ORCID Profile
0000-0003-3917-4828
Current Organisations
Bond University
,
Rajamangala University of Technology Thanyaburi
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Publisher: The Intelligent Networks and Systems Society
Date: 30-06-2018
Publisher: Institute of Electrical and Electronics Engineers (IEEE)
Date: 2021
Publisher: Future Science Ltd
Date: 03-2021
Abstract: Understanding the potential association between the poly (ADP-ribose) polymerase member 14 (PARP14) and the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) may aid in understanding the host immunopathological response to the virus. PARP14 has an emerging role in viral infections, and this article considers its potential mechanisms for action in either a pro- or anti-viral manner. It is evident that more experimental work is required however, PARP14 appears vital in controlling the interferon response to the SARS-CoV-2 infection and has potential roles in balancing the proinflammatory cytokines of the cytokine storm. Furthermore, the SARS-CoV-2 macrodomain can prevent the PARP14-mediated antiviral response, suggesting a more complex relationship between PARP14 activity and SARS-CoV-2 infections.
Publisher: IEEE
Date: 15-09-2020
Publisher: American Chemical Society (ACS)
Date: 04-12-2021
Publisher: IEEE
Date: 11-2015
Publisher: IEEE
Date: 06-2016
Publisher: Elsevier BV
Date: 03-2019
Publisher: Future Science Ltd
Date: 02-2023
Publisher: Future Science Ltd
Date: 12-2020
Abstract: Background: Due to the conserved nature of the poly(ADP-ribose) polymerase (PARP) catalytic domain, the identification of unique residues is critical for the design of selective inhibitors. With inhibitors of the DNA-dependent PARP members already clinically approved, new efforts lie in discovering selective inhibitors for PARP5a and beyond. Targeting the noncatalytic domains, such as the macro2 and WWE domains may also provide a way to achieve selectivity. Methodology & results: This paper details the in silico profiling of x-ray crystal structures and homology models of the PARP catalytic, WWE and macro2 domains. PARP10 was the least conserved catalytic domain, with the macro2 and WWE domains possessing more unique residues than their catalytic counterparts. Conclusion: Overall, we identify unique residues to target when designing selective PARP inhibitors including HIS1610, TYR1620, ALA1627 and ARG1658 of the PARP14 catalytic domain, along with multiple unique residues across the PARP WWE and macro2 domains.
Publisher: Bentham Science Publishers Ltd.
Date: 12-10-2018
DOI: 10.2174/1389557518666180816111749
Abstract: Poly(ADP-ribose)polymerase, member 14 (PARP14, alternatively named ARTD8, BAL2, and COAST6) is an intracellular mono(ADP-ribosyl) transferase. PARP14 transfers a negatively charged ADP-ribose unit from a donor NAD+ molecule onto a target protein, post-translationally. PARP14's domain architecture consists of three macrodomains (Macro1, Macro2 and Macro3), a WWE domain and an ARTD (or catalytic domain). The Macro2 and Macro3 domains bind ADPribose (ADPr) with high affinity, whereas the WWE domain stabilizes the protein structure by binding to ADPr derivatives. The catalytic domain is involved in binding the NAD+ and catalyzing the mono- ADP-ribosylation reaction. PARP14 has been identified as a possible anti-cancer and antiinflammatory target. Acting as a transcriptional co-activator for STAT6, PARP14 acts to promote the over activation of the Th2 immune response, thus promoting the metabolic change to an anaerobic state (Warburg effect) and activation of cell survival pathways through JNK2 and the PGI/AMF complex. These changes are consistent with the metabolic sophistication observed in cancer, and the immune imbalance in inflammatory diseases. Current literature on selective and unselective PARP14 inhibitors are reviewed and discussed. Although there is no evidence that selective PARP inhibitors would be advantageous we have proposed some strategies for future design of selective PARP14 inhibitors.
Publisher: IEEE
Date: 12-2007
Publisher: Wiley
Date: 08-04-2020
Publisher: Future Science Ltd
Date: 12-2020
Abstract: Poly(ADP-ribose) polymerase (PARP) members PARP1 and PARP14 belong to an 18-member superfamily of post-translational modifying enzymes. A library of 9 novel non-NAD analog amine compounds was designed, synthesized and evaluated for inhibitory activity against PARP1 and PARP14. Both in silico studies and in vitro assays identified compound 2 as a potential PARP1 inhibitor, inhibiting activity by 93 ± 2% (PARP14 inhibition: 0 ± 6%), and 7 as a potential PARP14 inhibitor, inhibiting activity by 91 ± 2% (PARP1 inhibition: 18 ± 4%), at 10-μm concentration. Key in silico interactions with TYR907 in PARP1 and TYR1620 and TYR1646 in PARP14 have been identified. Compound 2 and compound 7 have been identified as potential leads for the development of selective PARP inhibitors.
Publisher: IEEE
Date: 11-2016
Publisher: IEEE
Date: 11-2009
Publisher: Future Science Ltd
Date: 10-2020
Abstract: Aim: ADP-ribosyl transferase member 8 (ARTD8) of the ARTD superfamily has been identified as a possible anti-cancer, antiviral and anti-inflammatory target. Method: Pure actives from natural products with a documented anti-cancer activity were docked into the catalytic site of 3SMI.pdb using PyRx and AutoDock Vina. Results: Epigallocatechin gallate (EGCG), trans-resveratrol, indol-3-carbinol, curcumin, quercetin and naringenin were investigated, in vitro, against ARTD8, revealing EGCG and quercetin as lead compounds, with EGCG displaying complete inhibition at 10 μM. Both EGCG and quercetins docked poses spanned across both the nicotinamide and adenine subsites of the catalytic domain, interacting with conserved residues Ser1641 and/or Ser1607 and Tyr1646. Thereby, suggesting that the meta-hydroxy group on the catechin ring B backbone may be responsible for these inhibition effects.
Publisher: IEEE
Date: 10-2006
Publisher: IEEE
Date: 03-2019
Publisher: American Chemical Society (ACS)
Date: 31-01-2022
Publisher: IEEE
Date: 2006
Publisher: Elsevier BV
Date: 2011
Publisher: IEEE
Date: 03-2020
Publisher: IEEE
Date: 11-2007
Publisher: IEEE
Date: 03-2020
Publisher: Elsevier BV
Date: 2013
Publisher: Institute of Electrical and Electronics Engineers (IEEE)
Date: 2021
Publisher: IEEE
Date: 03-2018
Publisher: Future Science Ltd
Date: 09-2020
Abstract: This review aims to reflect upon the major developments in PARP14 research from late 2017 to early 2020. In doing so, this report will focus on the continual elucidation of PARP14’s function including an emerging role in viral replication. This is in addition to other functional developments in cancer and inflammation, along with reflecting upon the leads in inhibitor design, including the increased attention toward the macrodomain. This report will also include a brief recap on contemporary poly(ADP-ribose) polymerase inhibitors and reflect upon the development surrounding the other poly(ADP-ribose) polymerases to overall give a succinct update to assist the development of selective PARP14 inhibitors.
Publisher: IEEE
Date: 03-2019
Location: Germany
No related grants have been discovered for Dr. Krischonme Bhumkittipich.