Normal view MARC view ISBD view

An off-axis hydrothermal vent field near the Mid-Atlantic Ridge at 30 degrees N. [electronic resource]

By:

Kelley, D S

Contributor(s):

Producer: 20010802Description: 145-9 p. digitalISSN:

0028-0836

Subject(s):

Online resources:

Available from publisher's website

In: Nature vol. 412

Tags from this library: No tags from this library for this title. Log in to add tags.

Average rating: 0.0 (0 votes)

No physical items for this record

Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.

There are no comments on this title.

to post a comment.

Previous

Back to results

Next

1
2
3
4
5
6
7
8
9
10
11

1 Human RECQ5 helicase promotes repair of DNA double-strand breaks by synthesis-dependent strand annealing.
by Paliwal, Shreya
2 Human RECQ5beta helicase promotes strand exchange on synthetic DNA structures resembling a stalled replication fork.
by Kanagaraj, Radhakrishnan
3 BLM helicase measures DNA unwound before switching strands and hRPA promotes unwinding reinitiation.
by Yodh, Jaya G
4 DNA2 cooperates with the WRN and BLM RecQ helicases to mediate long-range DNA end resection in human cells.
by Sturzenegger, Andreas
5 MRE11 complex links RECQ5 helicase to sites of DNA damage.
by Zheng, Lu
6 Physical and functional interactions between Werner syndrome helicase and mismatch-repair initiation factors.
by Saydam, Nurten
7 RECQ5 helicase associates with the C-terminal repeat domain of RNA polymerase II during productive elongation phase of transcription.
by Kanagaraj, Radhakrishnan
8 Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity.
by Schwendener, Sybille
9 Involvement of Werner syndrome protein in MUTYH-mediated repair of oxidative DNA damage.
by Kanagaraj, Radhakrishnan
10 The zinc-binding motif of human RECQ5beta suppresses the intrinsic strand-annealing activity of its DExH helicase domain and is essential for the helicase activity of the enzyme.
by Ren, Hua
11 RECQ5 Helicase Cooperates with MUS81 Endonuclease in Processing Stalled Replication Forks at Common Fragile Sites during Mitosis.
by Di Marco, Stefano

Close