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Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 2393 - 12
Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates.... 
Binding | Translocation | Yeast | Polypeptides | ClpB protein | Homology | Trimers | Substrates | Proteins | Domains | Casein | HSP100 protein | Adenosine triphosphate
Journal Article
Biophysical Journal, ISSN 0006-3495, 05/2019, Volume 116, Issue 10, pp. 1856 - 1872
Heat shock protein (Hsp) 104 is a hexameric ATPases associated with diverse cellular activities motor protein that enables cells to survive extreme stress.... 
CLPA CHAPERONE | ATP-DEPENDENT TRANSLOCATION | BIOPHYSICS | DNA | ESCHERICHIA-COLI | STEP-SIZE | CENTRAL PORE | COMMON MECHANISM | SINGLE TURNOVER KINETICS | STOPPED-FLOW | PROTEIN DISAGGREGATION | Proteins | Hydrolysis | Medical colleges | Nervous system diseases | Analysis | Heat shock proteins | Adenosine triphosphatase | Protein binding
Journal Article
Biophysical Journal, ISSN 0006-3495, 01/2013, Volume 104, Issue 2, pp. 570a - 570a
Journal Article
Cell, ISSN 0092-8674, 01/2014, Volume 156, Issue 1-2, pp. 170 - 182
Journal Article
Minerva ginecologica, 02/2018, Volume 70, Issue 1, p. 53
The advent of flexible CO2 laser fiber to gynecology arena might represent a turning point in the use of laser energy on a large-scale basis in gynecological... 
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2014, Volume 9, Issue 10, p. e110115
Hsp104 is a hexameric AAA+ protein that utilizes energy from ATP hydrolysis to dissolve disordered protein aggregates as well as amyloid fibers. Interestingly,... 
FIREFLY LUCIFERASE | SACCHAROMYCES-CEREVISIAE HSP104 | AGENT GUANIDINIUM CHLORIDE | PRION PROPAGATION | MULTIDISCIPLINARY SCIENCES | AGGREGATED PROTEINS | PROMISCUOUS INHIBITORS | COMMON MECHANISM | NUCLEOTIDE-BINDING | MIDDLE DOMAIN | PROTEIN DISAGGREGATION | Molecular Chaperones | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Heat-Shock Proteins - metabolism | Adenosine Triphosphatases - metabolism | Heat-Shock Proteins - antagonists & inhibitors | Protein Aggregation, Pathological - drug therapy | Suramin - chemistry | Saccharomyces cerevisiae - metabolism | Adenosine Triphosphatases - antagonists & inhibitors | Small Molecule Libraries - chemistry | Animals | Protein Binding - drug effects | Saccharomyces cerevisiae Proteins - metabolism | Small Molecule Libraries - isolation & purification | Protein Aggregation, Pathological - metabolism | Suramin - pharmacology | Heat-Shock Proteins - chemistry | Protein Aggregates - drug effects | Protein Structure, Tertiary - drug effects | Saccharomyces cerevisiae Proteins - chemistry | Hydrolysis | Heat shock proteins | Adenosine triphosphatase | Suramin | ClpB protein | Disease | Homology | Biochemistry | Translocase | Parasites | Kinases | Fibers | Proteins | E coli | Cell cycle | Amyloid | Inhibition | African trypanosomiasis | Adenosine triphosphate | Vector-borne diseases | Hexamers | Glycerol | Hsp70 protein | Biophysics | Hsp40 protein | Medical screening | Side effects | Inhibitors | Collaboration | Mutation | Binding sites | Heat shock | Structure-function relationships
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Journal Article
Journal Article
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