2009
Backbone 1H, 13C, and 15N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR
MOTÁČKOVÁ, Veronika; Monika KUBÍČKOVÁ; Milan KOŽÍŠEK; Klára GRANTZ ŠAŠKOVÁ; Martin ŠVEC et al.Základní údaje
Originální název
Backbone 1H, 13C, and 15N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR
Název česky
Backbone 1H, 13C, and 15N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR
Autoři
MOTÁČKOVÁ, Veronika; Monika KUBÍČKOVÁ ORCID; Milan KOŽÍŠEK; Klára GRANTZ ŠAŠKOVÁ; Martin ŠVEC; Lukáš ŽÍDEK a Vladimír SKLENÁŘ
Vydání
Biomolecular NMR Assignments, Netherlands, Springer Netherlands, 2009, 1874-2718
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 0.750
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/09:00037169
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000271442700026
Klíčová slova anglicky
Retroviral protease; Murine intracisternal A-type particles; inMIA-14 PR; C-terminal domain; Homodimer; Assignment A-type particles \and inMIA-14 PR \and C-terminal domain; Homodimer; Assignment
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 2. 2. 2012 17:37, Mgr. Veronika Papoušková, Ph.D.
V originále
Proteases play a crucial role in the retroviral infection but so far the mechanism of their regulation remains unclear. Protease MIA-14 from murine intracisternal A-type particles, containing a C-terminal domain rich in glycines (G-patch), is responsible for binding of single-stranded oligo-nucleotides (both RNA and DNA) without inhibiting the proteolytic activity. For investigations of untill now poorly characterized protease--oligonucleotide interactions, assignments of the observed NMR frequencies are mandatory. An almost complete assignments of the main chain and 13Cbeta side chain resonances of the 34\,kDa homo-dimeric inMIA-14 PR is presented in this study.
Česky
Proteases play a crucial role in the retroviral infection but so far the mechanism of their regulation remains unclear. Protease MIA-14 from murine intracisternal A-type particles, containing a C-terminal domain rich in glycines (G-patch), is responsible for binding of single-stranded oligo-nucleotides (both RNA and DNA) without inhibiting the proteolytic activity. For investigations of untill now poorly characterized protease--oligonucleotide interactions, assignments of the observed NMR frequencies are mandatory. An almost complete assignments of the main chain and 13Cbeta side chain resonances of the 34\,kDa homo-dimeric inMIA-14 PR is presented in this study.
Návaznosti
| LC06030, projekt VaV |
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| MSM0021622413, záměr |
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