Biography Details
 
Dr. VERMA Chandra
Head of Division
 
Areas of Research Interest
 
  • Structural/Functional dynamics of biological molecules
  • Peptide/anti-microbial design
  • Virtual screening
 
Biography
 
Chandra Verma joined the Bioinformatics Institute (BII) A*STAR, Singapore, in November 2003. He heads the division of Biomolecular Modelling and Design and leads a group that applies physics based models to understand the links between protein sequence, structure and biological function. His group works closely with experimental laboratories where the hypotheses generated are tested. In addition, the group is also involved in designing peptides and small molecules (through virtual screening) both for interrogating biology as well as for therapeutic purposes. Prior to joining Singapore, he worked at the Structural Biology Laboratory in York, UK. He obtained his undergraduate degree at the Indian Institute of Technology, India and his D. Phil at the University of York.
 
Selected Publications
 
  1. Chen Y, Li T, Li J, Cheng S, Wang J, Verma C, Zhao Y, Wu C.
    Stabilization of peptides against proteolysis through disulfide-bridged conjugation with synthetic aromatics.
    Org Biomol Chem. 2017 Feb 8. doi: 10.1039/c6ob02786e.
    [Epub ahead of print] PubMed PMID: 28177025.
     
  2. Lin S, Koh JJ, Aung TT, Lim F, Li J, Zou H, Wang L, Lakshminarayanan R, Verma C, Wang Y, Tan DT, Cao D, Beuerman RW, Ren L, Liu S.
    Symmetrically Substituted Xanthone Amphiphiles Combat Gram-Positive Bacterial Resistance with Enhanced Membrane Selectivity.
    J Med Chem. 2017 Feb 13. doi: 10.1021/acs.jmedchem.6b01403.
    [Epub ahead of print] PubMed PMID: 28122182.
     
  3. Lua WH, Ling WL, Su CT, Yeo JY, Verma CS, Eisenhaber B, Eisenhaber F, Gan SK.
    Discovery of a novel splice variant of Fcar (CD89) unravels sequence segments necessary for efficient secretion: a story of bad signal peptides and good ones that nevertheless do not make it.
    Cell Cycle. 2017 Jan 19:0. doi:10.1080/15384101.2017.1281480.
    [Epub ahead of print] PubMed PMID: 28103138.
     
  4. Xu W, Lau YH, Fischer G, Tan YS, Chattopadhyay A, de la Roche M, Hyvönen M, Verma C, Spring DR, Itzhaki LS.
    Macrocyclized Extended Peptides: Inhibiting the Substrate-Recognition Domain of Tankyrase.
    J Am Chem Soc. 2017 Feb 7. doi: 10.1021/jacs.6b10234.
    [Epub ahead of print] PubMed PMID: 28084734.
     
  5. Tiwari G, Verma CS.
    Toward Understanding the Molecular Recognition of Albumin by p53-Activating Stapled Peptide ATSP-7041.
    J Phys Chem B. 2017 Feb 2;121(4):657-670. doi: 10.1021/acs.jpcb.6b09900.
    PubMed PMID: 28048940.
     
  6. Wiedmann MM, Tan YS, Wu Y, Aibara S, Xu W, Sore HF, Verma CS, Itzhaki L, Stewart M, Brenton JD, Spring DR.
    Development of Cell-Permeable, Non-Helical Constrained Peptides to Target a Key Protein-Protein Interaction in Ovarian Cancer.
    Angew Chem Int Ed Engl. 2017 Jan 9;56(2):524-529. doi: 10.1002/anie.201609427.
    PubMed PMID: 27918136; PubMed Central PMCID: PMC5291322.
     
  7. Lama D, Pradhan MR, Brown CJ, Eapen RS, Joseph TL, Kwoh CK, Lane DP, Verma CS.
    Water-Bridge Mediates Recognition of mRNA Cap in eIF4E.
    Structure. 2017 Jan 3;25(1):188-194. doi: 10.1016/j.str.2016.11.006.
    PubMed PMID: 27916520.
     
  8. Skotte NH, Sanders SS, Singaraja RR, Ehrnhoefer DE, Vaid K, Qiu X, Kannan S, Verma C, Hayden MR.
    Palmitoylation of caspase-6 by HIP14 regulates its activation.
    Cell Death Differ. 2016 Dec 2. doi: 10.1038/cdd.2016.139.
    [Epub ahead of print] PubMed PMID: 27911442.
     
  9. Siau JW, Coffill CR, Zhang WV, Tan YS, Hundt J, Lane D, Verma C, Ghadessy F.
    Functional characterization of p53 pathway components in the ancient metazoan Trichoplax adhaerens.
    Sci Rep. 2016 Sep 28;6:33972. doi: 10.1038/srep33972.
    PubMed PMID: 27678309; PubMed Central PMCID: PMC5039725.
     
  10. Nguyen MN, Sim AY, Wan Y, Madhusudhan MS, Verma C.
    Topology independent comparison of RNA 3D structures using the CLICK algorithm.
    Nucleic Acids Res. 2017 Jan 9;45(1):e5. doi: 10.1093/nar/gkw819.
    PubMed PMID: 27634929.
     
  11. Tan YS, Reeks J, Brown CJ, Thean D, Ferrer Gago FJ, Yuen TY, Goh ET, Lee XE, Jennings CE, Joseph TL, Lakshminarayanan R, Lane DP, Noble ME, Verma CS.
    Benzene Probes in Molecular Dynamics Simulations Reveal Novel Binding Sites for Ligand Design.
    J Phys Chem Lett. 2016 Sep 1;7(17):3452-7. doi: 10.1021/acs.jpclett.6b01525.
    PubMed PMID: 27532490.
     
  12. Castel P, Ellis H, Bago R, Toska E, Razavi P, Carmona FJ, Kannan S, Verma CS, Dickler M, Chandarlapaty S, Brogi E, Alessi DR, Baselga J, Scaltriti M.
    PDK1-SGK1 Signaling Sustains AKT-Independent mTORC1 Activation and Confers Resistance to PI3Ka Inhibition.
    Cancer Cell. 2016 Aug 8;30(2):229-42. doi: 10.1016/j.ccell.2016.06.004.
    PubMed PMID: 27451907; PubMed Central PMCID: PMC4982440.
     
  13. Marzinek JK, Holdbrook DA, Huber RG, Verma C, Bond PJ.
    Pushing the Envelope: Dengue Viral Membrane Coaxed into Shape by Molecular Simulations.
    Structure. 2016 Aug 2;24(8):1410-20. doi: 10.1016/j.str.2016.05.014.
    PubMed PMID: 27396828.
     
  14. Tan YS, Lane DP, Verma CS.
    Stapled peptide design: principles and roles of computation.
    Drug Discov Today. 2016 Oct;21(10):1642-1653. doi: 10.1016/j.drudis.2016.06.012. Review.
    PubMed PMID: 27326912.
     
  15. Ouaray Z, ElSawy KM, Lane DP, Essex JW, Verma C.
    Reactivation of mutant p53: Constraints on mechanism highlighted by principal component analysis of the DNA binding domain.
    Proteins. 2016 Oct;84(10):1443-61. doi: 10.1002/prot.25089.
    PubMed PMID: 27317883.
     
  16. Aronica PG, Verma C, Popovic B, Leatherbarrow RJ, Gould IR.
    The Parasol Protocol for computational mutagenesis.
    Protein Eng Des Sel. 2016 Jul;29(7):253-61. doi: 10.1093/protein/gzw009.
    PubMed PMID: 27255759.
     
  17. Lakshminarayanan R, Tan WX, Aung TT, Goh ET, Muruganantham N, Li J, Chang JY, Dikshit N, Saraswathi P, Lim RR, Kang TS, Balamuralidhar V, Sukumaran B, Verma CS, Sivaraman J, Chaurasia SS, Liu S, Beuerman RW.
    Branched Peptide, B2088, Disrupts the Supramolecular Organization of Lipopolysaccharides and Sensitizes the Gram-negative Bacteria.
    Sci Rep. 2016 May 13;6:25905. doi: 10.1038/srep25905.
    PubMed PMID: 27174567; PubMed Central PMCID: PMC4865820.
     
  18. Fox SJ, Fazil MH, Dhand C, Venkatesh M, Goh ET, Harini S, Eugene C, Lim RR, Ramakrishna S, Chaurasia SS, Beuerman RW, Verma CS, Verma NK, Loh XJ, Lakshminarayanan R.
    Insight into membrane selectivity of linear and branched polyethylenimines and their potential as biocides for advanced wound dressings.
    Acta Biomater. 2016 Jun;37:155-64. doi: 10.1016/j.actbio.2016.04.015.
    PubMed PMID: 27079762.
     
  19. Wei SJ, Chee S, Yurlova L, Lane D, Verma C, Brown C, Ghadessy F.
    Avoiding drug resistance through extended drug target interfaces: a case for stapled peptides. Oncotarget. 2016 May 31;7(22):32232-46. doi: 10.18632/oncotarget.8572.
    PubMed PMID: 27057630; PubMed Central PMCID: PMC5078010.
     
  20. Chattopadhyay A, O'Connor CJ, Zhang F, Galvagnion C, Galloway WR, Tan YS, Stokes JE, Rahman T, Verma C, Spring DR, Itzhaki LS.
    Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell.
    Sci Rep. 2016 Apr 5;6:23732. doi: 10.1038/srep23732.
    PubMed PMID: 27046077; PubMed Central PMCID: PMC4820706.
     
  21. Kannan S, Lane DP, Verma CS.
    Long range recognition and selection in IDPs : the interactions of the C-terminus of p53.
    Sci Rep. 2016 Mar 31;6:23750. doi: 10.1038/srep23750.
    PubMed PMID: 27030593; PubMed Central PMCID: PMC4814905.
     
  22. Ravi Kumar V, Verma C, Umapathy S.
    Molecular dynamics and simulations study on the vibrational and electronic solvatochromism of benzophenone.
    J Chem Phys. 2016 Feb 14;144(6):064302. doi: 10.1063/1.4941058.
    PubMed PMID: 26874483.
     
  23. Coffill CR, Lee AP, Siau JW, Chee SM, Joseph TL, Tan YS, Madhumalar A, Tay BH, Brenner S, Verma CS, Ghadessy FJ, Venkatesh B, Lane DP.
    The p53-Mdm2 interaction and the E3 ligase activity of Mdm2/Mdm4 are conserved from lampreys to humans.
    Genes Dev. 2016 Feb 1;30(3):281-92. doi: 10.1101/gad.274118.115.
    PubMed PMID: 26798135; PubMed Central PMCID: PMC4743058.
     
  24. Marzinek JK, Lakshminarayanan R, Goh E, Huber RG, Panzade S, Verma C, Bond PJ.
    Characterizing the Conformational Landscape of Flavivirus Fusion Peptides via Simulation and Experiment.
    Sci Rep. 2016 Jan 20;6:19160. doi: 10.1038/srep19160.
    PubMed PMID: 26785994; PubMed Central PMCID: PMC4726195.
     
  25. Lau YH, Wu Y, Rossmann M, Tan BX, de Andrade P, Tan YS, Verma C, McKenzie GJ, Venkitaraman AR, Hyvönen M, Spring DR.
    Double Strain-Promoted Macrocyclization for the Rapid Selection of Cell-Active Stapled Peptides.
    Angew Chem Int Ed Engl. 2015 Dec 14;54(51):15410-3. doi: 10.1002/anie.201508416.
    PubMed PMID: 26768531.
     
  26. ElSawy KM, Lane DP, Verma CS, Caves LS.
    Recognition Dynamics of p53 and MDM2: Implications for Peptide Design.
    J Phys Chem B. 2016 Jan 21;120(2):320-8. doi: 10.1021/acs.jpcb.5b11162.
    PubMed PMID: 26701330.
     
  27. Koh JJ, Zou H, Lin S, Lin H, Soh RT, Lim FH, Koh WL, Li J, Lakshminarayanan R, Verma C, Tan DT, Cao D, Beuerman RW, Liu S.
    Nonpeptidic Amphiphilic Xanthone Derivatives: Structure-Activity Relationship and Membrane-Targeting Properties.
    J Med Chem. 2016 Jan 14;59(1):171-93. doi: 10.1021/acs.jmedchem.5b01500.
    PubMed PMID: 26681070.
     
  28. Pradhan MR, Pal A, Hu Z, Kannan S, Chee Keong K, Lane DP, Verma CS.
    Wetting of nonconserved residue-backbones: A feature indicative of aggregation associated regions of proteins.
    Proteins. 2016 Feb;84(2):254-66. doi: 10.1002/prot.24976.
    PubMed PMID: 26677132.
     
  29. Tan YS, Spring DR, Abell C, Verma CS.
    The Application of Ligand-Mapping Molecular Dynamics Simulations to the Rational Design of Peptidic Modulators of Protein-Protein Interactions.
    J Chem Theory Comput. 2015 Jul 14;11(7):3199-210. doi: 10.1021/ct5010577.
    PubMed PMID: 26575757.
     
  30. Petrone L, Kumar A, Sutanto CN, Patil NJ, Kannan S, Palaniappan A, Amini S, Zappone B, Verma C, Miserez A.
    Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.
    Nat Commun. 2015 Oct 28;6:8737. doi: 10.1038/ncomms9737.
    PubMed PMID: 26508080; PubMed Central PMCID: PMC4640085.
     
  31. Ng JW, Lama D, Lukman S, Lane DP, Verma CS, Sim AY.
    R248Q mutation--Beyond p53-DNA binding.
    Proteins. 2015 Dec;83(12):2240-50. doi: 10.1002/prot.24940.
    PubMed PMID: 26442703.
     
  32. Iyengar PV, Jaynes P, Rodon L, Lama D, Law KP, Lim YP, Verma C, Seoane J, Eichhorn PJ.
    USP15 regulates SMURF2 kinetics through C-lobe mediated deubiquitination.
    Sci Rep. 2015 Oct 5;5:14733. doi: 10.1038/srep14733.
    PubMed PMID: 26435193; PubMed Central PMCID: PMC4593006.
     
  33. Lama D, Brown CJ, Lane DP, Verma CS.
    Gating by tryptophan 73 exposes a cryptic pocket at the protein-binding interface of the oncogenic eIF4E protein.
    Biochemistry. 2015 Oct 27;54(42):6535-44. doi: 10.1021/acs.biochem.5b00812.
    PubMed PMID: 26427906.
     
  34. Narayan V, Landré V, Ning J, Hernychova L, Muller P, Verma C, Walkinshaw MD, Blackburn EA, Ball KL.
    Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP).
    Mol Cell Proteomics. 2015 Nov;14(11):2973-87. doi: 10.1074/mcp.M115.051169.
    PubMed PMID: 26330542; PubMed Central PMCID: PMC4638040.
     
  35. Koh JJ, Lin H, Caroline V, Chew YS, Pang LM, Aung TT, Li J, Lakshminarayanan R, Tan DT, Verma C, Tan AL, Beuerman RW, Liu S.
    N-Lipidated Peptide Dimers: Effective Antibacterial Agents against Gram-Negative Pathogens through Lipopolysaccharide Permeabilization.
    J Med Chem. 2015 Aug 27;58(16):6533-48. doi: 10.1021/acs.jmedchem.5b00628.
    PubMed PMID: 26214729.
     
  36. Sim AY, Verma C.
    How does a hydrocarbon staple affect peptide hydrophobicity?
    J Comput Chem. 2015 Apr 15;36(10):773-84. doi: 10.1002/jcc.23859.
    PubMed PMID: 25706509.
     
  37. ElSawy KM, Sim A, Lane DP, Verma CS, Caves LS.
    A spatiotemporal characterization of the effect of p53 phosphorylation on its interaction with MDM2.
    Cell Cycle. 2015;14(2):179-88. doi: 10.4161/15384101.2014.989043.
    PubMed PMID: 25584963; PubMed Central PMCID: PMC4353223.
     
  38. Jiang Y, Tan CY, Tan SY, Wong MSF, Chen YF, Zhang L, Yao K, Gan SKE, Verma C, Tan YJ.
    SAW sensor for Influenza A virus detection enabled with efficient surface functionalization.
    Sensors and Actuators B: Chemical. 209:78-84. 2015 Nov. doi: 10.1016/j.snb.2014.11.103.
     
  39. Li J, Liu S, Koh JJ, Zou H, Lakshminarayanan R, Bai Y, Pervushin K, Zhou L, Verma C, Beuerman RW.
    A novel fragment based strategy for membrane active antimicrobials against MRSA.
    Biochim Biophys Acta. 2015 Apr;1848(4):1023-31. doi: 10.1016/j.bbamem.2015.01.001.
    PubMed PMID: 25582665.
     
  40. Ma W, Fuentes G, Shi X, Verma C, Radda GK, Han W.
    FoxO1 negatively regulates leptin-induced POMC transcription through its direct interaction with STAT3.
    Biochem J. 2015 Mar 1;466(2):291-8. doi: 10.1042/BJ20141109.
    PubMed PMID: 25510553.
     
  41. Koh JJ, Lin S, Aung TT, Lim F, Zou H, Bai Y, Li J, Lin H, Pang LM, Koh WL, Salleh SM, Lakshminarayanan R, Zhou L, Qiu S, Pervushin K, Verma C, Tan DT, Cao D, Liu S, Beuerman RW.
    Amino acid modified xanthone derivatives: novel, highly promising membrane-active antimicrobials for multidrug-resistant Gram-positive bacterial infections.
    J Med Chem. 2015 Jan 22;58(2):739-52. doi:10.1021/jm501285x.
    PubMed PMID: 25474410.
     
  42. Kannan S, Poulsen A, Yang HY, Ho M, Ang SH, Eldwin TS, Jeyaraj DA, Chennamaneni LR, Liu B, Hill J, Verma CS, Nacro K.
    Probing the binding mechanism of Mnk inhibitors by docking and molecular dynamics simulations.
    Biochemistry. 2015 Jan 13;54(1):32-46. doi: 10.1021/bi501261j.
    PubMed PMID: 25431995.
     
  43. Nguyen MN, Verma C.
    Rclick: a web server for comparison of RNA 3D structures.
    Bioinformatics. 2015 Mar 15;31(6):966-8. doi: 10.1093/bioinformatics/btu752.
    PubMed PMID: 25391398.
     
  44. Ng YZ, Kannan S, Lane DP, Fuentes G, Verma CS.
    mAb806 binding to epidermal growth factor receptor: a computational study.
    Proteins. 2015 Jan;83(1):153-68. doi: 10.1002/prot.24714.
    PubMed PMID: 25370927.
     
  45. Y. H. Lau, P. de Andrade, S.-T. Quah, M. Rossmann, L. Laraia, N. Skold, T. J. Sum, P. J. E. Rowling, T. L. Joseph, C. Verma, M. Hyvonen, L. S. Itzhaki, A. R. Venkitaraman, C. J. Brown, D. P. Lane, D. R. Spring.
    Functionalised staple linkages for modulating the cellular activity of stapled peptides.
    Chem. Sci. 2014, 5, 1804-1809.
     
  46. Lescar J, Meyer I, Akshita K, Srinivasaraghavan K, Verma C, Palous M, Mazier D, Datry A, Fekkar A.
    Aspergillus fumigatus harbouring the sole Y121F mutation shows decreased susceptibility to voriconazole but maintained susceptibility to itraconazole and posaconazole.
    J Antimicrob Chemother. 2014 Dec;69(12):3244-7.

  47. Chee SM, Wongsantichon J, Soo Tng Q, Robinson R, Joseph TL, Verma C, Lane DP, Brown CJ, Ghadessy FJ.
    Structure of a stapled peptide antagonist bound to nutlin-resistant mdm2.
    PLoS One. 2014 Aug 12;9:e104914.

  48. Nguyen PV, Verma CS, Gan SK.
    DNAApp: a mobile application for sequencing data analysis.
    Bioinformatics. 2014 Nov 15;30(22):3270-1.

  49. Sangith N, Srinivasaraghavan K, Sahu I, Desai A, Medipally S, Somavarappu AK, Verma C, Venkatraman P.
    Discovery of novel interacting partners of PSMD9, a proteasomal chaperone: Role of an Atypical and versatile PDZ-domain motif interaction and identification of putative functional modules.
    FEBS Open Bio. 2014 Jun 6;4:571-83.

  50. Tan YS, Spring DR, Abell C, Verma C.
    The use of chlorobenzene as a probe molecule in molecular dynamics simulations.
    J Chem Inf Model. 2014 Jul 28;54(7):1821-7.

  51. Lau YH, de Andrade P, Sköld N, McKenzie GJ, Venkitaraman AR, Verma C, Lane DP, Spring DR.
    Investigating peptide sequence variations for 'double-click' stapled p53 peptides.
    Org Biomol Chem. 2014 Jun 28;12(24):4074-7.

  52. Sim AYL, Joseph T, Lane DP, Verma C.
    Mechanism of stapled peptide binding to MDM2: possible consequences for peptide design.
    J Chem Theor Comput 2014, 10(4):1753-1761.

  53. Lau YH, de Andrade P, Quanh S-T, Rossmann M, Laraia L, Skold N, Sum TJ, Rowling PJE, Joseph TL, Verma C, Hyvonen M ,Itzhaki LS, Venkitaraman AR, Brown CJ, Lane DP, Spring DR.
    Functionalized staple linkages for modulating the cellular activity of stapled peptides.
    Chemical Science 2014 5:804-1809.

  54. Hoe KK, Verma CS, Lane DP.
    Drugging the p53 pathway: understanding the route to clinical efficacy.
    Nat Rev Drug Discov 13(3):217-236 (2014).

  55. Goh Wa, Lee MY, Joseph T, Quah S, Brown C, Verma C, Brenner S, Ghadessy F, Teo YN.
    Molecular rotors as conditionally fluorescent labels for rapid detection of biomolecular interactions.
    J Amer Chem Soc 2014 Apr 30;136(17):6159-62.

  56. Lakshminarayanan R, Liu S, Li J, Nandhakumar M, Aung TT, Goh E, Jamie CYT, Saraswathi P, Tang C, Safie SRB, Lin LY, Riezman H, Zhou L, Verma CS, Beuerman RW.
    Synthetic Multivalent Antifungal Peptides Effective against Fungi.
    PLoS One 9:e87730 (2014).

  57. *Lama D, Quah ST, Verma CS, Lakshminarayanan R, Beuerman RW, Lane DP, Brown C.
    Rational Optimization of Conformational Effects Induced By Hydrocarbon Staples in Peptides and their Binding Interfaces.
    Scientific Reports 3:3451 (2013).

  58. Lukman S, Lane DP, Verma CS.
    Mapping the Structural and Dynamical Features of Multiple p53 DNA Binding Domains: Insights into Loop 1 Intrinsic Dynamics.
    PLoS One 8:e80221 (2013).

  59. Wei SJ, Joseph T, Chee S, Li L, Yurlova L, Zolghadr K, Brown C, Lane D,Verma C, Ghadessy F.
    Inhibition of Nutlin-Resistant HDM2 Mutants by Stapled Peptides.
    PLoS One 8:e81068 (2013) .

  60. Elsawy KM, Verma CS, Lane DP, Caves LS.
    On the origin of the stereoselective affinity of Nutlin-3 geometrical isomers for the MDM2 protein.
    Cell Cycle 12:3727-35 (2013).

  61. Chan WT, Verma CS, Lane DP, Gan SK.
    A comparison and optimization of methods and factors affecting the transformation of Escherichia coli.
    Biosci Rep. 33:e00086 (2013).

  62. Pereira M, Verma CS, Fuentes G.
    Differences in the binding affinities of ErbB family: heterogeneity in the prediction of resistance mutants.
    PLoS One 8:e77054 (2013).

  63. Maity A, Yadav S, Verma CS, Ghosh Dastidar S.
    Dynamics of Bcl-xL in Water and Membrane: Molecular Simulations.
    PLoS One 8:e76837 (2013).

  64. Srinivasaraghavan K, Nacro K, Grüber G, Verma CS.
    Effect of Ser392 phosphorylation on the structure and dynamics of the polybasic domain of ADP ribosylation factor nucleotide site opener protein: a molecular simulation study.
    Biochemistry 52:7339-49 (2013).

  65. Hernychova L, Man P, Verma C, Nicholson J, Sharma CA, Ruckova E, Teo JY, Ball K, Vojtesek B, Hupp TR.
    Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry.
    Proteomics 13:2512-2525 (2013) .

  66. Wei SJ, Joseph T, Sim A, Yurlova L, Zolghadr K, Lane D, Verma C, Ghadessy F.
    In vitro selection of mutant HDM2 resistant to nutlin inhibition.
    PLos One 8:e62564 (2013) .

  67. Zou H, Koh JJ, Li J, Qiu S, Aung TT, Lin H, Lakshminarayanan R, Dai X, Tang C, Lim FH, Zhou L, Tan AL, Verma C, Tan DT, Chan HS, Saraswathi P, Cao D, Liu S, Beuerman RW.
    Design and synthesis of amphiphilic xanthone-based, membrane-targeting antimicrobials with improved membrane selectivity.
    J Med Chem 56:2359-73 (2013).

  68. ElSawy KM, Verma CS, Joseph TL, Lane DP, Twarock R, Caves LS.
    On the interaction mechanisms of a p53 peptide and nutlin with the MDM2 and MDMX proteins: a Brownian dynamics study.
    Cell Cycle. 12:394-404 (2013).

  69. Li J, Liu S, Lakshminarayanan R, Bai Y, Pervushin K, Verma C, Beuerman RW.
    Molecular simulations suggest how a branched antimicrobial peptide perturbs a bacterial membrane and enhances permeability.
    Biochim Biophys Acta. 1828:1112-21. (2013).

  70. Kreisberg JF, Ong NT, Krishna A, Joseph TL, Wang J, Ong C, Ooi HA, Sung JC, Siew CC, Chang GC, Biot F, Cuccui J, Wren BW, Chan J, Sivalingam SP, Zhang LH, Verma C, Tan P.
    Growth inhibition of pathogenic bacteria by sulfonylurea herbicides.
    Antimicrob Agents Chemother 57:1513-7. (2013).

  71. Brown CJ, Quah ST, Jong J, Goh AM, Chiam PC, Khoo KH, Choong ML, Lee MA, Yurlova L, Zolghadr K, Joseph TL, Verma CS, Lane DP.
    Stapled peptides with improved potency and specificity that activate p53.
    ACS Chem Biol 8:506-12 (2013).

  72. Koh JJ, Qiu S, Zou H, Lakshminarayanan R, Li J, Zhou X, Tang C, Saraswathi P, Verma C, Tan DT, Tan AL, Liu S, Beuerman RW.
    Rapid bactericidal action of alpha-mangostin against MRSA as an outcome of membrane targeting.
    Biochim Biophys Acta 1828:834-44 (2013).

  73. Li J, Lakshminarayanan R, Bai Y, Liu S, Zhou L, Pervushin K, Verma C, Beuerman RW.
    Molecular dynamics simulations of a new branched antimicrobial peptide: a comparison of force fields.
    J Chem Phys. 137:215101 (2012).

  74. Vinekar R, Verma C, Ghosh I.
    Functional relevance of dynamic properties of Dimeric NADP-dependent Isocitrate Dehydrogenases.
    BMC Bioinformatics 13 Suppl 17:S2 (2012).

  75. Joseph TL, Lane DP, Verma CS.
    Stapled BH3 peptides against MCL-1: mechanism and design using atomistic simulations.
    PLoS One 7:e43985 (2012).

  76. Zhou W, Quah ST, Verma CS, Liu Y, Lane DP, Brown CJ.
    Improved eIF4E binding peptides by phage display guided design: plasticity of interacting surfaces yield collective effects.
    PLoS One 7:e47235 (2012).

  77. Zhou W, Motakis E, Fuentes G, Verma CS.
    Macrostate identification from biomolecular simulations through time series analysis.
    J Chem Inf Model 52:2319-24 (2012).

  78. Lane DP, Verma C.
    Mdm2 in evolution.
    Genes & Cancer 3:320-4 (2012).

  79. Funston G, Goh W, Wei SJ, Tng QS, Brown C, Jiah Tong L, Verma C, Lane D, Ghadessy F.
    Binding of Translationally Controlled Tumour Protein to the N-Terminal Domain of HDM2 Is Inhibited by Nutlin-3.
    PLoS One. 2012;7(8):e42642.

  80. Bai Y, Liu S, Li J, Lakshminarayanan R, Sarawathi P, Tang C, Ho D, Verma C, Beuerman RW, Pervushin K.
    Progressive structuring of a branched antimicrobial Peptide on the path to the inner membrane target.
    J Biol Chem. 287:26606-17 (2012).

  81. Dastidar SG, Lane DP, Verma CS.
    Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding.
    Cell Cycle 11:2239-47 (2012).

  82. Fernandez-Recio J, Verma C.
    Theory and simulation: complexity and emergence.
    Curr Opin Struct Biol. 22:127-9 (2012).

  83. Sonkaria S, Fuentes G, Verma C, Narang R, Khare V, Fischer A, Faivre D.
    Insight into the Assembly Properties and Functional Organisation of the Magnetotactic Bacterial Actin-like Homolog, MamK.
    PLos One 7(5):e34189. (2012).

  84. ElSawy K, Twarock R, Verma C, Caves, L.
    Peptide inhibitors of viral assembly: a novel route to broad-spectrum antivirals.
    J Chem Inf Mod 52:770-6 (2012).

  85. Raghunathan D, Gayen S, Kumar A, Hunke C, Grüber G, Verma CS.
    Subunit F modulates ATP binding and migration in the nucleotide-binding subunit B of the A(1)A (O) ATP synthase of Methanosarcina mazei Gö1.
    J Bioenerg Biomembr. 44:213-24 (2012) .

  86. ElSawy K, Twarock R, Lane D, Verma C, Caves L.
    Characterisation of the ligand receptor encounter complex and its potential for in silico kinetics based drug development.
    Jl Chem Theor Comput 8:314-321(2012).

  87. Namboodiri S, Verma C, Dhar PK, Giuliani A, Nair AS.
    Sequence signatures of allosteric proteins towards rational design.
    Syst Synth Biol. 4:271-80 (2010).

  88. Lukman S, Robinson, R, Wales D, Verma C.
    Conformational dynamics of capping protein and interaction partners: simulation studies.
    Proteins: Str Fn Bioinf 80:1066-1077 (2012).

  89. Lane DP, Madhumalar A, Lee A, Tay B-H, Verma C, Brenner S, Venkatesh B.
    Conservation of all three p53 family members and Mdm2 and Mdm4 in the cartilaginous fish.
    Cell Cycle 10:4272-4279 (2011).

  90. Hussain S, Khan A, Gul S, Resmini M, Verma CS, Thomas EW, Brocklehurst K.
    Identification of interactions involved in the generation of nucleophilic reactivity and of catalytic competence in the catalytic site Cys/His ion pair of papain.
    Biochemistry. 50:10732-42 (2011).

  91. Dastidar SG, Brown CJ, Quah ST, Lim HA, Chia CSB, Verma CS.
    C-terminal substitution of MDM2 interacting peptides modulates binding affinity by distinctive mechanisms.
    Plos One 6:e24122 (2011).

  92. Lane D, Brown CJ, Verma C, ChitFang C.
    New insights into p53 based therapy.
    Discovery Medicine 12:107-111 (2011).

  93. Liu Y, Lane D, Verma C.
    Systematic mutational analysis of an MDM2 binding peptide: computational studies.
    Theoret Chem Acc 130: 1145 (2011).

  94. Fuentes G, Scaltriti M, Baselga J, Verma CS..
    Synergy between trastuzumab and pertuzumab for Her2 from colocalization: an in silico based mechanism.
    Breast Cancer Research 13:R54 (2011).

  95. Tan YS, Fuentes G, Verma C.
    A comparison of the dynamics of pantothenate synthetase from M. tuberculosis and E. coli: Computational studies.
    Proteins 79: 1715-1727 (2011) .

  96. Goudie DR, D'Alessandro M, Merriman B, Lee H, Szeverényi I, Avery S, O'Connor BD, Nelson SF, Coats SE, Stewart A, Christie L, Pichert G, Friedel J, Hayes I, Burrows N, Whittaker S, Gerdes AM, Broesby-Olsen S, Ferguson-Smith MA, Verma C, Lunny DP, Reversade B, Lane EB. Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1.
    Nat Genetics 43:365-369 (2011).

  97. Dastidar SG, Raghunathan D, Nicholson J, Hupp TR, Lane DP, Verma CS.
    Chemical states of the N-terminal "lid" of MDM2 regulate p53 binding: simulations reveal complexities of modulation.
    Cell Cycle 10:82-9 (2011).

  98. Cheok CF, Verma CS, Baselga J, Lane DP.
    Translating p53 into the clinic.
    Nat Rev Clinic Oncol 8:25-37 (2011).

  99. Brown CJ, Fang CC, Verma C, Lane DP.
    Reactivation of p53: from small molecules to peptides.
    Trends in Pharmac Sciences 32:53-62 (2011).

  100. Fuentes G, Dastidar SG, Madhumalar A, Verma CS.
    The role of protein flexibility in the discovery of new drugs.
    Drug Development Research 72:26-35 (2011).

  101. L Zhou, SP Liu, LY Chen, J Li, LB Ong, L Guo, T Wohland, CC Tang, R Lakshminarayanan, J Mavinahalli, C Verma, RW Beuerman.
    The structural parameters for antimicrobial activity, human epithelial cell cytotoxicity and killing mechanism of synthetic monomer and dimer analogues derived from hBD3 C-terminal region.
    Amino Acids (40:123-133 (2011).

  102. Pennell S, Westcott S, Ortiz-Lombardía M, Patel D, Li J, Nott TJ, Mohammed D, Buxton RS, Yaffe MB, Verma C, Smerdon SJ.
    Structural and functional analysis of phosphothreonine-dependent FHA domain interactions.
    Structure 18:1587-95 (2010).

  103. Brown CJ, Lim JJ, Joseph TL, Chia CSB, Verma CS, Lane DP.
    Stabilizing the eIF4G1 a-helix increases its binding affinity with eIF4E: implications for peptidomimetic design strategies.
    J Mol Biol 405:736-753 (2010).

  104. Joseph TL, Lane D, Verma CS.
    Stapled peptides in the p53 pathway: computer simulations reveal novel interactions of the staples with the target protein.
    Cell Cycle 9:4560-4568 (2010).

  105. Lane DP, Verma C, Fang CC.
    The p53 inducing drug dosage may determine quiescence or senescence.
    Aging 2:748 2010).

  106. Fraser JA, Madhumalar A, Blackwell E, Bramham J, Walkinshaw MD, Verma C, Hupp TR.
    A Novel p53 phosphorylation site within the MDM2 ubiquitination signal. II. A model in which phosphorylation at Ser269 induces a mutant conformation to p53.
    J Biol Chem 285:37773-37786 (2010).

  107. Y-W Ng, P Chan, D Raghunathan, DJ Smith, C H Lee, C Verma, E Manser.
    Why an A-loop phospho-mimetic fails to activate PAK1: understanding an inaccessible kinase state by molecular dynamics simulations.
    Structure 18:879-890 (2010).

  108. D Raghunathan, S Gayen, G Gruber, CS Verma.
    Crosstalk along the stalk: dynamics of the interaction of subunits B and F in the A(1)A(0)ATP synthase of Methanosarcina mazei Go1.
    Biochemistry 49:4181-4190 (2010).

  109. J Fernandez-Recio, C Verma.
    Theory and simulation: integrating models into experimental scenarios.
    Current Opin Struct Biol 20:139-141 (2010) .

  110. A Dey, DP Lane, CS Verma.
    Modulating the p53 pathway.
    Semin Cancer Biol 20:3-9 (2010) .

  111. TL Joseph, A Madhumalar, CJ Brown, DP Lane, C Verma.
    Differential binding of p53 and nutlin to MDM2 and MDMX: computational studies.
    Cell Cycle 9:1167-1181 (2010).

  112. DP Lane, CF Cheok, C Brown, A Madhumalar, FJ Ghadessy, C Verma.
    The Mdm2 and p53 genes are conserved in the Arachnids.
    Cell Cycle 9:748-754 (2010).

  113. DP Lane, CF Cheok, C Brown, A Madhumalar, FJ Ghadessy, C Verma.
    MDM2 and p53 are highly conserved from placozoans to man.
    Cell Cycle 9:54-547 (2010).

  114. CJ Brown, SG Dastidar, HY See, DW Coomber, M Ortiz-Lombardia, C Verma, DP Lane.
    Rational design and biophysical characterization of thioredoxi-based aptamers: insights into peptide grafting.
    J Mol Biol 395:871-873 (2010).

  115. MN Jagadeesh, A Madhumalar, RW Beuerman, DP Lane, CS Verma.
    Differences in the transactivation domains of p53 family members: a computational study.
    BMC Genomics Suppl 1:S5 (2010) .

  116. SG Dastidar, A Madhumalar, G Fuentes, DP Lane, CS Verma.
    Forces mediating protein--protein interactions: a computational study of p53 ''approaching'' MDM2.
    Theoretical Chemistry Accounts 125:621-635 (2010).

  117. CJ Brown, S Lain, CS Verma. AR Fersht, DP Lane.
    Awakening guardian angels: drugging the p53 pathway.
    Nat Rev Cancer 9:862-873 (2009) (invited).

  118. SG Dastidar, DP Lane, CS Verma.
    Modulation of p53 binding to MDM2: computational studies reveal important roles of Tyr100.
    BMC Bioinformatics 15:S6 (2009).

  119. A Madhumalar, HJ Lee, CJ Brown, DP Lane, CS Verma.
    Design of a novel MDM2 binding peptide based on the p53 family.
    Cell Cycle 8:2828-36 (2009).

  120. Y Bai, S Liu, P Jiang, L Zhou, J Li, C Tang, C Verma, Y Mu, RW Beuerman, K Pervushin.
    Structure-dependent charge density as a determinant oof antimicrobial activity of peptide analogues of defensin.
    Biochemistry 48:7229-7239 (2009).

  121. A Madhumalar, HJ Lee, DP Lane, CS Verma.
    Dimerization of the core domain of the p53 family: a computational study.
    Cell Cycle 8:137-148 (2009).

  122. M.Scaltriti, C Verma, M Guzman, J Jimenez, D J Smith, S Landolfi, S Ramon y Cajal, J Arribas, J Baselga.
    Lapatinib induces HER2 stabilization and enhances the antitumour activity of trastuzumab in vivo.
    Oncogene 28:803-814 (2009).

  123. CJ Brown, CS Verma, MD Walkinshaw, DP Lane.
    Crystallization of eIF4E complexed with eIF4G peptide and glycerol reveals distinct structural differences around the cap-binding site.
    Cell Cycle 8:1905-1911 (2009).

  124. S Liu, L Zhou, L Chen, S G Dastidar, C Verma, J Li, D Tan, R Beuerman.
    Effect of Structural Parameters of Peptides on Dimer Formation and Highly Oxidized Side Products in the Oxidation of Thiols of Linear Analogs of Human b-Defensin 3 by Dimethyl Sulfoxide.
    Jl Peptide Science 15:95-106 (2009).

  125. S G Dastidar, D P Lane, C S Verma.
    Multiple peptide conformations give rise to similar binding affinities: molecular simulations of p53-MDM2.
    J Am Chem Soc 130:1351-13515 (2008) .

  126. W G Lim, X Chen, J-P Liu, B J Tan, S Zhou, A Smith, N Lees, L Hou, F Gu, X Y Yu, Y Du, D Smith, C Verma, K Liu, W Duan.
    The C-terminus of PRK2/PKNg is required for optimal activation by RhoA in a GTP-dependent manner.
    Arch Biochem Biophys 479:170-178 (2008).

  127. J. Fernando-Recio, C Verma.
    Theory and simulation. Editorial overview.
    Curr Opin Struct Biol 18:131-133 (2008) (invited to edit volume).

  128. Nigham A, Tucker-Kellogg L, Mihalek I, Verma C, Hsu D.
    pFlexAna: detecting conformational changes in remotely related proteins.
    Nucleic Acids Res. 36:W246-251 (2008).

  129. G G Dodson, D P Lane, C Verma.
    Molecular simulations of protein dynamics: new windows on mechanisms in biology.
    EMBO Reports 9:144-150 (2008).

  130. C J Brown, D Srinivasan, L H Jun, D Coomber, C S Verma, D P Lane.
    The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides.
    Cell Cycle (2008).

  131. A Dey, C S Verma, D P Lane.
    Update on p53: modulation of p53 degradation as a therapeutic approach.
    British J Cancer 98:4-8 (2008).

  132. S Gul, M P. Thomas, S Hussain, C S Verma, E W Thomas, K Brocklehurst.
    Investigation of interactions within the active centre of papain using cationic reactivity probes designed to bind to Asp158 and react with the thiolate anion component of the (Cys25)–S–/(His159)–Im+H ion-pair.
    Biochemistry 47:2025-2035 (2008).

  133. S Liu, L Zhou, J Li, A. Suresh, C.S. Verma, Y H Foo, E.Yap, D. Tan and R.W. Beuerman.
    De Novo Linear Analogs of Human b-Defensin 3: Concept for Design of Antibacterial Peptides with Reduced Cytotoxicity to Mammalian Cells.
    ChemBioChem (2008).

  134. A Madhumular, D J smith, C Verma.
    Stability of the core domain of p53: insights from computer simulations.
    BMC Bioinformatics (2008) 9(Suppl 1):S17.

  135. H J Lee, D Srinivasan, D Coomber, D P Lane, C S Verma.
    Modulation of the p53-MDM2 interaction by phosphorylation of Thr18: a computational study.
    Cell Cycle 6:2604-11 (2007).

  136. C Verma, S Seebah, L Soo Mei, Z Lei, L Shou Ping, L Jing, R Beuerman.
    Defensins: Antimicrobial peptides for therapeutic development.
    Bitoechn J 2:1353-9 (2007).

  137. H J Lee, G H Chua, A Krishnan, D. P. Lane. C. S. Verma.
    Substrate specificity of Cyclins determined by electrostatics.
    Cell Cycle 6:2219-26 (2007).

  138. K H Kiat, H J Lee, B Veeravalli, C Verma.
    Wavelet analysis of protein dynamics.
    Lecture Notes in Bioinformatics (2007).

  139. G. Fuentes, A. Ballesteros, C S Verma.
    Enthalpic and entropic contributions in the transesterification of sucrose: computational study of lipases and subtilisin.
    J Biomol Str Dyn 25:145-55 (2007).

  140. C. L. Hill, C. H. Lee, D. J. Smith, C. S. Verma, G. Grogan.
    On the resolution of chiral substrates by a retro-Claisenase enzyme. Biotransformations of heteroannular bicylcic b-diketones by 6-oxo camphor hydrolase.
    Adv Synth Catal 349:1353-60 (2007).

  141. C. L. Hill, C. S. Verma, Gideon Grogan.
    Desymmetrisations of 1-alkylbicyclo[3.3.0]octane-2,8-diones by enzymatic retro-Claisen reaction yield optically enriched 2,3-substituted cyclopentanones.
    Adv Synth Catal 349:916-24 (2007).

  142. S Somani, C. P Chng, C. S. Verma.
    Hydration of hydrophobic moieties: A simulation study of interleukin-1beta.
    Proteins: Str Fn Gen 67:868 (2007).

  143. S. Seebah, A. Suresh, R. Beuerman, C. S. Verma.
    Defensins Knowledgebase: A manually curated database and information source focused on the defensins family of antimicrobial peptides.
    Nucleic Acids Res 35: D265 (2007).

  144. A Suresh, C Verma.
    Oligomerization in defensins: a modelling study across mammals.
    BMC Bioinformatics 7:S17 (2006) .

  145. M. Ortiz-Lombardia, C S Verma.
    Proteins as data storage devices: insights from computer models.
    J Phys: Conf Ser 34 7-14 (2006).

  146. W. G. Lim, B. J. Tan, Y Zhu, S. Zhou, J. S. Armstrong, Q. T. Li, Q. Dong, E. Chan, D. Smith, C. Verma, S-L Tan & W. Duan.
    The very C-terminus of PRK1/PRK is essential for its activation by RhoA and downstream signalling.
    Cellular Signalling 18:1473-1481 (2006).

  147. Leonard PM, Brzozowski AM, Lebedev A, Marshall CM, Smith, DJ, Verma, CS, Walton, NJ and Grogan G.
    The 1.8 Ĺ resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin.
    Acta Cryst. Sect D D62, 1494-1501 (2006) .

  148. S. S. Yeong, Y. Zhu, D. Smith, C. Verma, W. G. Lim, B. J. Tan, J. A. Armstrong, S. Zhou, S-L Tan, N.S. Cheung & W. Duan.
    The last ten amino acid residues beyond the hydrophobic motif are critical for the catalytic competence and function of protein kinase Ca.
    J. Biol. Chem 281:30768-30781 (2006).

  149. M Witkowska-Zimny; M M Hryniewicz; P Neumann; A J. Wilkinson; A M. Brzozowski; C S. Verma; J Zaim; G D. Bujacz.
    Structural Basis of the Sulfate Starvation Response in E. coli: Crystal Structure and Mutational Analysis of the Cofactor-Binding Domain of the Cbl Transcriptional Regulator E Stec.
    J Mol Biol 364:309-322 (2006).

  150. S. Vijayakrishnan, R. Qaamra, C. S. Verma, R. Sen & S. Mande.
    Molecular Dynamics Simulations of the M. tuberculosis chaperonin-10: the role of metal ions.
    J Biomol Str Dyn 23:365-375 (2006).

  151. Y. Zhu, D. Smith, C. Verma, W. G. Lim, B. J. Tan, J. S. Armstrong, S. Zhou, E. Chan, S-L Tan, Y-Z Zhu, N. S. Cheung & W. Duan.
    The very C-terminus of protein kinase C? is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependant kinase-1.
    Cellular Signalling 18:807-818 (2006).

  152. G G Dodson & C S Verma.
    Protein flexibility: role in structure and mechanism revealed by molecular simulations.
    Cell Mol Life Sci 63:207-219 (2006) .

  153. C. S. Allardyce, P. J. Dyson, C. S. Verma, J. Coffey & N. Johnson.
    Characterisation of the transferrin cisplatin-binding site using mass spectrometry and molecular modelling.
    ChemBioChem 6 1788-1795 (2005).

  154. M. Akif, K. Suhre, C. Verma, S.C. Mande.
    Conformational flexibility of M. tuberculosis Thiredoxin reductase: crystal structure and normal mode analysis.
    Acta Cryst Sect D D61:1603-1611 (2005).

  155. V. Renugopalakrishnan, M Ortiz-Lombardia, C Verma.
    Electrostatics of cytochrome-c assemblies.
    J Mol Model.11 :265-270 (2005).

  156. V Renugopalakrishnan, R Garduno-Juarez, G Narasimhan, C S Verma, X Wei and P Li.
    Rational design of thermally stable proteins: relevance to bionanotechnology (Review).
    Jl Nanosci Nanotech 5 1759-1767 (2005).

  157. A. De Simone, G. G. Dodson, C. S. Verma, A. Zagari, F. Fratarnali.
    Prion dry spots and water hot spots: key roles for structural stability.
    Proc Natl Acad Sci USA 102:7535-7540 (2005).

  158. K R Sakharkar, M K Sakharkar, C Verma, V T K Chow.
    Comparative study of overlapping genes in bacteria, with special reference to Rickettsia prowazekii and Rickettsia conorii.
    Int J Syst Evol Microbiol. 55 1205-9 (2005).

  159. C S Verma & S Fischer.
    Protein stability & ligand binding: new paradigms from in-silico experiments.
    Biophys Chem 115 295-302 (2005).

  160. A. Kumar, P. C. Mishra, M. Durai, C. S. Verma and V. Renugopalakrishnan.
    A Density Functional Study of the Heme Moiety of Cytochrome c.
    Int J Quant Chem 102 1002-1009 (2005).

  161. G. L. Fuentes, A. R. Ballesteros & C. S. Verma.
    Dynamic control of specificity in enzymes: computational study of transesterification of sucrose using lipases.
    Protein Science 13 3092-3103 (2004).

  162. R. B. Greaves, G. G. Dodson, C. S. Verma.
    Altered ionisation of the B13-Glu in insulin mutants: a computational analysis.
    Protein Eng. Des. Sel. 17 557 – 563 (2004).

  163. H. J. Dubbink, R. Hersmus, M. van Royen, C. S. Verma, J. van Tol, A. C. J. Ziel-van der Made, A. O. Brinkmann, A. B. Houtsmuller, A. C.W. Pike, J. Trapman.
    Distinct modes of recognition of FXXLF and LXXLL motifs by the androgen receptor.
    Molecular Endocrinology 18 2132-2150 (2004).

  164. J.L.Whittingham, I. Jonassen, S. Havelund, S. M. Roberts, E. J. Dodson, C. S. Verma and G. G. Dodson.
    Crystallographic analysis and solution studies of N-lithocholyl insulin: a new generation of prolonged-acting insulins.
    Biochemistry 43 5987-5995 (2004).

  165. M. Prabhakaran, S. H. Gursahani, C. S. Verma, R. Garduno- Juarez, and V. Renugopalakrishnan.
    Cytochrome C: The effect of temperature and pressure from molecular dynamics simulations.
    J. Phys. Chem. Solids 65 1615-1622 (2004).

  166. L. F. Haire, S. M. Whyte, N. Vashisht, A. C. Gill, C. Verma, E. J. Dodson, G. G. Dodson and P. M. Bayley.
    The crystal strucure of a truncated sheep prion protein.
    J. Mol. Biol 336 1175-1183 (2004).

(for full list please see http://web.bii.a-star.edu.sg/~chandra/allpubs)

 

Please contact us by email if you wish a reprint from any of the selected publications.
 
Feedback Login Site Map