Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Morana Dulic"'
Publikováno v:
Life, Vol 14, Iss 1, p 124 (2024)
Seryl-tRNA synthetases (SerRSs), members of the aminoacyl-tRNA synthetase family, interact with diverse proteins, enabling SerRSs to enhance their role in the translation of the genetic message or to perform alternative functions in cellular processe
Externí odkaz:
https://doaj.org/article/ad4502421a924cd18be37b664e946cb3
Autor:
Jan-Stefan Völler, Morana Dulic, Ulla I. M. Gerling-Driessen, Hernan Biava, Tobias Baumann, Nediljko Budisa, Ita Gruic-Sovulj, Beate Koksch
Publikováno v:
ACS Central Science, Vol 3, Iss 1, Pp 73-80 (2016)
Externí odkaz:
https://doaj.org/article/b4b14029840145e88e9051092a1fa838
Autor:
Ita Gruić-Sovulj, Stephen Cusack, Branimir Bertoša, Andrés Palencia, Igor Zivkovic, Morana Dulic, Nevena Cvetesic
Publikováno v:
Journal of Molecular Biology. 430:1-16
The intrinsic editing capacities of aminoacyl-tRNA synthetases ensure a high-fidelity translation of the amino acids that possess effective non-cognate aminoacylation surrogates. The dominant error-correction pathway comprises deacylation of misamino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b42a82356303c26ee33b808d82f76f3b
https://doi.org/10.1016/j.jmb.2017.10.024
https://doi.org/10.1016/j.jmb.2017.10.024
Autor:
Ita Gruić-Sovulj, Nediljko Budisa, Jan-Stefan Völler, Beate Koksch, Tobias Baumann, Ulla I. M. Gerling-Driessen, Hernan Biava, Morana Dulic
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
ACS Central Science
ACS Central Science, Vol 3, Iss 1, Pp 73-80 (2016)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
ACS Central Science
ACS Central Science, Vol 3, Iss 1, Pp 73-80 (2016)
Fluorine being not substantially present in the chemistry of living beings is an attractive element in tailoring novel chemical, biophysical, and pharmacokinetic properties of peptides and proteins. The hallmark of ribosome-mediated artificial amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f58e6c1b9af02a6149fb5e341770b3fd
https://doi.org/10.1021/acscentsci.6b00339
https://doi.org/10.1021/acscentsci.6b00339
Publikováno v:
Biochemistry
The accurate expression of genetic information relies on the fidelity of amino acid-tRNA coupling by aminoacyl-tRNA synthetases (aaRS). When the specificity against structurally similar noncognate amino acids in the synthetic reaction does not suppor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76149cf5c86450fbc0f8cbdda67a1782
https://doi.org/10.1021/bi5007699
https://doi.org/10.1021/bi5007699
Autor:
Nikolina Sostaric, Boris Lenhard, Nevena Cvetesic, Ita Gruić-Sovulj, Morana Dulic, Mirna Bilus
Publikováno v:
The Journal of Biological Chemistry
Isoleucyl-tRNA synthetase (IleRS) is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pre-transfer editing activity. Alongside the typical bacterial IleRS (such as Escherichia coli IleRS), some bacteria also have the enzymes (eukar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::640192ff2bab30adb5ba30ef020e9ba6
https://pubmed.ncbi.nlm.nih.gov/26921320
https://pubmed.ncbi.nlm.nih.gov/26921320
Autor:
Jasmina Rokov-Plavec, Sonja Lesjak, Morana Dulic, Ita Gruić-Sovulj, Marko Močibob, Ivana Weygand-Durasevic
Aminoacyl-tRNA synthetases (aaRSs) catalyze the attachment of amino acids to their cognate tRNAs to establish the genetic code. To obtain the high degree of accuracy that is observed in translation, these enzymes must exhibit strict substrate specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3f866a7ec77afdaad2e5775ba0e38b3
https://doi.org/10.1016/j.abb.2012.11.014
https://doi.org/10.1016/j.abb.2012.11.014
Publikováno v:
Biochimie. 93(10)
Seryl-tRNA synthetases (SerRS) covalently attach serine to cognate tRNASer. Atypical SerRSs, considerably different from canonical enzymes, have been found in methanogenic archaea. A crystal structure of methanogenic- type SerRS revealed a motif with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee7bf7f12eb94059fcfb295fe34bca58
https://pubmed.ncbi.nlm.nih.gov/21704670
https://pubmed.ncbi.nlm.nih.gov/21704670
Publikováno v:
Croatica Chemica Acta
Volume 84
Issue 2
Volume 84
Issue 2
Aminoacyl-tRNA synthetases (aaRSs) maintain fidelity of protein synthesis by matching only cognate amino acid-tRNA pairs. Aminoacylation occurs through activation of amino acid to yield aminoacyl- adenylate followed by transfer of acyl-moiety to tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5c0cb620a4a2b4d76980f881e4d09f7
https://www.bib.irb.hr/518713
https://www.bib.irb.hr/518713
Hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes occurs in a spatially separate do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67ae6079f801430165af5041d7337416
https://www.bib.irb.hr/471798
https://www.bib.irb.hr/471798