.crick.ac.uk/research/find-a-researcher/justin-molloy
Qualifications and history:
1983 BSc, Physiology, University of York, UK
1987 PhD Biophysics, University of York, UK
1989 NATO Post-Doctoral Fellow, University of Vermont, US
1995 Royal Society University Research Fellow & Reader in Biology, York, UK
2002 Head of Physical Biochemistry and Structural Biology,
MRC National Institute for Medical Research, London, UK
2015 Senior group leader, the Francis Crick Institute, London, UK
2022 Principal Group Leader, the Francis Crick Institute, London, UK
2022 Professor of Biophysics, Warwick Medical School, Coventry, UK
Justin trained as a biologist at the University of York, UK and went on to study the molecular mechanism of muscle contraction for his PhD. He held a NATO post-doctoral fellowship at the University of Vermont, working on the mechanical properties of insect flight muscle. He returned to the University of York where together with David White he developed optical tweezers to measure the force and movement produced by a single myosin molecule. He obtained a Royal Society University Research Fellowship and his new lab developed single molecule methods in order to study how biological molecules work both in vitro and within living cells. Justin later moved to the MRC National Institute for Medical Research and joined the Francis Crick Institute in 2015. His research team use single molecule techniques; including optical and magnetic tweezers, TIRF microscopy and atomic force microscopy to help increase our understanding of energy transduction by biological macromolecules.
Justin is Chair of the Board of Trustees for the National DeafBlind charity SENSE.
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Justin's research group studies the molecular machinery responsible for powering movement in living cells:
Layman's Version: Our muscles use chemical energy, derived from the food that we eat, in order to produce force and movement: muscles power the spectacular feats of athletes and the everyday beating of our hearts. On a microscopic scale we find that every single cell in our body is buzzing with movement and activity, much of which is generated by the same type of proteins that power our muscles, known as 'molecular motors'. These motors work by taking one molecule of fuel at a time and converting it into a tiny amount of force and movement. No man-made machine can yet rival their power and efficiency, so we want to know more about how these motors work and find out how they do various jobs inside cells. We have developed high-precision, laser based, instruments to track and manipulate individual molecules inside living cells or in test tubes, seeing how they work together with other cellular components to generate movement. Processes such as cell migration, muscle contraction, DNA copying and repair and even our hearing all rely on these motors, and they are critical for the body to function properly and healthily. They are important in very diverse forms of disease, from hearing loss and heart disease to cancer and infection by malarial parasites. By studying the fine details of molecular motors, we can understand more about how they work in healthy cells. We can also see what happens when they go wrong or are hijacked in disease, to help inform the development of new therapies.
Employment
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Education
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Publications (106)
- Dynamic phosphorylation of the Plasmodium falciparum Myosin A motor regulates motor speed and is important for asexual replication Save
- ATPγS unbiases kinesin Save
- The eduWOSM: a benchtop advanced microscope for education and research Save
- The eduWOSM: a benchtop advanced microscope for education and research Save
- The eduWOSM: a benchtop advanced microscope for education and research Save
- Hub stability in the calcium calmodulin-dependent protein kinase II Save
- Real-time single-molecule imaging of CaMKII-calmodulin interactions Save
- Single molecule dynamics in a virtual cell combining a 3-dimensional matrix model with random walks Save
- Using FRET to Determine How Myo10 Responds to Force in Filopodia Save
- Single-molecule force spectroscopy reveals binding and bridging dynamics of PARP1 and PARP2 at DNA double-strand breaks Save
- Altered Storage and Function of von Willebrand Factor in Human Cardiac Microvascular Endothelial Cells Isolated from Recipient Transplant Hearts Save
- P-selectin mobility undergoes a sol-gel transition as it diffuses from exocytosis sites into the cell membrane Save
- Efficient golden gate assembly of DNA constructs for single molecule force spectroscopy and imaging Save
- High-resolution structures of malaria parasite actomyosin and actin filaments Save
- Analysis of Plasmodium falciparum myosin B ATPase activity and structure in complex with the calmodulin-like domain of its light chain MLC-B Save
- Single-molecule measurements reveal that PARP1 condenses DNA by loop stabilization Save
- A method for imaging single molecules at the plasma membrane of live cells within tissue slices Save
- Behaviour and interactions of proteins and peptides with and within membranes; from simple models to cellular membranes: general discussion Save
- Heterogeneity of cell membrane structure studied by single molecule tracking Save
- Microfluidic flow-cell with passive flow control for microscopy applications. Save