about
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueOStructure of the intramolecular human telomeric G-quadruplex in potassium solution: a novel adenine triple formationStructural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency.Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry protocol for monitoring the progress of enzymatic (13)C/(15)N-labeled DNA syntheses.Oligomerization of nitrophorins.Diffusion-ordered nuclear magnetic resonance spectroscopy for analysis of DNA secondary structural elements.Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase.Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate.TP53 mutation hits energy metabolism and increases glycolysis in breast cancer.Human telomeric sequence forms a hybrid-type intramolecular G-quadruplex structure with mixed parallel/antiparallel strands in potassium solution.A direct and nondestructive approach to determine the folding structure of the I-motif DNA secondary structure by NMR.Human dihydrolipoamide dehydrogenase (E3) deficiency: Novel insights into the structural basis and molecular pathomechanism.Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components.Polyethylene glycol enhanced refolding of the recombinant human tissue transglutaminase.Calcium binding of transglutaminases: a 43Ca NMR study combined with surface polarity analysis.Solution structure of the biologically relevant G-quadruplex element in the human c-MYC promoter. Implications for G-quadruplex stabilization.A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2+ release from mitochondria.Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid.Total and semisynthesis and in vitro studies of both enantiomers of 20-fluorocamptothecin.Measurement of ROS homeostasis in isolated mitochondria.Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase.DNA binding of sunitinib: Spectroscopic evidence via circular dichroism and nuclear magnetic resonance.Triethylene glycol dimethacrylate impairs bioenergetic functions and induces oxidative stress in mitochondria via inhibiting respiratory Complex I.Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics - Implications in functional loss and modulation of reactive oxygen species generationMembrane potential and delta pH dependency of reverse electron transport-associated hydrogen peroxide production in brain and heart mitochondriaA multipronged approach unravels unprecedented protein-protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complexStimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenaseCrystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenaseStructure-function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with L-lysine metabolism disorderUnderlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variantsAn Updated View on the Molecular Pathomechanisms of Human Dihydrolipoamide Dehydrogenase Deficiency in Light of Novel Crystallographic EvidenceExclusive neuronal detection of KGDHC-specific subunits in the adult human brain cortex despite pancellular protein lysine succinylation
P50
Q27641405-D705AE4D-FD1A-47F9-9B0E-AE96DCA89391Q27644282-4B50927F-C845-4EC2-B5AE-A6D1BBFB6FD6Q30392030-E57577B9-F355-4FF4-A46A-A9DBB8C0EC6FQ30786331-A05EE62A-D258-4A7E-B401-97195DFAEDF3Q33238069-F4C1FD19-DF75-4B72-804F-E937273747DAQ33287767-A231FFF1-82A5-4361-90C5-0C2B1ACAFD73Q33374933-53794D4B-7743-4EDD-8EC5-030BF11201AEQ34396873-1032FAC1-6C7D-4340-BACE-C32DBE91304FQ34539146-59213361-2CAE-4BC5-8130-1109167FC8E0Q34623697-639A6B3A-3F3E-4A9C-BBCF-B2BF737A2907Q37358864-245879AC-662B-4618-91A3-05D6137FC4EBQ39349140-B4EF99B6-CCA9-4B26-8D47-4AA3F3D04DF3Q42656697-A07160C0-8CB8-43D4-814E-CFCD2D47D831Q43587592-17417244-700E-4496-878A-94B7C814F7EAQ43743821-66A8F822-0186-4D69-9C77-E18C7A0A91F3Q45255075-CDA5EF04-5266-4781-96CF-17EE3328CB6BQ46002267-930AADEA-25A6-4CEC-AB43-F8ED12C24B9CQ46037690-78D109F8-CCAA-4530-AF0A-D25847901E0AQ46685482-889CB0F4-BF23-4D2B-9502-EE4BDF0DB4F7Q46811557-63139838-DF9A-4A25-85B0-B5CD7556FC55Q46900151-E7CAEB81-1069-4E2C-99AF-DFB13FEADAA1Q49491867-8CCA9540-D874-426A-B734-79FF9C15DD2AQ52315287-00A27613-56BC-4D3C-802A-757BC3CEDB28Q55074315-E23FDE79-089A-4FE7-8776-298684ACE90FQ57095592-C68D49BF-08BE-460F-8CB9-96C9D427D79FQ57463355-6D556B6A-2644-43E7-872B-C718B04C847DQ57539864-F4302AEE-037C-4087-909B-ED9DC29572ACQ89123117-F25EB865-F134-4A9A-9C6E-6C8E9AE27B7DQ92024927-8B985119-BFF7-4416-ABCA-9A9941C7CD5DQ92113914-4A36F965-679B-4F85-8C54-61704598518FQ92215385-E44E8A75-C188-41D2-8E30-D6FAF2BB8591Q92946583-380E28FF-C1C9-430A-9010-79A2964C8C41
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Attila Ambrus
@ast
Attila Ambrus
@en
Attila Ambrus
@es
Attila Ambrus
@nl
type
label
Attila Ambrus
@ast
Attila Ambrus
@en
Attila Ambrus
@es
Attila Ambrus
@nl
prefLabel
Attila Ambrus
@ast
Attila Ambrus
@en
Attila Ambrus
@es
Attila Ambrus
@nl
P1053
O-4301-2017
P106
P1960
hKVjrQcAAAAJ
P21
P31
P3829
P496
0000-0001-6014-3175