Markos Koutmos
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View article: Figure S5 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S5 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S5 shows oxidative stress markers, apoptosis, systemic toxicity, and histological outcomes following in vivo auranofin treatments in mouse models.
View article: Figure S4 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S4 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S4 provides CETSA data to illustrate the absence of direct GPX4 interaction with the compound auranofin in treated cells.
View article: Figure S6 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S6 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S6 explores the functional importance of selenoproteins in CRC via CRISPR co-essentiality analyses, qPCR validations of AlkBH8 KD, and survival analyses of tRNA-sec biosynthetic pathway genes.
View article: Figure S7 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S7 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S7 shows the impact of AlkBH8 KD on GPX1/2 protein levels, CRC cell growth, colony formation, and tests the rescuing effects of sodium selenite under RSL3 and auranofin treatments.
View article: Figure S3 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S3 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S3 shows selenoprotein expression validations upon selenium supplementation and identifies RSL3 targets through AP-MS proteomic analysis.
View article: Data from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Data from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Ferroptosis is a nonapoptotic form of cell death driven by iron-dependent lipid peroxide accumulation. Colorectal cancer cells feature elevated intracellular iron and reactive oxygen species that heighten ferroptosis sensitivity. The ferro…
View article: Figure S2 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S2 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S2 validates GPX4 knockdown efficacy, details antioxidant enzyme activities under RSL3 and auranofin treatments, and includes kinetic assays for thioredoxin reductase activity in CRC cells.
View article: Figure S1 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Figure S1 from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
Supplementary Figure S1 shows GPX4 stability using CETSA assays and CRC cell growth responses to RSL3 treatment, with or without Liproxstatin-1 rescue.
View article: Supplementary Materials and Methods from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer
Supplementary Materials and Methods from Recharacterization of the Tumor Suppressive Mechanism of RSL3 Identifies the Selenoproteome as a Druggable Pathway in Colorectal Cancer Open
This methods details synthetic procedures for biotinylated analogs, including reagents, conditions, and yields.
View article: Orchestrating Improbable Chemistries: Structural Snapshots of B12-Dependent Methionine Synthase's Catalytic Choreography
Orchestrating Improbable Chemistries: Structural Snapshots of B12-Dependent Methionine Synthase's Catalytic Choreography Open
Cobalamin (vitamin B12) and its derivatives play an essential role in biological methylation, with cobalamin-dependent methionine synthase (MS) serving as a canonical example. MS catalyzes multiple methyl transfers within a sing…
View article: Orchestrating Improbable Chemistries: Structural Snapshots of B<sub>12</sub>-Dependent Methionine Synthase’s Catalytic Choreography
Orchestrating Improbable Chemistries: Structural Snapshots of B<sub>12</sub>-Dependent Methionine Synthase’s Catalytic Choreography Open
Cobalamin (vitamin B 12 ) and its derivatives play an essential role in biological methylation, with cobalamin-dependent methionine synthase (MS) serving as a canonical example. MS catalyzes multiple methyl transfers within a single, dynam…
View article: Recharacterization of RSL3 reveals that the selenoproteome is a druggable target in colorectal cancer
Recharacterization of RSL3 reveals that the selenoproteome is a druggable target in colorectal cancer Open
Ferroptosis is a non-apoptotic form of cell death resulting from the iron-dependent accumulation of lipid peroxides. Colorectal cancer (CRC) cells accumulate high levels of intracellular iron and reactive oxygen species (ROS) and are thus …
View article: Fluorescent Ligand Equilibrium Displacement: A High-Throughput Method for Identification of FMN Riboswitch-Binding Small Molecules
Fluorescent Ligand Equilibrium Displacement: A High-Throughput Method for Identification of FMN Riboswitch-Binding Small Molecules Open
Antibiotic resistance remains a pressing global concern, with most antibiotics targeting the bacterial ribosome or a limited range of proteins. One class of underexplored antibiotic targets is bacterial riboswitches, structured RNA element…
View article: Structural basis of<i>S</i>-adenosylmethionine-dependent Allosteric Transition from Active to Inactive States in Methylenetetrahydrofolate Reductase
Structural basis of<i>S</i>-adenosylmethionine-dependent Allosteric Transition from Active to Inactive States in Methylenetetrahydrofolate Reductase Open
Methylenetetrahydrofolate reductase (MTHFR) is a pivotal flavoprotein connecting the folate and methionine methyl cycles, catalyzing the conversion of methylenetetrahydrofolate to methyltetrahydrofolate. Human MTHFR ( h MTHFR) undergoes el…
View article: Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo
Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo Open
Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, S -adenosylmethionine…
View article: Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured<i>in crystallo</i>
Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured<i>in crystallo</i> Open
Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, S -adenosylmethionine…
View article: Mode of inhibition of RNase P by gambogic acid and juglone
Mode of inhibition of RNase P by gambogic acid and juglone Open
The first step in transfer RNA (tRNA) maturation is the cleavage of the 5’ end of precursor transfer RNA (pre-tRNA) catalyzed by ribonuclease P (RNase P). RNase P is either a ribonucleoprotein (RNP) complex with a catalytic RNA subunit or …
View article: Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions
Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions Open
View article: Radical Tropolone Biosynthesis
Radical Tropolone Biosynthesis Open
Non-heme iron (NHI) enzymes perform a variety of oxidative rearrangements to advance simple building blocks toward complex molecular scaffolds within secondary metabolite pathways. Many of these transformations occur with selectivity that …
View article: Radical Tropolone Biosynthesis
Radical Tropolone Biosynthesis Open
Non-heme iron (NHI) enzymes perform a variety of oxidative rearrangements to advance simple building blocks toward complex molecular scaffolds within secondary metabolite pathways. Many of these transformations occur with selectivity th…
View article: Disease associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation and tRNA processing by mtRNase P
Disease associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation and tRNA processing by mtRNase P Open
Mitochondrial diseases linked to mutations in mitochondrial(mt) tRNA sequences are abundant. However, the contributions of these tRNA mutations to the development of diseases is mostly unknown. Mutations may affect interactions with (mt)tR…
View article: Kinetic mechanism of human mitochondrial RNase P
Kinetic mechanism of human mitochondrial RNase P Open
A first step in processing mitochondrial precursor tRNA (pre-tRNA) is cleavage of the 5’ leader catalyzed by ribonuclease P (RNase P). Human mitochondrial RNase P (mtRNase P) is composed of three protein subunits: mitochondrial RNase P pro…
View article: Interplay between substrate recognition, 5’ end tRNA processing and methylation activity of human mitochondrial RNase P
Interplay between substrate recognition, 5’ end tRNA processing and methylation activity of human mitochondrial RNase P Open
Human mitochondrial ribonuclease P (mtRNase P) is an essential three protein complex that catalyzes the 5’ end maturation of mitochondrial precursor tRNAs (pre-tRNAs). MRPP3 (Mitochondrial RNase P Protein 3), a protein-only RNase P (PRORP)…
View article: Author Index
Author Index Open
View article: CCDC 1530214: Experimental Crystal Structure Determination
CCDC 1530214: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila
Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila Open
Proteins encoded by mitochondrial DNA are translated using mitochondrially encoded tRNAs and rRNAs. As with nuclear encoded tRNAs, mitochondrial tRNAs must be processed to become fully functional. The mitochondrial form of ribonuclease P (…
View article: Author Index
Author Index Open
View article: Evolutionary Analyses and Natural Selection of Betaine-Homocysteine S-Methyltransferase (BHMT) and BHMT2 Genes
Evolutionary Analyses and Natural Selection of Betaine-Homocysteine S-Methyltransferase (BHMT) and BHMT2 Genes Open
Betaine-homocysteine S-methyltransferase (BHMT) and BHMT2 convert homocysteine to methionine using betaine and S-methylmethionine, respectively, as methyl donor substrates. Increased levels of homocysteine in blood are associated with card…