Kupyaphores─Self-Assembling Diisocyanolipopeptide ZnIIIonophores in Mycobacterium tuberculosis ZnII/CuI/IIHomeostasis and Antibacterial Effects Tsung-Yun Wong, Sachin Sharma, Kritee Mehdiratta, Rashmi S. Bhosale, Kaavya Nimmakayala, Randall K. Wilharm, Arnab Chakraborty, Moyosore Orimoloye, Qiang Liu, Siddhesh S. Kamat, Valérie C. Pierre, Rajesh S. Gokhale, Courtney C. Aldrich Journal of the American Chemical Society, 2025 Mycobacterium tuberculosis ( Mtb ), the leading cause of infectious disease mortality from a single pathogen, requires essential metal ions to establish infection and persist in the host. Kupyaphores, a suite of recently identified amphiphilic diisocyanolipopeptides, were reported to assist with Zn II acquisition to support a multitude of Zn II -dependent metalloenzymes critical for Mtb ’s survival and pathogenicity. However, compared to well-studied Fe III acquisition systems in Mtb, the mechanisms for Zn II acquisition and homeostasis remain virtually unexplored. Herein, we reveal them as novel metal ionophores in Mtb ’s metal-fluctuating lipidic niche. A concise modular scalable synthesis was developed to assess the critical features required for activity. Synthetic kupyaphores were structurally and functionally validated, respectively, via LCMS and chemical complementation of kupyaphore-deficient (Δ rv0101 ) Mtb . MS, NMR, and IR evidence demonstrated that kupyaphores complex Zn II as a bidentate ligand. Fluorescence competition data indicated Zn II /Cu I/II binding capabilities, by which Mtb entraps excessive metals within o/w-type micelles against host-induced metal intoxication. The inhibition against Gram-positive Staphylococcus aureus and the low human toxicity imply the potential as a novel antibacterial scaffold. Collectively, this work provides insight into the Zn II /Cu I/II homeostasis of Mtb and a chemical basis for the development of mechanistic tools, therapeutic conjugates against Mtb, and antibiotics.
Metabolite dynamics over the course of anti-tuberculosis treatment in individuals with mild and severe tuberculosis Catherine H Kagemann, Senbagavalli Prakash Babu, Komala Ezhumalai, Arnab Chakraborty, Kalaivani Raghupathy, Siddhesh S Kamat, Vijay Viswanathan, Samantha L Huey, Prakash Babu Narasimhan, Pranay Sinha, Elaine A Yu, Saurabh Mehta, Sonali Sarkar, and Plos Global Public Health, 2025 Mycobacterium tuberculosis (Mtb) manipulates host metabolism to gain nutrients and increase virulence. Despite known alterations in metabolism in individuals with pulmonary tuberculosis (PTB) during anti-tuberculosis (TB) treatment, the effect of disease severity on metabolite dynamics in individuals with PTB remains understudied. We examined metabolite dynamics over the course of anti-TB treatment in individuals diagnosed with mild (N = 8; smear grade of 1 + /2+ and mild chest x-ray (CXR) abnormality) or severe drug-sensitive PTB (N = 8; 3 + smear grade and moderate/advanced CXR abnormality) in a pilot proof-of-concept study compared to controls without TB (N = 7). Semi-targeted metabolomic analysis of plasma was performed using tandem liquid chromatography-mass spectrometry and electrospray ionization mass spectrometry at baseline, one month, and six months after treatment initiation. Our analysis revealed disease severity-specific metabolic profiles as well as those unique to controls. Many metabolites specific to mild or severe TB were involved in the glycerophospholipid and sphingolipid pathways. A subset of glycerophospholipids were enriched at baseline, month 1, and at the endpoint in individuals with mild and severe TB, despite anti-TB treatment. Our results highlight the importance of glycerophospholipid and sphingolipid pathways during Mtb infection and treatment, regardless of disease severity, and suggest that Mtb could induce chronic effects on host metabolism even after treatment.
Enzymatic Pathway for Kupyaphore Degradation in Mycobacterium tuberculosis: Mechanism of Metal Homeostasis and Turnover Rashmi S. Bhosale, Arnab Chakraborty, Tsung-Yun Wong, Dattatraya P. Masal, Rahul Choudhury, Sonali Srivastava, D. Srinivasa Reddy, Courtney C. Aldrich, Siddhesh S. Kamat, Debasisa Mohanty, Rajesh S. Gokhale ACS Chemical Biology, 2025 Metallophores are essential for metal homeostasis, regulating availability, and mediating host–pathogen interactions. Kupyaphores are specialized metallophores produced by Mycobacterium tuberculosis (Mtb) that primarily chelate zinc to support bacterial survival. Elevated kupyaphore levels early in infection highlight their importance, while their rapid decline, despite increasing bacterial loads, indicates tightly regulated mechanisms of production, consumption, and degradation. However, the processes driving kupyaphore catabolism and their role in preventing zinc toxicity in Mtb remain unclear. Here, we show that covalent modification of the isonitrile moiety in kupyaphores releases zinc, triggering degradation through a sequential three-step enzymatic pathway encoded by Mtb. Isonitrile hydratase converts isonitrile groups into formamides, which are subsequently processed into amines by N-substituted formamide deformylase and ultimately oxidized to β-ketoesters by amine oxidases. The biological significance of this pathway is underscored by the upregulation of these genes under metal-depleted and biofilm-forming conditions. Mutant Mtb strains lacking these genes exhibit impaired growth in metal-limiting environments and reduced levels of biofilm formation. Catalytic intermediates detected in Mtb cultures and infected mouse lung tissues confirm the pathway’s in vivo activity. Further, genome mining reveals that similar enzymes are conserved across organisms producing isonitrile-containing metabolites, emphasizing the broader importance of this pathway. Understanding these processes could pave the way for novel therapeutic strategies targeting kupyaphore catabolism.
Tandem Biocatalysis to Generate Hydrogen Sulfide and Promote Endogenous Antioxidant Response Suman Manna, Simran M. Gupta, Prerona Bora, Arnab Chakraborty, T. Anand Kumar, Siddhesh S. Kamat, Harinath Chakrapani Angewandte Chemie International Edition, 2025 Promoting cellular protective responses during oxidative stress conditions through the generation of antioxidant persulfide (RS‐SH) and hydrogen sulfide (H 2 S) has tremendous therapeutic potential. Here, we report a bioinspired glycoconjugate, a candidate for tandem biocatalysis and generates persulfide/ H 2 S in response to oxidative stress. The glycoconjugate is cleaved by β‐galactosidase, an enzyme that is expressed during oxidative stress; the product of this reaction is a substrate for 3‐mercaptopyruvate sulfurtransferase (3‐MST), an enzyme that is involved in persulfide/ H 2 S biosynthesis. The catalytic systems are orthogonal to one another, and the glycoconjugate is efficiently cleaved by these enzymes to generate the potent antioxidant glutathione persulfide as well as H 2 S. We demonstrate the efficacy of this conjugate in mitigating inflammation in the brain in an animal model. Together, using rationally designed substrates and fully catalytic steps, we leverage tandem biocatalysis to direct the generation of persulfide/ H 2 S, and promote cells’ own antioxidant response.
Bioinformatics Analysis Identifies Sequence Determinants of Enzymatic Activity for the PHARC-Associated Lipase ABHD12 Arnab Chakraborty, Archit Devarajan, Kundan Kumar, Rohith C. S., M. S. Madhusudhan, Girish S. Ratnaparkhi, Siddhesh S. Kamat Biochemistry, 2025 In humans, PHARC (polyneuropathy, hearing loss, ataxia, retinitis pigmentosa, and cataract) is an early onset autosomal recessive neurological disorder caused by deleterious mutations to ABHD12 (α/β-hydrolase domain protein # 12). Biochemically, ABHD12 functions as a lipase and catalyzes the hydrolysis of lysophosphatidylserine (lyso-PS) (lyso-PS lipase). By doing so, it controls the concentrations and signaling pathways regulated by this potent signaling lysophospholipid in the mammalian brain. While genetic mapping efforts have identified over 30 mutations in ABHD12 from human PHARC subjects, the biochemical activity of these pathogenic mutants remains unknown. To understand this, here, we performed an exhaustive bioinformatics survey and collated ABHD12 protein sequences from various organisms across evolution. Next, based on sequence alignments and structural modeling, we identified functionally relevant conserved residues in the ABHD12 protein sequence that are potentially important for its enzymatic activity. To validate these in silico findings, we generated numerous mutants of murine ABHD12, including those associated with human PHARC subjects, and assayed them for their enzymatic activity. Taken together, these complementary in silico and biochemical studies provide the first thorough sequence-function relationship for mammalian ABHD12, especially relevant in the context of PHARC. Finally, our evolutionary analysis identified CG15111 as an ABHD12 ortholog in the fruit fly (Drosophila melanogaster), and enzymatic assays indeed confirmed that recombinant CG15111 has robust lyso-PS lipase activity. Flies serve as an excellent animal system to model various human neurological diseases, and the identification of CG15111 as a Drosophila melanogaster ABHD12 ortholog opens new avenues to study PHARC in fly models.
TCF7l2 Regulates Fatty Acid Chain Elongase HACD3 during Lipid-Induced Stress Atanu Mondal, Sandhik Nandi, Vipin Singh, Arnab Chakraborty, Indrakshi Banerjee, Sabyasachi Sen, Shrikanth S Gadad, Siddhartha Roy, Siddhesh S Kamat, Chandrima Das Biochemistry, 2025 The transcriptional regulation of metabolic genes is crucial for maintaining metabolic homeostasis under cellular stress conditions. Transcription factor 7-like 2 (TCF7l2 or TCF4) is associated with type 2 diabetes (T2D) and functions as a transcription factor for various gluconeogenic genes. T2D often coexists with metabolic dysfunction-associated steatotic liver disease (MASLD) due to common underlying mechanisms and shared risk factors such as insulin resistance and obesity. This study demonstrates the transcriptional regulation of one of the important fatty acid chain elongases implicated in T2D, HACD3 (encoded by PTPLAD1 gene), under palmitic acid (PA)-induced stress conditions. We observed that TCF7l2 is associated with histone H3K4me3-binder protein TCF19 and is corecruited to the promoter of PTPLAD1. Upon PA treatment, the TCF19-TCF7l2 complex dissociates from the lipid chain elongase gene due to the reduced level of H3K4me3 enrichment, leading to PTPLAD1 activation. Remarkably, gene expression analysis from the PA-injected mice and NAFLD patients indicates an anticorrelation whereby reduced TCF7l2 expression enhances HACD3-mediated chain elongation and triglyceride production, thereby promoting the development of MASLD. Our findings delineate that the epigenetic mechanism of activation of lipid chain elongase genes mediated by TCF7l2 in concert with TCF19 has important implications in metabolic disorders.
Identification of ABHD6 as a lysophosphatidylserine lipase in the mammalian liver and kidneys Arnab Chakraborty, Prajwal Punnamraju, Theja Sajeevan, Arshdeep Kaur, Ullas Kolthur-Seetharam, Siddhesh S. Kamat Journal of Biological Chemistry, 2025 Lysophosphatidylserine (lyso-PS) is a potent hormone-like signaling lysophospholipid, which regulates many facets of mammalian biology and dysregulation in its metabolism is associated with several human neurological and autoimmune diseases. Despite the physiological importance and causal relation with human pathophysiology, little is known about the metabolism of lyso-PS in tissues other than the nervous and immune systems. To address this problem, here, we attempted to identify one (or more) lipase(s) capable of degrading lyso-PS in different mammalian tissues. We found that the membrane fraction of most mammalian tissues possess lyso-PS lipase activity, yet interestingly, the only bona fide lyso-PS lipase ABHD12 displays this enzymatic activity and has control over lyso-PS metabolism only in the mammalian brain. Using an in vitro inhibitor screen against membrane fractions of different tissues, we find that another lipase from the metabolic serine hydrolase family, ABHD6, is a putative lyso-PS lipase in the mouse liver and kidney. Finally, using pharmacological tools, we validate the lyso-PS lipase activity of ABHD6 in vivo, and functionally designate this enzyme as a major lyso-PS lipase in primary hepatocytes, and the mammalian liver and kidneys.
Inhibiting de novo lipogenesis identifies a therapeutic vulnerability in therapy-resistant colorectal cancer Eeshrita Jog, Ashwin Kumar Jainarayanan, Alessandro La Ferlita, Arnab Chakraborty, Afiya Dalwai, Showket Yahya, Anusha Shivashankar, Bhagya Shree Choudhary, Aakash Chandramouli, Mufaddal Kazi, Darshan Jain, Nileema Khapare, Akshaya B, Bushra K. Khan, Poonam Gera, Prachi Patil, Rahul Thorat, Nandini Verma, Lalit Sehgal, Avanish Saklani, Siddhesh S. Kamat, Sorab N. Dalal, Nazia Chaudhary Redox Biology, 2025 A significant clinical challenge in patients with colorectal cancer (CRC), which adversely impacts patient survival, is the development of therapy resistance leading to a relapse. Therapy resistance and relapse in CRC is associated with the formation of lipid droplets (LD) by stimulating de novo lipogenesis (DNL). However, the molecular mechanisms underlying the increase in DNL and the susceptibility to DNL-targeted therapies remain unclear. Our study demonstrates that colorectal drug-tolerant persister cells (DTPs) over-express Lipin1 (LPIN1), which facilitates the sequestration of free fatty acids into LDs. The increased expression is mediated by the ETS1-PTPN1-c-Src-CEBPβ pathway. Blocking the conversion of free fatty acids into LDs by treatment with statins or inhibiting lipin1 expression disrupts lipid homeostasis, leading to lipotoxicity and ferroptotic cell death in both DTPs and patient-derived organoids (PDOs) in vitro . Ferroptosis inhibitors or N-acetylcysteine (NAC) can alleviate lipid ROS and cell death resulting from lipin1 inhibition. This strategy also significantly reduces tumor growth in CRC DTP mouse xenograft and patient-derived xenograft (PDX) models. Our findings highlight a new metabolic vulnerability in CRC DTPs, PDO, and PDX models and provide a framework for the rational repurposing of statins. Targeting the phosphatidic acid (PA) to diacylglycerol (DAG) conversion to prevent lipid droplet formation could be an effective therapeutic approach for therapy-resistant CRC. • A high level of LPIN1 correlates with poor survival in CRC patients. • Colorectal cancer cells that enter the DTP state show increased levels of lipin1. • In colorectal cancer DTPs, DGAT2, rather than DGAT1, is over-expressed, leading to increased TAG levels and lipid droplet formation. • ETS1-PTPN1-c-Src-CEBPβ pathway activation promotes the conversion of FFA to LDs, preventing toxic lipid accumulation in CRC. • Preventing PA to DAG conversion by pharmaceutical or genetic approaches inhibits CRC DTP cell proliferation, inducing ferroptosis. • Additionally, this approach significantly reduces tumor growth in CRC DTP mouse xenograft and PDX models. In Brief : Jog et al. report that drug resistance in colorectal cancer (CRC) drug-tolerant persister cells (DTPs) is dependent on the increased expression of lipin1 stimulated by the ETS1-PTPN1-c-Src-CEBPβ pathway. Lipin1 expression promotes lipid droplet formation and prevents lipotoxicity. Inhibiting lipin1 expression or using statins to prevent the conversion of phosphatidic acid (PA) to diacylglycerol (DAG) suppresses CRC growth by inducing ferroptosis. These findings suggest a potential therapeutic avenue for combating aggressive CRC.
Lysophosphatidylserine: A Signaling Lipid with Implications in Human Diseases Arnab Chakraborty, Siddhesh S. Kamat Chemical Reviews, 2024 Lysophosphatidylserine (lyso-PS) has emerged as yet another important signaling lysophospholipid in mammals, and deregulation in its metabolism has been directly linked to an array of human autoimmune and neurological disorders. It has an indispensable role in several biological processes in humans, and therefore, cellular concentrations of lyso-PS are tightly regulated to ensure optimal signaling and functioning in physiological settings. Given its biological importance, the past two decades have seen an explosion in the available literature toward our understanding of diverse aspects of lyso-PS metabolism and signaling and its association with human diseases. In this Review, we aim to comprehensively summarize different aspects of lyso-PS, such as its structure, biodistribution, chemical synthesis, and SAR studies with some synthetic analogs. From a biochemical perspective, we provide an exhaustive coverage of the diverse biological activities modulated by lyso-PSs, such as its metabolism and the receptors that respond to them in humans. We also briefly discuss the human diseases associated with aberrant lyso-PS metabolism and signaling and posit some future directions that may advance our understanding of lyso-PS-mediated mammalian physiology.
Metabolic transitions regulate global protein fatty acylation Manasi Talwadekar, Subhash Khatri, Chinthapalli Balaji, Arnab Chakraborty, Nandini-Pal Basak, Siddhesh S. Kamat, Ullas Kolthur-Seetharam Journal of Biological Chemistry, 2024 Intermediary metabolites and flux through various pathways have emerged as key determinants of post-translational modifications. Independently, dynamic fluctuations in their concentrations are known to drive cellular energetics in a bi-directional manner. Notably, intracellular fatty acid pools that drastically change during fed and fasted states act as precursors for both ATP production and fatty acylation of proteins. Protein fatty acylation is well regarded for its role in regulating structure and functions of diverse proteins; however, the effect of intracellular concentrations of fatty acids on protein modification is less understood. In this regard, we unequivocally demonstrate that metabolic contexts, viz. fed and fasted states, dictate the extent of global fatty acylation. Moreover, we show that presence or absence of glucose that influences cellular and mitochondrial uptake/utilization of fatty acids and affects palmitoylation and oleoylation, which is consistent with their intracellular abundance in fed and fasted states. Employing complementary approaches including click-chemistry, lipidomics, and imaging, we show the top-down control of cellular metabolic state. Importantly, our results establish the crucial role of mitochondria and retrograde signaling components like SIRT4, AMPK, and mTOR in orchestrating protein fatty acylation at a whole cell level. Specifically, pharmacogenetic perturbations that alter either mitochondrial functions and/or retrograde signaling affect protein fatty acylation. Besides illustrating the cross-talk between carbohydrate and lipid metabolism in mediating bulk post-translational modification, our findings also highlight the involvement of mitochondrial energetics.
Formulation and Evaluation of Poly Herbal Laxative in the Treatment of Chronic Constipation S Chakraborty, A Chakraborty, S Bhattacharya International Journal of Medical and Pharmaceutical Sciences 2 (04) , 2026 2026
Transcription factor 19 modulates fatty acid elongation and unfolded protein response to attenuate palmitic acid-induced hepatic dysfunction A Mondal, A Chakraborty, S Nandi, V Singh, SS Kamat, C Das Nature Communications , 2026 2026
LMNA Haploinsufficiency in Human iPSC-Derived Cardiac Organoids Reveals Early Fibrotic Signaling as a Therapeutically Targetable Process A Zuniga, R Dulce, K Asensi, A Chakraborty, B DeRosa, P Levitan, ... bioRxiv, 2026.03. 25.714182 , 2026 2026
Societal Readiness Thinking Process 2.0: Incorporating Epistemic Reflexivity for Responsible Innovation R Braun, MJ Bernstein, A Chakraborty, J Starkbaum, F Winkler Science and Engineering Ethics 31 (6), 42 , 2025 2025
Academic Institutions as Innovation Intermediaries; Co-creating knowledge and building the Gujarat agroecology learning alliance (GALA) D Dutta, A Chakraborty Environmental Innovation and Societal Transitions 57, 101033 , 2025 2025
Kupyaphores─Self-Assembling Diisocyanolipopeptide Zn II Ionophores in Mycobacterium tuberculosis Zn II /Cu I/II Homeostasis and Antibacterial Effects TY Wong, S Sharma, K Mehdiratta, RS Bhosale, K Nimmakayala, ... Journal of the American Chemical Society 147 (44), 40652-40663 , 2025 2025 Citations: 1
Metabolite dynamics over the course of anti-tuberculosis treatment in individuals with mild and severe tuberculosis CH Kagemann, SP Babu, K Ezhumalai, A Chakraborty, K Raghupathy, ... PLOS Global Public Health 5 (10), e0004925 , 2025 2025 Citations: 1
Enzymatic Pathway for Kupyaphore Degradation in Mycobacterium tuberculosis : Mechanism of Metal Homeostasis and Turnover RS Bhosale, A Chakraborty, TY Wong, DP Masal, R Choudhury, ... ACS Chemical Biology 20 (7), 1492-1504 , 2025 2025 Citations: 1
Tandem Biocatalysis to generate hydrogen sulfide and promote endogenous antioxidant response S Manna, SM Gupta, P Bora, A Chakraborty, TA Kumar, SS Kamat, ... Angewandte Chemie 137 (24), e202502917 , 2025 2025 Citations: 4
Wag31, a membrane tether, is crucial for lipid homeostasis in mycobacteria Y Kapoor, H Khurana, D Dutta, A Chakraborty, A Priya, A Singh, ... elife 14, RP104268 , 2025 2025 Citations: 4
Emergence of Dip2-mediated specific DAG-based PKC signalling axis in eukaryotes S Shambhavi, S Mondal, A Chakraborty, N Shukla, BK Panda, S Kumar, ... Elife 14, RP104011 , 2025 2025 Citations: 2
TCF7l2 Regulates Fatty Acid Chain Elongase HACD3 during Lipid-Induced Stress A Mondal, S Nandi, V Singh, A Chakraborty, I Banerjee, S Sen, SS Gadad, ... Biochemistry 64 (8), 1828-1840 , 2025 2025 Citations: 3
Bioinformatics analysis identifies sequence determinants of enzymatic activity for the PHARC-associated lipase ABHD12 A Chakraborty, A Devarajan, K Kumar, R CS, MS Madhusudhan, ... Biochemistry 64 (8), 1852-1863 , 2025 2025 Citations: 1
Developing epidermis acquires nutrients from the external milieu by mTOR-dependent macropinocytosis SR Shetty, A Chakraborty, S Dongre, SS Kamat, M Sonawane bioRxiv, 2025.03. 18.644068 , 2025 2025
Identification of ABHD6 as a lysophosphatidylserine lipase in the mammalian liver and kidneys A Chakraborty, P Punnamraju, T Sajeevan, A Kaur, U Kolthur-Seetharam, ... Journal of Biological Chemistry 301 (2), 108157 , 2025 2025 Citations: 13
Inhibiting de novo lipogenesis identifies a therapeutic vulnerability in therapy-resistant colorectal cancer E Jog, AK Jainarayanan, A La Ferlita, A Chakraborty, A Dalwai, S Yahya, ... Redox biology 79, 103458 , 2025 2025 Citations: 22
Enzymatic Pathway for Kupyaphore Degradation in Mycobacterium tuberculosis: Mechanism of Metal Homeostasis and Turnover A CHAKRABORTY, SS KAMAT, RS GOKHALE, RS Bhosale American Chemical Society , 2025 2025
TCF7l2 Regulates Fatty Acid Chain Elongase HACD3 during Lipid-Induced Stress SS KAMAT, S Nandi, I Banerjee, V Singh, SS Gadad, A CHAKRABORTY, ... American Chemical Society , 2025 2025
Exploring the metabolism of the signaling lipid lysophosphatidylserine in mammalian physiology and developing LC-MS-based lipidomics platforms A CHAKRABORTY 2025
Identification of ABHD6 as a lysophosphatidylserine lipase in the mammalian liver and kidneys SS KAMAT, T SAJEEVAN, P PUNNAMRAJU, U Kolthur-Seetharam, ... Elsevier BV , 2025 2025
MOST CITED SCHOLAR PUBLICATIONS
A quest for miRNA bio-marker: a track back approach from gingivo buccal cancer to two different types of precancers N De Sarkar, R Roy, JK Mitra, S Ghose, A Chakraborty, RR Paul, ... PloS one 9 (8), e104839 , 2014 2014 Citations: 51
Lysophosphatidylserine: A signaling lipid with implications in human diseases A Chakraborty, SS Kamat Chemical reviews 124 (9), 5470-5504 , 2024 2024 Citations: 25
Inhibiting de novo lipogenesis identifies a therapeutic vulnerability in therapy-resistant colorectal cancer E Jog, AK Jainarayanan, A La Ferlita, A Chakraborty, A Dalwai, S Yahya, ... Redox biology 79, 103458 , 2025 2025 Citations: 22
Molecular attributes associated with refolding of inclusion body proteins using the freeze–thaw method P Singhvi, J Verma, N Panwar, TQ Wani, A Singh, M Qudratullah, ... Frontiers in Microbiology 12, 618559 , 2021 2021 Citations: 19
Identification of ABHD6 as a lysophosphatidylserine lipase in the mammalian liver and kidneys A Chakraborty, P Punnamraju, T Sajeevan, A Kaur, U Kolthur-Seetharam, ... Journal of Biological Chemistry 301 (2), 108157 , 2025 2025 Citations: 13
Metabolic transitions regulate global protein fatty acylation M Talwadekar, S Khatri, C Balaji, A Chakraborty, NP Basak, SS Kamat, ... Journal of Biological Chemistry 300 (1) , 2024 2024 Citations: 11
Metabolic regulation of CTCF expression and chromatin association dictates starvation response in mice and flies D Sen, B Maniyadath, S Chowdhury, A Kaur, S Khatri, A Chakraborty, ... Iscience 26 (7) , 2023 2023 Citations: 10
Tandem Biocatalysis to generate hydrogen sulfide and promote endogenous antioxidant response S Manna, SM Gupta, P Bora, A Chakraborty, TA Kumar, SS Kamat, ... Angewandte Chemie 137 (24), e202502917 , 2025 2025 Citations: 4
Wag31, a membrane tether, is crucial for lipid homeostasis in mycobacteria Y Kapoor, H Khurana, D Dutta, A Chakraborty, A Priya, A Singh, ... elife 14, RP104268 , 2025 2025 Citations: 4
TCF7l2 Regulates Fatty Acid Chain Elongase HACD3 during Lipid-Induced Stress A Mondal, S Nandi, V Singh, A Chakraborty, I Banerjee, S Sen, SS Gadad, ... Biochemistry 64 (8), 1828-1840 , 2025 2025 Citations: 3
Emergence of Dip2-mediated specific DAG-based PKC signalling axis in eukaryotes S Shambhavi, S Mondal, A Chakraborty, N Shukla, BK Panda, S Kumar, ... Elife 14, RP104011 , 2025 2025 Citations: 2
Kupyaphores─Self-Assembling Diisocyanolipopeptide Zn II Ionophores in Mycobacterium tuberculosis Zn II /Cu I/II Homeostasis and Antibacterial Effects TY Wong, S Sharma, K Mehdiratta, RS Bhosale, K Nimmakayala, ... Journal of the American Chemical Society 147 (44), 40652-40663 , 2025 2025 Citations: 1
Metabolite dynamics over the course of anti-tuberculosis treatment in individuals with mild and severe tuberculosis CH Kagemann, SP Babu, K Ezhumalai, A Chakraborty, K Raghupathy, ... PLOS Global Public Health 5 (10), e0004925 , 2025 2025 Citations: 1
Enzymatic Pathway for Kupyaphore Degradation in Mycobacterium tuberculosis : Mechanism of Metal Homeostasis and Turnover RS Bhosale, A Chakraborty, TY Wong, DP Masal, R Choudhury, ... ACS Chemical Biology 20 (7), 1492-1504 , 2025 2025 Citations: 1
Bioinformatics analysis identifies sequence determinants of enzymatic activity for the PHARC-associated lipase ABHD12 A Chakraborty, A Devarajan, K Kumar, R CS, MS Madhusudhan, ... Biochemistry 64 (8), 1852-1863 , 2025 2025 Citations: 1
Identification of ABHD6 as a regulator of lysophosphatidylserines in the mammalian liver and kidneys A Chakraborty, P Punnamraju, T Sajeevan, A Kaur, U Kolthur-Seetharam, ... bioRxiv, 2024.06. 02.597019 , 2024 2024 Citations: 1
Collated, Sequential and ML Approaches of Multi-Variant Features of Users on Authentication. S Chakraborty, A Chakraborty, H Purohit Journal of Mines, Metals & Fuels 71 (5) , 2023 2023 Citations: 1
Formulation and Evaluation of Poly Herbal Laxative in the Treatment of Chronic Constipation S Chakraborty, A Chakraborty, S Bhattacharya International Journal of Medical and Pharmaceutical Sciences 2 (04) , 2026 2026
Transcription factor 19 modulates fatty acid elongation and unfolded protein response to attenuate palmitic acid-induced hepatic dysfunction A Mondal, A Chakraborty, S Nandi, V Singh, SS Kamat, C Das Nature Communications , 2026 2026
LMNA Haploinsufficiency in Human iPSC-Derived Cardiac Organoids Reveals Early Fibrotic Signaling as a Therapeutically Targetable Process A Zuniga, R Dulce, K Asensi, A Chakraborty, B DeRosa, P Levitan, ... bioRxiv, 2026.03. 25.714182 , 2026 2026
