Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Georges Lahoud"'
Publikováno v:
Chemistry & Biology. 21:1351-1360
Summary The catalytic mechanism of the majority of S -adenosyl methionine (AdoMet)-dependent methyl transferases requires no divalent metal ions. Here we report that methyl transfer from AdoMet to N 1 of G37-tRNA, catalyzed by the bacterial TrmD enzy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85ad70d7aea0945e0104e71ea3e2caf3
https://doi.org/10.1016/j.chembiol.2014.07.023
https://doi.org/10.1016/j.chembiol.2014.07.023
Autor:
Takuhiro Ito, Erika A. Taylor, Reiko Sakaguchi, Ya-Ming Hou, Thomas Christian, Agata P. Perlinska, Shigeyuki Yokoyama, Georges Lahoud, Joanna I. Sulkowska
Publikováno v:
Nature structuralmolecular biology. 23(10)
Proteins with knotted configurations are restricted in conformational space relative to unknotted proteins. Little is known if knotted proteins have sufficient dynamics to communicate between spatially separated substrate-binding sites. In bacteria,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b58e527f7f4a8eed95d46bae3ea0a5f6
https://pubmed.ncbi.nlm.nih.gov/27571175
https://pubmed.ncbi.nlm.nih.gov/27571175
Autor:
Saulius Klimašauskas, Anders M.B. Giessing, Joseph A. Piccirilli, Ya-Ming Hou, Qing Dai, Georges Lahoud, Zita Liutkeviciute, Finn Kirpekar, Reiko Sakaguchi
Publikováno v:
RNA. 18:1687-1701
Guanosines are important for biological activities through their specific functional groups that are recognized for RNA or protein interactions. One example is recognition of N1 of G37 in tRNA by S-adenosyl-methionine (AdoMet)–dependent tRNA methyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a080ad7b900afa63816fb81f45d77bb
https://doi.org/10.1261/rna.032029.111
https://doi.org/10.1261/rna.032029.111
Autor:
Shigeyuki Yokoyama, Sakurako Goto-Ito, Georges Lahoud, Ya-Ming Hou, Ken-ichi Yoshida, Takuhiro Ito
Publikováno v:
RNA. 17:1236-1246
Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N1 of G37, using catalytic motifs that share no sequence or structural homology. Here we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a097990349e3bf7287ce736ae7d05f29
https://doi.org/10.1261/rna.2706011
https://doi.org/10.1261/rna.2706011
Autor:
Cuiping Liu, Katherine Hoffmann, Ya-Ming Hou, Thomas Christian, Georges Lahoud, John J. Perona
Publikováno v:
RNA. 16:2484-2492
Trm5 is a eukaryal and archaeal tRNA methyltransferase that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to the N1 position of G37 directly 3′ to the anticodon. While the biological role of m1G37 in enhancing translational fidelity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e2349f159a0e849753e0f7c790b03ae
https://doi.org/10.1261/rna.2376210
https://doi.org/10.1261/rna.2376210
Autor:
Victor Timoshchuk, Georges Lahoud, Howard Gamper, Alexandre Lebedev, Khalil Arar, Ya-Ming Hou
Publikováno v:
Nucleic Acids Research
A straightforward enzymatic protocol for converting regular DNA into pseudo-complementary DNA could improve the performance of oligonucleotide microarrays by generating readily hybridizable structure-free targets. Here we screened several highly dest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b62484070c578d2b269d3c88f6453eec
https://doi.org/10.1093/nar/gkn797
https://doi.org/10.1093/nar/gkn797
Publikováno v:
Nucleic Acids Research
Sequence-specific recognition of DNA is a critical step in gene targeting. Here we describe unique oligonucleotide (ON) hybrids that can stably pair to both strands of a linear DNA target in a RecA-dependent reaction with ATP or ATPgammaS. One strand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4be21267e24f5494e99af740d0f17aa2
http://europepmc.org/articles/PMC2588519
http://europepmc.org/articles/PMC2588519
Autor:
Georges Lahoud, Ya-Ming Hou, Alexandre Lebedev, Miguel de Vega, Howard B. Gamper, Khalil Arar, Victor Timoshchuk, Margarita Salas
Publikováno v:
Nucleic Acids Research
Digital.CSIC. Repositorio Institucional del CSIC
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Digital.CSIC. Repositorio Institucional del CSIC
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Long single-stranded DNAs and RNAs possess considerable secondary structure under conditions that support stable hybrid formation with oligonucleotides. Consequently, different oligomeric probes can hybridize to the same target with efficiencies that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8e73a79969492077e9add2afe6f58fa
https://doi.org/10.1093/nar/gkn209
https://doi.org/10.1093/nar/gkn209
Enzymes that use distinct active site structures to perform identical reactions are known as analogous enzymes. The isolation of analogous enzymes suggests the existence of multiple enzyme structural pathways that can catalyze the same chemical react
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7a5fde189d0cb0827b5967369784036
https://europepmc.org/articles/PMC2892103/
https://europepmc.org/articles/PMC2892103/
Autor:
Georges Lahoud, Ya-Ming Hou
Publikováno v:
Nature Chemical Biology. 6:795-796
Aminoacylation of tRNA is the cellular process for providing aminoacyl donors for the ribosome synthesis of polypeptides. New research highlights an unexpected structural overlap between enzymes involved in this process and those involved in the bios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d531f68eb321fe93d340de1d7f40a4d1
https://doi.org/10.1038/nchembio.459
https://doi.org/10.1038/nchembio.459