Search Results - "RNA, Transfer/metabolism"

Cryo-EM structures of the MnmE–MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification

Authors: Laila Maes Israel Mares-Mejía Ella Martin et al.

Contributors: Laila Maes Israel Mares-Mejía Ella Martin et al.

Source: Nucleic Acids Research. 53

Subject Terms: Models, Molecular, RNA, Transfer/metabolism, Methyltransferases/chemistry, Protein Conformation, Flavin-Adenine Dinucleotide/metabolism, Escherichia coli Proteins/chemistry, Cryoelectron Microscopy, NAD/metabolism, Protein Binding, GTP Phosphohydrolases

Access URL: https://biblio.vub.ac.be/vubir/cryoem-structures-of-the-mnmemnmg-complex-reveal-large-conformational-changes-and-provide-new-insights-into-the-mechanism-of-trna-modification(e0a1d23a-e82f-4641-8e99-f03cd8c1729f).html

Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4

Authors: Sokołowski, Mikołaj Kwasna, Dominika Ravichandran, Keerthiraju E et al.

Source: Nucleic Acids Res

Subject Terms: Models, Molecular, 0301 basic medicine, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae Proteins Genetics, Saccharomyces cerevisiae Proteins Metabolism, Ubiquitin-Activating Enzymes, Saccharomyces cerevisiae, Saccharomyces Cerevisiae Genetics, RNA, Transfer Chemistry, Ubiquitin-Activating Enzymes Genetics, 03 medical and health sciences, Sulfhydryl Compounds Metabolism, Protein Domains, RNA, Transfer, RNA, Transfer Metabolism, Saccharomyces cerevisiae Metabolism, Sulfhydryl Compounds, Nucleotidyltransferases Chemistry, Ubiquitins, Ubiquitin-Activating Enzymes Chemistry, 0303 health sciences, Nucleotidyltransferases Metabolism, Ubiquitin-Activating Enzymes Metabolism, Ubiquitins Genetics, Cryoelectron Microscopy, Ubiquitins Metabolism, Molecular and Structural Biology, Nucleotidyltransferases, Ubiquitins Chemistry, Sulfhydryl Compounds Chemistry, Mutation, Nucleotidyltransferases Genetics, Saccharomyces cerevisiae Proteins Chemistry, Protein Binding

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/39673271
https://ruj.uj.edu.pl/handle/item/499751
https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkae1111/7914207

tRNA-derived fragments in T lymphocyte–beta cell crosstalk and in type 1 diabetes pathogenesis in NOD mice

Authors: Brozzi, F. Jacovetti, C. Cosentino, C. et al.

Source: Diabetologia
Diabetologia, vol. 67, no. 10, pp. 2260-2274

Subject Terms: CD4-Positive T-Lymphocytes, 0301 basic medicine, 0303 health sciences, RNA, Untranslated, T-Lymphocytes, Apoptosis, Article, Mice, Islets of Langerhans, Extracellular Vesicles, 03 medical and health sciences, Diabetes Mellitus, Type 1, RNA, Transfer, Mice, Inbred NOD, Insulin-Secreting Cells, Animals, Diabetes Mellitus, Type 1/immunology, Diabetes Mellitus, Type 1/metabolism, Diabetes Mellitus, Type 1/genetics, Insulin-Secreting Cells/metabolism, RNA, Transfer/genetics, RNA, Transfer/metabolism, Female, CD4-Positive T-Lymphocytes/metabolism, CD4-Positive T-Lymphocytes/immunology, Islets of Langerhans/metabolism, Islets of Langerhans/immunology, Extracellular Vesicles/metabolism, T-Lymphocytes/immunology, T-Lymphocytes/metabolism, RNA, Untranslated/genetics, Autoimmunity, Extracellular vesicles, Insulin, Pancreatic islet

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/38967669
https://serval.unil.ch/notice/serval:BIB_BF3CD8D4736F
https://serval.unil.ch/resource/serval:BIB_BF3CD8D4736F.P001/REF.pdf
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_BF3CD8D4736F9

tRNA binding to Kti12 is crucial for wobble uridine modification by Elongator

Authors: Scherf, David Hammermeister, Alexander Böhnert, Pauline et al.

Source: Nucleic Acids Res

Subject Terms: Bäckerhefe, Anticodon Metabolism, Saccharomyces cerevisiae Proteins, Uridine Metabolism, Saccharomyces Cerevisiae Proteins Genetics, Killer Factors, Yeast Metabolism, Saccharomyces cerevisiae, Saccharomyces Cerevisiae Genetics, RNA, Transfer Chemistry, Killer Factors, Yeast, Saccharomyces cerevisia Metabolism, RNA, Transfer, RNA, Transfer Metabolism, Mutation, Transfer-RNS, Saccharomyces Cerevisiae Proteins Metabolism, RNA and RNA-protein complexes, Anticodon, Amino Acid Sequence, Uridin, Uridine, Saccharomyces Cerevisiae Proteins Chemistry, Protein Binding

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/40226916
https://ruj.uj.edu.pl/handle/item/559194
https://phaidra.vetmeduni.ac.at/o:4101
https://doi.org/10.1093/nar/gkaf296

E4F1 coordinates pyruvate metabolism and the activity of the elongator complex to ensure translation fidelity during brain development.

Authors: Di Michele, Michela Attina, Aurore Roux, Pierre-François et al.

Source: Nature Communications, 16 (1), 67 (2025-01-02)

Subject Terms: Pyruvic Acid, Pyruvate Dehydrogenase Complex, RNA, Transfer, Dihydrolipoyllysine-Residue Acetyltransferase, Basic-Leucine Zipper Transcription Factors, Uridine, ELP3 protein, human, Nerve Tissue Proteins, Histone Acetyltransferases, Animals, Mice, Humans, Pyruvate Dehydrogenase Complex/metabolism, Pyruvate Dehydrogenase Complex/genetics, Leigh Disease/metabolism, Leigh Disease/genetics, Neurons/metabolism, RNA, Transfer/metabolism, RNA, Transfer/genetics, Protein Biosynthesis, Gene Expression Regulation, Developmental, Dihydrolipoyllysine-Residue Acetyltransferase/metabolism, Dihydrolipoyllysine-Residue Acetyltransferase/genetics, Basic-Leucine Zipper Transcription Factors/metabolism, Basic-Leucine Zipper Transcription Factors/genetics, Mice, Knockout, Mice, Inbred C57BL, Uridine/metabolism, Female, Brain/metabolism, Brain/embryology, Brain/growth & development, Pyruvic Acid/metabolism, Brain, Leigh Disease, Neurons, Chemistry (all), Biochemistry, Genetics and Molecular Biology (all), Physics and Astronomy (all), Human health sciences, Neurology, Sciences de la santé humaine, Neurologie

Relation: https://www.nature.com/articles/s41467-024-55444-y.pdf; urn:issn:2041-1723

Access URL: https://orbi.uliege.be/handle/2268/328564

Ribosome association primes the stringent factor Rel for tRNA-dependent locking in the A-site and activation of (p)ppGpp synthesis

Authors: Julien Caballero-Montes Pavel Kudrin Genki Akanuma et al.

Source: Nucleic Acids Res
Nucleic acids research, 49 (1
Nucleic Acids Research

Subject Terms: Models, Molecular, 0301 basic medicine, RNA Processing, Protein Conformation, Acylation, Ribosomes -- metabolism, Post-Transcriptional, Ribosome Subunits, Large, Bacterial, RNA, Transfer -- metabolism, Biochemistry, Microbiology in the medical area, GTP Pyrophosphokinase -- metabolism, GTP Pyrophosphokinase, 03 medical and health sciences, Genetic, Bacterial Proteins, RNA, Transfer, Models, Catalytic Domain, Ribosome Subunits, Mikrobiologi inom det medicinska området, Bacterial Proteins -- metabolism, RNA and RNA-protein complexes, RNA Processing, Post-Transcriptional, Biokemi, Molecular Biology, Ribosome Subunits, Large, Bacterial -- metabolism, 2. Zero hunger, Bacillus subtilis -- genetics -- metabolism, 0303 health sciences, Molekylärbiologi, Models, Genetic, Hydrolysis, Transfer -- metabolism, Guanosine Pentaphosphate, Molecular, Sciences bio-médicales et agricoles, Guanosine Pentaphosphate -- biosynthesis, RNA, Large, Bacterial -- metabolism, Biologie, Ribosomes, Allosteric Site, Bacillus subtilis

File Description: 1 full-text file(s): application/pdf; application/pdf

Access URL: https://academic.oup.com/nar/article-pdf/49/1/444/35597056/gkaa1187.pdf
https://pubmed.ncbi.nlm.nih.gov/33330919
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7797070
https://europepmc.org/articles/PMC7797070/
https://pubmed.ncbi.nlm.nih.gov/33330919/
https://academic.oup.com/nar/article/49/1/444/6039922
https://www.ncbi.nlm.nih.gov/pubmed/33330919
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7797070
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/326084
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-180658

Exploring pseudouridylation: dysregulation in disease and therapeutic potential

Authors: Maria Guillen-Angel Jean-Yves Roignant

Source: Current opinion in genetics & development, vol. 87, pp. 102210

Subject Terms: COVID-19 Vaccines, SARS-CoV-2, RNA Splicing, COVID-19, 3. Good health, Humans, Pseudouridine/metabolism, Pseudouridine/genetics, COVID-19/genetics, Neoplasms/genetics, Neoplasms/therapy, Neoplasms/metabolism, Neoplasms/pathology, SARS-CoV-2/genetics, RNA Processing, Post-Transcriptional/genetics, RNA, Messenger/genetics, RNA, Messenger/metabolism, Animals, Neurodevelopmental Disorders/genetics, Neurodevelopmental Disorders/therapy, Neurodevelopmental Disorders/metabolism, Neurodevelopmental Disorders/pathology, Protein Biosynthesis, RNA Splicing/genetics, RNA, Transfer/genetics, RNA, Transfer/metabolism, RNA, Transfer, Neurodevelopmental Disorders, Neoplasms, RNA, Messenger, RNA Processing, Post-Transcriptional, Pseudouridine

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/38833893
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_5728369E06963
https://serval.unil.ch/notice/serval:BIB_5728369E0696
https://serval.unil.ch/resource/serval:BIB_5728369E0696.P001/REF.pdf

The mitochondrial tRNA-derived fragment, mt-tRF-LeuTAA, couples mitochondrial metabolism to insulin secretion

Authors: Cecile Jacovetti Chris Donnelly Véronique Menoud et al.

Source: Mol Metab
Molecular Metabolism, Vol 84, Iss, Pp 101955-(2024)
Molecular metabolism, vol. 84, pp. 101955

Subject Terms: Male, RNA, Mitochondrial, Insulin secretion, Animals, Rats, Humans, Mitochondria/metabolism, Insulin Secretion, Insulin-Secreting Cells/metabolism, RNA, Transfer/metabolism, RNA, Transfer/genetics, Insulin/metabolism, Islets of Langerhans/metabolism, Diabetes Mellitus, Type 2/metabolism, RNA, Mitochondrial/metabolism, RNA, Mitochondrial/genetics, Mice, Rats, Wistar, Electron Transport, Mitochondrial OXPHOS, Mitochondrial tRNA-derived fragments, RC31-1245, Mitochondria, Islets of Langerhans, RNA, Transfer, Diabetes Mellitus, Type 2, Insulin-Secreting Cells, Insulin, Original Article, Internal medicine

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/38704026
https://doaj.org/article/21f86b06ee584a01b80a33b6b969d246
https://serval.unil.ch/notice/serval:BIB_A5399F025A1C
https://serval.unil.ch/resource/serval:BIB_A5399F025A1C.P001/REF.pdf
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_A5399F025A1C7

Pancreatic β-cell tRNA hypomethylation and fragmentation link TRMT10A deficiency with diabetes

Authors: Cosentino, Cristina Toivonen, Sanna Diaz Villamil, Esteban et al.

Contributors: Cosentino, Cristina Toivonen, Sanna Diaz Villamil, Esteban et al.

Source: Nucleic Acids Res
Nucleic Acids Research, Vol. 46, no.19, p. 10302-10318 (2018)
Nucleic acids research, 46 (19
Nucleic Acids Research

Subject Terms: 0301 basic medicine, Diabetes Mellitus -- genetics -- metabolism, Genetic Linkage, name=Genetics, Cells, Induced Pluripotent Stem Cells, Methyltransferases -- deficiency -- genetics -- metabolism, Apoptosis, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, DNA Fragmentation, RNA, Transfer -- metabolism, Induced Pluripotent Stem Cells -- physiology, 03 medical and health sciences, RNA, Transfer, Insulin-Secreting Cells, Genetics, Diabetes Mellitus, Animals, Humans, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, Cells, Cultured, Aged, Molecular Biology/Genomics [q-bio.GN], Cultured, [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, Apoptosis -- genetics, Cell Differentiation -- genetics, Cell Death, Nucleic Acid Enzymes, Transfer -- metabolism, Cell Differentiation, Methyltransferases, Sciences bio-médicales et agricoles, DNA Methylation, Middle Aged, Rats, 3. Good health, Mutation, RNA, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Cell Death -- genetics, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, Insulin-Secreting Cells -- metabolism -- physiology

File Description: 1 full-text file(s): application/pdf; application/pdf; 2 full-text file(s): application/vnd.openxmlformats-officedocument.wordprocessingml.document

Access URL: https://academic.oup.com/nar/article-pdf/46/19/10302/26334040/gky839.pdf
https://pubmed.ncbi.nlm.nih.gov/30247717
https://europepmc.org/abstract/MED/30247717
https://www.ncbi.nlm.nih.gov/pubmed/30247717
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/278004/Details
https://hal.archives-ouvertes.fr/hal-01945851
https://pubmed.ncbi.nlm.nih.gov/30247717/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6212784
https://hdl.handle.net/2078.1/206668
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/278004
https://hal.science/hal-01945851v1
https://doi.org/10.1093/nar/gky839
https://hal.science/hal-01945851v1/document
https://hdl.handle.net/11568/955035
https://doi.org/10.1093/nar/gky839

Small RNAs derived from tRNA fragmentation regulate the functional maturation of neonatal β cells

Authors: Mustafa Bilal Bayazit Cécile Jacovetti Cristina Cosentino et al.

Source: Cell reports, vol. 40, no. 2, pp. 111069

Subject Terms: Animals, Cell Proliferation, Insulin Secretion, Insulin-Secreting Cells/metabolism, RNA/metabolism, RNA, Transfer/genetics, RNA, Transfer/metabolism, Rats, CP: Developmental biology, CP: Metabolism, diabetes, insulin, metabolism, pancreatic islet, transfer RNA, RNA, Transfer, Insulin-Secreting Cells, RNA

File Description: application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/35830789
https://serval.unil.ch/notice/serval:BIB_CD2CB954E2CD
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_CD2CB954E2CD9
https://serval.unil.ch/resource/serval:BIB_CD2CB954E2CD.P001/REF.pdf

A multiplicity of factors contributes to selective RNA polymerase III occupancy of a subset of RNA polymerase III genes in mouse liver

Authors: Felix Naef Julia Cajan Guillaume Rey et al.

Contributors: Felix Naef Julia Cajan Guillaume Rey et al.

Source: Genome Research, vol. 22, no. 4, pp. 666-680

Subject Terms: Male, 0301 basic medicine, 2716 Genetics (clinical), Chromatin Immunoprecipitation, 0303 health sciences, Models, Genetic, Gene Expression Profiling, RNA Polymerase III, Genomics, Sequence Analysis, DNA, Mice, Inbred C57BL, Mice, 03 medical and health sciences, SX00 SystemsX.ch, 1311 Genetics, Liver, RNA, Transfer, 570 Life sciences, biology, Animals, Humans, SX04 CycliX, Chromatin Immunoprecipitation/methods, Genomics/methods, Liver/metabolism, Oligonucleotide Array Sequence Analysis, RNA Polymerase III/genetics, RNA Polymerase III/metabolism, RNA, Transfer/genetics, RNA, Transfer/metabolism, Sequence Analysis, DNA/methods

File Description: application/pdf; Genome_Res.-2012-Canella-666-80.pdf - application/pdf

Access URL: http://genome.cshlp.org/content/22/4/666.full.pdf
https://pubmed.ncbi.nlm.nih.gov/22287103
https://www.zora.uzh.ch/id/eprint/78971/
https://core.ac.uk/display/16487327
https://serval.unil.ch/en/notice/serval:BIB_AFFF7604F2F3
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317149/
https://serval.unil.ch/resource/serval:BIB_AFFF7604F2F3.P001/REF.pdf
https://www.zora.uzh.ch/id/eprint/78971/1/Genome_Res.-2012-Canella-666-80.pdf
https://serval.unil.ch/notice/serval:BIB_AFFF7604F2F3
https://serval.unil.ch/resource/serval:BIB_AFFF7604F2F3.P001/REF.pdf
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_AFFF7604F2F39

The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning

Authors: Wilson, D. N. Schluenzen, F. Harms, J. M. et al.

Source: Proceedings of the National Academy of Sciences of the United States of America 105, 13339-13344 (2008). doi:10.1073/pnas.0804276105

Subject Terms: Models, Molecular, 0301 basic medicine, RNA, Transfer: chemistry, Oxazolidinones: chemistry, Peptidyl Transferases: metabolism, Anti-Bacterial Agents: pharmacology, 03 medical and health sciences, RNA, Transfer, Oxazolidinones, Binding Sites, Oxazolidinones: pharmacology, Anti-Bacterial Agents: chemistry, Ribosomes: enzymology, Anti-Bacterial Agents, Protein Structure, Tertiary, 3. Good health, RNA, Transfer: metabolism, Peptidyl Transferases: chemistry, Peptidyl Transferases, Nucleic Acid Conformation, Ribosomes: drug effects, Deinococcus, Ribosomes, Deinococcus: enzymology, Deinococcus: drug effects, Protein Binding

Access URL: http://www.pnas.org/content/105/36/13339.full.pdf
https://pubmed.ncbi.nlm.nih.gov/18757750
http://www.ncbi.nlm.nih.gov/pubmed/18757750
https://www.pnas.org/content/105/36/13339
https://www.jstor.org/stable/25464045
http://ui.adsabs.harvard.edu/abs/2008PNAS..10513339W/abstract
http://www.rcsb.org/pdb/explore/explore.do?structureId=3DLL
https://bib-pubdb1.desy.de/record/84487

The YqfN protein of Bacillus subtilis is the tRNA: m 1 A22 methyltransferase (TrmK)

Authors: Roovers, Martine Kaminska, Katarzyna H Tkaczuk, Karolina L et al.

Source: Nucleic Acids Res
Nucleic acids research, 36 (10

Subject Terms: Models, Molecular, 0301 basic medicine, Bacterial Proteins -- genetics, tRNA Methyltransferases -- classification, Molecular Sequence Data, Sequence Homology, RNA, Transfer -- metabolism, 03 medical and health sciences, Bacillus subtilis -- growth & development, Bacterial Proteins, RNA, Transfer, Models, Transfer -- chemistry, Amino Acid Sequence, tRNA Methyltransferases -- chemistry, Molecular Biology, Bacillus subtilis -- enzymology, Phylogeny, tRNA Methyltransferases, 0303 health sciences, Base Sequence, Sequence Homology, Amino Acid, Bacterial Proteins -- chemistry, Transfer -- metabolism, Molecular, Sciences bio-médicales et agricoles, 3. Good health, Amino Acid, RNA, Transfer -- chemistry, RNA, tRNA Methyltransferases -- genetics, Bacterial Proteins -- classification, Bacillus subtilis

File Description: 2 full-text file(s): application/pdf; application/pdf

Access URL: https://academic.oup.com/nar/article-pdf/36/10/3252/16748246/gkn169.pdf
https://pubmed.ncbi.nlm.nih.gov/18420655
https://core.ac.uk/display/101034570
https://paperity.org/p/34594318/the-yqfn-protein-of-bacillus-subtilis-is-the-trna-m1a22-methyltransferase-trmk
https://academic.oup.com/nar/article/36/10/3252/2410272
https://www.ncbi.nlm.nih.gov/pubmed/18420655
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50479/Details
http://europepmc.org/articles/PMC2425500
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50479

Life at low temperatures: is disorder the driving force?

Authors: Feller, Georges

Source: Extremophiles. 11:211-216

Subject Terms: 0301 basic medicine, Membrane Fluidity, ligand binding, Entropy, Membrane Fluidity/physiology, Bacteria/growth & development/metabolism, Biochimie, biophysique & biologie moléculaire, 03 medical and health sciences, RNA, Transfer/metabolism, Bacterial Proteins, RNA, Transfer, psychrophiles, 0303 health sciences, RNA, Bacterial/metabolism, Bacteria, Bacterial Proteins/metabolism, stability, Life sciences, Adaptation, Physiological, proteins, 3. Good health, Fatty Acids, Unsaturated/metabolism, Cold Temperature, RNA, Bacterial, Sciences du vivant, Fatty Acids, Unsaturated, Biochemistry, biophysics & molecular biology

Access URL: https://pubmed.ncbi.nlm.nih.gov/17160345
http://orbi.ulg.ac.be/handle/2268/14513
https://link.springer.com/content/pdf/10.1007%2Fs00792-006-0050-1.pdf
https://link.springer.com/article/10.1007/s00792-006-0050-1
https://orbi.uliege.be/handle/2268/14513
https://hdl.handle.net/2268/14513
https://doi.org/10.1007/s00792-006-0050-1

Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria--evolutionary implications

Authors: Urbonavicius, Jaunius Skouloubris, Stéphane Myllykallio, Hannu et al.

Source: Nucleic Acids Res
Nucleic acids research, 33 (13

Subject Terms: Escherichia coli -- metabolism, 0301 basic medicine, Evolution, RNA, Transfer -- metabolism, Article, Flavins -- metabolism, Evolution, Molecular, 03 medical and health sciences, Bacterial Proteins, RNA, Transfer, Flavins, Escherichia coli, Bacterial Proteins -- chemistry -- classification, Uridine, Bacillus subtilis -- enzymology, Phylogeny, Bacteria -- enzymology, tRNA Methyltransferases, Bacteria, tRNA Methyltransferases -- classification -- genetics -- metabolism, Bacterial, Transfer -- metabolism, Molecular, Genomics, Sciences bio-médicales et agricoles, 3. Good health, Uridine -- analogs & derivatives -- metabolism, Genes, Genes, Bacterial, RNA, Bacillus subtilis

File Description: 1 full-text file(s): application/pdf

Access URL: https://pubmed.ncbi.nlm.nih.gov/16027442
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/177341/Details
https://paperity.org/p/34522484/identification-of-a-novel-gene-encoding-a-flavin-dependent-trna-m5u-methyltransferase-in
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1178002/
https://core.ac.uk/display/77537617
https://academic.oup.com/nar/article/33/13/3955/1094349
http://nar.oxfordjournals.org/content/33/13/3955.full
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/177341

Nuclear export of RNA

Authors: Rodriguez, Manuel S Dargemont, Catherine Stutz, Françoise

Source: Biology of the Cell, Vol. 96, No 8 (2004) pp. 639-55

Subject Terms: 0301 basic medicine, Nucleocytoplasmic Transport Proteins, Karyopherins/physiology, Active Transport, Cell Nucleus, Receptors, Cytoplasmic and Nuclear, Exportin 1 Protein, Ribonucleoproteins/biosynthesis/metabolism, Karyopherins, RNA Transport/physiology, Models, Biological, Nucleocytoplasmic Transport Proteins/physiology, RNA Transport, RNA, Ribosomal/metabolism, RNA, Small Nuclear/metabolism, RNA, Viral/metabolism, 03 medical and health sciences, RNA, Transfer/metabolism, Ran GTP-Binding Protein/physiology, RNA, Transfer, ddc:570, RNA, Small Nuclear, Animals, Humans, Active Transport, Cell Nucleus/physiology, Ribosomes/metabolism, RNA, Messenger, Nuclear Pore/physiology, RNA, Messenger/biosynthesis/metabolism, 0303 health sciences, RNA-Binding Proteins, beta Karyopherins, Receptors, Cytoplasmic and Nuclear/physiology, ran GTP-Binding Protein, Ribonucleoproteins, RNA, Ribosomal, Nuclear Pore, RNA-Binding Proteins/physiology, RNA, Viral, Ribosomes, Beta Karyopherins/physiology

File Description: application/pdf

Access URL: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.biolcel.2004.04.014
https://pubmed.ncbi.nlm.nih.gov/15519698
https://www.ncbi.nlm.nih.gov/pubmed/15519698
https://archive-ouverte.unige.ch/unige:19433
https://www.sciencedirect.com/science/article/abs/pii/S0248490004001224
http://doi.wiley.com/10.1016/j.biolcel.2004.04.014
https://onlinelibrary.wiley.com/doi/pdf/10.1016/j.biolcel.2004.04.014
https://pubmed.ncbi.nlm.nih.gov/15519698/
https://archive-ouverte.unige.ch/unige:19433
https://doi.org/10.1016/j.biolcel.2004.04.014
https://archive-ouverte.unige.ch/unige:19433

The ribose methylation enzyme FTSJ1 has a conserved role in neuron morphology and learning performance

Authors: Amélie Piton Elise Schaefer Virginie Marchand et al.

Contributors: Amélie Piton Elise Schaefer Virginie Marchand et al.

Source: Life Sci Alliance
Life science alliance, vol. 6, no. 4, pp. e202201877

Subject Terms: Neurons, 0301 basic medicine, Ribose, Sustainable Development Goals, Nuclear Proteins, Methyltransferases, Methylation, Humans, Intellectual Disability/genetics, Methyltransferases/genetics, RNA, Transfer/genetics, RNA, Transfer/metabolism, Neurons/metabolism, Nuclear Proteins/genetics, 3. Good health, Transfer, 03 medical and health sciences, pathogenic variant, RNA, Transfer, Intellectual Disability, morphology, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, cancer, RNA, genetics, Research Articles, SDG 3

File Description: application/pdf

Access URL: https://www.biorxiv.org/content/biorxiv/early/2021/05/22/2021.02.06.430044.full.pdf
https://pubmed.ncbi.nlm.nih.gov/36720500
https://www.biorxiv.org/content/biorxiv/early/2021/02/08/2021.02.06.430044.full.pdf
https://www.biorxiv.org/content/10.1101/2021.02.06.430044v1
https://europepmc.org/article/PPR/PPR279409
https://www.biorxiv.org/content/10.1101/2021.02.06.430044v2
http://www.biorxiv.org/content/10.1101/2021.02.06.430044v2
https://www.biorxiv.org/content/biorxiv/early/2021/05/22/2021.02.06.430044.full.pdf
https://serval.unil.ch/resource/serval:BIB_39AAE65032F8.P001/REF.pdf
https://serval.unil.ch/notice/serval:BIB_39AAE65032F8
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_39AAE65032F88

How Optimized Is the Translational Machinery in Escherichia coli, Salmonella typhimurium and Saccharomyces cerevisiae?

Authors: Xia, X

Source: Genetics. 149:37-44

Subject Terms: Salmonella typhimurium, 0301 basic medicine, RNA, Transfer - metabolism, Saccharomyces cerevisiae - genetics, Models, Genetic, Transfer - metabolism, RNA, Fungal, Saccharomyces cerevisiae, 3. Good health, RNA, Bacterial, 03 medical and health sciences, Genetic, RNA, Transfer, Models, Protein Biosynthesis, Escherichia coli, RNA, Codon, Escherichia coli - genetics

File Description: 418 bytes; text/html

Access URL: https://pubmed.ncbi.nlm.nih.gov/9584084
http://www.genetics.org/content/149/1/37.short
http://europepmc.org/articles/PMC1460137
http://hub.hku.hk/handle/10722/49029
https://www.genetics.org/content/genetics/149/1/37.full.pdf
https://academic.oup.com/genetics/article/149/1/37/6034245
https://www.ncbi.nlm.nih.gov/pubmed/9584084
http://hdl.handle.net/10722/49029

Identification of a tRNA-Specific Nuclear Export Receptor

Authors: Kutay, Ulrike Lipowsky, Gerd Izaurralde, Elisa et al.

Source: Molecular Cell. 1:359-369

Subject Terms: 0301 basic medicine, Cytoplasm, Nucleocytoplasmic Transport Proteins, RNA, Transfer, Leu, Xenopus, Molecular Sequence Data, Ran GTP-Binding Protein, Beta Karyopherins, Nuclear Proteins / genetics, Xenopus Proteins, 03 medical and health sciences, RNA, Transfer, GTP-Binding Proteins, Cytoplasm / metabolism, Cell Nucleus / chemistry, RNA, Messenger / analysis, Animals, Humans, Amino Acid Sequence, RNA, Messenger, GTP-Binding Proteins / metabolism, Cloning, Molecular, Molecular Biology, RNA, Transfer, Ser, Cell Nucleus, 0303 health sciences, Cell Nucleus / metabolism, Nuclear Proteins / metabolism, Protein Binding / physiology, GTPase-Activating Proteins, Carrier Proteins / metabolism, RNA, Transfer, Amino Acid-Specific / metabolism, Nuclear Proteins, Cell Biology, RNA, Transfer, Ser / metabolism, RNA, Transfer, Amino Acid-Specific, RNA, Transfer, Leu / metabolism, Oocytes, RNA, Transfer / metabolism, Carrier Proteins, Carrier Proteins / genetics, Oocytes / physiology, HeLa Cells, Protein Binding

File Description: application/pdf

Access URL: http://www.cell.com/article/S1097276500800362/pdf
https://pubmed.ncbi.nlm.nih.gov/9660920
https://edoc.mdc-berlin.de/3605/
https://pure.mpg.de/pubman/faces/ViewItemOverviewPage.jsp?itemId=item_2426548
https://www.sciencedirect.com/science/article/pii/S1097276500800362
https://europepmc.org/abstract/MED/9660920
https://www.cell.com/molecular-cell/fulltext/S1097-2765(00)80036-2
https://www.ncbi.nlm.nih.gov/pubmed/9660920
https://archive-ouverte.unige.ch/unige:173804
https://doi.org/10.1016/s1097-2765(00)80036-2

The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase

Authors: Françoise Van Vliet Janusz Marek Bujnicki Karolina L. Tkaczuk et al.

Source: BMC Mol Biol
BMC molecular biology, 18

Subject Terms: 0301 basic medicine, tRNA Methyltransferases, 0303 health sciences, tRNA Methyltransferases -- metabolism, Escherichia coli Proteins, Transfer -- metabolism, Sciences bio-médicales et agricoles, RNA, Transfer -- metabolism, Methylation, 3. Good health, 03 medical and health sciences, Eukaryotic Cells, tRNA Methyltransferases -- physiology, Prokaryotic Cells, RNA, Transfer, Escherichia coli Proteins -- physiology, Terminology as Topic, RNA, tRNA Methyltransferases -- genetics, Research Article

File Description: 1 full-text file(s): application/pdf

Access URL: https://bmcmolbiol.biomedcentral.com/track/pdf/10.1186/1471-2199-7-23
https://pubmed.ncbi.nlm.nih.gov/16848900
https://pubmed.ncbi.nlm.nih.gov/16848900/
https://bmcmolbiol.biomedcentral.com/articles/10.1186/1471-2199-7-23
https://link.springer.com/article/10.1186/1471-2199-7-23/fulltext.html
https://www.biomedcentral.com/1471-2199/7/23
http://www.biomedcentral.com/1471-2199/7/23
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50476