Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.
Sign Up to like & getrecommendations! Published in 2023 at "PLoS genetics"
DOI: 10.1371/journal.pgen.1010772
Abstract: Molecular chaperones play a key role in maintaining proteostasis and cellular health. The abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and activation of hundreds of newly synthesized or misfolded client… read more here.
Keywords: cycle; closed conformation; hsp90; hsp90 mutants ... See more keywords
Intramolecular Interaction with the E6 Region Stabilizes the Closed Conformation of the N-SH2 Domain and Concurs with the Self-Inhibitory Docking in Downregulating the Activity of the SHP2 Tyrosine Phosphatase: A Molecular Dynamics Study
Sign Up to like & getrecommendations! Published in 2022 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms23094794
Abstract: The localization and activity of the SHP2 tyrosine phosphatase across different cellular compartments to the target substrates are steered by the binding of phosphotyrosine (pY) peptides to the tandem SH2 domains. The most N-terminal domain… read more here.
Keywords: closed conformation; phosphatase; sh2 domain; domain ... See more keywords
In Silico Study of Polyunsaturated Fatty Acids as Potential SARS-CoV-2 Spike Protein Closed Conformation Stabilizers: Epidemiological and Computational Approaches
Sign Up to like & getrecommendations! Published in 2021 at "Molecules"
DOI: 10.3390/molecules26030711
Abstract: SARS-CoV-2 infects host cells by interacting its spike protein with surface angiotensin-converting enzyme 2 (ACE2) receptors, expressed in lung and other cell types. Although several risk factors could explain why some countries have lower incidence… read more here.
Keywords: protein; spike protein; sars cov; closed conformation ... See more keywords