about
Armless mitochondrial tRNAs in Enoplea (Nematoda)The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological FunctionsTrying on tRNA for Size: RNase P and the T-box Riboswitch as Molecular RulersEarly bioenergetic evolutionThe human mitochondrial transcriptome and the RNA-binding proteins that regulate its expressionThermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecturetRNA biology in mitochondriaA subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase--extensive moonlighting in mitochondrial tRNA biogenesisCRISPRmap: an automated classification of repeat conservation in prokaryotic adaptive immune systemsIdentification of the determinants of tRNA function and susceptibility to rapid tRNA decay by high-throughput in vivo analysis.New molecular engineering approaches for crystallographic studies of large RNAsIn vitro biosynthesis of a universal t6A tRNA modification in Archaea and EukaryaSystematic identification of tRNAome and its dynamics in Lactococcus lactisTopological constraints are major determinants of tRNA tertiary structure and dynamics and provide basis for tertiary folding cooperativity.Detecting riboSNitches with RNA folding algorithms: a genome-wide benchmark.Noncanonical secondary structure stabilizes mitochondrial tRNA(Ser(UCN)) by reducing the entropic cost of tertiary folding.Structural snapshots of actively translating human ribosomes.tRNA acceptor stem and anticodon bases form independent codes related to protein folding.Structure and mechanism of the T-box riboswitches.Mechanistic Studies Reveal Similar Catalytic Strategies for Phosphodiester Bond Hydrolysis by Protein-only and RNA-dependent Ribonuclease PThe concept of RNA-assisted protein folding: the role of tRNA.Structural insights into protein-only RNase P complexed with tRNA.Transfer RNA modifications: nature's combinatorial chemistry playground.The Conservation and Function of RNA Secondary Structure in Plants.The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.From end to end: tRNA editing at 5'- and 3'-terminal positions.Interaction of tRNA with eukaryotic ribosomeStructural Insights into tRNA Dynamics on the Ribosome.tRNA--the golden standard in molecular biology.RNA versatility governs tRNA function: Why tRNA flexibility is essential beyond the translation cycle.Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.tRNA Modifications: Impact on Structure and Thermal Adaptation.RNA structure, binding, and coordination in Arabidopsis.A hypertension-associated mitochondrial DNA mutation alters the tertiary interaction and function of tRNALeu(UUR).Structural effects of modified ribonucleotides and magnesium in transfer RNAs.Identifying the ligated amino acid of archaeal tRNAs based on positions outside the anticodontRNA structure and evolution and standardization to the three nucleotide genetic code.Repairing tRNA termini: News from the 3' end.'Z-DNA like' fragments in RNA: a recurring structural motif with implications for folding, RNA/protein recognition and immune response.SMORE: Synteny Modulator of Repetitive Elements.
P2860
Q24617591-032A795E-00C2-499E-9D00-400AC162363CQ26748917-FB166C8A-1D2E-4E93-8978-77937BFAB7C8Q26752547-BC4D5072-02A6-42D5-8587-5941909EDF91Q27011350-48A83936-1CAC-498F-9EF6-BCF59CAFF7ABQ27016551-994DB651-4384-4953-834B-FDACBBF4202EQ27675660-1F2FCA98-CA85-4B04-97EE-F06F77A95C52Q28080757-50321EB4-B3F3-4B83-91C0-F072FEFE2EABQ28118461-F41182B6-FDC4-4DA8-98DA-A836CE432723Q28679191-4EA89EE8-DEFC-4E75-B91F-73FA7EFEB472Q33984519-0F3AA059-9AD2-41D5-8E8E-B7DD3A26474EQ34021859-B9953E3E-C1C3-4E2D-B40A-C812227FD94FQ34034860-4A88ECC8-8EFA-4FCF-85D6-CE6369AB0208Q34115800-D9AC7B9C-3201-46EC-B74B-D4673FE8B0A4Q34312979-0E8BF6C6-9073-4B0F-80FA-A205FEED3396Q35089028-112A8AE1-4A12-4128-B72A-C64A74B6DDFBQ35447374-E61C38B9-7768-45EA-A539-A791FC339B3AQ35608572-3D422AA6-D6C9-42E1-A82E-C50C63E050DCQ35764501-A5589D42-3C87-4B2B-9077-1D2CB805B7BBQ35772362-1C9F5E58-E0DC-4603-803E-8A65D7B4469FQ35861007-A9F6C19F-7C13-4A41-B6CA-5B1E082C0F50Q35984354-2DB7E5D8-307E-4B41-ACB0-4673EE0D6204Q36582143-B089D920-5E1B-40F9-A83A-BA0CDA331BA6Q36922474-E9BBFFE4-4437-4D76-BDFE-DF8909744A56Q37445124-9626C036-043D-4084-89E4-8B9E20AF4C9DQ38262499-3A5F8A47-5EBE-48CD-A7C8-A5779DDB137DQ38298533-F205220D-8FD2-42AC-9151-6CF6DD3FC950Q38399151-35100C81-AF94-47B7-A8CB-E4ECF415BE93Q38459563-CF9BE822-3F65-48C7-80B9-31B4C7C67A58Q38628517-C35616F8-64DC-4516-AF59-E59BBFF79E30Q38779815-6D868645-9403-49BA-A7B3-F517B0B41ECBQ39142994-0F364739-F654-46A6-BB0E-6FE2052AE39FQ39218671-9406DCD4-0F51-48A3-947F-76794E28FDB9Q39404169-FB0C1C0F-4FEA-48BC-BD77-5A86C8C8FF36Q40146692-3A0963C1-0F02-47C9-A1E6-B1CB9FA8CCF3Q40672876-9396F64A-98D7-4239-BFEC-99AD20DBD4A5Q41131896-072C0D41-99EF-407F-8A13-DFFC2B041F63Q41544803-010EABA2-AB8C-475A-B38E-1FE8BF563E2CQ41697901-5CAEBF1E-3E74-4089-8CF9-3FCF449F2DD7Q42428480-B0680625-2D0A-4A74-8D68-7390DF5726C8Q46271532-87952666-A151-4613-BAE0-E87FA81C65EA
P2860
description
2012 nî lūn-bûn
@nan
2012 թուականին հրատարակուած գիտական յօդուած
@hyw
2012 թվականին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
name
Structure of transfer RNAs: similarity and variability
@ast
Structure of transfer RNAs: similarity and variability
@en
Structure of transfer RNAs: similarity and variability
@nl
type
label
Structure of transfer RNAs: similarity and variability
@ast
Structure of transfer RNAs: similarity and variability
@en
Structure of transfer RNAs: similarity and variability
@nl
prefLabel
Structure of transfer RNAs: similarity and variability
@ast
Structure of transfer RNAs: similarity and variability
@en
Structure of transfer RNAs: similarity and variability
@nl
P2093
P2860
P50
P3181
P356
P1476
Structure of transfer RNAs: similarity and variability
@en
P2093
Catherine Florentz
Frank Jühling
Joern Pütz
P2860
P3181
P356
10.1002/WRNA.103
P407
P577
2012-01-01T00:00:00Z