MOTÁČKOVÁ, Veronika, Monika KUBÍČKOVÁ, Milan KOŽÍŠEK, Klára GRANTZ ŠAŠKOVÁ, Martin ŠVEC, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. 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. Biomolecular NMR Assignments. Netherlands: Springer Netherlands, 2009, vol. 3, No 2, p. 261-264. ISSN 1874-2718.
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Basic information
Original name 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
Name in Czech 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
Authors MOTÁČKOVÁ, Veronika (203 Czech Republic, belonging to the institution), Monika KUBÍČKOVÁ (203 Czech Republic, belonging to the institution), Milan KOŽÍŠEK (203 Czech Republic), Klára GRANTZ ŠAŠKOVÁ (203 Czech Republic), Martin ŠVEC (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution).
Edition Biomolecular NMR Assignments, Netherlands, Springer Netherlands, 2009, 1874-2718.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 0.750
RIV identification code RIV/00216224:14310/09:00037169
Organization unit Faculty of Science
UT WoS 000271442700026
Keywords in English 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
Tags International impact, Reviewed
Changed by Changed by: Mgr. Veronika Papoušková, Ph.D., učo 106467. Changed: 2. 2. 2012 17:37.
Abstract
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.
Abstract (in Czech)
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.
Links
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Basic Research Center
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Research Intents
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