Disease‐related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development inDrosophila melanogaster-Reference-Cited by-同舟云学术

Disease‐related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development inDrosophila melanogaster

Published:2011-09-29 Issue:1 Volume:26 Page:192-202
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Kumita Janet R.¹,Helmfors Linda²,Williams Jocy³,Luheshi Leila M.¹,Menzer Linda⁴,Dumoulin Mireille⁴,Lomas David A.⁵,Crowther Damian C.⁶⁵,Dobson Christopher M.¹,Brorsson Ann‐Christin²

Affiliation:

1. Department of ChemistryUniversity of Cambridge Cambridge UK

2. Division of Molecular Biotechnology, Department of PhysicsChemistry and Biology, Linköping University Linköping Sweden

3. Department of BiochemistryUniversity of Cambridge Cambridge UK

4. Laboratory of Enzymology and Protein Folding, Centre of Protein EngineeringInstitute of Chemistry B6c, University of Lie'ge Lie'ge Belgium

5. Cambridge Institute for Medical Research Cambridge UK

6. Department of GeneticsUniversity of Cambridge Cambridge UK

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.11-185983

Reference53 articles.

1. On a remarkable bacteriolytic element found in tissues and secretions

2. Human lysozyme gene mutations cause hereditary systemic amyloidosis

3. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

4. Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family

5. A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis

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