about
The yeast Ess1 prolyl isomerase controls Swi6 and Whi5 nuclear localization.F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL Trap.Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit ε.Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.Spotlighting motors and controls of single FoF1-ATP synthase.Regulatory conformational changes of the ε subunit in single FRET-labeled FoF1-ATP synthase.A splicing-regulatory polymorphism in DRD2 disrupts ZRANB2 binding, impairs cognitive functioning and increases risk for schizophrenia in six Han Chinese samples.Bio-layer interferometry for measuring kinetics of protein-protein interactions and allosteric ligand effects.Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation.Exploiting the nitrilotriacetic acid moiety for biolabeling with ultrastable perylene dyes.Comparison of molecular dynamics averaged structures for complexes of normal and oncogenic ras-p21 with SOS nucleotide exchange protein, containing computed conformations for three crystallographically undefined domains, suggests a potential role ofNormal macromolecular clearance out of the ventricles is delayed in hydrocephalus.Structure of the nucleotide-binding domain in the beta-subunit of Escherichia coli F1-ATPase.Cryo-EM reveals distinct conformations of ATP synthase on exposure to ATPLipid-dependent membrane enzymes. Kinetic modelling of the activation of protein kinase C by phosphatidylserineRotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthaseTurbine enzyme's structure in the crosshairs to target tuberculosis
P50
Q27936882-ED7FA2AA-0F93-458F-87A0-5F398E4D6EB7Q30414148-DCCA2381-EB43-4CD2-B6C3-0A79CE8DB11BQ34303885-0642A176-06B5-4BAB-8C25-838BC0CA3BBBQ35978276-DC6B7BF4-E395-4E53-98D7-BC1CD4D4F2BCQ36375635-C541E5E9-C820-428C-8989-9BE9F4B67FA4Q36589192-C5445BE8-E37F-462D-AEAA-257DCDF51F63Q38141066-E27098C6-4ACB-4740-B513-1EE8B50C03B9Q39151141-2B8754E3-FE6D-430F-BC8C-B69E6D24199FQ41393508-E5962A86-F404-4EA2-BC5F-1BB4550FA031Q42018301-6FCF08E4-8B49-42FC-BDA8-3C7F04EBDF60Q44938119-FD30E965-BBF8-452B-90C6-42B420982CEBQ46674034-E910CBB2-7AC1-4F56-99AD-FF23D3DFD1E6Q47335662-2CE8B32D-B88A-4AEE-B488-075CA1AB1228Q48002609-2055E06D-94B6-4A99-A761-C4E7C002F532Q54773111-3F82AEC0-BEC5-4E5F-A382-088C17AFC5D4Q64117539-C1C48969-3969-4C06-9F4A-E1056C1DE714Q68030594-E194453D-9279-43F0-8EC8-46E0247CCB8FQ77580862-20264A70-2B74-4477-883C-DDCD50E1580BQ91725194-BD53A1E9-F8C0-4A28-BC62-E41DE59D6170
P50
description
researcher ORCID ID = 0000-0002-6432-4958
@en
name
Thomas M Duncan
@ast
Thomas M Duncan
@en
Thomas M Duncan
@es
Thomas M Duncan
@nl
type
label
Thomas M Duncan
@ast
Thomas M Duncan
@en
Thomas M Duncan
@es
Thomas M Duncan
@nl
prefLabel
Thomas M Duncan
@ast
Thomas M Duncan
@en
Thomas M Duncan
@es
Thomas M Duncan
@nl
P1153
7101691320
P31
P496
0000-0002-6432-4958