Abstract
O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.
Original language | English (US) |
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Article number | eaan2396 |
Journal | Science |
Volume | 357 |
Issue number | 6348 |
DOIs |
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State | Published - Jul 21 2017 |
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ASJC Scopus subject areas
- General
Cite this
Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”. / Baranovskiy, Andrey G.; Babayeva, Nigar D.; Zhang, Yinbo; Blanco, Luis; Pavlov, Youri I; Tahirov, Tahir H.
In: Science, Vol. 357, No. 6348, eaan2396, 21.07.2017.Research output: Contribution to journal › Comment/debate
}
TY - JOUR
T1 - Comment on “The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport”
AU - Baranovskiy, Andrey G.
AU - Babayeva, Nigar D.
AU - Zhang, Yinbo
AU - Blanco, Luis
AU - Pavlov, Youri I
AU - Tahirov, Tahir H
PY - 2017/7/21
Y1 - 2017/7/21
N2 - O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.
AB - O’Brien et al. (Research Article, 24 February 2017, eaag1789) proposed a novel mechanism of primase function based on redox activity of the iron-sulfur cluster buried inside the C-terminal domain of the large primase subunit (p58C). Serious problems in the experimental design and data interpretation raise concerns about the validity of the conclusions.
UR - http://www.scopus.com/inward/record.url?scp=85025481611&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85025481611&partnerID=8YFLogxK
U2 - 10.1126/science.aan2396
DO - 10.1126/science.aan2396
M3 - Comment/debate
C2 - 28729484
AN - SCOPUS:85025481611
VL - 357
JO - Science
JF - Science
SN - 0036-8075
IS - 6348
M1 - eaan2396
ER -