Yogendra Sharma

ORCID: 0000-0003-1345-8478
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About
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Research Areas
  • Connexins and lens biology
  • Enzyme Structure and Function
  • Neuroscience and Neuropharmacology Research
  • Heat shock proteins research
  • Yersinia bacterium, plague, ectoparasites research
  • Receptor Mechanisms and Signaling
  • Ion channel regulation and function
  • Protein Structure and Dynamics
  • S100 Proteins and Annexins
  • Leptospirosis research and findings
  • Cellular transport and secretion
  • Biochemical effects in animals
  • Advanced Glycation End Products research
  • Veterinary medicine and infectious diseases
  • Retinal Development and Disorders
  • Tuberculosis Research and Epidemiology
  • Calpain Protease Function and Regulation
  • Pancreatic function and diabetes
  • RNA and protein synthesis mechanisms
  • Corneal surgery and disorders
  • Intraocular Surgery and Lenses
  • Neuroscience and Neural Engineering
  • Neurobiology and Insect Physiology Research
  • Bacterial Genetics and Biotechnology
  • Ocular Surface and Contact Lens

Centre for Cellular and Molecular Biology
2014-2024

Academy of Scientific and Innovative Research
2016-2024

Indian Institute of Science Education and Research Berhampur
2019-2024

Council of Scientific and Industrial Research
2008-2013

Institut de Biologie Moléculaire et Cellulaire
2009-2012

National Eye Institute
2003

National Institutes of Health
2001

National Heart Lung and Blood Institute
2001

Regulation and dysregulation of intracellular calcium (Ca2+) signaling via the inositol 1,4,5-trisphosphate receptor (InsP3R) has been linked to many cellular processes pathological conditions. In present study, addition neuronal sensor-1 (NCS-1), a high-affinity, low-capacity, calcium-binding protein, purified InsP3R type 1 (InsP3R1) increased channel activity in both calcium-dependent -independent manner. intact cells, enhanced expression NCS-1 resulted release upon stimulation...

10.1172/jci22466 article EN Journal of Clinical Investigation 2006-05-12

Leptospira spp., the causative agents of leptospirosis, adhere to components extracellular matrix, a pivotal role for colonization host tissues during infection. Previously, we and others have shown that immunoglobulin-like proteins (Lig) spp. bind fibronectin, laminin, collagen, fibrinogen. In this study, report can be immobilized by human tropoelastin (HTE) or elastin from different tissues, including lung, skin, blood vessels, Lig HTE elastin. Moreover, both same LigB domains, LigBCon4,...

10.1074/jbc.m109.004531 article EN cc-by Journal of Biological Chemistry 2009-05-28

Leptospira spp. are pathogenic spirochetes that cause the zoonotic disease leptospirosis. Leptospiral immunoglobulin (Ig)-like protein B (LigB) contributes to binding of extracellular matrix proteins such as fibronectin, fibrinogen, laminin, elastin, tropoelastin and collagen. A high-affinity Fn-binding region LigB has been localized LigBCen2, which contains partial 11th full 12th Ig-like repeats (LigBCen2R) 47 amino acids non-repeat (LigBCen2NR) LigB. In this study, gelatin domain...

10.1371/journal.pone.0011301 article EN cc-by PLoS ONE 2010-06-24

Summary Transposon insertions in a novel 3.798 kb open reading frame (ORF) of the rice pathogen, Xanthomonas oryzae pv. ( Xoo ) cause virulence deficiency and altered colony/lawn morphology. This ORF encodes protein, XadA, 1265 amino acids that exhibits significant similarity to non‐fimbrial adhesins animal pathogenic bacteria such as Yersinia YadA Moraxella UspA1. An interesting feature is region repeated six times within XadA sequence encompasses almost entire length protein. Anti‐XadA...

10.1046/j.1365-2958.2002.03188.x article EN Molecular Microbiology 2002-10-31

The β- and γ-crystallins are closely related lens proteins that members of the βγ-crystallin superfamily, which also include many non-lens members. Although β-crystallin is known to be a calcium-binding protein, this property has not been reported in γ-crystallin. We have studied calcium binding properties γ-crystallin, we show it binds 4 mol eq with dissociation constant 90 µm. It calcium-mimic spectral probes, terbium Stains-all. Calcium does significantly influence protein secondary...

10.1074/jbc.m102164200 article EN cc-by Journal of Biological Chemistry 2001-10-01

Pathogenic Leptospira spp. express immunoglobulin-like proteins, LigA and LigB, which serve as adhesins to bind extracellular matrices mediate their attachment on host cells. However, nothing is known about the mechanism by these proteins are involved in pathogenesis. We demonstrate that LigBCen2 binds Ca2+, evidenced inductively coupled plasma optical emission spectrometry, energy dispersive 45Ca overlay, mass although there no motif for Ca2+ binding. four determined matrix-assisted laser...

10.1074/jbc.m801350200 article EN cc-by Journal of Biological Chemistry 2008-07-15

Abnormal levels of endogenous calcium ions are known to induce eye lens opacity, and a variety causative factors has been proposed, including calcium-mediated aggregation precipitation the proteins crystallins. We have specifically looked in some detail at interaction Ca2+ with various crystallins its consequences. Lenses incubated solutions containing 10 mM or 5 Tb3+ opacified. Fluorescence titration TbCl3 revealed that this ion binds delta- beta-crystallins solution. Equilibrium dialysis...

10.1016/s0021-9258(18)51556-8 article EN cc-by Journal of Biological Chemistry 1989-08-01

Phosphatidylinositol 4-OH kinase IIIbeta (PI-4Kbeta) is involved in the regulated local synthesis of phospholipids that are crucial for trans-Golgi network (TGN)-to-plasma membrane trafficking. In this study, we show calcium sensor proteins calneuron-1 and calneuron-2 physically associate with PI-4Kbeta, inhibit enzyme profoundly at resting low levels, negatively interfere Golgi-to-plasma At high levels inhibition released PI-4Kbeta activated via a preferential association neuronal sensor-1...

10.1073/pnas.0903001106 article EN Proceedings of the National Academy of Sciences 2009-05-20

The βγ-crystallin superfamily consists of evolutionarily related proteins with domain topology similar to lens β- and γ-crystallins, formed from duplicated Greek key motifs. Ca2+ binding was found in a few members earlier, although its prevalence diversity as inherent molecular properties among the are not well studied. To increase our understanding various βγ-crystallins, we undertook comprehensive structural Ca2+-binding studies seven bacteria, archaea, vertebrates, including determination...

10.1021/bi9017076 article EN Biochemistry 2009-11-18

Crystallins are the major proteins of a mammalian eye lens. The topologically similar lens proteins, beta- and gamma-crystallins, prototype founding members betagamma-crystallin superfamily. Betagamma-crystallins have until recently been regarded as structural proteins. However, calcium-binding properties few potential role betagamma-crystallins in fertility being investigated. Because elements other member such spherulin 3a, not present betaB2-crystallin from fish genomes, it was argued...

10.1111/j.1742-4658.2007.05941.x article EN FEBS Journal 2007-07-25

Leptospira immunoglobulin-like (Lig) proteins including LigA and LigB are adhesins that bind to fibronectin, collagen, laminin elastin. In addition, Lig fibrinogen (Fg)-binding proteins, although the physiological role of Lig-Fg interaction is unclear. this study, a previously identified Fg-binding region, LigBCen2 (amino acids 1014-1165 LigB), has been further localized LigBCen2R, which consists partial 11th entire 12th Ig-like domain 1014-1119). LigBCen2R was found C-terminal αC Fg (FgαCC;...

10.1111/j.1365-2958.2010.07510.x article EN cc-by Molecular Microbiology 2010-12-14

purpose. Previous studies have identified sequences encoding vascular endothelial growth factor (VEGF)-A and one of the VEGF receptors (VEGFR2, Flk-1, KDR) in lens fiber cells. The current study was undertaken to determine distribution VEGF-A protein lens, whether signaling through occurs cells, pattern expression during development, effect hypoxia on expression. methods. VEGFR2 were localized using immunocytochemistry. quantified by Western blot analysis. Activated (tyrosine phosphorylated)...

10.1167/iovs.02-1226 article EN Investigative Ophthalmology & Visual Science 2003-08-25

Background Many bacterial surface exposed proteins mediate the host-pathogen interaction more effectively in presence of Ca2+. Leptospiral immunoglobulin-like (Lig) proteins, LigA and LigB, are containing Bacterial immunoglobulin like (Big) domains. The function which contain Big fold is not known. Based on possible similarities βγ-crystallin folds, we here explore important question whether Ca2+ binds to a domains, would provide novel functional role fold. Principal Findings We selected six...

10.1371/journal.pone.0014377 article EN cc-by PLoS ONE 2010-12-29

To understand the disease mechanism and to identify potential tumor markers that would help in therapeutics, comparative proteomic analysis of 29 retinoblastoma (RB) tumors was performed using 14 non-neoplastic retinas (age ranged from 45 89 years) as control tissues.2-DE MALDI-TOF-TOF MS/MS were used differentially expressed proteins.Twenty-seven distinct proteins identified, including 16 upregulated 11 downregulated proteins. Significantly, higher mRNA levels apolipoprotein A1 (p<0.001),...

10.1002/prca.200900069 article EN PROTEOMICS - CLINICAL APPLICATIONS 2010-01-28

Neuronal calcium sensor-1 (NCS-1), a Ca2+-binding protein, plays an important role in the modulation of neurotransmitter release and phosphatidylinositol signaling pathway. It is known that physiological activity NCS-1 governed by its myristoylation. Here, we present myristoylation NSC-1 governing Ca2+ binding Ca2+-induced conformational changes as compared with nonmyristoylated protein. The 45Ca isothermal titration calorimetric data show increases degree cooperativity; thus, myristoylated...

10.1074/jbc.m312172200 article EN cc-by Journal of Biological Chemistry 2004-06-01
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