User profiles for Neil A. Ranson
 | Neil A RansonAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Verified email at leeds.ac.uk Cited by 7399 |
[HTML][HTML] An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology
Transmission electron microscopy (EM) is a versatile technique that can be used to image
biological specimens ranging from intact eukaryotic cells to individual proteins >150 kDa. …
biological specimens ranging from intact eukaryotic cells to individual proteins >150 kDa. …
A new era for understanding amyloid structures and disease
…, MP Jackson, EW Hewitt, NA Ranson… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition of …
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition of …
[HTML][HTML] ATP-bound states of GroEL captured by cryo-electron microscopy
The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one
of its two rings, priming that ring to become folding-active upon GroES binding, while …
of its two rings, priming that ring to become folding-active upon GroES binding, while …
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
…, AS Hunter, SP Wood, SG Burston, NA Ranson… - Nature, 1994 - nature.com
PROTEIN folding mediated by the molecular chaperone GroEL occurs by its binding to non-native
polypeptide substrates and is driven by ATP hydrolysis 1 . Both of these processes are …
polypeptide substrates and is driven by ATP hydrolysis 1 . Both of these processes are …
[HTML][HTML] Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM
…, AE Ashcroft, SE Radford, NA Ranson - Nature …, 2016 - nature.com
The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA–E),
which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel …
which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel …
[HTML][HTML] Amyloid structures: much more than just a cross-β fold
… We thank the Ranson and Radford laboratories especially members of our amyloid team
for many helpful discussions and comments. We acknowledge with thanks funding from the …
for many helpful discussions and comments. We acknowledge with thanks funding from the …
[HTML][HTML] Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
The chaperonin GroEL binds nonnative substrate protein in the central cavity of an open ring
through exposed hydrophobic residues at the inside aspect of the apical domains and then …
through exposed hydrophobic residues at the inside aspect of the apical domains and then …
[HTML][HTML] Approaches to altering particle distributions in cryo-electron microscopy sample preparation
Cryo-electron microscopy (cryo-EM) can now be used to determine high-resolution structural
information on a diverse range of biological specimens. Recent advances have been …
information on a diverse range of biological specimens. Recent advances have been …
Chaperonins
NA RANSON, HE WHITE, HR SAIBIL - Biochemical Journal, 1998 - portlandpress.com
The molecular chaperones are a diverse set of protein families required for the correct
folding, transport and degradation of other proteins in vivo. There has been great progress in …
folding, transport and degradation of other proteins in vivo. There has been great progress in …
[HTML][HTML] The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins
associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-…
associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-…