Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Anjali P. Mascarenhas"'
Publikováno v:
RNA Biology. 7:754-774
The HIV -1 nucleocapsid protein (NC) is a nucleic acid chaperone, which remodels nucleic acid structures so that the most thermodynamically stable conformations are formed. This activity is essential for virus replication and has a critical role in m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3548d429cf5c6324d8b4618ffabaf337
https://doi.org/10.4161/rna.7.6.14115
https://doi.org/10.4161/rna.7.6.14115
Publikováno v:
FEBS Journal. 276:6118-6127
HIV-1 is a retrovirus that causes AIDS in humans. The RNA genome of the virus encodes a Gag polyprotein, which is further processed into matrix, capsid and nucleocapsid proteins. These proteins play a significant role at several steps in the viral li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cff821debfa409f333dc20cdd2fea922
https://doi.org/10.1111/j.1742-4658.2009.07315.x
https://doi.org/10.1111/j.1742-4658.2009.07315.x
Publikováno v:
The FEBS journal. 276(21)
HIV-1 is a retrovirus that causes AIDS in humans. The RNA genome of the virus encodes a Gag polyprotein, which is further processed into matrix, capsid and nucleocapsid proteins. These proteins play a significant role at several steps in the viral li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::71660ad7c27de7c5038594a39052465f
https://pubmed.ncbi.nlm.nih.gov/19825046
https://pubmed.ncbi.nlm.nih.gov/19825046
Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is disti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f01e3db7548930886497f553ee73f40
https://europepmc.org/articles/PMC2807821/
https://europepmc.org/articles/PMC2807821/
Publikováno v:
Protein Engineering ISBN: 9783540709374
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a3e4d205969a68fd1110398aabdce05
https://doi.org/10.1007/978-3-540-70941-1_6
https://doi.org/10.1007/978-3-540-70941-1_6
Publikováno v:
Biochemistry. 47(16)
Some aminoacyl-tRNA synthetases (AARSs) employ an editing mechanism to ensure the fidelity of protein synthesis. Leucyl-tRNA synthetase (LeuRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) share a common insertion, called the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32a7118a377434a9df39964120401d0f
https://pubmed.ncbi.nlm.nih.gov/18363380
https://pubmed.ncbi.nlm.nih.gov/18363380
Leucyl-tRNA synthetase (LeuRS) has evolved an editing function to clear misactivated amino acids. An Escherichia coli -based assay was established to identify amino acids that compromise the fidelity of LeuRS and translation. Multiple nonstandard as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb5d25de96a66925baa6b465e604f77b
https://europepmc.org/articles/PMC2168938/
https://europepmc.org/articles/PMC2168938/
Autor:
Neira, José L.1,2 jlneira@umh.es
Publikováno v:
FEBS Journal. Nov2009, Vol. 276 Issue 21, p6110-6117. 8p. 3 Diagrams.