scholarly journals Reply to the ‘Comment on “Investigation of Zr(iv) and 89Zr(iv) complexation with hydroxamates: progress towards designing a better chelator than desferrioxamine B for immuno-PET imaging”’ by A. Bianchi and M. Savastano, Chem. Commun., 2020, 56, D0CC01189D

2020 ◽  
Vol 56 (83) ◽  
pp. 12667-12668
Author(s):  
François Guérard ◽  
Yong-Sok Lee ◽  
Raphaël Tripier ◽  
Lawrence P. Szajek ◽  
Jeffrey R. Deschamps ◽  
...  

The relevance of simplified models used for potentiometric data interpretation is discussed in the context of radiolabelling chemistry (herein the complexation of a radiometal, 89Zr, by a ligand L).

2015 ◽  
Vol 44 (11) ◽  
pp. 4884-4900 ◽  
Author(s):  
Michelle T. Ma ◽  
Levente K. Meszaros ◽  
Brett M. Paterson ◽  
David J. Berry ◽  
Maggie S. Cooper ◽  
...  

A tris(hydroxypyridinone) chelator coordinates the PET imaging isotope, 89Zr4+, rapidly and quantitatively under ambient conditions, but a 89Zr-labelled tris(hydroxypyridinone)-immunoconjugate is not stable to in vivo demetallation.


2013 ◽  
Vol 49 (10) ◽  
pp. 1002-1004 ◽  
Author(s):  
François Guérard ◽  
Yong-Sok Lee ◽  
Raphaël Tripier ◽  
Lawrence P. Szajek ◽  
Jeffrey R. Deschamps ◽  
...  

Crystallography, quantum chemistry and potentiometry of Zr(iv) hydroxamate complexes: a combination of tools to improve the development of 89Zr chelation for nuclear imaging.


2020 ◽  
Vol 56 (83) ◽  
pp. 12664-12666 ◽  
Author(s):  
Antonio Bianchi ◽  
Matteo Savastano

Our results show that Zr(iv) has no special properties in the formation of hydroxamate complexes and confirm that it is able to bind up to four hydroxamate groups in solution, although with a normal decreasing ability in the successive steps.


Author(s):  
H.A. Cohen ◽  
T.W. Jeng ◽  
W. Chiu

This tutorial will discuss the methodology of low dose electron diffraction and imaging of crystalline biological objects, the problems of data interpretation for two-dimensional projected density maps of glucose embedded protein crystals, the factors to be considered in combining tilt data from three-dimensional crystals, and finally, the prospects of achieving a high resolution three-dimensional density map of a biological crystal. This methodology will be illustrated using two proteins under investigation in our laboratory, the T4 DNA helix destabilizing protein gp32*I and the crotoxin complex crystal.


2001 ◽  
Vol 120 (5) ◽  
pp. A637-A637
Author(s):  
Y RINGEL ◽  
D DROSSMAN ◽  
T TURKINGTON ◽  
B BRADSHAW ◽  
R COLEMAN ◽  
...  

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S323-S323
Author(s):  
Carolyn C Meltzer ◽  
Julie C Price ◽  
Scott K Ziolko ◽  
Chester A Mathis ◽  
Lisa A Weissfeld ◽  
...  

2011 ◽  
Vol 50 (04) ◽  
pp. N39-N39 ◽  
Author(s):  
H. W. E. Prechtel ◽  
F. A. Verburg ◽  
K. J. Dautzenberg ◽  
F. M. Mottaghy ◽  
F. F. Behrendt ◽  
...  
Keyword(s):  

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