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P1346
Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondriaTransterm: a database to aid the analysis of regulatory sequences in mRNAsTreatment of beta amyloid 1-42 (Aβ(1-42))-induced basal forebrain cholinergic damage by a non-classical estrogen signaling activator in vivoThe type 2 anti-Müllerian hormone receptor has splice variants that are dominant-negative inhibitorsHIV-1 and Human PEG10 Frameshift Elements Are Functionally Distinct and Distinguished by Novel Small Molecule ModulatorsThe transition from noncoded to coded protein synthesis: did coding mRNAs arise from stability-enhancing binding partners to tRNA?Evidence from glycine transfer RNA of a frozen accident at the dawn of the genetic code.Temporal profiling of gene networks associated with the late phase of long-term potentiation in vivo.Mutation in the TCRα subunit constant gene (TRAC) leads to a human immunodeficiency disorder characterized by a lack of TCRαβ+ T cellsComparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organismsTime-dependent changes in gene expression induced by secreted amyloid precursor protein-alpha in the rat hippocampusThe highly conserved codon following the slippery sequence supports -1 frameshift efficiency at the HIV-1 frameshift site.Ribosomal frameshifting and dual-target antiactivation restrict quorum-sensing-activated transfer of a mobile genetic element.Primordial soup or vinaigrette: did the RNA world evolve at acidic pH?Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome.Secreted amyloid precursor proteins promote proliferation and glial differentiation of adult hippocampal neural progenitor cells.Secreted amyloid precursor protein-alpha can restore novel object location memory and hippocampal LTP in aged rats.A homogeneous cell-based bicistronic fluorescence assay for high-throughput identification of drugs that perturb viral gene recoding and read-through of nonsense stop codons.Production, purification and functional validation of human secreted amyloid precursor proteins for use as neuropharmacological reagents.The Shine and Dalgarno hypothesis for termination: the 3' terminus of the 16S rRNA of the Escherichia coli ribosome can be modified or base-paired with a complementary oligonucleotide without affecting termination in vitro.The codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop.Maintenance of long-term potentiation in rat dentate gyrus requires protein synthesis but not messenger RNA synthesis immediately post-tetanization.Mammalian gene PEG10 expresses two reading frames by high efficiency -1 frameshifting in embryonic-associated tissues.Partial purification and characterization of a formylmethionine deformylase from rat small intestine.Secreted amyloid precursor protein-alpha upregulates synaptic protein synthesis by a protein kinase G-dependent mechanism.Endogenous secreted amyloid precursor protein-alpha regulates hippocampal NMDA receptor function, long-term potentiation and spatial memory.Differential trafficking of AMPA and NMDA receptors during long-term potentiation in awake adult animals.Rapidly induced gene networks following induction of long-term potentiation at perforant path synapses in vivo.Differential biosynthesis of proteins in separated gastric mucosal cells.Developmental expression and cDNA cloning of globin genes from the brine shrimp, Artemia.Localization of the release factor-2 binding site on 70 S ribosomes by immuno-electron microscopy.The ribosomal domain of the bacterial release factors. The carboxyl-terminal domain of the dimer of Escherichia coli ribosomal protein L7/L12 located in the body of the ribosome is important for release factor interaction.Isolation of a rat mitochondrial release factor. Accommodation of the changed genetic code for termination.Ribosomes from a relC mutant strain of Escherichia coli show altered activity with bacterial release factor-1.Interaction of the release factor with the Escherichia coli ribosome: inhibition of the 30S subunit domain by specific antibodiesIsolation of Escherichia coli release factor-2/ribosome complexes facilitated by efficient crosslinking and sensitive immunodetection of the ligand on the macromolecular particleThe peptidyltransferase centre of the Escherichia coli ribosome. The histidine of protein L16 affects the reconstitution and control of the active centre but is not essential for release-factor-mediated peptidyl-tRNA hydrolysis and peptide bond formaThe ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2A ribonuclease assay: Separation of product from undegraded aminoacyl-transfer RNA substrate
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Q24609364-76B47252-B8DD-4498-9755-44771C1EB30DQ24655920-5F0F471D-4F4A-4265-8589-E0E42831E508Q27349070-BAB51DD7-4700-4212-B5D4-DB880A4157FAQ28511212-0592878B-475B-4B60-8D72-8A5609BB3CA4Q28550143-A070D08F-D4DE-4C04-9BAE-AC25B8B7C227Q28752446-0C6B1392-C8F2-4E94-B6E1-7C02BF874F14Q30485621-CA2EE3D4-9954-4B04-87DC-27DFD771F2BAQ34339730-3D05D652-DCE8-433A-8A66-4AF4EBF763AEQ34519819-A1F385FC-B711-472A-A765-E67D08162EA7Q34538456-FF89568A-D784-4AB4-AE89-F2FA20B35A8AQ34761829-E25788F0-3EFA-4920-B900-E87CFA164FA3Q35217237-A17E4A2E-617E-43A2-95BC-AE49EDDA0E03Q35280072-AB75240F-F4F1-462B-AABC-3D0B4C698B1EQ36025633-894551B8-4285-407D-8842-5D70996648E6Q36875497-45A13D8F-CFEC-4497-B17C-B0CE095FD9AAQ39432106-6F634787-58EA-42D2-A667-02B67738B617Q39493482-D7E30B82-44D0-490D-8EB5-43B5B3C83B46Q39836673-AEB0BF53-7375-4E12-B191-0714CCC61C86Q40126256-8BBEF279-6399-42C6-8DDC-A10F220CB6A5Q41566461-5AE6F206-E960-4035-9589-4B98A55F87D8Q41827192-65C8C7C7-FE64-4A02-8FC6-522A60B5B59BQ42036310-C938915F-B5D0-473F-96F8-E753E78C2D62Q42634716-C66A598F-C869-4162-8E09-3B5223120A71Q42821029-762FD5FB-2877-408A-B1A1-8E1B978D00B7Q45999808-EDF38BD2-4917-42A5-B096-FF11AA511A8FQ46515073-9FE0CAF7-5225-400C-AD96-0B51925FD420Q46840625-D8EECD4A-088A-4BC0-BF16-0B60DFB33C87Q48330341-FD9AF743-82B3-4CDC-BC28-E40070941E1FQ51659453-8C5FDA74-B003-4F69-9629-1707EE4679FEQ52243700-75FDC6BB-25EB-40B4-AB70-0C5DCF6BDC83Q54715872-A2FF325C-F5CE-4211-B0B6-9EEBE971DD34Q54717148-07BA933B-D3B4-463C-8FCE-E3663CE17077Q54766568-968D14A4-ECC6-492E-8255-57F5B8B48C69Q54796671-26606DAC-322D-4510-A159-D9B796B1C386Q60421992-4969CE29-624B-416E-B747-2BD836B09E83Q60422001-4335CC06-5F36-4F98-97C4-31CE3779D92BQ60422007-3C9B7794-40F5-4F4B-B053-5D96AB9651DEQ60422046-950985C9-3D54-407A-AB2C-E2A192407384Q60422054-9B220435-D21E-480D-82A3-05F785F41C45Q60422066-C4BD349F-8E4C-47E0-BC0D-538DE4DA2785
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description
New Zealand biochemist and researcher
@en
biochemicus uit Nieuw-Zeeland
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name
Warren P Tate
@es
Warren Tate
@en
Warren Tate
@fr
Warren Tate
@nl
Warren Tate
@sl
Warren Tate
@sq
type
label
Warren P Tate
@es
Warren Tate
@en
Warren Tate
@fr
Warren Tate
@nl
Warren Tate
@sl
Warren Tate
@sq
altLabel
W. P. Tate
@en
Warren P Tate
@en
Warren P. Tate
@en
Warren Perry Tate
@en
prefLabel
Warren P Tate
@es
Warren Tate
@en
Warren Tate
@fr
Warren Tate
@nl
Warren Tate
@sl
Warren Tate
@sq
P166
P1153
57119197100
P21
P27
P31
P496
0000-0002-6971-7734