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Journal Article
Journal Article
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1501 - 13
The R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like... 
TEL2 | DOMAIN | COCHAPERONE | MECHANISM | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | HUMAN TRANSCRIPTION MACHINERY | DIMERIZATION | PROTEIN-INTERACTION NETWORK | BINDING | REVEALS | Molecular Chaperones - metabolism | Saccharomyces cerevisiae - genetics | Humans | Molecular Chaperones - chemistry | ATPases Associated with Diverse Cellular Activities - chemistry | ATPases Associated with Diverse Cellular Activities - genetics | Saccharomyces cerevisiae - metabolism | ATPases Associated with Diverse Cellular Activities - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Apoptosis Regulatory Proteins - genetics | HSP90 Heat-Shock Proteins - chemistry | Carrier Proteins - chemistry | HSP90 Heat-Shock Proteins - genetics | Protein Interaction Domains and Motifs | Binding Sites | DNA Helicases - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | DNA Helicases - chemistry | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Apoptosis Regulatory Proteins - chemistry | Molecular Chaperones - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Cryoelectron Microscopy | Carrier Proteins - genetics | DNA Helicases - metabolism | Animals | Carrier Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | HSP90 Heat-Shock Proteins - metabolism | Protein Binding | TOR protein | Hsp90 protein | Yeast | RNA polymerase | Kinases | DNA-directed RNA polymerase | 1-Phosphatidylinositol 3-kinase | Proteins | Polymerase | Ribonucleic acids | Scaffolds | Assembly | Adenosine triphosphatase | RNA polymerase II
Journal Article
Protein Science, ISSN 0961-8368, 09/2019, Volume 28, Issue 9, pp. 1545 - 1551
Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co‐chaperone Aha1, which is the... 
Hsp90 | Aha1 | co‐chaperone | structure | allostery | CONTACTS | ACTIVATION | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEOTIDE | co-chaperone | N-TERMINAL DOMAIN | REVEALS | CYCLE | Magnetic resonance spectroscopy | Hsp90 protein | Stimulators | Eukaryotes | Allosteric properties | Nuclear magnetic resonance--NMR | Nucleotides | NMR spectroscopy | Binding sites | Adenosine triphosphatase | Accelerated Communication
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2019, Volume 294, Issue 14, pp. 5246 - 5260
Cumulative evidence suggests that the heat shock protein 90 (Hsp90) co-chaperone UNC-45 myosin chaperone A (UNC45A) contributes to tumorigenesis and that its... 
UNC45A | glucocorticoid receptor | UCS DOMAIN | KEK7 | NIMA-FAMILY KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROLIFERATION | UNC-45 CHAPERONE | mitosis | centrosome | UNC-45A | CANCER | Hsp90 | molecular chaperone | KINESIN EG5 | cancer biology | MYOSIN CHAPERONE | SEPARATION | PROTEINS | CENTROSOMES | Heat shock protein 90
Journal Article