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Cell Reports, ISSN 2211-1247, 08/2019, Volume 28, Issue 8, pp. 2080 - 2095.e6
Hsp104 is an AAA+ protein disaggregase, which can be potentiated via diverse mutations in its autoregulatory middle domain (MD) to mitigate toxic misfolding of... 
aberrant phase separation | disaggregase | Hsp104 | FUS | TDP-43 | FTD | ALS | engineering | alpha-synuclein | RNA-BINDING PROTEINS | OVEREXPRESSION | DOMAIN | VARIANTS | CLPB | ELIMINATION | GENE-THERAPY | HSP104 DISAGGREGASE | MODEL | AGGREGATION | CELL BIOLOGY
Journal Article
Journal Article
NATURE COMMUNICATIONS, ISSN 2041-1723, 06/2019, Volume 10
Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates.... 
SYSTEM | AMINO-TERMINAL DOMAIN | MECHANISM | RECOGNITION | MULTIDISCIPLINARY SCIENCES | CENTRAL PORE | HSP104 DISAGGREGASE | CHAPERONE | BINDING | PROTEIN DISAGGREGATION | REVEALS
Journal Article
Cell Reports, ISSN 2211-1247, 01/2019, Volume 26, Issue 1, pp. 29 - 36.e3
Hsp104 is a ring-forming, ATP-driven molecular machine that recovers functional protein from both stress-denatured and amyloid-forming aggregates. Although... 
molecular chaperone | AAA+ | Hsp104 | ATPase | ClpB | cryo-EM | protein disaggregase | MOLECULAR CHAPERONE | CLPB | MECHANISM | THERMOTOLERANCE | CELL BIOLOGY
Journal Article
SCIENTIFIC REPORTS, ISSN 2045-2322, 03/2014, Volume 4
Moyamoya disease is an idiopathic human cerebrovascular disorder that is characterized by progressive stenosis and abnormal collateral vessels. We recently... 
EPIDEMIOLOGIC FEATURES | SYSTEM | WILLIS | RNF213 | C.14576G-GREATER-THAN-A VARIANT | SPONTANEOUS OCCLUSION | MULTIDISCIPLINARY SCIENCES | CHAPERONE | DISAGGREGASE | DOMAINS | BINDING
Journal Article
2017, ISBN 2889451259
Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing... 
Misfolding diseases | proteostasis | Disaggregase | Heat-Shock Proteins | unfoldase
eBook
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2018, Volume 115, Issue 41, pp. E9560 - E9569
The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In M.... 
AAA-ATPase | Proteostasis | Mycobacterium tuberculosis | Cryo-EM | Disaggregase | SYSTEM | HSP104 | HSP70 | MULTIDISCIPLINARY SCIENCES | proteostasis | DISAGGREGATION | disaggregase | DNAK | MOLECULAR CHAPERONE | PROTEINS | cryo-EM | CRYO-EM STRUCTURE | Physiological aspects | Genetic aspects | Translocation (Genetics) | Peptides | Observations | Biological Sciences | PNAS Plus
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 05/2019, Volume 294, Issue 18, pp. 7115 - 7127
Journal Article