My Research

Selected Publications

1) Masood, M., A. Mohammad, Md. Z. Malik, A. Islam, R. Chaturvedi, M. M. Haque (2026). “Arginine Substitution of Conserved Lys609 and Lys733 Impairs FMN Dynamics, Electron Transfer, and Nitric Oxide Production in Endothelial Nitric Oxide Synthase.” International Journal of Biological Macromolecules,151772.

2) Masood, M., S. Khan, D. Yameen, A. Anwar, F. Khan, S. Iqbal, R. Chaturvedi, A. Shamsi and M. M. Haque (2025). "Glutamine Substitution at Lysine609 in the Autoinhibitory Region Modulates Catalysis, Uncoupling, and Conformational Dynamics of Endothelial Nitric Oxide Synthase." ACS Omega.

3) Masood, M., P. Singh, D. Hariss, F. Khan, D. Yameen, S. Siraj, A. Islam, R. Dohare and M. Mahfuzul Haque (2024). "Nitric oxide as a double-edged sword in pulmonary viral infections: Mechanistic insights and potential therapeutic implications." Gene 899: 148148.

4) Anwar, A., D. Yameen, M. Masood, S. Parvez and M. M. Haque (2025). "Neuronal Nitric Oxide Synthase (nNOS) uncoupling in ischemic stroke: Mechanisms of oxidative/nitrosative stress and opportunities for neuroprotection: A review." International Journal of Biological Macromolecules 332: 148589.

5) Khan, S., M. Masood, H. Gaur, S. Ahmad and M. A. Syed (2021). "Long non-coding RNA: An immune cells perspective." Life Sciences 271: 119152.

6) Khan, S., A. Zaki, M. Masood, A. Khan, M. Mohsin, A. Verma, P. C. Wilson, S. Ali and M. A. Syed (2025). "Combating sepsis-induced acute lung injury: PARP1 inhibition mediates oxidative stress mitigation and miR-135a-5p/SMAD5/Nanog axis drives regeneration." International Immunopharmacology 148: 114166.

7) Akand, S. K., A. Rahman, M. Masood, S. Tabrez, J. J. Jawed, M. Z. Ahmed, Y. Akhter, M. M. Haque and A. Rub (2025). "Leishmania donovani alters the host sphingolipid biosynthetic pathway regulatory microRNA hsa-miR-15a-5p for its survival." Microbial Pathogenesis 208: 108019.

8) Akand, S. K., A. Rahman, M. Masood, S. Tabrez, M. Saleem, M. Z. Ahmed, Y. Akhter, M. M. Haque and A. Rub (2025). "hsa-miR-330-5p regulates serine palmitoyl transferase long chain base subunit 1 and augments host protective immune response against Leishmania donovani infection." Archives of Microbiology 207(6): 123.

9) Yameen, D., S. Siraj, Z. A. Parray, M. Masood, A. Islam and M. M. Haque (2022). "Soft interactions versus hard core repulsions: A journey of cytochrome c from acid-induced denaturation to native protein via pre-molten globule and molten globule conformations exploiting dextran and its monomer glucose." Journal of Molecular Liquids 366: 120257.

Selected Conference Abstracts

1. Masood, M. et al. (2026). "Charge Neutralization at Lys609 Modulates Catalysis and Interdomain Dynamics of Endothelial Nitric Oxide Synthase" ASBMB Annual Meeting Program Abstracts Washington, D.C., USA, March 7-11, 2026.

2. Masood, M. et al. (2025). " Conserved Lysines in the FMN Domain of eNOS Govern Biochemical Catalysis Through Regulation of Interdomain Electron Transfer." ASHG Annual Meeting Program Abstracts Boston, USA, October 14-18, 2025.

3. Masood, M. et al. (2025). " Conserved Lysines in the FMN Domain of eNOS Govern Biochemical Catalysis Through Regulation of Interdomain Electron Transfer " FEBS Congress Abstracts Istanbul, Turkey, July 5-9, 2025.

4. Masood, M. et al. (2025). " Acetylation governs catalytic efficiency and uncoupling in Endothelial Nitric Oxide Synthase." Drug Discovery 2025 Abstract Book New Delhi, India, February 24-26, 2025.

5. Masood, M. et al. (2024). " Acetylation governs uncoupling in Endothelial Nitric Oxide Synthase " Young Scholar's Meet Abstract Book New Delhi, India, October 9, 2024.

Current topic of Interest

NOS O2activation steps and the accompanying BH4 redox transitions that occur during the Arg and NOHA oxidation reactions. The catalysisstarts with the ferric enzyme being reduced by an electron from the reductase domain (FMNH). This allows the haem to bind O2and formthe haem-dioxy species, which is then reduced by BH4 to form the reactivehaem-oxy species that react either with Arg or with NOHA as indicated.After Arg is oxidized to NOHA, the reductase domain provides an electron to reduce the NOS-bound BH4 radical back to BH4 and, in doing so,resets the ferric enzyme for catalysis of NOHA oxidation. During the NOHA reaction, the BH4 radical that forms receives an electron from a NOSreaction/product species, and this allows generation of the enzyme ferric haem-NO species that releases NO

NOS enzyme productive and futile cycling during catalysis. The reduction of ferric enzyme (kr) is the rate-limiting step for the NO biosyntheticreactions (central linear portion). This electron transfer is needed to reduce the ferric haem before each catalytic step (kr,kr0)andalsotoreduce the BH4 radical between the Arg and NOHA oxidation reactions (kr0). Thekcat1andkcat2are the conversion rates of the NOShaem-dioxy species (FeIIO2) to products in the L-Arg and NOHA reactions respectively. The ferric haem-NO product complex (FeIIINO) caneither release NO according to ratekdas part of a productive cycle or be reduced by the reductase domain according to ratekr000to a ferroushaem–NO complex (FeIINO), which reacts with O2according to ratekoxin an NO dioxygenase reaction as part of a futile cycle, to generatenitrate and the ferric enzyme.

Absorption spectra of cyt c at pH 2.0 and 7.0 in the presence of (a) different concentrations of dextran (0–300 mg ml1 ) and 0.5 M KCl at 25 C, (b) glucose (0–300 mg ml1 ) and 0.5 M KCl at 25 C

Intrinsic fluorescence spectra of cyt c at pH 2.0 and 7.0 in the presence of (a) different concentrations of dextran (0–300 mg ml) at 25 C, (b)glucose (0–300 mg ml) at 25 C.

ANS fluorescence spectra of cyt c at pH 2.0 and 7.0 in the presence of (a) different concentrations of dextran (0–300 mg ml-1) at 25 C, (b) glucose (0–300 mg ml-1) at 25 C

Far-UV CD spectra of cyt c in the presence of (a) 300 mg ml-1 of dextran and glucose at pH 2.0 at and native state cyt c at pH 7.0 at 25 C, (b) 300 mg ml-1 of glucose at pH 2.0 at and native state cyt c at pH 7.0 at 25 C

Thermo gram of cyt c with (a) dextran, (b) glucose showing response in upper panel and isothermal binding in lower panel at pH 2.0 and 25 C

Molecular docking showing (A) surface image, (B) and (C) interaction of cyt c with (a) glucose and (b) dextran 70

(1) LncRNA act as a sponge for microRNA, therefore regulating the microRNA mediated downregulation of mRNA. (2) LncRNA act as miRNAs precursors. (3) LncRNA work as scaffolds for ribonucleoproteins. (4) LncRNA serves as a decoy through removing genomic regulatory factors. (5) LncRNA can downregulate or upregulate genetic expression via acting as guide RNA. (6) LncRNA helps in chromatin loop formation, thereby acting in gene regulation

The diagram shows important lncRNAs along with their respective molecular targets and associated diseases/functions in macrophages, dendritic cells, T cells, NK cells, B cells, neutrophils, eosinophils, and microglial cells.

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