Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Erik Malta"'
Autor:
Rohith Srivas, Thomas Costelloe, Anne-Ruxandra Carvunis, Sovan Sarkar, Erik Malta, Su Ming Sun, Marijke Pool, Katherine Licon, Tibor van Welsem, Fred van Leeuwen, Peter J. McHugh, Haico van Attikum, Trey Ideker
Publikováno v:
Cell Reports, Vol 5, Iss 6, Pp 1714-1724 (2013)
Efficient repair of UV-induced DNA damage requires the precise coordination of nucleotide excision repair (NER) with numerous other biological processes. To map this crosstalk, we generated a differential genetic interaction map centered on quantitat
Externí odkaz:
https://doaj.org/article/49b48a24b019447baf1e06106fc31587
Autor:
Maja Berden Zrimec, Erik Malta, Martha Bonnet Dunbar, Ana Cerar, Robert Reinhardt, Rok Mihelič
Publikováno v:
Sustainable Global Resources Of Seaweeds Volume 1 ISBN: 9783030919542
Sustainable Global Resources Of Seaweeds Volume 1
Sustainable Global Resources Of Seaweeds Volume 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7b63a0d70d8147c04f918e72fb7e17e
https://doi.org/10.1007/978-3-030-91955-9_23
https://doi.org/10.1007/978-3-030-91955-9_23
Autor:
Erik Malta, Nora Goosen, Wouter F. J. Hogendorf, Gijsbert A. van der Marel, Carlo P. Verhagen, Herman S. Overkleeft, Dmitri V. Filippov
Publikováno v:
Tetrahedron. 65:10430-10435
An efficient synthetic route to the phosphoramidite of a menthol functionalized guanosine analog is presented. Two procedures were executed for the key introduction of the 6′-allyl menthyl moiety. Stille vinylation on 6- O -tosylguanosine followed
Autor:
Carlo P. Verhagen, Erik Malta, Nora Goosen, Gijs A. van der Marel, Dmitri V. Filippov, Geri F. Moolenaar
Publikováno v:
DNA Repair. 7:1647-1658
UvrB is the main damage recognition protein in bacterial nucleotide excision repair and is capable of recognizing various structurally unrelated types of damage. Previously we have shown that upon binding of Escherichia coli UvrB to damaged DNA two n
Publikováno v:
Biochemistry. 46:9080-9088
UvrB plays a key role in bacterial nucleotide excision repair. It is the ultimate damage-binding protein that interacts with both UvrA and UvrC. The oligomeric state of UvrB and the UvrAB complex have been subject of debate for a long time. Using flu
Publikováno v:
Journal of Biological Chemistry, 281(4), 2184-2194
Journal of Biological Chemistry
Journal of Biological Chemistry
UvrB, the ultimate damage-binding protein in bacterial nucleotide excision repair is capable of binding a vast array of structurally unrelated lesions. A beta-hairpin structure in the protein plays an important role in damage-specific binding. In thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3bfc1b8c9a8d8a876bfc074c0279741
https://doi.org/10.1074/jbc.m508901200
https://doi.org/10.1074/jbc.m508901200