about
Homology modelling of transferrin-binding protein A from Neisseria meningitidis.Structure and function of AMP-activated protein kinase.Autophosphorylation of CaMKK2 generates autonomous activity that is disrupted by a T85S mutation linked to anxiety and bipolar disorderCa2+/Calmodulin-dependent protein kinase kinase beta is regulated by multisite phosphorylation.Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding.Cyclin-dependent kinase-mediated phosphorylation of breast cancer metastasis suppressor 1 (BRMS1) affects cell migration.β-subunit myristoylation functions as an energy sensor by modulating the dynamics of AMP-activated Protein Kinase.Metformin and salicylate synergistically activate liver AMPK, inhibit lipogenesis and improve insulin sensitivity.Impact of Genetic Variation on Human CaMKK2 Regulation by Ca2+-Calmodulin and Multisite Phosphorylation.AMPK functions as an adenylate charge-regulated protein kinase.The sweet side of AMPK signaling: regulation of GFAT1.Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.Meningococcal transferrin-binding proteins A and B show cooperation in their binding kinetics for human transferrin.SnRK1 from Arabidopsis thaliana is an atypical AMPK.Inhibition of AMP-Activated Protein Kinase at the Allosteric Drug-Binding Site Promotes Islet Insulin Release.Expression and purification of functional recombinant meningococcal transferrin-binding protein A.ATP sensitive bi-quinoline activator of the AMP-activated protein kinase.AMPK-independent pathways regulate skeletal muscle fatty acid oxidation.Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes.Mdivi-1 Protects Human W8B2+ Cardiac Stem Cells from Oxidative Stress and Simulated Ischemia-Reperfusion Injury.AMP-activated protein kinase subunit interactions: beta1:gamma1 association requires beta1 Thr-263 and Tyr-267.AMPK structure and regulation from three angles.Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion.AMP-activated protein kinase selectively inhibited by the type II inhibitor SBI-0206965.Transient Expression of AMPK Heterotrimer Complexes in Mammalian Cells.Structural Determinants for Small-Molecule Activation of Skeletal Muscle AMPK α2β2γ1 by the Glucose Importagog SC4.Small molecule drug A-769662 and AMP synergistically activate naive AMPK independent of upstream kinase signaling.AMPK is a direct adenylate charge-regulated protein kinase.Are genuine changes in protein expression being overlooked? Reassessing Western blotting.1,2,6-Thiadiazinones as Novel Narrow Spectrum Calcium/Calmodulin-Dependent Protein Kinase Kinase 2 (CaMKK2) Inhibitors.Adipose tissue as an endocrine organQuantitative proteomic analyses of dynamic signalling events in cortical neurons undergoing excitotoxic cell deathImport of extracellular ATP in yeast and man modulates AMPK and TORC1 signallingInsight into the structure and function of the transferrin receptor from Neisseria meningitidis using microcalorimetric techniquesVisualizing AMPK Drug Binding Sites Through Crystallization of Full-Length Phosphorylated α2β1γ1 HeterotrimerMetabolism: Energy sensing through a sugar diphosphateAllosteric regulation of AMP-activated protein kinase by adenylate nucleotides and small-molecule drugsFunctional analysis of an R311C variant of Ca2+ -calmodulin-dependent protein kinase kinase-2 (CaMKK2) found as a de novo mutation in a patient with bipolar disorderATP synthase inhibitory factor 1 (IF1), a novel myokine, regulates glucose metabolism by AMPK and Akt dual pathwaysAuthor Correction: Increased autophagy in EphrinB2-deficient osteocytes is associated with elevated secondary mineralization and brittle bone
P50
Q30160272-8EE25430-02E6-4328-A69A-E68CB9DCFE28Q30375195-DEBE5D85-7A40-4E7B-89FA-2B3E23C50B89Q30402306-D175991A-7F5F-4864-96D2-63AEA53BEE9DQ35150085-09B33B31-1EB9-4C02-9BF9-788E1580C209Q36674861-CDB62300-5731-4AC6-912E-33EE99238A59Q36781251-58863B28-E3EA-4265-9E00-9D6530B11EAEQ37522391-3BD94ED4-8D89-4952-B4A2-B6944C040257Q37583668-5E5384A1-5131-4999-B17A-5C7BF8DCFD16Q37661100-59DDB44F-746C-4BDA-BE47-E8CDD6ACB127Q37979423-3EB3C21A-7244-4073-B762-52C5187E9CD4Q38710903-D204EA1D-97D3-48F5-B944-25AA9F3E8116Q40025254-D216C5E2-518F-4566-84B6-94740240EE74Q40993333-06E14B1F-08D4-4A8A-8050-59AED66AAA53Q41305824-B29BECA6-0545-4832-A5B8-9EE19AF9B954Q42701436-11691871-1D21-40BD-A067-0E47357C257CQ43001885-ACF261A3-60FC-499A-B16C-D822EFFFEE3BQ45325809-B5E651E2-16B7-4CAB-824B-25F01C6AB349Q45915520-05543052-C388-4124-953C-F2A7E0AC8BCBQ46236023-3E7F58C6-B983-4770-A9EC-5BD65B14AB80Q46279157-97324B6A-E24D-4034-9A1A-D6A2C23B497CQ46851056-AE07C5BF-2BD0-4E34-A6EF-A5D7794CC8B3Q46949692-B3F456FE-76CB-4643-91A2-E5A8817365D8Q47304500-68E4CCCF-3C88-4C66-8056-17101CCE673AQ52309562-1D9A2F18-E239-40E1-97F5-DA1259F3E4F7Q52373014-2B9BAC0A-6FF9-4EC3-881D-E6FF078834B3Q52587437-B192F67C-1CA8-4F55-9E02-25995C33AFDFQ54358946-FF51C5B3-19ED-4921-8147-8B6E83C6CD44Q54580866-35469D19-308B-4994-B23C-CD410598C3CFQ54771707-490B808B-0B68-4098-B999-1BBA981D099EQ54978646-693B0C64-64BF-470B-8376-4AC4643223BEQ57257904-28ABF25F-58B6-4718-A617-3CA81515CCC5Q63246394-A20CE986-EFB3-409A-98F1-5A687634B3CDQ64080640-48A89EBF-551E-422F-978A-633C46E0B543Q78900575-0F0238AD-B289-45E2-BAF8-D97092F9F2A3Q87878326-6369FF31-ED33-4BE3-8201-866BEB9029A2Q88556173-88A5524C-DCEA-49ED-860F-F302569FF0ACQ89996587-5C2173AD-F7D5-4B59-9DA2-9695683FF304Q90678035-54F94D07-6A36-49A1-92E4-34F0E313B352Q91034268-0806904E-AFE4-4956-882B-9615082923FDQ91105672-F1DD2196-9C46-4568-AAC5-2CFAFAF33B00
P50
description
researcher
@en
wetenschapper
@nl
name
Jonathan S Oakhill
@en
Jonathan S Oakhill
@nl
type
label
Jonathan S Oakhill
@en
Jonathan S Oakhill
@nl
prefLabel
Jonathan S Oakhill
@en
Jonathan S Oakhill
@nl
P108
P106
P31
P496
0000-0002-9475-1440