The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

We have studied the effects of the extracellular molecular chaperone, clusterin, on the in vitro aggregation of mutational variants of human lysozyme, including one associated with familial amyloid disease. The aggregation of the amyloidogenic variant I56T is inhibited significantly at clusterin to...

Бүрэн тодорхойлолт

Номзүйн дэлгэрэнгүй
Үндсэн зохиолчид:	Kumita, JR, Poon, S, Caddy, G, Hagan, C, Dumoulin, M, Yerbury, J, Stewart, E, Robinson, C, Wilson, MR, Dobson, C
Формат:	Journal article
Хэл сонгох:	English
Хэвлэсэн:	2007

Ижил төстэй зүйлс

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
-н: Johnson, R, зэрэг
Хэвлэсэн: (2005)

The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
-н: Patricia Yuste-Checa, зэрэг
Хэвлэсэн: (2021-08-01)

The significance of the location of mutations for the native-state dynamics of human lysozyme
-н: Ahn, M, зэрэг
Хэвлэсэн: (2016)

The Extracellular Molecular Chaperone Clusterin Inhibits Amyloid Fibril Formation and Suppresses Cytotoxicity Associated with Semen-Derived Enhancer of Virus Infection (SEVI)
-н: Abigail K. Elias, зэрэг
Хэвлэсэн: (2022-10-01)

Expression and purification of chaperone-active recombinant clusterin.
-н: Rebecca A Dabbs, зэрэг
Хэвлэсэн: (2014-01-01)

Molecular mechanisms at the basis of the protective effect exerted by EPPS on neurodegeneration induced by prefibrillar amyloid oligomers
-н: Beatrice Zarrilli, зэрэг
Хэвлэсэн: (2024-11-01)

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
-н: De Genst, E, зэрэг
Хэвлэсэн: (2013)

Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.
-н: Chan, P, зэрэг
Хэвлэсэн: (2008)

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.
-н: Hagan, C, зэрэг
Хэвлэсэн: (2010)

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
-н: Dumoulin, M, зэрэг
Хэвлэсэн: (2003)

Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.
-н: Kumita, JR, зэрэг
Хэвлэсэн: (2006)

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
-н: Booth, DR, зэрэг
Хэвлэсэн: (1997)

Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain.
-н: Krebs, MR, зэрэг
Хэвлэсэн: (2000)

BIOT 243-Biophysical study of the aggregation of human lysozyme into amyloid fibrils
-н: Dhulesia, A, зэрэг
Хэвлэсэн: (2008)

Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain
-н: Yuki Yoshikawa, зэрэг
Хэвлэсэн: (2022-06-01)

Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
-н: Rasool Suhail, зэрэг
Хэвлэсэн: (2007-09-01)

Investigation of non-covalent interactions of amyloidogenic human lysozyme variants and camelid antibodies
-н: Caddy, G, зэрэг
Хэвлэсэн: (2002)

The conformation of lysozyme in solution
-н: Dobson, C, зэрэг
Хэвлэсэн: (1975)

Association of clusterin with the BRI2-derived amyloid molecules ABri and ADan
-н: Agueda Rostagno, зэрэг
Хэвлэсэн: (2021-10-01)

Insights into amyloid fibril formation from mass spectrometry.
-н: Caddy, G, зэрэг
Хэвлэсэн: (2006)

Interaction of the molecular chaperone alpha B-crystallin with alpha-synuclein: Effects on amyloid fibril formation and chaperone activity
-н: Rekas, A, зэрэг
Хэвлэсэн: (2004)

Clusterin is required for β-Amyloid toxicity in human iPSC-derived neurons
-н: Robbins, J, зэрэг
Хэвлэсэн: (2018)

Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.
-н: Rekas, A, зэрэг
Хэвлэсэн: (2004)

Apolipoprotein E and clusterin inhibit the early phase of amyloid-β aggregation in an in vitro model of cerebral amyloid angiopathy
-н: Yoshinori Endo, зэрэг
Хэвлэсэн: (2019-01-01)

Conformational dynamics and protein unfolding in lysozyme amyloidosis
-н: Sunde, M, зэрэг
Хэвлэсэн: (1999)

Effects of model membranes on lysozyme amyloid aggregation
-н: Burrelli Annaclaudia, зэрэг
Хэвлэсэн: (2023-08-01)

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
-н: Dumoulin, M, зэрэг
Хэвлэсэн: (2005)

BACE1 regulates expression of Clusterin in astrocytes for enhancing clearance of β-amyloid peptides
-н: John Zhou, зэрэг
Хэвлэсэн: (2023-05-01)

Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
-н: Eyles, S, зэрэг
Хэвлэсэн: (1994)

Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
-н: van den Berg, B, зэрэг
Хэвлэсэн: (1999)

Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Aβ oligomers
-н: Yeung Stephen, зэрэг
Хэвлэсэн: (2010-12-01)

Molecular recycling within amyloid fibrils.
-н: Carulla, N, зэрэг
Хэвлэсэн: (2005)

Structure of hen lysozyme in solution.
-н: Smith, L, зэрэг
Хэвлэсэн: (1993)

The origin of the alpha-domain intermediate in the folding of hen lysozyme.
-н: Matagne, A, зэрэг
Хэвлэсэн: (1998)

Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.
-н: Minkoo Ahn, зэрэг
Хэвлэсэн: (2012-01-01)

The biology of extracellular molecular chaperones /
-н: Chadwick, Derek, зэрэг
Хэвлэсэн: (2008)

Molecular Docking of Monomethine Cyanine Dyes to Lysozyme Amyloid Fibrils
-н: Olga Zhytniakivska, зэрэг
Хэвлэсэн: (2022-09-01)

Inhibition of Lysozyme Amyloid Fibrillation by Silybin Diastereoisomers: The Effects of Stereochemistry
-н: Xuanyu Chen, зэрэг
Хэвлэсэн: (2021-01-01)

Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme.
-н: Josephine W Wu, зэрэг
Хэвлэсэн: (2013-01-01)

Pathways to Alzheimer’s Disease: The Intersecting Roles of Clusterin and Apolipoprotein E in Amyloid-β Regulation and Neuronal Health
-н: Alexandru Laslo, зэрэг
Хэвлэсэн: (2024-10-01)