Murray S Junop
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Explore the profile of Murray S Junop including associated specialties, affiliations and a list of published articles.
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42
Citations
807
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Recent Articles
1.
Akanmori N, Junop M, Gupta R, Park J
Int J Biol Macromol
. 2025 Jan;
299:140109.
PMID: 39837438
d-ribose is a critical sugar substrate involved in the biosynthesis of nucleotides, amino acids, and cofactors, with its phosphorylation to ribose-5-phosphate by ribokinase (RK) constituting the initial step in its...
2.
Moreau F, Atamanyuk D, Blaukopf M, Barath M, Herczeg M, Xavier N, et al.
J Med Chem
. 2024 Apr;
67(8):6610-6623.
PMID: 38598312
Inhibition of the biosynthesis of bacterial heptoses opens novel perspectives for antimicrobial therapies. The enzyme GmhA responsible for the first committed biosynthetic step catalyzes the conversion of sedoheptulose 7-phosphate into...
3.
Balachandran N, Grainger R, Rob T, Liuni P, Wilson D, Junop M, et al.
Biochemistry
. 2022 Oct;
61(20):2229-2240.
PMID: 36197914
α-Carboxyketose synthases, including 3-deoxy-d-heptulosonate 7-phosphate synthase (DAHPS), are long-standing targets for inhibition. They are challenging targets to create tight-binding inhibitors against, and inhibitors often display half-of-sites binding and partial inhibition....
4.
Heimhalt M, Mukherjee P, Grainger R, Szabla R, Brown C, Turner R, et al.
ACS Infect Dis
. 2021 Nov;
7(12):3292-3302.
PMID: 34761906
3-Deoxy-d-heptulosonate-7-phosphate (DAHP) synthase catalyzes the first step in the shikimate biosynthetic pathway and is an antimicrobial target. We used an inhibitor-in-pieces approach, based on the previously reported inhibitor DAHP oxime,...
5.
Carfrae L, MacNair C, Brown C, Tsai C, Weber B, Zlitni S, et al.
Nat Microbiol
. 2019 Oct;
5(1):93-101.
PMID: 31659298
To revitalize the antibiotic pipeline, it is critical to identify and validate new antimicrobial targets. In Mycobacteria tuberculosis and Francisella tularensis, biotin biosynthesis is a key fitness determinant during infection,...
6.
Laforet M, McMurrough T, Vu M, Brown C, Zhang K, Junop M, et al.
Nucleic Acids Res
. 2019 Oct;
47(20):10830-10841.
PMID: 31602462
Identifying and validating intermolecular covariation between proteins and their DNA-binding sites can provide insights into mechanisms that regulate selectivity and starting points for engineering new specificity. LAGLIDADG homing endonucleases (meganucleases)...
7.
NeuNAc Oxime: A Slow-Binding and Effectively Irreversible Inhibitor of the Sialic Acid Synthase NeuB
Popovic V, Morrison E, Rosanally A, Balachandran N, Senson A, Szabla R, et al.
Biochemistry
. 2019 Sep;
58(41):4236-4245.
PMID: 31549502
NeuB is a bacterial sialic acid synthase used by neuroinvasive bacteria to synthesize -acetylneuraminate (NeuNAc), helping them to evade the host immune system. NeuNAc oxime is a potent slow-binding NeuB...
8.
Mok M, Campalans A, Pillon M, Guarne A, Radicella J, Junop M
Sci Rep
. 2019 Mar;
9(1):3095.
PMID: 30816207
Repair of two major forms of DNA damage, single strand breaks and base modifications, are dependent on XRCC1. XRCC1 orchestrates these repair processes by temporally and spatially coordinating interactions between...
9.
McMurrough T, Brown C, Zhang K, Hausner G, Junop M, Gloor G, et al.
Nucleic Acids Res
. 2018 Oct;
46(22):11990-12007.
PMID: 30357419
LAGLIDADG homing endonucleases (meganucleases) are site-specific mobile endonucleases that can be adapted for genome-editing applications. However, one problem when reprogramming meganucleases on non-native substrates is indirect readout of DNA shape...
10.
Buzon B, Grainger R, Huang S, Rzadki C, Junop M
Nucleic Acids Res
. 2018 Aug;
46(17):9057-9066.
PMID: 30165656
DNA interstrand crosslinks (ICLs) covalently join opposing strands, blocking both replication and transcription, therefore making ICL-inducing compounds highly toxic and ideal anti-cancer agents. While incisions surrounding the ICL are required...