Biochemical Basis of Sestrin Physiological Activities.
Ho, Allison; Cho, Chun-Seok; Namkoong, Sim; Cho, Uhn-Soo; Lee, Jun Hee.
Trends Biochem Sci
; 41(7): 621-632, 2016 07.
Artigo em Inglês | MEDLINE | ID: mdl-27174209
Remembering the Past: A New Form of Protein-Based Inheritance.
It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.
[A study of recombinant human sestrin 1 and sestrin 2 proteins produced in a prokaryotic system].
Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution.
Theoretical insights into the mechanism of redox switch in heat shock protein Hsp33.
Order out of disorder: working cycle of an intrinsically unfolded chaperone.
Visualizing GroEL/ES in the act of encapsulating a folding protein.
The trimeric coiled-coil HSBP1 protein promotes WASH complex assembly at centrosomes.
Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling.