2012
DOI: 10.18632/aging.100506
View full text |Buy / Rent full text
|
Sign up to set email alerts
|

Abstract: RECQL4 is one of five members of the human RecQ helicase family, and is implicated in three syndromes displaying accelerating aging, developmental abnormalities and a predisposition to cancer. In this study, we purified three variants of RECQL4 carrying previously reported patient mutations. These three mutant proteins were analyzed for the known biochemical activities of RECQL4: DNA binding, unwinding of duplex DNA, ATP hydrolysis and annealing of simplex DNA. Further, the mutant proteins were evaluated for s… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
8
0

Year Published

2014
2014
2018
2018

Publication Types

Select...
5

Relationship

3
2

Authors

Journals

citations
Cited by 9 publications
(9 citation statements)
references
References 47 publications
(83 reference statements)
1
8
0
Order By: Relevance
“…5F). Consistent with previous findings (Jensen et al, 2012; Keller et al, 2014), RECQL4 binds to ssDNA, dsDNA and 3’ tailed dsDNA substrates (Fig. 5F).…”
Section: Resultssupporting
confidence: 93%
“…5F). Consistent with previous findings (Jensen et al, 2012; Keller et al, 2014), RECQL4 binds to ssDNA, dsDNA and 3’ tailed dsDNA substrates (Fig. 5F).…”
Section: Resultssupporting
confidence: 93%
“…However, of the missense mutations available for analysis, those that compromise RECQL4 structurally segregate with RTS, whereas those that impair helicase activity segregate with RAPADILINO syndrome (83, 84). Additional mutational analysis of RECQL4 is warranted.…”
Section: The Recq Protein Familymentioning
confidence: 99%
“…Defects in DNA repair processes are associated with chromosomal abnormalities and carcinogenesis (15,16). Recently, we reported that the helicase and ATPase activities of RECQL4 are compromised in patients with RECQL4-associated diseases (17,18). Interestingly, the trend is that RECQL4 patient mutations, which cause protein instability segregate with RTS, whereas those mutations which cause reduced helicase activity are associated with RAPA.…”
Section: Introductionmentioning
confidence: 99%