about
Biological chromodynamics: a general method for measuring protein occupancy across the genome by calibrating ChIP-seq.Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactionsCohesin's DNA exit gate is distinct from its entrance gate and is regulated by acetylation.Genomic screening in vivo reveals the role played by vacuolar H+ ATPase and cytosolic acidification in sensitivity to DNA-damaging agents such as cisplatin.ATP hydrolysis is required for relocating cohesin from sites occupied by its Scc2/4 loading complex.Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.An Smc3 acetylation cycle is essential for establishment of sister chromatid cohesion.Releasing Activity Disengages Cohesin's Smc3/Scc1 Interface in a Process Blocked by Acetylation.Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machineryBoth interaction surfaces within cohesin's hinge domain are essential for its stable chromosomal association.Scc2 Is a Potent Activator of Cohesin's ATPase that Promotes Loading by Binding Scc1 without Pds5.A folded conformation of MukBEF and CohesinThe Cohesin Ring Uses Its Hinge to Organize DNA Using Non-topological as well as Topological MechanismsA set of novel CRISPR-based integrative vectors forExpressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicolScc2 counteracts a Wapl-independent mechanism that releases cohesin from chromosomes during G1A folded conformation of MukBEF and cohesin
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description
researcher ORCID: 0000-0001-6316-2830
@en
name
Bin Hu
@ast
Bin Hu
@en
Bin Hu
@nl
Bin Hu
@sl
type
label
Bin Hu
@ast
Bin Hu
@en
Bin Hu
@nl
Bin Hu
@sl
prefLabel
Bin Hu
@ast
Bin Hu
@en
Bin Hu
@nl
Bin Hu
@sl
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0000-0001-6316-2830