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Our research focus is to screen molecules with anti-cancer properties and understand their mode of action with respect to cell death.  Many cancer cells are apoptosis resistant; we are trying to target them by an alternative cell death pathway known as “paraptosis” or cytoplasmic vacuolation mediated cell death.We are also interested in the studies of protein homeostasis and cell death in case of neuronal and pancreatic cells.

We are also trying to understand the biology of the extracellular matrix (ECM) in health and disease relevant to India with special reference to malnutrition. Focus is on cell adhesion protein fibronectin and its interaction with different cell surface proteins from both host (MMP-2, heparin, collagen) and guest [fibronectin/collagen binding proteins (FBP /CBP) from microbes].

Research Projects

  • Paraptosis: a newer approach to target cancer / Funded by DST
  • Characterization of Fibronectin isoforms and proteolytic fragments affecting cell behaviour / Funded by Amrita Vishwa Vidyapeetham
  • Factors affecting gelatinase (MMP-2) mediated fragmentation of fibronectin / Funded by Amrita Vishwa Vidyapeetham
  • Fibronectin and collagen binding proteins from probiotics and viruses (bacteriophages)/ Funded by Amrita Vishwa Vidyapeetham

Publications

Publication Type: Journal Article

Year of Publication Publication Type Title

2018

Journal Article

S. Nair and LLerena, A., “New perspectives in personalised medicine for ethnicity in cancer: population pharmacogenomics and pharmacometrics.”, Drug Metab Pers Ther, vol. 33, no. 2, pp. 61-64, 2018.

2011

Journal Article

X. Xu, Mikhailova, M., Chen, Z., Dr. Sanjay Pal, Robichaud, T. K., Lafer, E. M., Baber, S., and Steffensen, B., “Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2)”, Matrix Biology, vol. 30, pp. 404–412, 2011.[Abstract]


Cellular activation of latent matrix metalloproteinase-2 (proMMP-2) requires formation of a cell membrane-associated activation complex that involves specific binding between the hemopexin domain of proMMP-2 (PEX) and the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (C-TIMP-2). In this study, we tested the feasibility of inhibiting activation of proMMP-2 by exogenous inhibitors, which block the binding between PEX and TIMP-2. The recombinant C-TIMP-2 and synthetic peptides from C-TIMP-2 were used as inhibitors for proMMP-2 activation. Recombinant C-TIMP-2 bound specifically to both the catalytically inactive MMP-2(E404A) and the C-terminal domain of MMP-2 (PEX) in a concentration dependent manner with apparent K(d) of 3.9×10(-7)M and 1.7×10(-7)M, respectively. Moreover, C-TIMP-2 competed the binding between MMP-2(E404A) and full-length TIMP-2. Finally, activity assays showed that addition of C-TIMP-2 to HT-1080 fibrosarcoma cells inhibited proMMP-2 activation in a concentration-dependent manner. We then designed a synthetic peptide, P175L, consisting of 20 residues from the PEX-binding tail region of C-TIMP-2. P175L bound PEX and inhibited cell membrane-mediated activation of proMMP-2 in a concentration dependent manner. Deletion of the last 9 tail residues of C-TIMP-2 in P175L abrogated the inhibitory activities of the peptide showing that these residues were essential for function. Overall, these experiments have demonstrated that proMMP-2 activation can be inhibited by exogenous inhibitors which points to a potential strategy for MMP-2 specific inhibition.

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2011

Journal Article

B. Steffensen, Chen, Z., Dr. Sanjay Pal, Mikhailova, M., Su, J., Wang, Y., and Xu, X., “Fragmentation of fibronectin by inherent autolytic and matrix metalloproteinase activities”, Matrix Biology, vol. 30, pp. 34–42, 2011.[Abstract]


Fibronectin (FN) purified by gelatin affinity chromatography is unstable and undergoes fragmentation. The cleavage has been ascribed to inherent autolytic protease activities as well as co-purified matrix metalloproteinases (MMP). Understanding the mechanism by which the proteolysis of FN occurs is important, because the FN fragments have biological activities that differ from those of intact FN. Having excluded contributions of other plasma-derived proteases, the present experiments demonstrated that cleavage of FN by MMP-2 to distinct fragments occurred in synergy with inherent FN activities. Limited heat treatment of FN at 56 °C for 30 min inactivated the inherent protease activities sharply reducing autolysis of FN in a manner similar to that seen in the presence of serine proteinase inhibitors. Heat treatment did not alter cell attachment to FN, but significantly increased the susceptibility of FN to enzymatic cleavage by MMP-2. The carboxyl-terminal hemopexin-like domain (PEX) of MMP-2 was shown to possess critical exodomain properties required for the interactions of MMP-2 with FN, and FN was cleaved at a significantly reduced rate by an MMP-2 variant with deletion of PEX. Verifying the specificity of interactions, isolated PEX competed FN cleavage by MMP-2 in a concentration-dependent manner. These results have further elucidated the synergistic contributions of inherent autolytic serine protease-like activities and MMP-2 to fragmentation of FN and provide the rationale and basis for modified preparation and handling of FN used in biological research. More »»

2010

Journal Article

Dr. Nandita Mishra, Kar, R., Singha, P. K., Venkatachalam, M. A., McEwen, D. G., and Saikumar, P., “Inhibition of Mitochondrial Division Through Covalent Modification of Drp1 Protein by 15 deoxy-Delta(12,14)-prostaglandin J2”, Biochemical and biophysical research communications, vol. 395, pp. 17–24, 2010.[Abstract]


Arachidonic acid derived endogenous electrophile 15d-PGJ2 has gained much attention in recent years due to its potent anti-proliferative and anti-inflammatory actions mediated through thiol modification of cysteine residues in its target proteins. Here, we show that 15d-PGJ2 at 1µM concentration converts normal mitochondria into large elongated and interconnected mitochondria through direct binding to mitochondrial fission protein Drp1 and partial inhibition of its GTPase activity. Mitochondrial elongation induced by 15d-PGJ2 is accompanied by increased assembly of Drp1 into large oligomeric complexes through plausible intermolecular interactions. The role of decreased GTPase activity of Drp1 in the formation of large oligomeric complexes is evident when Drp1 is incubated with a non-cleavable GTP analog, GTPγS or by a mutation that inactivated GTPase activity of Drp1 (K38A). The mutation of cysteine residue (Cys644) in the GTPase effector domain, a reported target for modification by reactive electrophiles, to alanine mimicked K38A mutation induced Drp1 oligomerization and mitochondrial elongation, suggesting the importance of cysteine in GED to regulate the GTPase activity and mitochondrial morphology. Interestingly, treatment of K38A and C644A mutants with 15d-PGJ2 resulted in super oligomerization of both mutant Drp1s indicating that 15d-PGJ2 may further stabilize Drp1 oligomers formed by loss of GTPase activity through covalent modification of middle domain cysteine residues. The present study documents for the first time the regulation of a mitochondrial fission activity by a prostaglandin, which will provide clues for understanding the pathological and physiological consequences of accumulation of reactive electrophiles during oxidative stress, inflammation and degeneration.

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2010

Journal Article

R. Kar, Dr. Nandita Mishra, Singha, P. K., Venkatachalam, M. A., and Saikumar, P., “Mitochondrial Remodeling Following Fission Inhibition by 15d-PGJ2 Involves Molecular Changes in Mitochondrial Fusion Protein OPA1”, Biochemical and biophysical research communications, vol. 399, pp. 548–554, 2010.[Abstract]


We showed earlier that 15 deoxy Δ12, 14 prostaglandin J2 (15d-PGJ2) inactivates Drp1 and induces mitochondrial fusion [1]. However, prolonged incubation of cells with 15d-PGJ2 resulted in remodeling of fused mitochondria into large swollen mitochondria with irregular cristae structure. While initial fusion of mitochondria by 15d-PGJ2 required the presence of both outer (Mfn1 and Mfn2) and inner (OPA1) mitochondrial membrane fusion proteins, later mitochondrial changes involved increased degradation of the fusion protein OPA1 and ubiquitination of newly synthesized OPA1 along with decreased expression of Mfn1 and Mfn2, which likely contributed to the loss of tubular rigidity, disorganization of cristae, and formation of large swollen degenerated dysfunctional mitochondria. Similar to inhibition of Drp1 by 15d-PGJ2, decreased expression of fission protein Drp1 by siRNA also resulted in the loss of fusion proteins. Prevention of 15d-PGJ2 induced mitochondrial elongation by thiol antioxidants prevented not only loss of OPA1 isoforms but also its ubiquitination. These findings provide novel insights into unforeseen complexity of molecular events that modulate mitochondrial plasticity.

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2010

Journal Article

Dr. Sanjay Pal, Chen, Z., Xu, X., Mikhailova, M., and Steffensen, B., “Co-purified gelatinases alter the stability and biological activities of human plasma fibronectin preparations”, Journal of periodontal research, vol. 45, pp. 292–295, 2010.[Abstract]


Background and Objective: Fibronectin (FN) is an important cell adhesion molecule that is used widely to characterize cell behavior. Preparations of FN purified from human plasma by gelatin-Sepharose affinity chromatography typically also contain gelatin-binding gelatinases that may cleave FN, reduce its stability and alter its biological activities. Available methods for separating gelatinases from FN are resource demanding. Therefore, our objective was to devise a time- and cost-efficient protocol for purification of gelatinase-free FN. Material and Methods: Experiments tested the elution profiles for FN and gelatinases from gelatin-Sepharose using a concentration range (1-7%) of dimethyl sulfoxide (DMSO) and 4 m urea as eluants. Subsequently, we explored the sequential application of those eluants for differential elution of gelatinases and FN using a single affinity column. Finally, experiments characterized the stability of purified FN with or without contaminating gelatinases, as well as the effects of FN degradation on cell attachment and migration. Results: Assay optimization demonstrated that pre-elution with 3% DMSO efficiently eliminated gelatinases but not FN from gelatin-Sepharose, whereas subsequent elution with 4 m urea released FN. Sequential elutions with DMSO and urea produced gelatinase-free FN, which was more stable than FN eluted by urea only. Fibronectin degradation did not affect human gingival fibroblast attachment, but increased cell migration significantly. Conclusion: The present experiments devised a time- and cost-efficient protocol for eliminating gelatinases during purification of human plasma FN. Gelatinase-free FN preparations had greater stability, which may be essential for experiments because FN fragments have altered biological activities compared with intact FN. © 2009 The Authors. Journal compilation © 2009 Blackwell Munksgaard. More »»

2010

Journal Article

X. ZHU, Xu, X., Chen, Z., Mikhailova, M., Dr. Sanjay Pal, and Steffensen, B., “Fibronectin and Collagen Glycation Alter MMP Expression in Periodontal Fibroblasts”, J Dent Res, vol. 89, no. A, p. #1458, 2010.

2009

Journal Article

X. Xu, Mikhailova, M., Ilangovan, U., Chen, Z., Yu, A., Dr. Sanjay Pal, Hinck, A. P., and Steffensen, B., “Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2”, Biochemistry, vol. 48, pp. 5822–5831, 2009.[Abstract]


Interactions of matrix metalloproteinase-2 (MMP-2) with native and denatured forms of several types of collagen are mediated by the collagen binding domain (CBD). CBD positions substrates relative to the catalytic site and is essential for their cleavage. Our previous studies identified a CBD binding site on the α1(I) collagen chain. The corresponding synthetic collagen peptide P713 bound CBD with high affinity and was used in this study to identify specific collagen binding residues by NMR analysis of 15N-labeled CBD complexed with P713. Results obtained showed that P713 caused chemical shift perturbations of several surface-exposed CBD backbone amide resonances in a concentration-dependent manner. The 10 residues that underwent the largest chemical shift perturbations (R252 in module 1, R296, F297, Y302, E321, Y323, and Y329 in module 2, and R368, W374, and Y381 in module 3) were investigated by site-specific substitution with alanine. The structural integrity of the CBD variants was also analyzed by one-dimensional 1H NMR. Surface plasmon resonance and microwell protein binding assays of control and CBD variants showed that residues in all three CBD modules contributed to collagen binding. Single-residue substitutions altered the affinity for peptide P713, as well as native and denatured type I collagen, with the greatest effects observed for residues in modules 2 and 3. Additional alanine substitutions involving residues in two or three modules simultaneously further reduced the level of binding of CBD to native and denatured type I collagen and demonstrated that all three modules contribute to substrate binding. These results have localized and confirmed the key collagen binding site residues in the three fibronectin type II-like modules of MMP-2.

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2008

Journal Article

C. M. Stanley, Wang, Y., Dr. Sanjay Pal, Klebe, R. J., Harkless, L. B., Xu, X., Chen, Z., and Steffensen, B., “Fibronectin fragmentation is a feature of periodontal disease sites and diabetic foot and leg wounds and modifies cell behavior”, Journal of periodontology, vol. 79, pp. 861–875, 2008.[Abstract]


Background: Fibronectin (FN) undergoes fragmentation in periodontal disease sites and in poorly healing diabetic wounds. The biologic effects of FN fragments on wound healing remain unresolved. This study characterized the pattern of FN fragmentation and its effects on cellular behavior compared to intact FN. Methods: Polyclonal antibodies were raised against FN and three defined recombinant segments of FN and used to analyze gingival crevicular fluid from periodontal disease sites in systemically healthy subjects and in subjects with diabetes, as well as chronic leg and foot wound exudates from subjects with diabetes. Subsequently, the behavior of human gingival fibroblasts (hGFs) and HT1080 reference cells were analyzed by measuring cell attachment, migration, and chemotaxis in the presence of intact FN or recombinant FN fragments. Results: FN fragmentation was evident in fluids from periodontal disease sites and diabetic leg and foot wounds. However, no fragmentation pattern distinguished systemically healthy subjects from subjects with diabetes. hGFs and HT1080 cells required significantly higher concentrations of FN fragments to achieve attachment comparable to intact FN. Cells cultured on FN fragments also were morphologically different from cells cultured on full-length FN. Migration was reduced for hGFs cultured on FN fragments relative to full-length FN. In contrast, FN fragments increased HT1080 fibrosarcoma cell migration over intact FN. Conclusions: FN fragmentation is a prominent feature of periodontal and chronic leg and foot wounds in diabetes. Furthermore, cell culture assays confirmed the hypothesis that exposure to defined FN fragments significantly alters cell behavior. More »»

2008

Journal Article

J. Murillo, Wang, Y., Xu, X., Klebe, R. J., Chen, Z., Zardeneta, G., Dr. Sanjay Pal, Mikhailova, M., and Steffensen, B., “Advanced glycation of type I collagen and fibronectin modifies periodontal cell behavior”, Journal of periodontology, vol. 79, pp. 2190–2199, 2008.[Abstract]


Background: Advanced glycation end products (AGEs) have been linked to pathogenic mechanisms of diabetes mellitus. However, little is known about the contribution of protein glycation to periodontal disease in patients with diabetes. Therefore, this study investigated whether glycation of type I collagen (COLI) and fibronectin (FN) modified the behavior of human gingival fibroblasts (hGFs) and periodontal ligament fibroblasts (hPDLs). Methods: Procedures for rapid in vitro glycation of COLI and FN used methylglyoxal (MG). Formation of AGEs was analyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting with antibodies specific for MG-glycated proteins. Experiments then characterized the effects of glycated FN and COLI on the behavior of hGFs and hPDLs. Results: MG glycated COLI and FN in <6 hours. Confirming the specificity of the reactions, antibodies specific for MG-induced AGEs reacted with glycated FN and COLI but not with control proteins. In cell culture experiments, glycated FN was significantly less efficient in supporting the attachment of hGFs and hPDLs (P <0.05). Moreover, the morphologic parameters, including length, area, perimeter, and shape factor, were altered (P <0.001) for cells on both glycated proteins. Finally, cell migration was reduced on glycated FN and COLI (P <0.001). Conclusions: MG treatment efficiently glycated COLI and FN, providing a new tool to study the effects of diabetes on periodontal disease. The substantial effects of glycated COLI and FN on hGF and hPDL behavior indicated that protein glycation contributed to the pathogenesis and altered periodontal wound healing observed in patients with diabetes. More »»

2008

Journal Article

S. BABER, B, S., Z, C., M, M., Dr. Sanjay Pal, and Xu, X., “Competitive Inhibition of proMMP-2 Activation”, J Dent Res , vol. 87, no. A, p. 1012, 2008.[Abstract]


Objectives: Activation of proMMP-2 by membrane type matrix metalloproteinase-1 (MT1-MMP) requires formation of an activation complex involving the hemopexin-like domain of proMMP-2 (PEX), the carboxyl-terminal domain of TIMP-2 (C-TIMP-2) and MT1-MMP. The goal of these experiments was to demonstrate that excess of extraneous recombinant (r) PEX or rC-TIMP-2 may interrupt the activation complex and therefore inhibit MMP-2 activation. Methods: rC-TIMP-2 and rPEX were expressed in E. coli and purified to homogeneity by Ni3+ affinity chromatography as determined by SDS-PAGE. Human fibrosarcoma (HT1080) and rat osteosarcoma (ROS) cell lines were co-cultured with a concentration range of either purified rC-TIMP-2 or rPEX for 24 hours. The level of activation of proMMP-2 secreted into the culture medium was analyzed by gelatin zymography for relative amounts of latent 66 kDa and activated 59-kDa forms of MMP-2. Gel images were digitized and intensities of the two forms of MMP-2 were quantified. Results: With concanavlin-A induction, the ratio of active:latent MMP-2 was 78.6 in HT1080 and 2.5 in ROS culture media. When treated with 7 μM rC-TIMP-2, these ratios decreased to 2.8 in HT1080 and 0.5 in ROS conditioned media, reflecting 96% and 80% inhibition of proMMP-2 activation for HT1080 and ROS cells, respectively. Addition of 2.2 μM rPEX decreased the ratio to 1.5 and 0.22 for HT1080 and ROS, respectively, corresponding to 98% and 91% inhibition of proMMP-2 activation. The inhibition of proMMP-2 activation by rC-TIMP-2 and rPEX was concentration dependent. Conclusion: These results showed that rC-TIMP-2 and rPEX can inhibit activation of proMMP-2 in cancer cells by a mechanism that most likely involves competitive interruption of the interactions between PEX and TIMP-2. This approach constitutes a potential future strategy for MMP-2 inhibition in periodontal disease and oral cancer. (Supported by DE 017139 (COSTAR), DE 018135 and DE 017139). More »»

2007

Journal Article

M. R, B, S., Z, C., A, Y., Dr. Sanjay Pal, E, K., and X, X., “Cloning and Expression of Treponema Denticola Fibronectin-binding Protein (Fbp)”, J Dent Res , vol. 86, no. A, p. 2873, 2007.[Abstract]


Objectives: The bacterium T. denticola is a periodontal pathogen. The ability of T. denticola to bind fibronectin (FN) may be critical to its pathogenicity. Several T. denticola FN binding proteins (Fbps) have been identified previously by Western Blotting, but have not been characterized in detail. A gene (fbp) with significant homology to known Fbps genes from other bacteria was identified from the T. denticola genome sequence. To investigate this potential virulence factor, we cloned the fbp gene and initiated characterization of the encoded protein. Methods: The fbp gene was amplified from T. denticola strain 35405 genomic DNA by high fidelity PCR after digestion with HindIII, cloned into pRSETA with an N-terminal His tag, and verified by DNA sequencing. Fbp was then expressed in E. coli BL21(DE3) and purified by metal affinity chromatography. Interactions of Fbp with FN were analyzed in microwell-based protein-protein binding assays. Results: The amplified fbp gene from T. denticola ATCC 35405 genomic DNA had a size of 1.4 Kb. The fbp reading frame encoded a 471 amino acid Fbp, precisely matching the GenBank database sequence (accession number AE017226.1). Recombinant Fbp expressed in soluble form with a mass of 54 kDa after induction with IPTG. Fbp was purified to a purity >90% as assessed by scanning of images of SDS-PAGE gels. Initial protein binding assays demonstrated specific interactions between the T. denticola Fbp and FN. Studies are now verifying the role of Fbp in binding T. denticola to FN. Conclusion: These experiments cloned a gene (fbp) from T. denticola which encoded a FN binding protein (Fbp). Understanding the specific contribution of Fbp to T. denticola interactions with FN may provide important clues to the virulence mechanisms of this microorganism. Supported by NIDCR grants DE12818, DE14236, and DE016312 as well as DE14318 for CO STAR. More »»

2006

Journal Article

N. Mishra, Dr. Sanjay Pal, K, M. T., and S, D., “Production and characterization of arabinogalactan protein (AGP) from a hairy root line of Catharanthus roseus (L.) G. Don”, Indian Journal of Biotechnology, vol. 5, pp. 211-216, 2006.[Abstract]


Arabinogalactan protein (AGP), a class of cell wall proteoglycan, was isolated from the hairy root cultures of a newly developed hairy root line IIT-BT/D1 of Catharanthus roseus (L.) G. Don. AGP was found to be present both in the roots (0.3 mg/g fresh weight) and in the spent media (47 mg/L). The compositional analysis revealed the predominance of arabinose and galactose sugar, a characteristic feature of AGP. More »»

2003

Journal Article

Dr. Sanjay Pal, Das, S., and Dey, S., “Peroxidase and arabinogalactan protein as by-products during somatic embryo cultivation in air-lift bioreactor”, Process Biochemistry, vol. 38, pp. 1471–1477, 2003.[Abstract]


The spent medium after somatic embryo production has been analysed with respect to various enzymes, arabinogalactan protein and sandal oil. Apart from various hydrolases, a high level of peroxidase activity (32 200 U/ltre medium, with specific activity of 1.3417 U/μg protein) has been obtained. The peroxidase with an optimum activity at 50 °C was reasonably stable at 70 °C. The enzyme was active in the pH range 5–11, with an optimum at pH 6. The enzyme showed a Km of 10.91 mM and Vmax of 14.88 μM/min. Arabinogalactan protein (26–35 mg/l) has also been recovered from the extracellular medium. Sandal oil could not be detected by thin layer chromatography in the spent biomass or somatic embryos or the cell free medium, probably indicating its very low concentration. More »»

1999

Journal Article

S. Das, Das, S., Dr. Sanjay Pal, Mujib, A., Sahoo, S. S., Ponde, N. R., S Gupta, D., and Dey, S., “A novel process for rapid mass propagation of the aromatic plant Santalum album in liquid media and bioreactor”, Acta Horticulturae,(Proc. WOCMAP II 1999) Volume, vol. 3, pp. 281–288, 1999.[Abstract]


A rapid mass propagation method for Santalum album through in vitro cultivation in liquid media and airlift bioreactor has been developed. Embryogenesis, maturation, and germination were performed in the same bioreactor by the removal of exhausted medium and the input of fresh medium without any subculturing. In comparison to the propagation in agar solidified medium, this process of propagation increases the efficiency of production reduces the time required, and minimizes abnormalities. In the bioreactor, about 3000 somatic seedlings were obtained (59.3% were abnormal) in 6 weeks time, per liter of medium, against about 800 (88.9% abnormality) in 12 weeks in the case of solid medium. About 70% of the somatic seedlings grew to healthy plantlets and tolerated hardening trials, something that was rarely possible for somatic seedlings raised on solid media. More »»

1998

Journal Article

D. S, S, D., A, M., Dr. Sanjay Pal, and S, D., “Optimization of sucrose and dissolved oxygen level for somatic embryo production of Santalum album in airlift bioreactor”, Prensa Aromatica, vol. 14, pp. 12-13, 1998.

Publication Type: Patent

Year of Publication Publication Type Title

2018

Patent

S. Bhuniya, Dr. Nandita Mishra, Velusamy, N., Anupama Binoy, Bobba, K. Naidu, and Divya Nedungadi, “Flourescent Exomarker Probes for Hydrogen Sulfide Detection”, U.S. Patent 15 / 956 , 4742018.[Abstract]


A fluorescence probe with mitochondrial targeting and two-photon property, its preparation method and application in detecting and tracking endogenous H2S in samples or living cells. The fluorescent probe is prepared by a four-step preparation method and demonstrates a UV-vis absorption increment λab=395 nm and ˜43 fold higher fluorescence intensity in the presence of H2S. The probe further demonstrates stability, selectivity for H2S over competing agents and sensitivity as low as 20 nm. A method of detecting endogenous H2S rapidly in the absence of any external stimulators is provided. Samples are contacted with the probe and the changes in fluorescence are monitored to detect H2S levels. The disclosed probe is non-toxic and suitable as a biomarker and therapeutic molecule in cancer and other diseases.

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2000

Patent

Dr. Sanjay Pal, Dey, S., and Das, S., “Herbal skin nourishing gel”, 2000.

Publication Type: Conference Proceedings

Year of Publication Publication Type Title

2011

Conference Proceedings

N. Mishra, Kar, R., Singha, P. K., Venkatachalam, M. A., and Saikumar, P., “Ethacrynic acid induced mitochondrial fusion is mediated by Inhibition of fission protein Drp1”, XXXV All India Cell Biology Conference,16th – 18th Dec . NISER, Bhubaneswar, India, 2011.

2011

Conference Proceedings

Dr. Sanjay Pal, “Characterization of the Probiotic attributes of a Gelatin binding Lactobacillus from local curd”, XXXV Cell biology conference, 16-18 Dec. NISER, Bhubaneswar, Orissa, 2011.

2010

Conference Proceedings

P. K. Singha, Dr. Nandita Mishra, Kar, R., Pandeswara, S., Venkatachalam, M. A., and Saikumar, P., “Targeting LC3-SQSTM1 (p62) signaling axis to treat apoptosis resistant and metastatic breast cancers”, American Association for Cancer Research Annual Meeting, April 17-21. Washington DC , 2010.

2010

Conference Proceedings

S. B, Dr. Sanjay Pal, Z, C., X, X., M, M., H, Y., and Y, W., “Proteolytic processing of fibronectin by MMP-2 produces fragments with distinct biological properties”, Gordon Research Conference on Proteases and Inhibitors. Il Ciocco, Italy, 2010.

2010

Conference Proceedings

M. M, X, X., Dr. Sanjay Pal, and B, S., “Collagen Binding Site Residues are Key to MMP-2 Enzymatic Activities”, 28th Annual Dental Science Symposium, UTHSCSA and Cancer Development and Progression Program Retreat, San Antonio. 2010.

2009

Conference Proceedings

N. Mishra, R, K., PK, S., MA, V., and P, S., “Inhibition of Drp1 disassembly on mitochondrial remodeling”, Keystone Symposium, March 22-27. Whistler, Canada, 2009.

2009

Conference Proceedings

X. X, M, M., U, I., Z, C., A, Y., Dr. Sanjay Pal, AP, H., and B, S., “Mapping and Functional Confirmation of the Collagen Binding Sites of MMP-2”, Gordon Research Conference on Matrix Metalloproteinases. Les Diablerets, Switzerland, 2009.

2009

Conference Proceedings

M. M, X, X., Z, C., Dr. Sanjay Pal, and B, S., “Identical amino acids on MMP-2 position different types of collagen for cleavage”, The 27th Annual Dental Science Symposium, UTHSCSA and The Cancer Development and Progression Program Retreat, San Antonio. 2009.

2008

Conference Proceedings

N. Mishra, R, K., PK, S., MA, V., and P, S., “Mitochondrial Fusion Precedes Cell Death Induced by 15-Deoxy Δ12, 14 Prostaglandin J2”, The American Society for Cell Biology Conference . San Francisco , 2008.

2008

Conference Proceedings

Dr. Sanjay Pal, Z, C., X, X., M, M., Y, W., and B, S., “Cleavage of fibronectin by MMP-2 generates fragments with distinct biological activities”, The American Society for Cell Biology Annual Meeting Special Poster Session. Washington, DC, 2008.

2008

Conference Proceedings

X. X, S, B., Z, C., Dr. Sanjay Pal, M, M., and B, S., “Inhibition of proMMP-2 activation by carboxyl-terminal domain of TIMP-2 in vitro”, The American Society for Cell Biology Annual Meeting Special Poster Session. Washington, DC, 2008.

2007

Conference Proceedings

Dr. Sanjay Pal, Z, C., X, X., M, M., RJ, K., and B, S., “Enhanced strategy for separating human plasma fibronectin from MMPs by affinity chromatography”, The American Society for Cell Biology Annual Meeting Special Poster Session. Washington, DC, 2007.

2004

Conference Proceedings

N. Mishra and S, D., “Metabolite profiling in hairy root cultures of Catharanthus roseus”, IUPAC International Conference on Biodiversity and Natural products:Chemistry and Medical Applications, Jan. 26-31. New Delhi, 2004.

2004

Conference Proceedings

Dr. Sanjay Pal, S, D., A, M., and S, D., “Characterization Of Spent Media During Somatic Embryogenesis Of Sandalwood In Suspension Culture: Exploring Value Addition”, IUPAC International Conference on biodiversity and natural products: Chemistry and Medical Applications, Jan. 26-31. New Delhi, India, 2004.

2003

Conference Proceedings

N. Mishra, B, C., W, B., and S, D., “Arabinogalactan proteins from hairy root cultures of Catharanthus roseus”, 51st Annual Congress of the Society for Medicinal Plant Research, August 31st-Sep 4th. Kiel, Germany, 2003.

2001

Conference Proceedings

N. Mishra and S, D., “Hairy root cultures of Catharanthus roseus: Production of important alkaloids”, XXV All India Cell Biology Conference, Nov 1-3. IISc, Bangalore, India, 2001.

2001

Conference Proceedings

Dr. Sanjay Pal, S, D., and S, D., “Purification and characterization of arabinogalactan protein (AGP) during somatic embryogenesis in sandalwood (Santalum album L.)”, XXV All India Cell Biology Conference, Nov 1-3. IISc, Bangalore, India., 2001.

Publication Type: Book Chapter

Year of Publication Publication Type Title

1998

Book Chapter

S. Das, .Mujib, A., Das, S., Dr. Sanjay Pal, and .Dey, S., “Biotechnology of medicinal plants: Recent advances and potential”, in Role of biotechnology in medicinal and aromatic plants, vol. 2, Ukaaz Publication, Hyderabad, India, 1998, pp. 126-139.

1998

Book Chapter

A. .Mujib, Das, S., Das, S., Dr. Sanjay Pal, and .Dey, S., “Biotechnological Routes of Mass Propagation of Santalum album”, in Role of biotechnology in medicinal and aromatic plants - I. A Khan (ed.) , vol. I, Ukaaz Publication, Hyderabad, India, 1998, pp. 83-94.

1998

Book Chapter

S. Das, Das, S., .Mujib, A., Dr. Sanjay Pal, and .Dey, S., “Influence of carbon and pH on rapid mass propagation of Santalum album through somatic embryogenesis: Biotechnology application in agroforestry”, in Sandal and Its Products, AICAR, Canberra, Australia, 1998, pp. 66-68.

Publication Type: Conference Paper

Year of Publication Publication Type Title

1997

Conference Paper

D. S, S, D., Dr. Sanjay Pal, A, M., S, S., NR, P., S, D., and S, D., “A novel process for rapid mass propagation of the aromatic plant Sandal (Santalum album) in liquid media and bioreactor”, in World Congress on Medicinal and Aromatic Plants for Human Welfare, Nov.10-15, ICMAP-ISHS-SAIPA, Mendoza, Republica Argentina, 1997.