scholarly journals Synthesis, Structural Characterization, and Physical Properties of Cs2Ga2S5, and Redetermination of the Crystal Structure of Cs2S6

2014 ◽  
Vol 21 (4) ◽  
pp. 1811-1817 ◽  
Author(s):  
Daniel Friedrich ◽  
Florian Pielnhofer ◽  
Marc Schlosser ◽  
Richard Weihrich ◽  
Arno Pfitzner
ChemInform ◽  
2015 ◽  
Vol 46 (15) ◽  
pp. no-no
Author(s):  
Daniel Friedrich ◽  
Florian Pielnhofer ◽  
Marc Schlosser ◽  
Richard Weihrich ◽  
Arno Pfitzner

2020 ◽  
Vol 4 (10) ◽  
Author(s):  
F. Guillou ◽  
H. Yibole ◽  
R. Hamane ◽  
V. Hardy ◽  
Y. B. Sun ◽  
...  

RSC Advances ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 1164-1171
Author(s):  
Xiangmei Wang ◽  
Zeliang Gao ◽  
Chunyan Wang ◽  
Xiaojie Guo ◽  
Youxuan Sun ◽  
...  

This work reports the crystal structure and physical properties of the Y2Mo4O15 crystal and its potential use in the Raman laser.


Author(s):  
Manimuthu Periyasamy ◽  
Lokanath Patra ◽  
Øystein S. Fjellvåg ◽  
Ponniah Ravindran ◽  
Magnus H. Sørby ◽  
...  

1999 ◽  
Vol 148 (2) ◽  
pp. 295-301 ◽  
Author(s):  
Said Nadir ◽  
J.S. Swinnea ◽  
H. Steinfink

2014 ◽  
Vol 70 (a1) ◽  
pp. C305-C305
Author(s):  
Alan Ji ◽  
Gilbert Privé

Cullin3 (Cul3) is an ubiquitin E3 ligase responsible for catalyzing the transfer of an ubiquitin moiety from an E2 enzyme to a target substrate protein. The C-terminal region of Cul3 binds RBX1/E2-ubiquitin, while, the N-terminal region interacts with various BTB domain proteins which serve as substrate adaptors. Previously, our group determined the crystal structures of the homodimeric BTB proteins SPOP and KLHL3 in complex with the N-terminal domain of Cul3, revealing the determinants responsible for the BTB/Cul3 interaction [1, 2]. A second class of BTB-domain containing proteins, the KCTD proteins, are also Cul3 substrate adaptors but these do not share many of the previously determined features for Cul3 binding. Furthermore, KCTD proteins form homotetramers and homopentamers via BTB oligomerization rather than the previously described homodimers. Despite these differences, many KCTD proteins interact with Cul3 with dissociation constants of approximately 50 nM. While the target substrates for many of the KCTD/Cul3 E3 ligase complexes are unknown, recent studies have implicated the GABAβ2 receptor as an interactor of KCTD 8, 12, 12b and 16. Here, we report the pentameric crystal structure of the KCTD9 BTB domain and our progress on the structural characterization of Cul3/KCTD/substrate complexes.


2017 ◽  
Vol 86 (12) ◽  
pp. 124802 ◽  
Author(s):  
Yudai Hijikata ◽  
Tomohiro Abe ◽  
Chikako Moriyoshi ◽  
Yoshihiro Kuroiwa ◽  
Yosuke Goto ◽  
...  

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