Publications by authors named "Rahul Modak"

L-asparagine is an essential amino acid for cell growth and common constituent of all the proteins. During high temperature food processing it reacts with reducing sugars and leads to acrylamide production through a complex process known as Maillard reaction. L-asparaginase hydrolyses the amine-group of L-asparagine to produce aspartic acid and ammonia.

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Hsp16.3 plays a vital role in the slow growth of Mycobacterium tuberculosis via its chaperone function. Many secretory proteins, including Hsp16.

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Article Synopsis
  • Prokaryotic deacetylases are divided into NAD-dependent sirtuins and Zn-dependent deacetylases, with NAD playing a key role in energy metabolism.*
  • CobB is a well-studied bacterial deacetylase with a known structure, existing in two isoforms (SeCobB and SeCobB) that differ by 37 amino acids in their N-terminal domain.*
  • Zinc has a notable influence on the stability and function of SeCobB, including reduced thermal stability and altered enzymatic activity, highlighting the importance of the N-terminal domain in zinc binding.*
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The regulation of gene expression is a dynamic process that is influenced by both internal and external factors. Alteration in the epigenetic profile is a key mechanism in the regulation process. Epigenetic regulators, such as enzymes and proteins involved in posttranslational modification (PTM), use different cofactors and substrates derived from dietary sources.

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Gram-negative intracellular pathogen Vibrio parahaemolyticus manifests its infection through a series of effector proteins released into the host via the type III secretion system. Most of these effector proteins alter signalling pathways of the host to facilitate survival and proliferation of bacteria inside host cells. Here, we report V.

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Retinoblastoma is usually initiated by biallelic gene inactivation. In addition, copy number alterations also contribute to RB pathogenesis. However, expression, its role in disease progression and correlation with RB histological risk factors are not well understood.

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Purpose: The key differences in cell death mechanisms in the trabecular meshwork (TM) in adult moderate and severe primary glaucoma remain still unanswered. This study explored key differences in cell death mechanisms in the trabecular meshwork (TM) in adult moderate and severe primary glaucoma.

Design: In-vitro laboratory study on surgical specimens and primary cell lines.

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Protein lysine acetylation is a conserved posttranslational modification that modulates several cellular processes. Protein acetylation and its physiological implications in eukaryotes are well understood; however, its role in bacteria is emerging. Lysine acetylation in bacteria is fine-tuned by the concerted action of lysine acetyltransferases (KATs), protein deacetylases (KDACs), and metabolic intermediates, e.

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Purpose: Pseudoexfoliation (PXF) is a unique form of glaucoma characterized by accumulation of exfoliative material in the eyes. Changes in tear profile in disease stages may give us insights into molecular mechanisms involved in causing glaucoma in the eye.

Methods: All patients were categorized into three main categories; pseudoexfoliation (PXF), pseudoexfoliation glaucoma (PXG) and cataract, which served as control.

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Purpose: Prostaglandin analogues (PGA's) are the mainstay and first line of treatment in current glaucoma practise. Though latanoprost and bimatoprost are the most commonly used PGA's with minimal side effects at lower concentrations like bimaotoprost 0.01%, direct comparison of their cytokine/MMP profile in tears has not been evaluated earlier.

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Purpose: To evaluate the differential expression of tear matrix metalloproteinases (MMP) 2 and 9 in of patients with various forms of glaucoma.

Methods: Tear samples were collected with a Schirmer's strip from 148 eyes of 113 patients (medically naïve patients with primary open-angle [POAG] or angle closure glaucoma [PACG] and those with pseudoexfoliation syndrome [PXF] or glaucoma [PXG]). These were compared to patients undergoing cataract surgery (controls) for this cross-sectional study.

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Background: There is renewed interest towards understanding the host-pathogen interaction in the light of epigenetic modifications. Although epithelial tissue is the major site for host-pathogen interactions, there is handful of studies to show how epithelial cells respond to pathogens. Bacterial infection in the mammary gland parenchyma induces local and subsequently systemic inflammation that results in a complex disease called mastitis.

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PCAF (KAT2B) belongs to the GNAT family of lysine acetyltransferases (KAT) and specifically acetylates the histone H3K9 residue and several nonhistone proteins. PCAF is also a transcriptional coactivator. Due to the lack of a PCAF KAT-specific small molecule inhibitor, the exclusive role of the acetyltransferase activity of PCAF is not well understood.

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The recent developments in the field of epigenetics have changed the way the covalent modifications were perceived from mere chemical tags to important biological recruiting platforms as well as decisive factors in the process of transcriptional regulation and gene expression. Over the years, the parallel investigations in the area of epigenetics and disease have also shown the significance of the epigenetic modifications as important regulatory nodes that exhibit dysfunction in disease states. In the present scenario where epigenetic therapy is also being considered at par with the conventional therapeutic strategies, this article reviews the role of histone acetylation as an epigenetic mark involved in different biological processes associated with normal as well as abnormal gene expression states, modulation of this acetylation by small molecules and warrants the possibility of acetylation as a therapeutic target.

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Mastitis is a multietiological complex disease, defined as inflammation of parenchyma of mammary glands. Bacterial infection is the predominant cause of mastitis, though fungal, viral and mycoplasma infections also have been reported. Based on the severity of the disease, mastitis can be classified into subclinical, clinical and chronic forms.

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Acyl carrier protein (ACP), an abundant protein in every cell, plays a central role in a number of metabolic processes requiring acyl group transfer. Conformational flexibility while crucial for its function remains substantially unaddressed. By dual polarization interferometry we establish correlation between the chain length of aliphatic groups covalently linked to Escherichia coli and Plasmodium falciparum ACP and their respective partial molar volumes in solution which helps to subserve the aforesaid goal.

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The type II fatty acid synthase (FAS) pathway of Plasmodium falciparum is a validated unique target for developing novel antimalarials, due to its intrinsic differences from the typeI pathway operating in humans. beta-Ketoacyl acyl carrier protein (ACP) reductase (FabG) performs the NADPH-dependent reduction of beta-ketoacyl-ACP to beta-hydroxyacyl-ACP, the first reductive step in the elongation cycle of fatty acid biosynthesis. In this article, we report intensive studies on the direct interactions of Plasmodium FabG and Plasmodium ACP in solution, in the presence and absence of its cofactor, NADPH, by monitoring the change in intrinsic fluorescence of P.

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The unfolding pathways of the two forms of Plasmodium falciparum acyl carrier protein, the apo and holo forms, were determined by guanidine hydrochloride-induced denaturation. Both the apo form and the holo form displayed a reversible two-state unfolding mechanism. The analysis of isothermal denaturation data provides values for the conformational stability of the two proteins.

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The emergence of strains of Plasmodium falciparum resistant to the commonly used antimalarials warrants the development of new antimalarial agents. The discovery of type II fatty acid synthase (FAS) in Plasmodium distinct from the FAS in its human host (type I FAS) opened up new avenues for the development of novel antimalarials. The process of fatty acid synthesis takes place by iterative elongation of butyryl-acyl carrier protein (butyryl-ACP) by two carbon units, with the successive action of four enzymes constituting the elongation module of FAS until the desired acyl length is obtained.

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Acyl carrier protein (ACP) plays a central role in fatty acid biosynthesis by transferring the acyl groups from one enzyme to another for the completion of the fatty acid synthesis cycle. Holo-ACP is the obligatory substrate for the synthesis of acyl-ACPs which act as the carrier and donor for various metabolic reactions. Despite its interactions with numerous proteins in the cell, its mode of interaction is poorly understood.

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Article Synopsis
  • The growing issue of drug-resistant malaria highlights the urgent need for new treatment options, focusing on the unique fatty acid biosynthesis pathway of the Plasmodium falciparum parasite as a promising target.
  • Researchers successfully cloned and overexpressed the P. falciparum beta-hydroxyacyl-acyl carrier protein dehydratase (PffabZ) gene, which plays a crucial role in the fatty acid synthesis process of the parasite.
  • Two inhibitors, NAS-91 and NAS-21, were identified that effectively hinder the enzyme activity and growth of P. falciparum, offering potential new strategies for malaria treatment by disrupting its fatty acid synthesis pathway.
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