about
A family of insulin-like growth factor II mRNA-binding proteins represses translation in late developmentHuman Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codonCommunication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1Multiple processing body factors and the ARE binding protein TTP activate mRNA decappingUpf1 ATPase-dependent mRNP disassembly is required for completion of nonsense- mediated mRNA decayA competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decayAn unconventional human Ccr4-Caf1 deadenylase complex in nuclear cajal bodiesNuclear transit of human zipcode-binding protein IMP1Stress granules and processing bodies are dynamically linked sites of mRNP remodelingTTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elementsRecruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding proteinA human microprotein that interacts with the mRNA decapping complexHow and where are nonsense mRNAs degraded in mammalian cells?Biallelic mutations in the 3' exonuclease TOE1 cause pontocerebellar hypoplasia and uncover a role in snRNA processing.Protein footprinting approach to mapping DNA binding sites of two archaeal homing enzymes: evidence for a two-domain protein structure.mRNA quality control: Marking the message for life or death.Emerging roles for ribonucleoprotein modification and remodeling in controlling RNA fateArchaeal introns: splicing, intercellular mobility and evolution.Messenger RNA surveillance: neutralizing natural nonsense.Communication with the exon-junction complex and activation of nonsense-mediated decay by human Upf proteins occur in the cytoplasm.hnRNP F complexes with tristetraprolin and stimulates ARE-mRNA decay.New insights into the formation of active nonsense-mediated decay complexes.Translational coregulation of 5'TOP mRNAs by TIA-1 and TIAR.Identification of elements in human long 3' UTRs that inhibit nonsense-mediated decay.Post-transcriptional regulation of satellite cell quiescence by TTP-mediated mRNA decay.Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.DDX6 Orchestrates Mammalian Progenitor Function through the mRNA Degradation and Translation Pathways.RNA decapping inside and outside of processing bodies.Target Discrimination in Nonsense-Mediated mRNA Decay Requires Upf1 ATPase ActivityRecruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements.The control of mRNA decapping and P-body formation.The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation.Hyperphosphorylation amplifies UPF1 activity to resolve stalls in nonsense-mediated mRNA decay.Execution of nonsense-mediated mRNA decay: what defines a substrate?Protecting the proteome: Eukaryotic cotranslational quality control pathways.Regulated and quality-control mRNA turnover pathways in eukaryotes.Structural and functional control of the eukaryotic mRNA decapping machinery.The C-terminal carboxy group of T7 RNA polymerase ensures efficient magnesium ion-dependent catalysis.Structural characteristics of the stable RNA introns of archaeal hyperthermophiles and their splicing junctions.
P50
Q22008676-C6380CEB-898B-482A-90BA-E704B8DC1338Q24290775-114FB718-45A8-430A-9327-049E7B1FB358Q24291664-63BF4F3D-052E-4030-9EFC-0A4E699C82CBQ24299303-69D82C1E-FCB6-4EAC-977A-E6032FDD7239Q24314490-6A11CC3D-4650-4BF0-BA7A-44432B9F54ECQ24336651-BBD1176C-45D5-4724-9700-A0B98FF41A62Q24337378-D34DF760-C122-4856-964C-BFD238E6E3F3Q24530552-AF8574D3-C380-4DFE-B851-34ECDDF860ABQ24678779-C40F4873-3D2C-4809-BD0F-D312214C8316Q28117692-7104E194-4A7B-4ABD-9B6D-76C1297517B0Q28118675-A28A315E-FBE5-4DF8-8D70-49485C7106AFQ28139674-C558CD16-FCA3-442B-9509-336F2CA4FE36Q28596559-EED1E5A0-70B7-42AB-836D-0BEB497655ECQ28636081-F56C3D2D-833A-4159-9BB3-98243AED7D5EQ30090225-7D12E289-401F-4859-85B7-EFC0F70829DCQ30425809-BFB1DCB9-19E9-41E7-B624-BC020232653EQ34169710-05FDA0FA-81D9-42E5-A9FD-3F0AA2FB90DFQ34350089-74783C51-2232-4B7B-9190-9E35F6668C1CQ34439616-1482E6DA-38B9-4244-B1F1-5D057B8B9F02Q34559634-6161608E-8E56-4DE1-A827-C3BC789F19A8Q34679556-23687002-C90E-404B-B674-20E98686BBE1Q35197924-D0ADE323-AF83-4CDB-A923-0E1E381AAAC2Q35296033-85CD2354-B7CF-4313-9671-68A56584F838Q35393305-A88B3431-E577-48C1-A3AD-4135C142DFB6Q35534974-D599E251-5448-4AA1-AEBB-A4FFEA347C20Q35555408-FE3F7EB0-F141-43F3-920A-9544EDAA337AQ35626088-1711AE11-93C6-4686-9247-264EC1B7E059Q36118101-ED9E6C39-A2B6-4F27-A13A-2640EE01F8ADQ36131538-0AD798C2-8DC0-44D3-AFC1-C5005D7B34B0Q36358461-055147D1-2FCB-4040-B14D-04E52A99AFC7Q36566593-62659652-1373-40EE-A414-0881E6A5A009Q37071772-5A6B14B4-3505-48F6-A176-E0F8695D40FDQ37177771-A87FFB8A-5AD7-4348-9441-E3FEE202C7EBQ37181245-6F5BBF76-0EBF-464D-BE9B-7E6BE094ADA9Q37440143-D7CE0F33-2711-46D4-BD1E-E11FA11009DAQ37589357-D0C444F7-C333-4DFB-97F1-3AA4A98323CEQ37813741-B3E942C1-5276-4426-B24D-729BDC2F66ADQ38071446-F2A6E240-63A8-4E44-BD68-1C4D6FFA6242Q39726029-572CFBC3-1A52-4DBF-9477-BCCDED262744Q42594591-8EC75A60-177B-4A0D-8559-DA74209F27A9
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
J Lykke-Andersen
@ast
J Lykke-Andersen
@en
J Lykke-Andersen
@es
J Lykke-Andersen
@nl
J Lykke-Andersen
@sl
type
label
J Lykke-Andersen
@ast
J Lykke-Andersen
@en
J Lykke-Andersen
@es
J Lykke-Andersen
@nl
J Lykke-Andersen
@sl
altLabel
Jens Lykke-Andersen
@en
prefLabel
J Lykke-Andersen
@ast
J Lykke-Andersen
@en
J Lykke-Andersen
@es
J Lykke-Andersen
@nl
J Lykke-Andersen
@sl
P106
P31
P496
0000-0003-1821-0754