Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Lucia M, Morstadt"'
Autor:
Alisa E. Lisova, Andrey G. Baranovskiy, Lucia M. Morstadt, Nigar D. Babayeva, Elena I. Stepchenkova, Tahir H. Tahirov
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-10 (2022)
Abstract DNA polymerase ε (Polε) is a key enzyme for DNA replication in eukaryotes. Recently it was shown that the catalytic domain of yeast Polε (PolεCD) contains a [4Fe-4S] cluster located at the base of the processivity domain (P-domain) and c
Externí odkaz:
https://doaj.org/article/3d5dcdb546944de08fa654143054573a
Autor:
Alisa E. Lisova, Andrey G. Baranovskiy, Lucia M. Morstadt, Nigar D. Babayeva, Tahir H. Tahirov
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-11 (2022)
Abstract DNA polymerase ε (Polε) performs bulk synthesis of DNA on the leading strand during genome replication. Polε binds two substrates, a template:primer and dNTP, and catalyzes a covalent attachment of dNMP to the 3' end of the primer. Previo
Externí odkaz:
https://doaj.org/article/a2a7e71ed2084ab08ba0394d0b565418
Autor:
Qixiang He, Andrey G. Baranovskiy, Lucia M. Morstadt, Alisa E. Lisova, Nigar D. Babayeva, Benjamin L. Lusk, Ci Ji Lim, Tahir H. Tahirov
Publikováno v:
Nature Structural & Molecular Biology. 30:579-583
Publikováno v:
Nucleic Acids Research. 50:6264-6270
The human primosome, a four-subunit complex of primase and DNA polymerase alpha (Polα), synthesizes chimeric RNA–DNA primers of a limited length for DNA polymerases delta and epsilon to initiate DNA replication on both chromosome strands. Despite
Publikováno v:
Nucleic acids research. 50(21)
DNA polymerase α (Polα) is essential for DNA replication initiation and makes a notable contribution to genome mutagenesis. The activity and fidelity of Polα during the early steps of DNA replication have not been well studied. Here we show that a
Autor:
Alisa E. Lisova, Andrey G. Baranovskiy, Lucia M. Morstadt, Nigar D. Babayeva, Elena I. Stepchenkova, Tahir H. Tahirov
DNA polymerase ε (Polε) is a key enzyme for DNA replication in eukaryotes. It is attached to a helicase and performs DNA synthesis on the leading strand. Recently it was shown that the catalytic domain of yeast Polε (PolεCD) contains a [4Fe-4S] c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7c6b29af36432b6cbad1e0cc613b949
https://doi.org/10.1101/2022.05.05.490830
https://doi.org/10.1101/2022.05.05.490830
Autor:
Andrey G. Baranovskiy, Alisa E. Lisova, Lucia M. Morstadt, Nigar D. Babayeva, Tahir H. Tahirov
The human primosome, a four-subunit complex of primase and DNA polymerase alpha (Polα), synthesizes chimeric RNA-DNA primers for DNA polymerases delta and epsilon to initiate DNA replication on both chromosome strands. Despite recent structural insi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f07c78386c03c9effa3ec6584881054
https://doi.org/10.1101/2022.05.02.490354
https://doi.org/10.1101/2022.05.02.490354
Autor:
Andrey G. Baranovskiy, Nigar D. Babayeva, Alisa E. Lisova, Lucia M. Morstadt, Tahir H. Tahirov
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Human DNA polymerase α (Polα) does not possess proofreading ability and plays an important role in genome replication and mutagenesis. Polα extends the RNA primers generated by primase and provides a springboard for loading other replication facto
Autor:
Alisa E. Lisova, Andrey G. Baranovskiy, Lucia M. Morstadt, Nigar D. Babayeva, Tahir H. Tahirov
DNA polymerase ε (Polε) performs bulk synthesis of DNA on the leading strand during genome replication. Polε binds two substrates, a template:primer and dNTP, and catalyzes a covalent attachment of dNMP to the 3' end of the primer. Previous studie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48400c31690bd08f708ca39a56c72be5
https://doi.org/10.21203/rs.3.rs-1507192/v1
https://doi.org/10.21203/rs.3.rs-1507192/v1
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824:1409-1415
A monomeric four-α-helix bundle protein Aα 4 was designed as a step towards investigating the interaction of volatile general anesthetics with their putative membrane protein targets. The alpha helices, connected by glycine loops, have the sequence