نتایج جستجو برای: chemical chaperones

تعداد نتایج: 384481  

Journal: :acta medica iranica 0
hossein mirmiranpour department of biochemistry, school of medicine, alborz university of medical sciences, karaj, iran. and department of clinical biochemistry, school of medicine, tehran university of medical sciences, tehran, iran. shahnaz khaghani department of clinical biochemistry, school of medicine, tehran university of medical sciences, tehran, iran. s. zahra bathaie department of clinical biochemistry, school of medical sciences, tarbiat modares university, tehran, iran. manouchehr nakhjavani endocrinology and metabolism research center, vali-asr hospital, tehran university of medical sciences, tehran, iran. abbas kebriaeezadeh departments of toxicology/ pharmacology, school of pharmacy, tehran university of medical sciences, tehran, iran. maryam ebadi endocrinology and metabolism research center, vali-asr hospital, tehran university of medical sciences, tehran, iran.

lysozyme is a bactericidal enzyme whose structure and functions change in diabetes. chemical chaperones are small molecules including polyamines (e.g. spermine), amino acids (e.g. l-lysine) and polyols (e.g. glycerol). they can improve protein conformation in several stressful conditions such as glycation. in this study, the authors aimed to observe the effect of l-lysine as a chemical chaperon...

Journal: :Applied sciences 2021

Molecular chaperones are a family of proteins that highly conserved during phylogenesis [...]

Journal: :Chemistry & biology 2011
Elisa Leung Alessandro Datti Michele Cossette Jordan Goodreid Shannon E McCaw Michelle Mah Alina Nakhamchik Koji Ogata Majida El Bakkouri Yi-Qiang Cheng Shoshana J Wodak Bryan T Eger Emil F Pai Jun Liu Scott Gray-Owen Robert A Batey Walid A Houry

ClpP is a cylindrical serine protease whose ability to degrade proteins is regulated by the unfoldase ATP-dependent chaperones. ClpP on its own can only degrade small peptides. Here, we used ClpP as a target in a high-throughput screen for compounds, which activate the protease and allow it to degrade larger proteins, hence, abolishing the specificity arising from the ATP-dependent chaperones. ...

Journal: :Cell stem cell 2016
Valgardur Sigurdsson Hajime Takei Svetlana Soboleva Visnja Radulovic Roman Galeev Kavitha Siva L M Fredrik Leeb-Lundberg Takashi Iida Hiroshi Nittono Kenichi Miharada

During development, hematopoietic stem cells (HSCs) undergo a rapid expansion in the fetal liver (FL) before settling in the adult bone marrow. We recently reported that proliferating adult HSCs are vulnerable to ER stress caused by accumulation of mis-folded proteins. Here, we find that FL-HSCs, despite an increased protein synthesis rate and a requirement for protein folding, do not upregulat...

Journal: :Human Vaccines & Immunotherapeutics 2013

Journal: :Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology 2010
Silvia Muro

This review discusses the multiple bio- and nanotechnological strategies developed in the last few decades for treatment of a group of fatal genetic diseases termed lysosomal storage disorders. Some basic foundation on the biomedical causes and social and clinical relevance of these diseases is provided. Several treatment modalities, from those currently available to novel therapeutic approache...

H. Mirzahoseini

Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. On the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into Escherichia coli along with human basic Fibroblast Grow...

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