The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA
about
The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcriptTrmt61B is a methyltransferase responsible for 1-methyladenosine at position 58 of human mitochondrial tRNAsIdentification of the human mitochondrial S-adenosylmethionine transporter: bacterial expression, reconstitution, functional characterization and tissue distributionA human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionineModification at position 9 with 1-methyladenosine is crucial for structure and function of nematode mitochondrial tRNAs lacking the entire T-armA new mechanism for mtDNA pathogenesis: impairment of post-transcriptional maturation leads to severe depletion of mitochondrial tRNASer(UCN) caused by T7512C and G7497A point mutations.A T-stem slip in human mitochondrial tRNALeu(CUN) governs its charging capacityPost-transcriptional nucleotide modification and alternative folding of RNANucleoside modifications in the regulation of gene expression: focus on tRNARegulation of cell death by transfer RNAMethylated nucleosides in tRNA and tRNA methyltransferasesCrystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substratetRNA biology in mitochondriaTranscriptome-wide mapping reveals reversible and dynamic N(1)-methyladenosine methylomeThe arginine methyltransferase NDUFAF7 is essential for complex I assembly and early vertebrate embryogenesisRecessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies.A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase--extensive moonlighting in mitochondrial tRNA biogenesisStructure of the nuclease subunit of human mitochondrial RNase PWobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial diseaseS-adenosylmethionine prevents chronic alcohol-induced mitochondrial dysfunction in the rat liverMg2+ binding and archaeosine modification stabilize the G15 C48 Levitt base pair in tRNAsA manually curated database of tetrapod mitochondrially encoded tRNA sequences and secondary structuresIntegrated genomic analysis of mitochondrial RNA processing in human cancers.The deafness-associated mitochondrial DNA mutation at position 7445, which affects tRNASer(UCN) precursor processing, has long-range effects on NADH dehydrogenase subunit ND6 gene expression.Genome-wide analysis of N1-methyl-adenosine modification in human tRNAsA compendium of human mitochondrial gene expression machinery with links to disease.RNA folding with soft constraints: reconciliation of probing data and thermodynamic secondary structure prediction.An enzyme-coupled high-throughput assay for screening RNA methyltransferase activity in E. coli cell lysate.N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota.Search for characteristic structural features of mammalian mitochondrial tRNAs.Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants.Prediction of uridine modifications in tRNA sequencesCrystallization and preliminary X-ray diffraction crystallographic study of tRNA m(1)A58 methyltransferase from Saccharomyces cerevisiae.On secondary structure rearrangements and equilibria of small RNAs.A counterintuitive Mg2+-dependent and modification-assisted functional folding of mitochondrial tRNAsMitochondrial transcript maturation and its disordersMitochondrial tRNA 3' end metabolism and human disease.Alcohol-induced S-adenosylhomocysteine accumulation in the liver sensitizes to TNF hepatotoxicity: possible involvement of mitochondrial S-adenosylmethionine transport.Decreased aminoacylation in pathology-related mutants of mitochondrial tRNATyr is associated with structural perturbations in tRNA architecture.Short peptides from leucyl-tRNA synthetase rescue disease-causing mitochondrial tRNA point mutations.
P2860
Q24290128-BEA4C85B-4EF9-4F0A-B088-188A5F5DF795Q24301756-2DA81B99-C9AD-4C9D-B4D5-BF1AB604F1DBQ24301845-E50C13F8-6762-4CBB-AE8A-619E341DEB5FQ24537551-6CA5CB0C-F494-41D9-9811-EB7E5E96B7E9Q24804778-A8984BA7-0AEA-4B3D-ABC5-4965876FA3AAQ24810699-D2F0E867-3AC2-44B9-BD42-75CD1A23C5CCQ24811807-336497B3-4045-45D9-981A-2D561887EF4DQ25255871-52111854-9643-4052-A7F9-FB9F6C9D223AQ26752314-75B661D1-C916-44E4-80B8-2D3627D64D18Q27003645-FB6E7C4D-4B02-4E4C-AF94-A70D8E1B886BQ27010570-917A7C43-AD87-4C23-BA37-DF0ACFC494D3Q27680113-D8BF5778-15A4-4FB0-964D-D992127C8606Q28080757-E7EAE763-057B-4764-A23F-87C547342762Q28115015-AE832FAB-3505-419C-99AD-85AE280CA1CBQ28115372-8BED7406-A99F-49C0-88F0-295738FB7D73Q28118354-12825098-E30D-449C-9581-AEC3D6B8D506Q28118461-AC5C92E9-E994-4A74-8F98-6CC557713B0DQ28118791-53E64970-42AF-40CF-B9FD-AAA5D1A5F720Q28348375-9F4BB645-5D92-4227-9324-F4CB52D18170Q28577149-5DC77300-C933-4C55-A7E1-1329BC0E8514Q29048148-28683730-D699-4560-9609-491E8B67E644Q30838656-6460BB88-7BD0-4B75-AE77-C85DA2AF2739Q33577254-F369F9B7-47C6-4F47-B63B-1CC54204C585Q33780674-057955A2-FEEB-40B3-BAAB-13B48AFBACEFQ33913260-FF4F4D49-14C3-42FF-84E4-9CDE5304E604Q33915896-55B2E9CD-AF82-4264-8BA8-9AF46D8589A6Q34144418-336DA0D2-8181-41CD-9640-C9D5F7219077Q34276675-C45479E7-9287-4810-9837-CE47506AA43CQ34328358-7C8A7C6C-FB41-47C2-8E49-EC4387E582D0Q34363047-83DCF170-522F-4517-A6B4-FB7B07DA8173Q34365724-06E6F25C-EB12-4833-99FD-0417599B6E04Q35292030-4100E8ED-F587-4C99-8C2E-3DABC7CE8EE0Q35539400-F7AE0452-ECC3-49BE-9602-E1FECD4A179AQ35549352-24274F4F-6DA6-49D6-856A-00536EE0B46CQ35610021-DF76A1B5-4782-4211-B1AD-D81CEBEC76C4Q35825874-B719E554-12BC-4F8F-B6AD-C5B0AAE7AF38Q35914830-7AE6E226-6D8D-4F26-8F55-0B6A13A05B78Q36016487-D5A573E8-61FF-4ADA-8E43-48E742104D52Q36503796-7458687D-C6A2-4510-907B-E93077A01BCCQ36581385-D4FA0B69-754E-4EA4-B241-A195A52D2AC0
P2860
The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA
description
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1998
@ast
im April 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/04/01)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/04/01)
@nl
наукова стаття, опублікована у квітні 1998
@uk
مقالة علمية (نشرت في أبريل 1998)
@ar
name
The presence of modified nucle ...... of a human mitochondrial tRNA
@ast
The presence of modified nucle ...... of a human mitochondrial tRNA
@en
The presence of modified nucle ...... of a human mitochondrial tRNA
@nl
type
label
The presence of modified nucle ...... of a human mitochondrial tRNA
@ast
The presence of modified nucle ...... of a human mitochondrial tRNA
@en
The presence of modified nucle ...... of a human mitochondrial tRNA
@nl
prefLabel
The presence of modified nucle ...... of a human mitochondrial tRNA
@ast
The presence of modified nucle ...... of a human mitochondrial tRNA
@en
The presence of modified nucle ...... of a human mitochondrial tRNA
@nl
P2093
P2860
P3181
P356
P1476
The presence of modified nucle ...... of a human mitochondrial tRNA
@en
P2093
P2860
P304
P3181
P356
10.1093/NAR/26.7.1636
P407
P50
P577
1998-04-01T00:00:00Z