about
Circularly permuted tRNA genes: their expression and implications for their physiological relevance and developmentComparative genomics and evolution of proteins involved in RNA metabolismStructure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reactionCharacterization of the Saccharomyces cerevisiae cyclic nucleotide phosphodiesterase involved in the metabolism of ADP-ribose 1",2"-cyclic phosphate.Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligasesMolecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligasesDetection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamilyMechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathway.Mutational analysis of yeast mRNA capping enzyme.tRNA splicing.Branchiostoma floridae has separate healing and sealing enzymes for 5'-phosphate RNA ligation.Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domainsStructural evidence that brain cyclic nucleotide phosphodiesterase is a member of the 2H phosphodiesterase superfamily.Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligasesJunction phosphate is derived from the precursor in the tRNA spliced by the archaeon Haloferax volcanii cell extract.Identification of essential residues in Thermus thermophilus DNA ligase.Two distinct DNA ligase activities in mitotic extracts of the yeast Saccharomyces cerevisiae.RNA damage in biological conflicts and the diversity of responding RNA repair systemsThe structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94 A resolution reveals a possible open form with a wider active-site cleft.Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate formation, and GMP transfer to RNA.Location of the active site for enzyme-adenylate formation in DNA ligases.Diversity and roles of (t)RNA ligases.The myelin membrane-associated enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase: on a highway to structure and functionHandling tRNA introns, archaeal way and eukaryotic way.Preferential binding of yeast tRNA ligase to pre-tRNA substrates.Cloning, nucleotide sequence, and engineered expression of Thermus thermophilus DNA ligase, a homolog of Escherichia coli DNA ligase.A kinetic framework for tRNA ligase and enforcement of a 2'-phosphate requirement for ligation highlights the design logic of an RNA repair machine.Structure-function analysis of yeast tRNA ligase.Mutational analysis of bacteriophage T4 RNA ligase 1. Different functional groups are required for the nucleotidyl transfer and phosphodiester bond formation steps of the ligation reaction.Genetic and biochemical analysis of the functional domains of yeast tRNA ligase.Characterization of a baculovirus enzyme with RNA ligase, polynucleotide 5'-kinase, and polynucleotide 3'-phosphatase activities.
P2860
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P2860
description
1990 nî lūn-bûn
@nan
1990 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Domain structure in yeast tRNA ligase.
@ast
Domain structure in yeast tRNA ligase.
@en
Domain structure in yeast tRNA ligase.
@nl
type
label
Domain structure in yeast tRNA ligase.
@ast
Domain structure in yeast tRNA ligase.
@en
Domain structure in yeast tRNA ligase.
@nl
prefLabel
Domain structure in yeast tRNA ligase.
@ast
Domain structure in yeast tRNA ligase.
@en
Domain structure in yeast tRNA ligase.
@nl
P2093
P3181
P356
P1433
P1476
Domain structure in yeast tRNA ligase.
@en
P2093
P304
P3181
P356
10.1021/BI00478A004
P407
P577
1990-07-03T00:00:00Z