Solution Structure and Dynamics, Stability, and NIR Emission Properties of Lanthanide Complexes with a Carboxylated Bispyrazolylpyridyl Ligand

2009 ◽  
Vol 48 (4) ◽  
pp. 1507-1518 ◽  
Author(s):  
Marta Mato-Iglesias ◽  
Teresa Rodríguez-Blas ◽  
Carlos Platas-Iglesias ◽  
Matthieu Starck ◽  
Pascal Kadjane ◽  
...  
Polyhedron ◽  
2019 ◽  
Vol 171 ◽  
pp. 212-220
Author(s):  
Ali Alhafeez Abdulrheem Shamshoom ◽  
Huan-Huan Meng ◽  
Wei Xi ◽  
Xue-Qin Song

2019 ◽  
Vol 111 ◽  
pp. 294-300 ◽  
Author(s):  
Shreekrishna Karthik H.G. ◽  
Samvit G. Menon ◽  
Deepak Hebbar N. ◽  
K.S. Choudhari ◽  
Santhosh C. ◽  
...  

2018 ◽  
pp. 203-224 ◽  
Author(s):  
M. S. Sajna ◽  
V. P. Prakashan ◽  
M. S. Sanu ◽  
Gejo George ◽  
Cyriac Joseph ◽  
...  

2018 ◽  
Vol 1866 (10) ◽  
pp. 1008-1020 ◽  
Author(s):  
Diva Maheshwari ◽  
Vaibhav Kumar Shukla ◽  
Anupam Jain ◽  
Sarita Tripathi ◽  
Dinesh Kumar ◽  
...  

2020 ◽  
Vol 28 (10) ◽  
pp. 14186 ◽  
Author(s):  
Xinjie Shen ◽  
Lizhang Xia ◽  
Yu Zhang ◽  
Jun Li ◽  
Gaobo Yang ◽  
...  

2019 ◽  
Vol 116 (43) ◽  
pp. 21529-21538 ◽  
Author(s):  
Theodoros K. Karamanos ◽  
Vitali Tugarinov ◽  
G. Marius Clore

J-domain chaperones are involved in the efficient handover of misfolded/partially folded proteins to Hsp70 but also function independently to protect against cell death. Due to their high flexibility, the mechanism by which they regulate the Hsp70 cycle and how specific substrate recognition is performed remains unknown. Here we focus on DNAJB6b, which has been implicated in various human diseases and represents a key player in protection against neurodegeneration and protein aggregation. Using a variant that exists mainly in a monomeric form, we report the solution structure of an Hsp40 containing not only the J and C-terminal substrate binding (CTD) domains but also the functionally important linkers. The structure reveals a highly dynamic protein in which part of the linker region masks the Hsp70 binding site. Transient interdomain interactions via regions crucial for Hsp70 binding create a closed, autoinhibited state and help retain the monomeric form of the protein. Detailed NMR analysis shows that the CTD (but not the J domain) self-associates to form an oligomer comprising ∼35 monomeric units, revealing an intricate balance between intramolecular and intermolecular interactions. The results shed light on the mechanism of autoregulation of the Hsp70 cycle via conserved parts of the linker region and reveal the mechanism of DNAJB6b oligomerization and potentially antiaggregation.


2015 ◽  
Vol 44 (28) ◽  
pp. 12660-12669 ◽  
Author(s):  
V. V. Utochnikova ◽  
A. D. Kovalenko ◽  
A. S. Burlov ◽  
L. Marciniak ◽  
I. V. Ananyev ◽  
...  

New NIR emitting materials were found among the lanthanide complexes with 2-(tosylamino)benzylidene-N-benzoylhydrazone.


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