Taweewat Deemagarn
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Explore the profile of Taweewat Deemagarn including associated specialties, affiliations and a list of published articles.
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10
Citations
122
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Recent Articles
1.
Salman M, Venkateswaran D, Prakash A, Nguyen Q, Suntisukwattana R, Atthaapa W, et al.
Animals (Basel)
. 2024 Sep;
14(17).
PMID: 39272387
African swine fever virus (ASFV) has been responsible for the globally devastating epidemics in wild and domesticated pigs. Of the 24 identified ASFV genotypes, genotype II is the primary cause...
2.
Suwankitwat N, Deemagarn T, Bhakha K, Songkasupa T, Vitoonpong R, Trakunjaroonkit P, et al.
Vet Sci
. 2024 Jan;
11(1).
PMID: 38250916
Lumpy skin disease (LSD) is a viral infection that impacts the cattle industry. The most efficient approach to prevent disease involves the utilization of live-attenuated LSD vaccines (LAVs), which stands...
3.
Suwankitwat N, Songkasupa T, Boonpornprasert P, Sripipattanakul P, Theerawatanasirikul S, Deemagarn T, et al.
Vet Sci
. 2022 Oct;
9(10).
PMID: 36288155
The emergence of the lumpy skin disease virus (LSDV) was first detected in north-eastern Thailand in March 2021. Since then, the abrupt increase of LSD cases was observed throughout the...
4.
Singh R, Wiseman B, Deemagarn T, Jha V, Switala J, Loewen P
Arch Biochem Biophys
. 2008 Jan;
471(2):207-14.
PMID: 18178143
Catalase-peroxidases or KatGs from seven different organisms, including Archaeoglobus fulgidus,Bacillus stearothermophilus, Burkholderia pseudomallei, Escherichia coli, Mycobacterium tuberculosis, Rhodobacter capsulatus and Synechocystis PCC 6803, have been characterized to provide a comparative...
5.
Deemagarn T, Wiseman B, Carpena X, Ivancich A, Fita I, Loewen P
Proteins
. 2006 Oct;
66(1):219-28.
PMID: 17063492
Five residues in the multifunctional catalase-peroxidase KatG of Burkholderia pesudomallei are essential for catalase, but not peroxidase, activity. Asp141 is the only one of these catalase-specific residues not related with...
6.
Carpena X, Wiseman B, Deemagarn T, Herguedas B, Ivancich A, Singh R, et al.
Biochemistry
. 2006 Apr;
45(16):5171-9.
PMID: 16618106
Crystals of Burkholderia pseudomallei KatG retain their ability to diffract X-rays at high resolution after adjustment of the pH from 5.6 to 4.5, 6.5, 7.5, and 8.5, providing a unique...
7.
Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, et al.
EMBO Rep
. 2005 Oct;
6(12):1156-62.
PMID: 16211084
The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations,...
8.
Deemagarn T, Carpena X, Singh R, Wiseman B, Fita I, Loewen P
J Mol Biol
. 2004 Nov;
345(1):21-8.
PMID: 15567407
The Ser315Thr variant of the catalase-peroxidase KatG from Mycobacterium tuberculosis imparts resistance to the pro-drug isonicotinic acid hydrazide (isoniazid) through a failure to convert it to the active drug, isonicotinoyl-NAD....
9.
Singh R, Wiseman B, Deemagarn T, Donald L, Duckworth H, Carpena X, et al.
J Biol Chem
. 2004 Jul;
279(41):43098-106.
PMID: 15280362
Catalase-peroxidases (KatG) produced by Burkholderia pseudomallei, Escherichia coli, and Mycobacterium tuberculosis catalyze the oxidation of NADH to form NAD+ and either H2O2 or superoxide radical depending on pH. The NADH...
10.
Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry
Donald L, Krokhin O, Duckworth H, Wiseman B, Deemagarn T, Singh R, et al.
J Biol Chem
. 2003 Jul;
278(37):35687-92.
PMID: 12832453
The electron density maps of the catalase-peroxidase from Burkholderia pseudomallei (BpKatG) presented two unusual covalent modifications. A covalent structure linked the active site Trp111 with Tyr238 and Tyr238 with Met264,...