scholarly journals Structural Insights into the Pre-Amyloid Tetramer of β-2-Microglobulin from Covalent Labeling and Mass Spectrometry

Biochemistry ◽  
2011 ◽  
Vol 50 (31) ◽  
pp. 6711-6722 ◽  
Author(s):  
Vanessa Leah Mendoza ◽  
Mario A. Barón-Rodríguez ◽  
Cristian Blanco ◽  
Richard W. Vachet
2019 ◽  
Vol 476 (21) ◽  
pp. 3125-3139 ◽  
Author(s):  
Daniel Shiu-Hin Chan ◽  
Jeannine Hess ◽  
Elen Shaw ◽  
Christina Spry ◽  
Robert Starley ◽  
...  

Abstract CoaBC, part of the vital coenzyme A biosynthetic pathway in bacteria, has recently been validated as a promising antimicrobial target. In this work, we employed native ion mobility–mass spectrometry to gain structural insights into the phosphopantothenoylcysteine synthetase domain of E. coli CoaBC. Moreover, native mass spectrometry was validated as a screening tool to identify novel inhibitors of this enzyme, highlighting the utility and versatility of this technique both for structural biology and for drug discovery.


2021 ◽  
Vol 116 ◽  
Author(s):  
Jhenifer Yonara de Lima ◽  
Marlon Dias Mariano Santos ◽  
Mario Tyago Murakami ◽  
Paulo Costa Carvalho ◽  
Tatiana de Arruda Campos Brasil de Souza

Biochemistry ◽  
2013 ◽  
Vol 52 (32) ◽  
pp. 5491-5502 ◽  
Author(s):  
James J. Marsh ◽  
Henry S. Guan ◽  
Sheng Li ◽  
Peter G. Chiles ◽  
Danny Tran ◽  
...  

2018 ◽  
Vol 72 (8) ◽  
Author(s):  
Clothilde Comby-Zerbino ◽  
Franck Bertorelle ◽  
Fabien Chirot ◽  
Philippe Dugourd ◽  
Rodolphe Antoine

2017 ◽  
Vol 53 (25) ◽  
pp. 3527-3530 ◽  
Author(s):  
Daniel Shiu-Hin Chan ◽  
Wei-Guang Seetoh ◽  
Brendan N. McConnell ◽  
Dijana Matak-Vinković ◽  
Sherine E. Thomas ◽  
...  

The interaction between Mycobacterium tuberculosis EthR and its operator DNA has been studied by native mass spectrometry, revealing an interesting stoichiometry.


2003 ◽  
Vol 9 (4) ◽  
pp. 944-950 ◽  
Author(s):  
Colin P. G. Butcher ◽  
Paul J. Dyson ◽  
Brian F. G. Johnson ◽  
Tetyana Khimyak ◽  
J. Scott McIndoe

2014 ◽  
Vol 395 (7-8) ◽  
pp. 763-768 ◽  
Author(s):  
Sabine Herbst ◽  
Noa Lipstein ◽  
Olaf Jahn ◽  
Andrea Sinz

Abstract Munc13 proteins are essential presynaptic regulators that mediate synaptic vesicle priming and play a role in the regulation of neuronal short-term synaptic plasticity. All four Munc13 isoforms share a common domain structure, including a calmodulin (CaM) binding site in their otherwise divergent N-termini. Here, we summarize recent results on the investigation of the CaM/Munc13 interaction. By combining chemical cross-linking, photoaffinity labeling, and mass spectrometry, we showed that all neuronal Munc13 isoforms exhibit similar CaM binding modes. Moreover, we demonstrated that the 1-5-8-26 CaM binding motif discovered in Munc13-1 cannot be induced in the classical CaM target skMLCK, indicating unique features of the Munc13 CaM binding motif.


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