Associated Papers
Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis.
Karimi-Farsijani S et al.
Nature Communications, 2024
First Report of Lysozyme Amyloidosis with p.F21L/T88N Amino Acid Substitutions in a Russian Family.
Suvorina MY et al.
International Journal of Molecular Sciences, 2023
Lysozyme amyloidosis-a report on a large German cohort and the characterisation of a novel amyloidogenic lysozyme gene variant.
Anker S et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2022
Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.
Vettore N et al.
Biophysical Chemistry, 2021
Complex p.T88N/W130R mutation in the lysozyme gene leading to hereditary lysozyme amyloidosis with biopsy-proven cardiac involvement.
Sperry BW et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2017
The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.
Ahn M et al.
Biophysical Journal, 2016
Analysis of protein-coding genetic variation in 60,706 humans.
Lek M et al.
Nature, 2016
Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP.
Kamada Y et al.
International Journal of Biological Sciences, 2016
Serum Amyloid P Component Ameliorates Neurological Damage Caused by Expressing a Lysozyme Variant in the Central Nervous System of Drosophila melanogaster.
Helmfors L et al.
Plos One, 2016
Amyloidogenic lysozymes accumulate in the endoplasmic reticulum accompanied by the augmentation of ER stress signals.
Kamada Y et al.
Biochimica Et Biophysica Acta, 2015
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
De Genst E et al.
The Journal of Physical Chemistry. B, 2013
Small molecules that target protein misfolding.
Gavrin LK et al.
Journal of Medicinal Chemistry, 2012
A new lysozyme tyr54asn mutation causing amyloidosis in a family of Swedish ancestry with gastrointestinal symptoms.
Girnius S et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2012
Hereditary lysozyme amyloidosis -- phenotypic heterogeneity and the role of solid organ transplantation.
Sattianayagam PT et al.
Journal of Internal Medicine, 2012
Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster.
Kumita JR et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2012
Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.
Ahn M et al.
Plos One, 2012
Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.
Dhulesia A et al.
Journal of the American Chemical Society, 2010
A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.
Hagan CL et al.
Protein Engineering, Design & Selection : Peds, 2010
Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.
Chan PH et al.
Biochemistry, 2008
Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.
Kumita JR et al.
The Febs Journal, 2006
ALys amyloidosis caused by compound heterozygosity in exon 2 (Thr70Asn) and exon 4 (Trp112Arg) of the lysozyme gene.
Röcken C et al.
Human Mutation, 2006
Lysozyme amyloidosis: report of 4 cases and a review of the literature.
Granel B et al.
Medicine, 2006
Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
Johnson RJ et al.
Journal of Molecular Biology, 2005
Lysozyme: a paradigmatic molecule for the investigation of protein structure, function and misfolding.
Merlini G et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 2005
Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
Dumoulin M et al.
Journal of Molecular Biology, 2005
A highly amyloidogenic region of hen lysozyme.
Frare E et al.
Journal of Molecular Biology, 2004
Structural and folding dynamic properties of the T70N variant of human lysozyme.
Esposito G et al.
The Journal of Biological Chemistry, 2003
A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis.
Yazaki M et al.
Kidney International, 2003
Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family.
Valleix S et al.
Kidney International, 2002
A novel variant of human lysozyme (T70N) is common in the normal population.
Booth DR et al.
Human Mutation, 2000
Insights into the conformational changes of several human lysozyme variants associated with hereditary systemic amyloidosis.
Liu HL et al.
Biotechnology Progress, 0