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Journal of Molecular Biology, ISSN 0022-2836, 05/2019, Volume 431, Issue 11, pp. 2180 - 2196
Hsp104 is a yeast chaperone that rescues misfolded proteins from aggregates associated with proteotoxic stress and aging. Hsp104 consists of N-terminal domain,... 
protein quality control | protein refolding | molecular chaperones | protein disaggregation | protein misfolding | Proteins | Fluorescence | Heat shock proteins | Phenylalanine | Protein binding
Journal Article
PLoS Genetics, ISSN 1553-7404, 10/2019, Volume 15, Issue 10, p. e1008479
Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones that bind to aggregation-prone polypeptides at stress conditions. sHsps... 
Proteins | Heat shock proteins | Phylogeny | Escherichia coli | Biotechnology | Polypeptides | ClpB protein | Genes | Disaggregation | Hsp70 protein | Chaperones | Small heat shock proteins | Solubilization | Heat | Cellular biology | E coli | Quality control | DnaK protein | Phylogenetics | Bacteria | Gene duplication | Bioinformatics
Journal Article
Acta Crystallographica Section A Foundations and Advances, ISSN 2053-2733, 08/2016, Volume 72, Issue a1, pp. s247 - s247
Journal Article
Cell Stress & Chaperones, ISSN 1355-8145, 7/2017, Volume 22, Issue 4, pp. 601 - 611
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 4, pp. 2857 - 2869
Journal Article
Journal Article
Cell Stress and Chaperones, ISSN 1355-8145, 01/2019, Volume 24, Issue 1, pp. 7 - 15
Journal Article