about
GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factorProteins surrounding hairpin IIIe of the hepatitis C virus internal ribosome entry site on the human 40S ribosomal subunitHCV IRES interacts with the 18S rRNA to activate the 40S ribosome for subsequent steps of translation initiationFunctional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexesTranslation of 5' leaders is pervasive in genes resistant to eIF2 repressionCanonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entryOxygen and glucose deprivation induces widespread alterations in mRNA translation within 20 minutesPSF acts through the human immunodeficiency virus type 1 mRNA instability elements to regulate virus expressionCap- and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs.Transcriptome-wide studies uncover the diversity of modes of mRNA recruitment to eukaryotic ribosomes.Positive and negative effects of the major mammalian messenger ribonucleoprotein p50 on binding of 40 S ribosomal subunits to the initiation codon of beta-globin mRNA.Sliding of a 43S ribosomal complex from the recognized AUG codon triggered by a delay in eIF2-bound GTP hydrolysisPros and cons of pDNA and mRNA transfection to study mRNA translation in mammalian cells.Does HIV-1 mRNA 5'-untranslated region bear an internal ribosome entry site?A researcher's guide to the galaxy of IRESs.The 5' untranslated region of Apaf-1 mRNA directs translation under apoptosis conditions via a 5' end-dependent scanning mechanism.Influence of the hepatitis C virus 3'-untranslated region on IRES-dependent and cap-dependent translation initiation.Differential contribution of the m7G-cap to the 5' end-dependent translation initiation of mammalian mRNAs.Eukaryotic translation initiation machinery can operate in a bacterial-like mode without eIF2.The role of ribonucleic acids in the organization and functioning of ribosomes of E. coli.Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5' untranslated regions.Unusual ribosome binding properties of mRNA encoding bacteriophage lambda repressor.A complex RNA sequence determines the internal initiation of encephalomyocarditis virus RNA translation.[Determination of the Minimal Fragment of the Poliovirus IRES Necessary for the Formation of a Specific Complex with the Human Glycyl-tRNA Synthetase].A factor that specifically binds to the 5'-untranslated region of encephalomyocarditis virus RNA.A novel mechanism of eukaryotic translation initiation that is neither m7G-cap-, nor IRES-dependent.Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs.A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry.Differential factor requirement to assemble translation initiation complexes at the alternative start codons of foot-and-mouth disease virus RNA.Proteins of the human 40S ribosomal subunit involved in hepatitis C IRES binding as revealed from fluorescent labeling.Conversion of 48S translation preinitiation complexes into 80S initiation complexes as revealed by toeprinting.Cap-independent translation initiation of apaf-1 mRNA based on a scanning mechanism is determined by some features of the secondary structure of its 5' untranslated region.Translation eukaryotic initiation factor 4G recognizes a specific structural element within the internal ribosome entry site of encephalomyocarditis virus RNA.Pyrimidine tract binding protein strongly stimulates in vitro encephalomyocarditis virus RNA translation at the level of preinitiation complex formation.Transition of the mRNA sequence downstream from the initiation codon into a single-stranded conformation is strongly promoted by binding of the initiator tRNA.Topography of RNA in the ribosome: location of the 5 S RNA residues A39 and U40 on the central protuberance of the 50 S subunit.Structure of the ribosomal 16 S RNA-protein S4 complex as revealed by electron microscopyTopography of RNA in the ribosome: location of the 3'-end of 5 S RNA on the central protuberance of the 50 S subunitTopography of RNA in the ribosome: localization of the 3'-end of the 23 S rna on the surface of the 50 S ribosomal subunit by immune electron microscopySpatial organization of template polynucleotides on the ribosome determined by fluorescence methods
P50
Q24324687-3821E703-D51D-458B-B590-691D7A50497AQ27473136-9E1456BB-4A6E-4002-B354-2C7BB7B1BAFEQ28294967-402133AD-07A1-4B10-A69E-DDF97885A1FCQ28608941-01933DF4-222D-41BE-B364-047523CE5210Q28771734-94361B84-F148-4253-A296-9257F4496FA6Q29614570-FA333C7C-26F2-4826-8A02-24EAC1744FA6Q35622581-78B9FE01-E4C8-4623-890D-D3DC3E0CDF8BQ35920650-5A632B5D-7B88-4ECC-9D46-1B13FB85A45CQ37807291-97EB6A05-CC5B-437F-9C9A-B3608705E209Q38187430-AC62EA19-D6DA-4281-8492-18970CB77381Q38291862-8A40B094-8D76-40CC-AF45-CCAA293C23C1Q38667758-240EF4B4-EEEA-4F61-B5F8-E3BB32C24B53Q38672753-473325AA-6106-4208-9963-D5C255DDCE45Q38809392-611D0075-DC57-40DB-A74A-17E4580445FFQ39010626-D0D94CF2-2F58-4F9D-B4D9-D94A0A3E2058Q39256003-EADE4207-3274-4017-9C82-ACDFBA78F6EDQ39751295-7971D3A0-0E59-453C-8AE1-435DB369F4C8Q39810210-42A12D07-7C64-40A3-B8D4-E83ED5D0E666Q39964572-AA5E2FBF-3B44-436D-AED6-659C050CB012Q40295824-9A34CE6D-74C8-493B-B227-8209EE8BC93AQ40407765-F7EB7B91-BDE4-499C-8411-DD02A1F22176Q40411828-17C7C376-A819-40CC-9EBD-57150892DB2FQ40531241-F311D605-37CF-4510-B9D5-4C01AF51AF62Q40748121-1EF033B1-84E6-4760-A850-D637EA887F79Q41743490-1A27F529-1BD6-4F6C-9A64-23D3F7E460BFQ42112656-89343044-CD6D-4284-9FB9-39CEA3089DCCQ42122012-E758697C-D8D7-4DCA-A09B-FFCE895E7CD1Q42214815-962AA884-7916-437F-8ECE-517BA3D963DFQ42530147-3E2767B0-2A27-4EB0-913B-0B59EAB59B0AQ42685938-043718A9-067D-440C-9746-FE1B5F091700Q44264736-40B07E93-A51B-405C-BC76-8535906F9A7EQ45336092-11C606B5-D1C4-433E-AC72-36A3BE6BA5CDQ45754900-4724F817-7F60-4CE7-8594-882A5FACCD83Q45780320-EAD5FB36-6A72-45B9-B5D8-90BA2400D506Q54709823-6774F6A8-C885-4E5F-88AF-9F4409F4D422Q54796345-BE3891A7-6140-491C-A711-41EFEA63D7A4Q67042076-60CD2FA1-039E-4E05-A7D7-9459C7962632Q67266473-839AC30D-5BE8-4E35-88CC-94E9478E1EEBQ67276245-9EF444F3-DB75-40FB-82F0-0B3A8D9FAA65Q67701463-1EC1FFCC-F979-4E3C-ABC3-14400938D6FC
P50
description
Forscher
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investigador
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researcher
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ricercatore
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wetenschapper
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研究者
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name
Ivan Shatsky
@en
Iwan Nikolajewitsch Schatski
@de
Shatsky IN
@ast
Shatsky IN
@es
Shatsky IN
@nl
Иван Николаевич Шатский
@ru
type
label
Ivan Shatsky
@en
Iwan Nikolajewitsch Schatski
@de
Shatsky IN
@ast
Shatsky IN
@es
Shatsky IN
@nl
Иван Николаевич Шатский
@ru
altLabel
Ivan N. Shatsky
@en
Ivan Nikolayevich Shatsky
@en
Iwan Schatski
@de
Shatsky IN
@en
prefLabel
Ivan Shatsky
@en
Iwan Nikolajewitsch Schatski
@de
Shatsky IN
@ast
Shatsky IN
@es
Shatsky IN
@nl
Иван Николаевич Шатский
@ru
P106
P21
P31
P496
0000-0002-4428-9905