Mapping of the ligand-binding site on the b′ domain of human PDI: interaction with peptide ligands and the x-linker region
LJ Byrne, A Sidhu, AK Wallis, LW Ruddock… - Biochemical …, 2009 - portlandpress.com
… Ateesh Sidhu and Katrine Wallis expressed, purified and … , and Lee Byrne, Katrine Wallis
and Ateesh Sidhu assigned … , Richard Williamson and Katrine Wallis generated the Figures, …
and Ateesh Sidhu assigned … , Richard Williamson and Katrine Wallis generated the Figures, …
[HTML][HTML] Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome
…, T Yoshizaki, K Ohtani, JE Marshall, AK Wallis… - BMC biology, 2015 - Springer
Background Collectin-K1 (CL-K1, or CL-11) is a multifunctional Ca 2+ -dependent lectin
with roles in innate immunity, apoptosis and embryogenesis. It binds to carbohydrates on …
with roles in innate immunity, apoptosis and embryogenesis. It binds to carbohydrates on …
[HTML][HTML] Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance
Protein disulfide isomerase (PDI), which consists of multiple domains arranged as abb′xa′c,
is a key enzyme responsible for oxidative folding in the endoplasmic reticulum. In this …
is a key enzyme responsible for oxidative folding in the endoplasmic reticulum. In this …
'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)
…, MJ Howard, N Sanghera, KL Walker, AK Wallis… - … et Biophysica Acta (BBA …, 2017 - Elsevier
Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as
catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular …
catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular …
[HTML][HTML] Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway
AG Irvine, AK Wallis, N Sanghera, ML Rowe… - PloS one, 2014 - journals.plos.org
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein
disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (…
disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (…
[HTML][HTML] Flexibility and mobility of SARS-CoV-2-related protein structures
RA Römer, NS Römer, AK Wallis - Scientific Reports, 2021 - nature.com
The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of
the scientific community to develop a potent antiviral drug and vaccine as soon as possible. …
the scientific community to develop a potent antiviral drug and vaccine as soon as possible. …
Assisting oxidative protein folding: how do protein disulphide-isomerases couple conformational and chemical processes in protein folding?
AK Wallis, RB Freedman - Molecular Chaperones, 2013 - Springer
Oxidative folding is the simultaneous process of forming disulphide bonds and native
structure in proteins. Pathways of oxidative folding are highly diverse and in eukaryotes are …
structure in proteins. Pathways of oxidative folding are highly diverse and in eukaryotes are …
High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility
NT Amin, AK Wallis, SA Wells, ML Rowe… - Biochemical …, 2013 - portlandpress.com
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase)
localized to the endoplasmic reticulum. ERp27 is predicted to consist of two …
localized to the endoplasmic reticulum. ERp27 is predicted to consist of two …
[HTML][HTML] Sex-specific effects of dietary methionine restriction on the intestinal microbiome
KF Wallis, SB Melnyk, IR Miousse - Nutrients, 2020 - mdpi.com
Dietary methionine restriction is associated with improved health outcomes and an increase
in lifespan in animal models. We have previously shown that an increase in dietary …
in lifespan in animal models. We have previously shown that an increase in dietary …
Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b'domain
VD Nguyen, K Wallis, MJ Howard… - Journal of molecular …, 2008 - Elsevier
Protein disulphide isomerase (PDI) is a key multi-domain protein folding catalyst in the
endoplasmic reticulum. The b’ domain of PDI is essential for the non-covalent binding of …
endoplasmic reticulum. The b’ domain of PDI is essential for the non-covalent binding of …