about
Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxisGaseous O2, NO, and CO in signal transduction: structure and function relationships of heme-based gas sensors and heme-redox sensors.Highly conserved nucleotide phosphatase essential for membrane lipid homeostasis in Streptococcus pneumoniae.Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2alpha kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins.Pressure effects reveal that changes in the redox states of the heme iron complexes in the sensor domains of two heme-based oxygen sensor proteins, EcDOS and YddV, have profound effects on their flexibility.3-aminobenzanthrone, a human metabolite of the carcinogenic environmental pollutant 3-nitrobenzanthrone, induces biotransformation enzymes in rat kidney and lung.Introduction of water into the heme distal side by Leu65 mutations of an oxygen sensor, YddV, generates verdoheme and carbon monoxide, exerting the heme oxygenase reaction.Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction.Structural characterization of the heme-based oxygen sensor, AfGcHK, its interactions with the cognate response regulator, and their combined mechanism of action in a bacterial two-component signaling system.Identification of Cys385 in the isolated kinase insertion domain of heme-regulated eIF2 alpha kinase (HRI) as the heme axial ligand by site-directed mutagenesis and spectral characterization.Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS).Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK.Catalytic enhancement of the heme-based oxygen-sensing phosphodiesterase EcDOS by hydrogen sulfide is caused by changes in heme coordination structure.Ultrafast Spectroscopy Evidence for Picosecond Ligand Exchange at the Binding Site of a Heme Protein: Heme-Based Sensor YddV.Probing the ligand recognition and discrimination environment of the globin-coupled oxygen sensor protein YddV by FTIR and time-resolved step-scan FTIR spectroscopy.The capacity and effectiveness of diosmectite and charcoal in trapping the compounds causing the most frequent intoxications in acute medicine: A comparative study.Kinetic Analysis of a Globin-Coupled Histidine Kinase, AfGcHK: Effects of the Heme Iron Complex, Response Regulator, and Metal Cations on Autophosphorylation Activity.Exposure to endocrine disruptors 17alpha-ethinylestradiol and estradiol influences cytochrome P450 1A1-mediated genotoxicity of benzo[a]pyrene and expression of this enzyme in ratsFormation, Persistence, and Identification of DNA Adducts Formed by the Carcinogenic Environmental Pollutant o-Anisidine in RatsHuman cytochrome-P450 enzymes metabolize N-(2-methoxyphenyl)hydroxylamine, a metabolite of the carcinogens o-anisidine and o-nitroanisole, thereby dictating its genotoxicityEukaryotic initiation factor 2alpha kinase is a nitric oxide-responsive mercury sensor enzyme: potent inhibition of catalysis by the mercury cation and reversal by nitric oxideDisruption of the dimerization interface of the sensing domain in the dimeric heme-based oxygen sensor AfGcHK abolishes bacterial signal transduction
P50
Q37201164-10B328B7-F78A-4A6F-B46C-87D600122046Q38506342-830D95DA-BFDC-40FB-B7FB-EA627C948E11Q40862499-10548C73-9721-4844-AC5D-C86A44E84177Q43613659-38810A8F-296F-42A3-B8BA-E9A6B82D607DQ44566730-641DF7F1-2D07-4D85-899B-9831893E1E9CQ46034772-4AA7A426-E460-4502-840B-4E4FC7C6E21BQ46863741-0C55E06E-7019-4303-91AF-A3A84737673CQ47390329-ABC630D2-2EE7-4A88-8B96-833AF40C190FQ48209789-80166143-158A-4AF2-A505-59E7F93034A5Q50689939-7A662FA8-6EFF-4FE4-8119-D84A08AF9C33Q50936799-E1F0BA81-3EEA-433E-9B80-44E3353019CEQ53001265-440DBF2E-18EF-4D05-9501-2ED4DC6ABB27Q53093276-340D45CF-942B-4F44-A657-4BBF3BCD136DQ53254719-978ED164-35FB-4F6B-B94B-2CF6601A0EC5Q53471184-DB6A19AC-B8A7-4A3D-A000-0A6FDD6DAE93Q54178151-1B1351CC-B526-48D2-982F-22B2F04180C4Q55052351-381E099C-CFDD-42C0-BA5D-768047357AC7Q62023491-ED194FC5-4DDA-499B-A49A-2D3F5400C0E3Q63253343-CE842E49-5A52-4D18-87DD-480931F487BEQ63253351-C6A754A3-DEBE-45F3-9B4E-D5898197D62EQ80774448-4715D173-1435-4F9B-AA97-C1586DADDDA0Q92497891-0D597F34-BBF2-439E-BC19-3962AA5F2A8F
P50
description
biochemička, vysokoškolská pedagožka
@cs
researcher, ORCID id # 0000-0002-0865-8785
@en
wetenschapper
@nl
name
Markéta Martínková
@ast
Markéta Martínková
@cs
Markéta Martínková
@en
Markéta Martínková
@es
Markéta Martínková
@nl
type
label
Markéta Martínková
@ast
Markéta Martínková
@cs
Markéta Martínková
@en
Markéta Martínková
@es
Markéta Martínková
@nl
prefLabel
Markéta Martínková
@ast
Markéta Martínková
@cs
Markéta Martínková
@en
Markéta Martínková
@es
Markéta Martínková
@nl
P106
P214
P19
P21
P214
P31
P496
0000-0002-0865-8785
P569
1976-01-01T00:00:00Z
P691
P7859
viaf-101607289