A Surolia

Summary

Country: India

Publications

  1. pmc 'FAS't inhibition of malaria
    Avadhesha Surolia
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India or
    Biochem J 383:401-12. 2004
  2. ncbi request reprint Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies
    D D Singh
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, Karnataka, India
    Glycobiology 15:1025-32. 2005
  3. ncbi request reprint Paradigm shifts in malaria parasite biochemistry and anti-malarial chemotherapy
    Namita Surolia
    Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560 064, India
    Bioessays 24:192-6. 2002
  4. ncbi request reprint Cell surface receptor directed targeting of toxin to human malaria parasite, Plasmodium falciparum
    N Surolia
    Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore, India
    FEBS Lett 396:57-61. 1996
  5. ncbi request reprint Unusual structural stability and ligand induced alterations in oligomerization of a galectin
    A Surolia
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    FEBS Lett 409:417-20. 1997
  6. ncbi request reprint Exploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases
    Jayaraman Muralidharan
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biomol Struct Dyn 20:589-94. 2003
  7. ncbi request reprint Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin
    N Manoj
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    J Mol Biol 302:1129-37. 2000
  8. ncbi request reprint The reversible two-state unfolding of a monocot mannose-binding lectin from garlic bulbs reveals the dominant role of the dimeric interface in its stabilization
    K Bachhawat
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Biochemistry 40:7291-300. 2001
  9. ncbi request reprint Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution
    M M Prabu
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Mol Biol 276:787-96. 1998
  10. doi request reprint Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
    Bhaskar Chetnani
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    Acta Crystallogr D Biol Crystallogr 65:312-25. 2009

Collaborators

Detail Information

Publications49

  1. pmc 'FAS't inhibition of malaria
    Avadhesha Surolia
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India or
    Biochem J 383:401-12. 2004
    ..The present review describes the role of these enzymes, the status of their molecular characterization and the current advancements in the area of developing inhibitors against each of the enzymes of the pathway...
  2. ncbi request reprint Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies
    D D Singh
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, Karnataka, India
    Glycobiology 15:1025-32. 2005
    ..A comparison of the dimeric banana lectin with other beta-prism I fold lectins, provides interesting insights into the variability in their quaternary structure...
  3. ncbi request reprint Paradigm shifts in malaria parasite biochemistry and anti-malarial chemotherapy
    Namita Surolia
    Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560 064, India
    Bioessays 24:192-6. 2002
    ....
  4. ncbi request reprint Cell surface receptor directed targeting of toxin to human malaria parasite, Plasmodium falciparum
    N Surolia
    Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore, India
    FEBS Lett 396:57-61. 1996
    ..The transferrin toxin conjugate is significantly toxic to parasite growth and is 25 times more potent than toxin alone in inhibiting parasite protein synthesis. The mechanism of its entry into the intraerythrocytic parasite is discussed...
  5. ncbi request reprint Unusual structural stability and ligand induced alterations in oligomerization of a galectin
    A Surolia
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    FEBS Lett 409:417-20. 1997
    ....
  6. ncbi request reprint Exploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases
    Jayaraman Muralidharan
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biomol Struct Dyn 20:589-94. 2003
    ..e., B. napus, E. coli and P. falciparum. A comparison of their binding propensities thus determined should aid in the design of effective inhibitors for the respective enzymes...
  7. ncbi request reprint Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin
    N Manoj
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    J Mol Biol 302:1129-37. 2000
    ....
  8. ncbi request reprint The reversible two-state unfolding of a monocot mannose-binding lectin from garlic bulbs reveals the dominant role of the dimeric interface in its stabilization
    K Bachhawat
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Biochemistry 40:7291-300. 2001
    ..The small DeltaC(p) for the unfolding of ASAI reflects a relatively small, buried hydrophobic core in the folded dimeric protein...
  9. ncbi request reprint Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution
    M M Prabu
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Mol Biol 276:787-96. 1998
    ..A relationship among the non-canonical modes of dimeric association in legume lectins is presented...
  10. doi request reprint Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action
    Bhaskar Chetnani
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    Acta Crystallogr D Biol Crystallogr 65:312-25. 2009
    ..Therefore, the results have to be treated with caution. However, the changes in the locations of ligands exhibited by M. tuberculosis pantothenate kinase are remarkable and novel...
  11. ncbi request reprint Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors
    M Kapoor
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    Biochem Biophys Res Commun 289:832-7. 2001
    ..Triclosan shows competitive kinetics with respect to NADH but is uncompetitive with respect to NAD(+), which shows that the binding of triclosan to the enzyme is facilitated in the presence of NAD(+)...
  12. ncbi request reprint M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations
    Bhaskar Chetnani
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    J Mol Biol 400:171-85. 2010
    ..Furthermore, the dual specificity of the mycobacterial enzyme appears to have been caused by a biological necessity...
  13. ncbi request reprint Structural basis for the energetics of jacalin-sugar interactions: promiscuity versus specificity
    A Arockia Jeyaprakash
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Mol Biol 347:181-8. 2005
    ..These results and other available evidence suggest that jacalin is specific to O-glycans and its affinity to N-glycans is extremely weak or non-existent and therefore of limited value in processes involving biological recognition...
  14. ncbi request reprint Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure
    S Kundhavai Natchiar
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr D Biol Crystallogr 60:211-9. 2004
    ..Small consistent movements occur in the combining site upon sugar binding, although the site is essentially preformed...
  15. ncbi request reprint Thermodynamics of substrate binding to the chaperone SecB
    V G Panse
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Biochemistry 39:2420-7. 2000
    ..The data are consistent with a model where SecB binds substrate molecules at an exposed hydrophobic cleft. SecB aggregation in the absence of substrate is prevented by electrostatic repulsion between negatively charged SecB tetramers...
  16. ncbi request reprint Structural basis for triclosan and NAD binding to enoyl-ACP reductase of Plasmodium falciparum
    K Suguna
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India
    Biochem Biophys Res Commun 283:224-8. 2001
    ..The model indeed provided the structural rationale for its interaction with ligands and the cofactor and revealed unique characteristics of its binding site which could be exploited for improving the specificity of the inhibitors...
  17. ncbi request reprint Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization
    V R Srinivas
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012
    Biochim Biophys Acta 1527:102-11. 2001
    ....
  18. ncbi request reprint Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins
    R Ravishankar
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr D Biol Crystallogr 55:1375-82. 1999
    ..The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars...
  19. ncbi request reprint Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site
    R Ravishankar
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    Proteins 43:260-70. 2001
    ..A comparison of the neutral and acidic pH crystal structures indicates that the molecular packing in the latter is directed to a substantial extent by the increased affinity of the peptide loop to the combining site at acidic pH...
  20. ncbi request reprint Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity
    A Arockia Jeyaprakash
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Mol Biol 338:757-70. 2004
    ..This loop is four residues longer in artocarpin than in heltuba, providing an instance where variation in loop length is used as a strategy for generating carbohydrate specificity...
  21. ncbi request reprint Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes
    A Arockia Jeyaprakash
    Molecular Biophysics Unit, Indian Institute of Science, UGC Centre of Advanced Science, Bangalore, India
    J Mol Biol 321:637-45. 2002
    ..In either case, most of the lectin-disaccharide interactions are at the primary binding site. The conformation of T-antigen in the five complexes is nearly the same...
  22. ncbi request reprint Structural basis of the carbohydrate specificities of jacalin: an X-ray and modeling study
    A Arockia Jeyaprakash
    Molecular Biophysics Unit, UGC Centre of Advanced Study, Indian Institute of Science, Bangalore 560 012, India
    J Mol Biol 332:217-28. 2003
    ..They also lead to fresh insights into the nature of the binding of glycoproteins by jacalin...
  23. ncbi request reprint Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK
    Satyabrata Das
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Acta Crystallogr D Biol Crystallogr 62:628-38. 2006
    ..The strong correlation between structural plasticity, evolutionary conservation and variability and function exhibited by the molecule could be important in the design of species-specific inhibitors of the enzyme...
  24. ncbi request reprint Effect of glycosylation on the structure of Erythrina corallodendron lectin
    K A Kulkarni
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    Proteins 56:821-7. 2004
    ..The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation...
  25. pmc Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding
    J Krupakar
    Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bangalore 560 012, India
    Biochem J 338:273-9. 1999
    ..mol-1.K-1 for the B-subunit and 20+/-1 kJ.mol-1.K-1 for the A-subunit. These values have been used to calculate the thermal stability of abrin II and to surmise the mechanism of its transmembrane translocation...
  26. ncbi request reprint Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity
    J V Pratap
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    J Mol Biol 317:237-47. 2002
    ....
  27. pmc Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery
    R Krishna
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Nucleic Acids Res 34:2186-95. 2006
    ....
  28. ncbi request reprint Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    N Surolia
    Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore, India
    Nat Med 7:167-73. 2001
    ..falciparum. We establish the existence of the de novo fatty acid biosynthetic pathway in this parasite, and identify a key enzyme of this pathway for the development of new antimalarials...
  29. ncbi request reprint Expression of winged bean basic agglutinin in Spodoptera frugiperda insect cell expression system
    V R Srinivas
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    Biosci Rep 21:361-7. 2001
    ..Hence, a role for glycosylation in modulation of dimerization of WBA I is ruled out unlike Erythrina corallodendron (EcorL). Despite this the protein is active, with its sugar specificity unaltered...
  30. ncbi request reprint Purification, crystallization and preliminary X-ray structure analysis of the banana lectin from Musa paradisiaca
    D D Singh
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr D Biol Crystallogr 60:2104-6. 2004
    ..The trigonal crystals contain one dimeric molecule in the asymmetric unit. The structure has been solved using molecular replacement to a resolution of 3 A. The structure of the subunit is similar to that of jacalin-like lectins...
  31. pmc Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis
    Satyabrata Das
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:65-7. 2005
    ..3, c = 115.45 A and a = b = 107.63, c = 89.85 A, respectively, were collected at room temperature on a home X-ray source. Structures of both crystal forms were solved for one subunit in the asymmetric unit by molecular replacement...
  32. ncbi request reprint Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin
    S Kundhavai Natchiar
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Acta Crystallogr D Biol Crystallogr 62:1413-21. 2006
    ..Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature...
  33. ncbi request reprint The combination of molecular dynamics with crystallography for elucidating protein-ligand interactions: a case study involving peanut lectin complexes with T-antigen and lactose
    J V Pratap
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr D Biol Crystallogr 57:1584-94. 2001
    ....
  34. ncbi request reprint Computational analysis of multivalency in lectins: structures of garlic lectin-oligosaccharide complexes and their aggregates
    Gosu Ramachandraiah
    Molecular Biophysics Unit, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Glycobiology 13:765-75. 2003
    ..In addition to their immediate relevance to garlic lectin, these studies are of general interest in relation to lectin-oligosaccharide interactions...
  35. ncbi request reprint Thermodynamic analysis of the binding of galactose and poly-N-acetyllactosamine derivatives to human galectin-3
    K Bachhawat-Sikder
    Molecular Bioiphysics Unit, Indian Institute of Science, Bangalore 560012, India
    FEBS Lett 500:75-9. 2001
    ..Binding thermodynamics of galectin-3 with the galactose derivatives are essentially enthalpically driven and exhibit compensatory changes in DeltaH degrees and TDeltaS owing to solvent reorganization...
  36. ncbi request reprint Unfolding thermodynamics of the tetrameric chaperone, SecB
    V G Panse
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Biochemistry 39:2362-9. 2000
    ..The thermodynamic data suggest that SecB is a stable, well-folded, and tightly packed tetramer and that substrate binding occurs at a surface site rather than at an interior cavity...
  37. ncbi request reprint Kinetic and thermodynamic analysis of the interactions of 23-residue peptides with endotoxin
    C J Thomas
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biol Chem 276:35701-6. 2001
    ..Peptides that improve these features further are expected to perform better as endotoxin-neutralizing agents...
  38. doi request reprint Location and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action
    Bhaskar Chetnani
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    Acta Crystallogr D Biol Crystallogr 67:774-83. 2011
    ..The present investigation also suggests that N-alkylpantothenamides could be phosphorylated by the enzyme in the same manner as pantothenate...
  39. ncbi request reprint Mutational analysis at Asn-41 in peanut agglutinin. A residue critical for the binding of the tumor-associated Thomsen-Friedenreich antigen
    P Adhikari
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biol Chem 276:40734-9. 2001
    ..This study strengthens the theory that in lectins the nonprimary contacts generally made through water bridges are involved in imparting exquisite specificity...
  40. pmc Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [Artocarpus integrifolia (jack fruit) agglutinin]. Evidence for the presence of an internal repeat
    S K Mahanta
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    Biochem J 284:95-101. 1992
    ..Analyses of the sequence showed the presence of an internal repeat spanning residues 7-64 and 76-130. The internal repeat was found to be statistically significant...
  41. ncbi request reprint Studies on the aggregation and possible channel formation in membranes of a cyclic hexapeptide, cyclo (D-Ala-L-Pro-L-Ala)2
    J Ramesh
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    J Pept Res 61:63-70. 2003
    ..Reduction of the phase transition temperature and the maximum heat capacity of the lipid bilayer (DPPC) for gel-to-liquid crystalline phase transition indicates a strong interaction of the peptide with the lipid bilayer...
  42. ncbi request reprint Variability of calcium binding to EF-hand motifs probed by electrospray ionization mass spectrometry
    A K Moorthy
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore
    J Am Soc Mass Spectrom 12:1296-301. 2001
    ....
  43. ncbi request reprint Re-refinement using reprocessed data to improve the quality of the structure: a case study involving garlic lectin
    Gosu Ramachandraiah
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India
    Acta Crystallogr D Biol Crystallogr 58:414-20. 2002
    ..It could be established that the crystal asymmetric unit contains two identical heterodimers. The new refined structure also provided a better definition of other finer structural details...
  44. ncbi request reprint Insights into the substrate specificity of a thioesterase Rv0098 of mycobacterium tuberculosis through X-ray crystallographic and molecular dynamics studies
    Koustav Maity
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biomol Struct Dyn 29:973-83. 2012
    ..A combination of crystallographic and molecular dynamics studies thus explained the structural basis of accommodating long chain substrates by Rv0098 of M. tuberculosis...
  45. pmc Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis
    A Paul
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    Acta Crystallogr Sect F Struct Biol Cryst Commun 69:1422-4. 2013
    ..Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule...
  46. ncbi request reprint Exploiting lectin affinity chromatography in clinical diagnosis
    P R Satish
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
    J Biochem Biophys Methods 49:625-40. 2001
    ..in the diagnosis of certain pathological conditions, and the possibility of using this knowledge in designing treatments for various diseases, is discussed...
  47. ncbi request reprint In vitro antimalarial activity of extracts of three plants used in the traditional medicine of India
    G P Bhat
    Molecular Biology and Genetics Unit, Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore, Karnataka State, India
    Am J Trop Med Hyg 65:304-8. 2001
    ..Among the 3 plants tested, 2 had significant inhibitory effect on P. falciparum in vitro...
  48. ncbi request reprint Plasmepsin inhibitors: design, synthesis, inhibitory studies and crystal structure analysis
    M M Kesavulu
    Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India
    J Pept Res 66:211-9. 2005
    ..In this paper, we discuss the synthesis, crystal structures and inhibitory nature of these two compounds which have a potential to inhibit plasmepsins...
  49. ncbi request reprint Napin from Brassica juncea: thermodynamic and structural analysis of stability
    T C Jyothi
    Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Mysore 570020, India
    Biochim Biophys Acta 1774:907-19. 2007
    ..The internal repeats may contribute to the greater stability of napin. A thorough understanding of the structure and stability of these proteins is essential before they can be exploited for genetic improvements for nutrition...