TY  - JOUR
AU  - Martino, Fabrizio
AU  - Pal, Mohinder
AU  - Muñoz-Hernández, Hugo
AU  - Rodríguez, Carlos F
AU  - Núñez-Ramírez, Rafael
AU  - Gil-Carton, David
AU  - Degliesposti, Gianluca
AU  - Skehel, J Mark
AU  - Roe, S Mark
AU  - Prodromou, Chrisostomos
AU  - Pearl, Laurence H
AU  - Llorca Blanco, Oscar Antonio
PY  - 2018
DO  - 10.1038/s41467-018-03942-1
SN  - 2041-1723
UR  - http://hdl.handle.net/20.500.12105/6506
AB  - 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 kinases such as mTOR. However, the mechanism by which this occurs is poorly understood....
LA  - eng
PB  - Nature Publishing Group
KW  - HUMAN TRANSCRIPTION MACHINERY
KW  - CHROMATIN-REMODELING COMPLEX
KW  - PROTEIN-INTERACTION NETWORK
KW  - RNA-POLYMERASE-II
KW  - COCHAPERONE COMPLEX
KW  - STRUCTURAL BASIS
KW  - TEL2
KW  - BINDING
KW  - TAH1
KW  - RESOLUTION
TI  - RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
TY  - journal article
ER  -