Human Rad17 C-terminal tail is phosphorylated by concerted action of CK1δ/ε and CK2 to promote interaction with the 9–1–1 complex

2019 ◽  
Vol 517 (2) ◽  
pp. 310-316
Author(s):  
Yasunori Fukumoto ◽  
Yuji Nakayama ◽  
Naoto Yamaguchi
Keyword(s):  
2021 ◽  
Vol 10 (2) ◽  
pp. 51
Author(s):  
Vincenzo Ruggiero

Power entails the ability to act and overcome the obstacles erected by those who are subject to it. It also entails the capacity to make one’s crimes acceptable, while formulating criminal imputations against others. The crimes of the powerful, in this contribution, are examined through the lenses of a number of intertwined variables: coercion, legitimacy, violence, secrecy, consensus, and hegemony. Ostentation, imitation, and admiration are also considered as components of these types of crimes and the feelings they elicit. While the controversies surrounding legal responses to the crimes of the powerful are discussed, the efficacy of concerted action against them is optimistically invoked.


2011 ◽  
Vol 14 (2) ◽  
pp. 68-69 ◽  
Author(s):  
Otto Cars ◽  
Anna Hedin ◽  
Andreas Heddini
Keyword(s):  

Nature ◽  
1963 ◽  
Vol 199 (4900) ◽  
pp. 1299-1300 ◽  
Author(s):  
S. R. PAI ◽  
R. S. YAMAMOTO ◽  
J. H. WEISBURGER

1970 ◽  
Vol 119 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Michiko Nishida-Fukuda ◽  
Fujio Egami

1. A multienzyme system capable of degrading keratosulphates to yield galactose, N-acetylglucosamine and sulphate was found in the liver extract of a marine gastropod, Charonia lampas. 2. During the degradation, neither oligosaccharides nor sulphated sugars were produced. 3. It is suggested that the degradation could be attributed to the concerted action of β-galactosidase, β-N-acetylglucosaminidase and a sulphatase (sulphohydrolase), tentatively designated keratosulphatase. 4. Two forms of keratosulphatase (I and II) were separated by DEAE-Sephadex column chromatography. Both forms could release all the sulphate from keratosulphates and neither appeared to be identical with glycosulphatase or chondrosulphatase, both of which are also present in Charonia lampas. 5. β-Galactosidase and β-N-acetylglucosaminidase could degrade keratopolysulphate to a greater extent in the presence of keratosulphatase than in its absence. 6. It is suggested that keratosulphate was first desulphated by the action of keratosulphatase, and the desulphated polymer was then degraded to galactose and N-acetylglucosamine by the action of β-galactosidase and β-N-acetylglucosaminidase. 7. β-Galactosidase alone released a small amount of galactose from shark cartilage keratopolysulphate, but β-N-acetylglucosaminidase alone did not release N-acetylglucosamine. This indicates that unsulphated galactose residues occupy all the non-reducing terminal positions in keratopolysulphate chains.


1999 ◽  
Vol 3 (4) ◽  
pp. 8-9 ◽  
Author(s):  
Nicoline Wrisberg ◽  
Roland Clift

2010 ◽  
Vol 31 (4) ◽  
pp. 309-326 ◽  
Author(s):  
Monika Kędra ◽  
Sławomira Gromisz ◽  
Radomir Jaskuła ◽  
Joanna Legeżyńska ◽  
Barbara Maciejewska ◽  
...  

Soft bottom macrofauna of an All Taxa Biodiversity Site: Hornsund (77○N, Svalbard) Hornsund, an Arctic fjord in the west coast of Spitsbergen (Svalbard), was selected as All Taxa Biodiversity Inventory (ATBI) site under EU 5th Framework Concerted Action BIOMARE (2000-2002), especially due to its pristine, undisturbed natural character. On the base of large material (89 stations located throughout the fjord and 129 Van Veen grab samples) collected during cruises of RV Oceania in July in 2002, 2003, 2005 and 2007 and literature search a comprehensive list of species recorded within Hornsund area, on the soft bottom with depth range of 30-250 m is provided. Over 220 species were identified including 93 species of Polychaeta, 62 species of Mollusca and 58 species of Crustacea. Species list is supported by information on the zoogeographical status, body length and biological traits of dominant species. Need for further research on Hornsund soft bottom fauna with more sampling effort is highlighted.


2004 ◽  
Vol 2 (4) ◽  
pp. 673-674 ◽  
Author(s):  
H. H. Versteeg ◽  
D. J. Richel ◽  
M. P. Peppelenbosch ◽  
C. A. Spek

Sign in / Sign up

Export Citation Format

Share Document