Publications by authors named "M A Haque"

1,504 Publications

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Targeting α-synuclein aggregation and its role in mitochondrial dysfunction in Parkinson's disease.

Br J Pharmacol 2021 Sep 15. Epub 2021 Sep 15.

Department of Applied Life Science, Graduate School, BK21 Program, Konkuk University, Chungju, Republic of Korea.

Lewy bodies that contain aggregated α-synuclein (α-syn) in the dopaminergic (DA) neuron are the main culprit behind neurodegeneration in Parkinson's disease (PD). Besides, mitochondrial dysfunction has a well established and prominent role in the pathogenesis of PD. However, the exact mechanism by which α-syn causes dopaminergic neuronal loss was unclear. Recent evidence suggests that aggregated α-syn localises in the mitochondria and contributes to oxidative stress-mediated apoptosis in neurons. Therefore, the involvement of aggregated α-syn in mitochondrial dysfunction-mediated neuronal loss has made it an emerging drug target for the treatment of PD. However, the exact mechanism by which α-syn permeabilises through the mitochondrial membrane and affects the electron transport chain remains under investigation. In the present study, we describe mitochondria-α-syn interactions and how α-syn aggregation modulates mitochondrial homeostasis in PD pathogenesis. We also discuss recent therapeutic interventions targeting α-syn aggregation that may help researchers to design novel therapeutic treatments for PD.
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http://dx.doi.org/10.1111/bph.15684DOI Listing
September 2021

Biotechnology of Plastic Waste Degradation, Recycling, and Valorization: Current Advances and Future Perspectives.

ChemSusChem 2021 Sep 14. Epub 2021 Sep 14.

School of Energy and Environment, City University of Hong Kong, Hong Kong.

Invited for this month's cover is the collaborative group of Dr. Carol Sze Ki Lin and Dr. Xiang Wang. The image illustrates the biodegradation of plastics and the potential for plastic waste recycling and valorization to address the plastic waste dilemma. The Minireview itself is available at 10.1002/cssc.202100752.
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http://dx.doi.org/10.1002/cssc.202101825DOI Listing
September 2021

Biocompatible silver nanoparticles: An investigation into their protein binding efficacies, anti-bacterial effects and cell cytotoxicity studies.

J Pharm Anal 2021 Aug 8;11(4):422-434. Epub 2020 Dec 8.

Department of Chemistry, National Institute of Technology Meghalaya, Shillong, 793003, India.

Green synthesis of silver nanoparticles (AgNPs) has garnered tremendous interest as conventional methods include the use and production of toxic chemicals, products, by-products and reagents. In this regard, the synthesis of AgNPs using green tea (GT) extract and two of its components, (-)-epigallocatechin gallate (EGCG) and (+)-catechin (Ct) as capping/stabilizing agents, is reported. The synthesized AgNPs showed antibacterial activity against the bacterial strains and along with anticancer activity against HeLa cells. After administering nanoparticles to the body, they come in contact with proteins and results in the formation of a protein corona; hence we studied the interactions of these biocompatible AgNPs with hen egg white lysozyme (HEWL) as a carrier protein. Static quenching mechanism was accountable for the quenching of HEWL fluorescence by the AgNPs. The binding constant ( ) was found to be higher for EGCG-AgNPs ((2.309 ± 0.018) × 10 M) than for GT-AgNPs and Ct-AgNPs towards HEWL. EGCG-AgNPs increased the polarity near the binding site while Ct-AgNPs caused the opposite effect, but GT-AgNPs had no such observable effects. Circular dichroism studies indicated that the AgNPs had no such appreciable impact on the secondary structure of HEWL. The key findings of this research included the synthesis of AgNPs using GT extract and its constituent polyphenols, and showed significant antibacterial, anticancer and protein-binding properties. The -OH groups of the polyphenols drive the in situ capping/stabilization of the AgNPs during synthesis, which might offer new opportunities having implications for nanomedicine and nanodiagnostics.
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http://dx.doi.org/10.1016/j.jpha.2020.12.003DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8424387PMC
August 2021

ABO Blood Group and Outcomes in Patients with COVID-19 Admitted in the Intensive Care Unit (ICU): A Retrospective Study in a Tertiary-Level Hospital in Bangladesh.

J Multidiscip Healthc 2021 2;14:2429-2436. Epub 2021 Sep 2.

Department of Public Health, North South University, Dhaka, Bangladesh.

Purpose: The world is heavily suffering from the COVID-19 pandemic for more than a year, with over 191 million confirmed cases and more than 4.1 million deaths to date. Previous studies have explored several risk factors for coronavirus disease 2019 (COVID-19), but there is still a lack of association with ABO blood type. This study aimed to find out the relationship between the ABO blood group and COVID-19 outcomes in Bangladesh.

Subjects And Methods: This retrospective cross-sectional study was conducted in the intensive care unit (ICU) of a tertiary-level COVID-dedicated hospital in Dhaka city, Bangladesh, between April 2020 and November 2020. Records from 771 critically ill patients were extracted who were confirmed for COVID-19 by reverse transcriptase-polymerase chain reaction (RT-PCR) assay, and blood grouping records were available in the health records.

Results: The blood groups were 37.35%, 17.38%, 26.46%, and 18.81% for A, B, AB, and O type, respectively. Clinical symptoms were significantly more common in patients with blood type A ( < 0.05). Patients with blood type A had higher WBC counts and peak serum ferritin levels and both were statistically significant ( < 0.001). Patients with blood type A had a greater need for supplemental oxygen, and they were more likely to die in comparison to the patients with other blood types ( < 0.05). In multivariable analysis, our primary outcome death was significantly associated with blood type A (AOR: 3.49, 95% CI: 1.57-7.73) while adjusting for age, male gender, and non-communicable diseases.

Conclusion: Based on this study results, it can be concluded that the COVID-19 patients with blood type A have a higher chance of death and other complications. The authors recommend blood grouping before treating the COVID-19 patients, and healthcare workers should prioritize treating the patients based on that result.
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http://dx.doi.org/10.2147/JMDH.S330958DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8421326PMC
September 2021

Mining of a novel esterase (est3S) gene from a cow rumen metagenomic library with organosphosphorus insecticides degrading capability: Catalytic insights by site directed mutations, docking, and molecular dynamic simulations.

Int J Biol Macromol 2021 Sep 7;190:441-455. Epub 2021 Sep 7.

Department of Food Science, Gyeongsang National University, Jinju 52725, Republic of Korea. Electronic address:

A novel esterase (est3S) gene, 1026 bp in size, was cloned from a metagenomic library made of uncultured microorganisms from the contents of cow rumen. The esterolytic enzyme (Est3S) is composed of 342 amino acids and shows the highest identity with EstGK1 (71.7%) and EstZ3 (63.78%) esterases from the uncultured bacterium. The Est3S did not cluster in any up-to-date classes (I to XVIII) of esterase and lipase. Est3S protein molecular weight was determined to be 38 kDa by gel electrophoresis and showed optimum activity at pH 7.0 and 40 °C and is partially resistant to organic solvents. Est3S activity was enhanced by K, Na, Mg, and Ca and its highest activity was observed toward the short-chain p-nitrophenyl esters. Additionally, Est3S can degrade chlorpyrifos (CP) and methyl parathion (70% to 80%) in an hour. A mutated Est3S (Ser132-Ala132) did not show any activity toward CP and ester substrates. Notably, the GHS132QG motif is superimposed with the homolog esterase and cutinase-like esterase. Therefore, Ser132 is the critical amino acid like other esterases. The Est3S is relatively stable with ester compounds, and the methyl parathion complex was confirmed by molecular dynamics simulation. NOVELTY STATEMENT: A novel esterase gene (est3S) expressing esters and organophosphorus insecticide degradation traits was isolated from the uncultured bacterium in the contents of cow rumen. The Est3S protein did not cluster in any up-to-date classes (I to XVIII) of esterase/lipase proteins. Est3S was stable with the ligands up to 100 ns during the molecular dynamic simulations.
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http://dx.doi.org/10.1016/j.ijbiomac.2021.08.224DOI Listing
September 2021
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