scholarly journals Classifications of schematic solutions of the geokhod knife operating body and the interaction surface of the geokhod operating body with bottom rock

Author(s):  
V V Aksenov ◽  
A B Efremenkov ◽  
V Yu Sadovets ◽  
D A Pashkov ◽  
V A Efremenkov
Biochemistry ◽  
1995 ◽  
Vol 34 (21) ◽  
pp. 6911-6918 ◽  
Author(s):  
S. Donald Emerson ◽  
Vincent S. Madison ◽  
Robert E. Palermo ◽  
David S. Waugh ◽  
Julie E. Scheffler ◽  
...  

1881 ◽  
Vol 8 (5) ◽  
pp. 194-197 ◽  
Author(s):  
R. D. Roberts

A discussion has more than once arisen, in the course of the last two years, respecting the true position or the quartz conglomerate exposed near Twt Hill, Carnarvon, which was first described by Prof. Bonney and Mr. Houghton in the Quarterly Journal of the Geological Society, vol. xxxv. p. 321. The typical quarry is situated on the S.E. side of the ridge, close underneath Twt Hill, and the exposure there shows the quartz conglomerate in juxtaposition to the granitoid rock that constitutes the axis of the ridge. The authors describe a passage between the granitoidite below and the conglomerate above, and state that the latter “passes lip into a rock which has some resemblance to the bottom rock” (granitoidite). In the GEOL. MAG. for March, 1880, p. 118, Dr. Callaway writes: “Messrs. Bonney and Houghton have detected at Twt Hill a passage between the granitoidite and a quartzose conglomerate with a S.E. dip. I have visited this section, and having examined the rock inch by inch, I can entirely confirm their identification.”


Biochemistry ◽  
2004 ◽  
Vol 43 (4) ◽  
pp. 904-908 ◽  
Author(s):  
Andrew C. Vendel ◽  
Kevin J. Lumb
Keyword(s):  

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Gisela Schimmack ◽  
Kenji Schorpp ◽  
Kerstin Kutzner ◽  
Torben Gehring ◽  
Jara Kerstin Brenke ◽  
...  

The ubiquitin ligase TRAF6 is a key regulator of canonical IκB kinase (IKK)/NF-κB signaling in response to interleukin-1 (IL-1) stimulation. Here, we identified the deubiquitinating enzyme YOD1 (OTUD2) as a novel interactor of TRAF6 in human cells. YOD1 binds to the C-terminal TRAF homology domain of TRAF6 that also serves as the interaction surface for the adaptor p62/Sequestosome-1, which is required for IL-1 signaling to NF-κB. We show that YOD1 competes with p62 for TRAF6 association and abolishes the sequestration of TRAF6 to cytosolic p62 aggregates by a non-catalytic mechanism. YOD1 associates with TRAF6 in unstimulated cells but is released upon IL-1β stimulation, thereby facilitating TRAF6 auto-ubiquitination as well as NEMO/IKKγ substrate ubiquitination. Further, IL-1 triggered IKK/NF-κB signaling and induction of target genes is decreased by YOD1 overexpression and augmented after YOD1 depletion. Hence, our data define that YOD1 antagonizes TRAF6/p62-dependent IL-1 signaling to NF-κB.


Biochemistry ◽  
2005 ◽  
Vol 44 (31) ◽  
pp. 10593-10604 ◽  
Author(s):  
Tara L. Davis ◽  
Tabetha M. Bonacci ◽  
Stephen R. Sprang ◽  
Alan V. Smrcka

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