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Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismFaster STORM using compressed sensingHigh-resolution restoration of 3D structures from widefield images with extreme low signal-to-noise-ratio.NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13C-methyl alanine.Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity.Internal Structure and Preferential Protein Binding of Colloidal Aggregates.Liquid droplet formation by HP1α suggests a role for phase separation in heterochromatin.Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity
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Q27681454-96FB7E28-8762-47CB-B370-866AAAC9D337Q30459604-7DB1667F-4993-40CA-8917-76D07728FA62Q30554429-F8556BEF-3C0C-4EED-ACAA-8B8EB9A8B74DQ38707757-BD2F49DE-82CC-4364-85A8-5024E0A9B684Q41329945-7CC1873C-B681-4B07-9CE5-033EB8685258Q42653705-4C2A72C8-743B-4033-8A28-53FD74853D2CQ45952056-500B7609-EAF8-440E-B397-7BA6B1049B07Q46018754-7F5F5F54-01F5-41C1-B4C6-2BC3ABE007D2Q89507389-2BED0A9F-70F7-40EA-8B82-F925D583D360
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description
onderzoeker
@nl
researcher
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հետազոտող
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name
Daniel Elnatan
@ast
Daniel Elnatan
@en
Daniel Elnatan
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Daniel Elnatan
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type
label
Daniel Elnatan
@ast
Daniel Elnatan
@en
Daniel Elnatan
@es
Daniel Elnatan
@nl
prefLabel
Daniel Elnatan
@ast
Daniel Elnatan
@en
Daniel Elnatan
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Daniel Elnatan
@nl
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P31
P496
0000-0002-8359-0522