about
sameAs
MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP poolStructural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3Crystal structure of human MTH1 and the 8-oxo-dGMP product complexStereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategyHypoxic Signaling and the Cellular Redox Tumor Environment Determine Sensitivity to MTH1 InhibitionNUDT15 Hydrolyzes 6-Thio-DeoxyGTP to Mediate the Anticancer Efficacy of 6-ThioguanineCrystal structure, biochemical and cellular activities demonstrate separate functions of MTH1 and MTH2CyDNA: synthesis and replication of highly Cy-dye substituted DNA by an evolved polymerase.Addiction to MTH1 protein results in intense expression in human breast cancer tissue as measured by liquid chromatography-isotope-dilution tandem mass spectrometry.Validation and development of MTH1 inhibitors for treatment of cancer.Targeting SAMHD1 with the Vpx protein to improve cytarabine therapy for hematological malignancies.Processing of protein ADP-ribosylation by Nudix hydrolases.Discovery of the First Potent and Selective Inhibitors of Human dCTP Pyrophosphatase 1Production, Purification, and Characterization of ¹⁵N-Labeled DNA Repair Proteins as Internal Standards for Mass Spectrometric Measurements.PARP is activated at stalled forks to mediate Mre11-dependent replication restart and recombination.Piperazin-1-ylpyridazine Derivatives Are a Novel Class of Human dCTP Pyrophosphatase 1 Inhibitors.PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNAdUTPase inhibition augments replication defects of 5-Fluorouracil.Corrigendum: MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool.A comprehensive structural, biochemical and biological profiling of the human NUDIX hydrolase family.Correction to Piperazin-1-ylpyridazine Derivatives Are a Novel Class of Human dCTP Pyrophosphatase 1 Inhibitors.Targeted NUDT5 inhibitors block hormone signaling in breast cancer cells.Identification of Triazolothiadiazoles as Potent Inhibitors of the dCTP Pyrophosphatase 1.Crystal Structures and Inhibitor Interactions of Mouse and Dog MTH1 Reveal Species-Specific Differences in Affinity.Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold.Crystal Structure of the Emerging Cancer Target MTHFD2 in Complex with a Substrate-Based Inhibitor.Diverse heterocyclic scaffolds as dCTP pyrophosphatase 1 inhibitors. Part 1: Triazoles, triazolopyrimidines, triazinoindoles, quinoline hydrazones and arylpiperazines.Diverse heterocyclic scaffolds as dCTP pyrophosphatase 1 inhibitors. Part 2: Pyridone- and pyrimidinone-derived systems.MutT homologue 1 (MTH1) catalyzes the hydrolysis of mutagenic O6-methyl-dGTPPARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNA.: FIGURE 2Germline variation in the oxidative DNA repair genes NUDT1 and OGG1 is not associated with hereditary colorectal cancer or polyposisMutT homologue 1 (MTH1) removes N6-methyl-dATP from the dNTP poolCrystal Structure and Substrate Specificity of the 8-oxo-dGTP Hydrolase NUDT1 from Arabidopsis thalianaSmall-molecule inhibitor of OGG1 suppresses proinflammatory gene expression and inflammation
P50
Q27643976-BC3EB2D4-2906-4A78-93FE-FCF4273C0F56Q27654592-88916908-AC0D-43CD-AF51-1C7C0B2D6B87Q27670989-344FE96B-9473-4DBB-B3F2-168775F28145Q27682798-D2F4DF2C-2202-48B6-BFA4-7C9ECE8FAE06Q27703996-EC2AF0EE-032A-4A8B-A74B-7E412982E524Q27727699-4DFD9039-99AE-4B98-9BFD-B5237BD96B84Q28115448-A0AF49BD-9FD7-4E7E-9336-E71D7662B7D0Q33773349-60D89F70-C395-4C59-8000-72C2C3264170Q34486440-8E84770F-F877-430F-8807-6065F6D65482Q34544355-2B451021-5892-4B0E-9833-761AC27EB01AQ34548815-7C4948AC-0FCA-4B02-BDE0-E4A9BD9185BDQ35581139-DC0EFF8B-C272-43A8-BD73-29E4AE9CD7AFQ36580244-6E7D489D-6840-4F0E-9EC0-20814342EEDAQ36955832-EDC3E1F3-27FF-4DAD-963C-AD2133A0F3D1Q37334922-E8C34D67-5EB3-4EFA-B6C3-203A0669751CQ38703379-FCCE3F2C-BBDC-4A3B-97C9-7A3AE4F3B956Q39430828-2E318E40-0F4C-4AA3-9287-AD29BFFF4F97Q41767730-81CE19F8-DB95-468F-9348-50FD3E0F1B9EQ43362105-BF30F239-065B-4440-BB16-BC957A7BAAB9Q47163230-F29251CE-7982-495E-97AD-E90C0BFD0565Q48140775-78F36DF6-51BC-4C9B-A339-5180E3F96DB5Q48223029-FBD0C287-E666-4C50-93C6-D6580569CD30Q48289734-7BABB8BA-100A-42B1-9282-EA2141C4B0AFQ48343092-B31CC90E-2AAB-4250-A50D-3F6DB7FC1449Q50138912-42F082CA-3A65-44D0-84E3-C62D7DFB3D8DQ51296834-7C65D35F-D102-42EB-BEDB-8F1720317965Q52763252-87621587-2461-46F9-BC27-5CF6ED417062Q52764427-C022A41E-4583-44E4-B102-5E62B9D9EA20Q57285701-F8950631-66D5-417B-811F-53792BF37199Q58319232-61141A9A-C6EF-4832-8D96-DCB620B4371CQ64044984-0AFEF976-CA8E-4E4A-AE79-01CB64D07C96Q90117407-A306D6B4-2E1F-4A65-9ADD-092E55AD674CQ90917525-9AA2B54B-8BE9-48EA-80C8-C7A8387026DAQ93160517-74251C74-0EBD-4A35-A5AC-8D067F486C50
P50
description
Zweeds onderzoekster
@nl
hulumtuese
@sq
researcher
@en
taighdeoir
@ga
հետազոտող
@hy
name
Ann-Sofie Jemth
@ast
Ann-Sofie Jemth
@en
Ann-Sofie Jemth
@es
Ann-Sofie Jemth
@ga
Ann-Sofie Jemth
@nl
Ann-Sofie Jemth
@sl
Ann-Sofie Jemth
@sq
type
label
Ann-Sofie Jemth
@ast
Ann-Sofie Jemth
@en
Ann-Sofie Jemth
@es
Ann-Sofie Jemth
@ga
Ann-Sofie Jemth
@nl
Ann-Sofie Jemth
@sl
Ann-Sofie Jemth
@sq
prefLabel
Ann-Sofie Jemth
@ast
Ann-Sofie Jemth
@en
Ann-Sofie Jemth
@es
Ann-Sofie Jemth
@ga
Ann-Sofie Jemth
@nl
Ann-Sofie Jemth
@sl
Ann-Sofie Jemth
@sq
P106
P21
P27
P31
P496
0000-0002-7550-1833