Publications

163. Avershina E, Sharma P, Taxt AM, Singh H, Frye SA, Paul K, Kapil A, Naseer U, Kaur P, Ahmad R (2021) AMR-Diag: Neural network based genotype-to-phenotype prediction of resistance towards β-lactams in Escherichia coli and Klebsiella pneumoniae. Comp. Struct.Biotech. J. 19,1896-1906, doi:10.1016/j.csbj.2021.03.027.

162. Gupta D, Tiwari P, Haque MA, Sachdeva E, Hassan MI, Ethayathulla AS, Kaur P. (2021) Structural insights into the transient closed conformation and pH dependent ATPase activity of S.Typhi Gyrase B N- terminal domain. Arch Biochem Biophys. Apr 15;701:108786. doi: 10.1016/j.abb.2021.108786.

161. Gupta D, Sharma P, Singh M, Kumar M, Ethayathulla AS, Kaur P. (2021) Structural and functional insights into the spike protein mutations of emerging SARS-CoV-2 variants. Cell Mol Life Sci. 78:7967-7989. doi: 10.1007/s00018-021-04008-0. (Review)

160. Tripathi MK, Nath A, Singh TP, Ethayathulla AS, Kaur P (2021) Evolving scenario of big data and Artificial Intelligence (AI) in drug discovery Mol Divers 25(3):1439-1460. doi: 10.1007/s11030-021-10256-w.

159. Katiyar A, Kaur G, Rani L, Jena L, Singh H, Kumar L, Sharma A, Kaur P*, Gupta R*. (2021) Genome-wide identification of potential biomarkers in multiple myeloma using meta-analysis of mRNA and miRNA expression data. Sci Rep. 11(1):10957. doi: 10.1038/s41598-021-90424-y. (Co-Corresponding authors)

158. Singh PK, Pandey S, Rani C, Ahmad N, Viswanathan V, Sharma P, Kaur P, Sharma S, Singh TP (2021) Potassium-induced partial inhibition of lactoperoxidase: structure of the complex of lactoperoxidase with potassium ion at 2.20 Å resolution. J Biol Inorg Chem. 26(1):149-159. doi: 10.1007/s00775-020-01844-6.

157. Singh PK, Sharma P, Bhushan A, Kaur P, Sharma S, Singh TP. (2021) Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. J Inorg Biochem. 220:111461. doi: 10.1016/j.jinorgbio.2021.111461.

156. Gupta A, Vijayan V, Pant P., Kaur P, Singh, TP, Sharma P, Sharma S (2021) Structure prediction and discovery of inhibitors against phosphopanthothenoyl cysteine synthetase of Acinetobacter baumannii. J. Biomol Struct Dyn Aug 4:1-13.

155. Singh M, Malhotra L, Haque MA, Kumar M, Tikhomirov A, Litvinova V, Korolev AM, Ethayathulla AS, Das U, Shchekotikhin AE, Kaur P. (2021) Heteroarene-fused anthraquinone derivatives as potential modulators for human aurora kinase B. Biochimie. 182:152-165. doi: 10.1016/j.biochi.2020.12.024.

154. Malhotra L, Goyal HKV, Jhuria S, Dev K, Kumar S, Kumar M, Kaur P, Ethayathulla AS. (2021) Curcumin rescue p53Y220C in BxPC-3 pancreatic adenocarcinomas cell line: Evidence-based on computational, biophysical, and in vivo studies. Biochim Biophys Acta Gen Subj. 1865:129807. doi: 10.1016/j.bbagen.2020.129807.

153. Gupta A, Singh PK, Sharma P, Kaur P, Sharma S, Singh TP. (2020) Structural and biochemical studies of phosphopantetheine adenylyltransferase from Acinetobacter baumannii with dephospho-coenzyme A and coenzyme A. Int J Biol Macromol. 142:181-190. doi: 10.1016/j.ijbiomac.2019.09.090.

152. Gupta A, Rani C, Pant P, Vijayan V, Vikram N, Kaur P, Singh TP, Sharma S, Sharma P. (2020) Structure-Based Virtual Screening and Biochemical Validation to Discover a Potential Inhibitor of the SARS-CoV-2 Main Protease.ACS Omega. 5:33151-33161. doi: 10.1021/acsomega.0c04808.

151. Naz F, Mashkoor M, Sharma P, Haque MA, Kapil A, Kumar M, Kaur P, Abdul Samath E.(2020) Drug repurposing approach to target FtsZ cell division protein from Salmonella Typhi. Int J Biol Macromol. 159:1073-1083. doi: 10.1016/j.ijbiomac.2020.05.063.

150. Sachdeva, E., Kaur, G., Tiwari, P., Gupta, D, Singh TP, Ethayathulla, AS, Kaur P. (2020). The pivot point arginines identified in the β-pinwheel structure of C-terminal domain from Salmonella Typhi DNA Gyrase A subunit. Sci Rep 10, 7817 https://doi.org/10.1038/s41598-020-64792-w

149. Tripathi MK, Singh P, Sharma S, Singh TP, Ethayathulla AS, Kaur P (2020) Identification of bioactive molecule from Withania somnifera (Ashwagandha) as SARS-CoV-2 main protease inhibitor J. Biomol Struc. Dyn. doi.org/10.1080/07391102.2020.1790425

148. Vijayan V, Pant , Vikram N, Kaur P, Singh TP, Sharma S, Sharma P. (2020) Identification of promising drug candidates against NSP16 of SARS-CoV-2 through computational drug repurposing study. J. Biomol Struc. Dyn. doi.org/10.1080/07391102.2020.1802349

147. Katiyar A, Sharma P, Dahiya S, Singh H, Kapil A, Kaur P (2020) Genomic profiling of antimicrobial resistance genes in clinical isolates of Salmonella Typhi from patients infected with Typhoid fever in India. Sci. Rep. 10:8299. doi: 10.1038/s41598-020-64934-0.

146. Bansal R Haque MA, Hassan MI, Ethayathulla AS, Kaur P. (2020) Structural and conformational behavior of MurE ligase from Salmonella enterica serovar Typhi at different temperature and pH conditions Int J Biol Macromol. 150:389-399. doi: 10.1016/j.ijbiomac.2020.01.306

145. Sharma P, Vijayan V , Pant P, Sharma M, Vikram N, Kaur P, Singh TP, Sharma S (2020) Identification of potential drug candidates to combat COVID-19: a structural study using the main protease (mpro) of SARS-CoV-2 J. Biomol Struc. Dyn. doi.org/10.1080/07391102.2020.1798286

144. Tiwari A, Kumar M, Kaur P, Kumar B, Sarada SK Sagi (2020) Efficacy of Quercetin as a potent sensitizer of β2 AR in combating the impairment of fluid clearance in lungs of rats under hypoxia. Respiratory Physiology & Neurobiology 273: 103334

143. Verma D, Gupta S, Saxena R, Kaur P, Srivastava S, Gupta V. (2020) Allosteric inhibition and kinetic characterization of Klebsiella pneumoniae CysE: An emerging drug target. Int J Biol Macromol. 151:1240‐1249. doi:10.1016/j.ijbiomac.2019.10.170

142. Kumar A, Jain V, Chowdhury MR, Kumar M, Kaur P, Kabra M. (2020) Pathogenic/likely pathogenic variants in the SHOX, GHR and IGFALS genes among Indian children with idiopathic short stature. J Pediatr Endocrinol Metab 33:79-88. doi: 10.1515/jpem-2019-0234.

141. Sudarshan S, Kumar M, Kaur P, Kumar A, Sethuraman G, Sapra S, Gulati S, Gupta N, Kabra M, Chowdhury MR (2019) Decoding of novel missense TSC2 gene variants using in-silico methods. BMC Med Genet. 20, 164

140. Mishra S, Rastogi YP, Jabin S, Kaur P, Amir M, Khatoon S. (2019) A bacterial phyla dataset for protein function prediction. Data Brief. 28, 105002

139. Mishra S, Rastogi YP, Jabin S, Kaur P, Amir M, Khatoon S. (2019) A deep learning ensemble for function prediction of hypothetical proteins from pathogenic bacterial species. Comput Biol Chem. 83, 107147

138. Pandey G, Bakhshi S, Kumar M, Thakur B, Jain P, Kaur P, Chauhan SS. (2019) Prognostic and therapeutic relevance of cathepsin B in pediatric acute myeloid leukemia. Am J Cancer Res 9 2634-2649

137. Yadav P, Kumar M, Bansal R, Kaur P, Ethayathulla AS (2019) Structure model of ferrochelatase from Salmonella Typhi elucidating metalation mechanism. Int.J. Biol. Macromol. 127: 585-593

136. Kumar A, Jain V, Chowdhury MR, Kumar M, Kaur P, Kabra M. (2019) Pathogenic/likely pathogenic variants in the SHOX, GHR and IGFALS genes among Indian children with idiopathic short stature. J Pediatr Endocrinol Metab. 33, 79-88

135. Katiyar A, Sharma S, Singh TP and Kaur P (2018) Identification of Shared Molecular Signatures Indicate the Susceptibility of Endometriosis to Multiple Sclerosis. Front. Genet. 9:42.

134. Chaudhary A, Kumar V, Singh PK, Sharma P, Bairagya HR, Kaur P, Sharma S, Chauhan SS, Singh TP. (2018) A glycoprotein from mammary gland secreted during involution promotes apoptosis: Structural and biological studies. Arch Biochem Biophys. 644:72-80.

133. Tikhomirov AS, Lin CY, Volodina YL, Dezhenkova LG, Tatarskiy VV, Schols D, Shtil AA, Kaur P, Chueh PJ, Shchekotikhin AE. (2018) New antitumor anthra[2,3-b]furan-3-carboxamides: Synthesis and structure-activity relationship. Eur J Med Chem. 148:128-139.

132. Kaushik S, Iqbal N, Singh N, Sikarwar JS, Singh PK, Sharma P, Kaur P, Sharma S, Owais M, Singh TP. (2018) Search of multiple hot spots on the surface of peptidyl-tRNA hydrolase: structural, binding and antibacterial studies. Biochem J. 475:547-560.

131. Bansal R Haque MA, Yadav P Gupta D, Ethayathulla AS, Hassan MI, Kaur P. (2018) Estimation of structure and stability of MurE ligase from Salmonella enterica serovar Typhi. Int J Biol Macromol. 109:375-382.

130. Singh PK, Iqbal N, Sirohi HV, Bairagya HR, Kaur P, Sharma S, Singh TP. (2018) Structural basis of activation of mammalian heme peroxidases. Prog Biophys Mol Biol. 133:49-55.

129. Yadav SP, Singh PK, Sharma P, Iqbal N, Kaur P, Sharma S, Singh TP. (2017) Structure and binding studies of proliferating cell nuclear antigen from Leishmania donovani Biochim Biophys Acta. 186:1395-1405. d

128. Gupta N, Tewari VV, Kumar M, Langeh N, Gupta A, Mishra P, Kaur P, Ramprasad V, Murugan S, Kumar R, Jana M, Kabra M. (2017) Asparagine Synthetase deficiency-report of a novel mutation and review of literature. Metab Brain Dis. 2017 Aug 3. doi: 10.1007/s11011-017-0073-6. [Epub ahead of print]

127. Sirohi HV, Singh PK, Iqbal N, Sharma P, Singh AK, Kaur P, Sharma S, Singh TP. (2017) Design of anti-thyroid drugs: Binding studies and structure determination of the complex of lactoperoxidase with 2-mercaptoimidazole at 2.30 Å resolution. Proteins. 85:1882-1890.

126. Gupta D Sachdeva E Haque MA Rahman S Bansal R Ethayathulla AS Hassan MI Kaur P (2017) Effect of chemical denaturants on the conformational stability of GyrB subunit of DNA gyrase from Salmonella enterica serovar Typhi. Int J Biol Macromol.103:165-174.

125. Yenamandra VK, Vellarikkal SK, Kumar M, Chowdhury MR, Jayarajan R, Verma A, Scaria V, Sivasubbu S, Ray SB, Dinda AK, Kabra M, Kaur P, Sharma VK, Sethuraman G. (2017) Application of whole exome sequencing in elucidating the phenotype and genotype spectrum of junctional epidermolysis bullosa: A preliminary experience of a tertiary care centre in India. J Dermatol Sci. 86:30-36. doi: 10.1016/j.jdermsci.2016.12.020. Epub 2016 Dec 29.

124. Singh PK, Sirohi HV, Iqbal N, Tiwari P, Kaur P, Sharma S, Singh TP. (2017) Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution. Biochim Biophys Acta. Mar;1865(3):329-335. doi: 10.1016/j.bbapap.2016.12.006.

123. Iqbal N, Kumar M, Sharma P, Yadav SP, Kaur P, Sharma S, Singh TP. (2017) Binding studies and structure determination of the recombinantly produced type-II 3-dehydroquinate dehydratase from Acinetobacter baumannii. Int J Biol Macromol. Jan;94(Pt A):459-465. doi: 10.1016/j.ijbiomac.2016.10.049.

122. Singh RP, Singh A, Sirohi HV, Singh AK, Kaur P, Sharma S, Singh TP. (2016) Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution. FEBS Open Bio. Jun 14;6(7):640-50. doi: 10.1002/2211-5463.12051. eCollection 2016 Jul.

121. Rastogi N, Singh A, Singh PK, Tyagi TK, Pandey S, Shin K, Kaur P, Sharma S, Singh TP. (2016) Structure of iron saturated C-lobe of bovine lactoferrin at pH 6.8 indicates a weakening of iron coordination. Proteins. May;84(5):591-9. doi: 10.1002/prot.25004. Epub 2016 Feb 24.

120. Dube D, Tiwari P, Kaur P. (2016) The hunt for antimitotic agents: An overview of structure-based design strategies. Expert Opin Drug Discov. 11, 579-97.

119. Rani L, Mathur N, Gogia A, Vishnubhatla S, Kumar L, Sharma A, Dube D, Kaur P, Gupta R. (2016) Immunoglobulin heavy chain variable region gene repertoire and B-cell receptor stereotypes in Indian patients with chronic lymphocytic leukemia. Leuk Lymphoma. 2016 Mar 4:1-12. [Epub ahead of print] PMID:26942309

118. Kumar M, Dahiya S, Sharma P, Sharma S, Singh TP, Kapil A, Kaur P. (2015) Structure based in silico analysis of quinolone resistance in clinical isolates of Salmonella Typhi from India. PLoS One. May 11;10(5):e0126560. doi: 10.1371

117. Gupta N, Singh PK, Kumar M, Shastri S, Gulati S, Kumar A, Agarwala A, Kapoor S, Nair M, Sapra S, Dubey S, Singh A, Kaur P, Kabra M. (2015) Glutaric Acidemia Type 1-Clinico-Molecular Profile and Novel Mutations in GCDH Gene in Indian Patients. JIMD Rep. 21:45-55.

116. Vedithi SC, Lavania M, Kumar M, Kaur P, Turankar RP, Singh I, Nigam A, Sengupta U. (2015) A report of rifampin-resistant leprosy from northern and eastern India: identification and in silico analysis of molecular interactions. Med Microbiol Immunol. 204:193-203.

115. Shukla PK, Gautam L, Sinha M, Kaur P, Sharma S, Singh TP. (2015) Structures and binding studies of the complexes of phospholipase A2 with five inhibitors. Biochim Biophys Acta. 1854:269-77.

114. Kumar M, Pydi SP, Sharma S, Singh TP, Kaur P. (2014) Identification of a high affinity selective inhibitor of Polo-like kinase 1 for cancer chemotherapy by computational approach. J Mol Graph Model. 51:104-112.

113. Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP (2014) Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft. FEBS Open Bio. 4:915-922.

112. Dube, D., Sharma, S., Singh, T.P. and Kaur, P. (2014) Pharmacophore Mapping, In Silico Screening and Molecular Docking to Identify Selective Trypanosoma brucei Pteridine Reductase Inhibitors Molecular Informatics 33, 124–134

111. Singh A, Kumar A, Gautam L, Sharma P, Sinha M, Bhushan A,Kaur P, Sharma S, Arora A, Singh TP. (2014) Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase. Biochem J. 463:329-337.

110. Rastogi N, Singh A, Pandey SN, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. (2014) Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut. FEBS J. 281: 2871-2882.

109. Sharma S, Kaushik S, Sinha M, Kushwaha GS, Singh A, Sikarwar J, Chaudhary A, Gupta A, Kaur P, Singh TP. (2014) Structural and functional insights into peptidyl-tRNA hydrolase. Biochim Biophys Acta. 1844:1279-88

108. Sinha M, Singh RP, Kushwaha GS, Iqbal N, Singh A, Kaushik S,Kaur P, Sharma S, Singh TP. (2014) Current overview of allergens of plant pathogenesis related protein families. ScientificWorldJournal. Feb 16; 2014:543195.

107. Rastogi N, Nagpal N, Alam H, Pandey S, Gautam L, Sinha M, Shin K, Manzoor N, Virdi JS, Kaur P, Sharma S, Singh TP. (2014) Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin. PLoS One. Mar 3;9(3):e90011.

106. Madhuprakash J, Singh A, Kumar S, Sinha M, Kaur P, Sharma S, Podile AR, and and Singh TP. (2013) Structure of chitinase D from Serratia proteamaculans reveals the structural basis of its dual action of hydrolysis and transglycosylation. Int J Biochem Mol Biol. 4, 166-178.

105. Ramachandran G, Kumar M, Selvi Rani D, Annanthapur V, Calambur N, Nallari P, and Kaur P. (2013) An in silico analysis of troponin I mutations in hypertrophic cardiomyopathy of Indian origin. PLoS One. 2013 Aug 13;8(8):e70704.

104. Kumar M, Kaur P, Kumar M, Khokhar S, and Dada R. (2013) Molecular and structural analysis of genetic variations in congenital cataract. Mol Vis. 19, 2436-2450.

103. Sharma M, Gupta M, Singh D, Kumar M, and Kaur P. (2013). Synthesis, evaluation and molecular docking of prolyl-fluoropyrrolidine derivatives as dipeptidyl peptidase IV inhibitors. Chem Biol Drug Des. 82, 156-166.

102. Sharma S, Singh AK, Kaushik S, Sinha M, Singh RP, Sharma P, Sirohi H, Kaur P, and Singh TP. (2013) Lactoperoxidase: structural insights into the function,ligand binding and inhibition. Int J Biochem Mol Biol.4, 108-128..

101. Sinha M, Singh A, Shokeen A, Sharma P, Kaushik S, Mitra DK, Kaur P, Sharma S, and Singh TP. (2013). Evidence of a novel allergenic protein Narcin in the bulbs of Narcissus tazetta. Int J Biochem Mol Biol. 4, 95-

100. Kaushik S, Singh N, Yamini S, Singh A, Sinha M, Arora A, Kaur P, Sharma S, and Singh TP. (2013) The mode of inhibitor binding to peptidyl-tRNA hydrolase: binding studies and structure determination of unbound and bound peptidyl-tRNA hydrolase from Acinetobacter baumannii. PLoS One. 8(7):e67547.

99. Sharma S, Sinha M, Kaushik S, Kaur P, and Singh TP. (2013) C-lobe of lactoferrin: the whole story of the half-molecule. Biochem Res Int. 2013;2013:271641.

98. Kaushik S, Singh A, Sinha M, Kaur P, Sharma S, and Singh TP. (2013) Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 653-656.

97. Sikarwar J, Kaushik S, Sinha M, Kaur P, Sharma S, and Singh TP. (2013) Cloning, Expression, and Purification of Nucleoside Diphosphate Kinase from Acinetobacter baumannii. Enzyme Res. 2013;2013:597028.

96. Sinha M, Gautam L, Shukla PK, Kaur P, Sharma S, and Singh TP. (2013) Current perspectives in NSAID-induced gastropathy. Mediators Inflamm. 2013;2013:258209.

95. Sinha M, Kaushik S, Kaur P, Sharma S, and Singh TP (2013) Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein. Int J Pept. 2013:390230.

94. Sharma, P., Dube, D., Sinha, M., Yadav, S., Kaur, P., Sharma, S. and Singh, T.P. (2013) Structural Insights into the Dual Strategy of Recognition by Peptidoglycan Recognition Protein, PGRP-S: Structure of the Ternary Complex of PGRP-S with Lipopolysaccharide and Stearic Acid. PLoS One. 8(1):e53756. doi: 10.1371/journal.pone.0053756. Epub 2013 Jan 9.

93. Kushwaha, G.S., Yamini, S., Kumar, M., Sinha, M., Kaur, P., Sharma, S. and Singh, T.P. (2013) First structural evidence of sequestration of mRNA cap structures by type 1 ribosome inactivating protein from Momordica balsamina. Proteins. 81:896-905

92. Sharma, P., Yamini, S., Dube, D., Singh, A., Mal, G., Pandey, N., Sinha, M., Singh, A.K., Dey, S, Kaur, P., Mitra, D.K., Sharma, S. and Singh, T.P. (2013) Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site. Arch Biochem Biophys. 529, 1-10.

91. Singh, A.K., Smith, M.L., Yamini, S., Ohlsson, P.I., Sinha, M., Kaur, P., Sharma, S., Paul, J.A., Singh, T.P. and Paul, K.G. (2012) Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH. Protein J. 31, 598-608.

90. Kumar, M., Kaur, P , Kumar, M., Saxena, R., Sharma, P., Dada, R. (2012) Clinical characterization and mitochondrial DNA sequence variations in Leber hereditary optic neuropathy. Mol. Vis. 18, 2687-2699.

89. Kumar, M., Gupta, M., Singh, D., Kumar, M. and Kaur, P. (2012) Synthesis, evaluation and molecular docking of thiazolopyrimidine derivatives as dipeptidyl peptidase IV inhibitors. Chem. Biol. Drug Des. 80, 918-928.

88. Dube, D., Periwal, V., Kumar, M., Sharma, S., Singh, T.P. and Kaur, P. (2012) 3D-QSAR based pharmacophore modeling and virtual screening for identification of novel pteridine reductase inhibitors. J. Mol. Model 18, 1701-1711.

87 Kushwaha, G.S., Pandey, N., Sinha, M., Singh, S.B., Kaur, P., Sharma, S. and Singh, T.P. (2012). Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states. Biochim. Biophys. Acta. 1824, 679-691.

86. Hariprasad, G., Kaur, P., Srinivasan, A., Singh, T.P, and Kumar, M. (2012). Structural analysis of secretory phospholipase A(2) from Clonorchis sinensis: therapeutic implications for hepatic fibrosis. J. Mol. Model 18, 3139-3145.

85. Hariprasad, G., Kumar, M., Rani, K., Kaur, P. and Srinivasan, A. (2012) Aminoglycoside induced nephrotoxicity: molecular modeling studies of calreticulin-gentamicin complex. J. Mol. Model 18, 2645-2652.

84. Kulsum, U., Singh, V., Sharma, S., Srinivasan, A., Singh, T.P. and Kaur, P. (2011) RASOnD - A comprehensive resource and search tool for RAS superfamily oncogenes from various species. BMC Genomics 12, 341.

83. Singh, A.K., Pandey, N., Sinha, M., Kaur, P., Sharma, S. and Singh, T.P. (2011) Structural evidence for the order of preference of inorganic substrates in mammalian heme peroxidases: crystal structure of the complex of lactoperoxidase with four inorganic substrates, SCN, I, Br and Cl. Int. J. Biochem. Mol. Biol. 2, 328-339.

82. Sharma, P., Dube, D., Sinha, M., Dey, S., Kaur, P., Sharma, S. and Singh, T.P. (2012) Structural basis of heparin binding to camel peptidoglycan recognition protein-S. Int. J. Biochem. Mol. Biol. 3, 86-94.

81 Sharma, P., Dube, D., Sinha, M., Mishra, B., Dey, S., Mal, G., Pathak, K.M., Kaur, P., Sharma, S. and Singh, T.P. (2011) Multiligand specificity of pathogen-associated molecular pattern-binding site in peptidoglycan recognition protein. J. Biol. Chem. 286, 31723-31730.

80. Kang, T.S., Geogieva, D., Genov, N., Murakami, M., Sinha, M., Kumar, R.P., Kaur, P., Kumar, S., Dey, S., Sharma, S., Vrielink, A., Betzel, Ch., Takeda, S., Arni, R.K., Singh, T.P. and Kini, R.M. (2011). Enzymatic toxins from snake venom: Structural characterization and mechanism of catalysis: FEBS J. 278, 4544-4576.

79. Sharma, P., Dube, D., Singh, A., Mishra, B., Singh, N., Sinha, M., Dey, S., Kaur, P., Mitra, D.K., Sharma, S. and Singh, T.P. (2011) Structural basis of recognition of pathogen associated molecular patterns and inhibition of pro-inflammatory cytokines by peptidoglycan recognition protein-S. J. Biol. Chem. 286, 16208-16217.

78. Kumar, M., Sharma, S., Srinivasan, A., Singh, T.P. and Kaur, P. (2011) Structure-based in-silico rational design of a selective peptide inhibitor for thymidine monophosphate kinase of mycobacterium tuberculosis. J. Mol. Model 17, 1173-1182.

77. Hariprasad, G., Kumar, M., Srinivasan, A., Kaur, P., Singh, T.P. and Jithesh, O. (2011) Structural analysis of a group III Glu-62 phospholipase A2 from the scorpion Mesobuthus tumulus: Targeting and reversible inhibition by native peptides. Int. J. Biol. Macromol. 48, 423–431.

76. Kumar M., Agarwal T., Khokhar S., Kumar M., Kaur P., Roy T.S. and Dada R. (2011) Mutation screening and genotype phenotype correlation of α-crystallin, γ-crystallin and GJA8 gene in congenital cataract. Mol. Vis. 17: 693-707.

75. Bora H., Garg S., Sen P., Kumar D, Kaur P., Khan, R.H., and Sharma Y.D. (2011) Plasmodium vivax Tryptophan-Rich Antigen PvTRAg33.5 Contains Alpha Helical Structure and Multidomain Architecture. PLoS One V-6: e162934.

74. Shukla P., Vasisht S., Srivastava R., Gupta N., Ghosh, M., Kumar M., Sharma R., Gupta A.K., Kaur P., Kamate M., Gulati S., Kalra V., Phadke S., Singhi P., Dherai A.J. and Kabra M. (2011) Molecular and structural analysis of metachromatic leukodystrophy patients in Indian population. J. Neurolog. Sci. 301: 38-34.

73. Paliwal, P., Tandon, R., Dube, D., Kaur, P., Sharma, A. (2011) Familial segregation of a VSX1 mutation adds a new dimension to its role in the causation of keratoconus. Mol. Vis. 17, 481-485.

72. Kumar, M., Verma, S., Sharma, S., Srinivasan, A., Singh, T.P. and Kaur, P. (2010) Structure-based in silico design of a high-affinity dipeptide inhibitor for novel protein drug target Shikimate kinase of Mycobacterium tuberculosis. Chem. Biol. Drug. Des. 76, 277-284.

71. Kumar, S., Singh, N., Mishra, B., Dube, D., Sinha, M., Singh, S.B., Dey, S., Kaur, P., Sharma, S. and Singh, T.P. (2010) Modulation of inhibitory activity of xylanase-α-amylase inhibitor protein (XAIP): binding studies and crystal structure determination of XAIP-II from Scadoxus multiflorus at 1.2 Å resolution. BMC Struct. Biol. 10, 41.

70. Hariprasad, G., Kumar, M., Kaur, P., Singh, T.P. and Kumar, R.P. (2010) Human group III PLA(2) as a drug target: Structural analysis and inhibitor binding studies. Int. J. Biol. Macromol. 47, 496-501.

69. Singh, A.K., Singh, N., Tiwari, A., Sinha, M., Kushwaha, G.S., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2010). First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases. J. Biol. Inorg. Chem. 15, 1099-1107.

68. Soni, B.R., Hasan, M.I., Parmar, A., Ethayathulla, A.S., Kumar, P., Singh, N.K., Sinha, M., Kaur, P., Yadav, S., Sharma, S., Madamwar, D. and Singh, T.P. (2010) Structure of the novel 14kDa fragment of alpha-subunit of phycoerythrin from the starving cyanobacterium Phormidium tenue. J. Struct. Biol. 171, 247-255.

67. Mir, R., Singh, N., Vikram, G., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2010) Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory drugs (NSAIDs). Arch. Biochem. Biophys. 500, 196-202.

66. Paliwal, P., Sharma, A., Tandon, R., Sharma, N., Titiyal, J.S., Sen, S., Kaur, P., Dube, D. and Vajpayee, R.B. (2010) TGFBI mutation screening and genotype-phenotype correlation in north Indian patients with corneal dystrophies. Mol. Vis. 16, 1429-1438.

65. Paliwal, P., Gupta, J., Tandon, R., Sharma, N., Titiyal, J.S., Kashyap, S., Sen, S., Kaur, P., Dube, D., Sharma, A. and Vajpayee, R.B. (2010). Identification and characterization of a novel TACSTD2 mutation in gelatinous drop-like corneal dystrophy. Mol. Vis. 16, 729-739.

64. Tomar N, Bora H, Singh R, Gupta N, Kaur P, Chauhan SS, Sharma YD, Goswami R. (2010). Presence and significance of a R110W mutation in the DNA-binding domain of GCM2 gene in patients with isolated hypoparathyroidism and their family members. Eur. J. Endocrinol. 162, 407-421.

63. Kumar, S., Singh, N., Sinha, M., Dube, D., Singh, S.B., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2010) Crystal structure determination and inhibition studies of a novel xylanase and alpha-amylase inhibitor protein (XAIP) from Scadoxus multiflorus. FEBS J. 277, 2868-2882.

62. Mir, R., Kumar, R.P., Singh, N., Vikram, G., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2010) Specific interactions of C-terminal half (C-lobe) of lactoferrin protein with edible sugars: binding and structural studies with implications on diabetes. Int. J. Biol. Macromol. 47, 50-59.

61. Mir, R., Singh, N., Vikram, G., Kumar, R.P., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2009) The structural basis for the prevention of nonsteroidal antiinflammatory drug-induced gastrointestinal tract damage by the C-lobe of bovine colostrum lactoferrin. Biophys. J. 97, 3178-3186.

60. Singh, A.K., Kumar, R.P., Pandey, N., Singh, N., Sinha, M., Bhushan, A., Kaur, P., Sharma, S. and Singh, T.P. (2010) Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases: Binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7 Å resolution. J. Biol. Chem. 285, 1569-1576.

59. Kumar, S., Singh, N., Sinha, M., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2009) Isolation, purification, crystallization and preliminary crystallographic studies of amaryllin, a plant pathogenesis-related protein from Amaryllis belladonna. Acta Crystallogr. F65, 635-637.

58. Singh, A.K., Singh, N., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2009) Binding modes of aromatic ligands to mammalian heme peroxidases with associated functional implications: crystal structures of lactoperoxidase complexes with acetylsalicylic acid, salicylhydroxamic acid, and benzylhydroxamic acid. J. Biol. Chem. 284, 20311-20318.

57. Singh, N., Kumar, R.P., Kumar, S., Sharma, S., Mir, R., Kaur, P., Srinivasan, A. and Singh, T. P. (2009) Simultaneous inhibition of anti-coagulation and inflammation: crystal structure of phospholipase A2 complexed with indomethacin at 1.4 Å resolution reveals the presence of the new common ligand-binding site. .J. Mol. Recognit. 22, 437-445.

56. Mishra, P., Prem Kumar, R., Ethayathulla, A.S., Singh, N., Sharma, S., Perbandt, M., Betzel, C., Kaur, P., Srinivasan, A., Bhakuni, V. and Singh, T.P. (2009) Polysaccharide binding sites in hyaluronate lyase--crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose. FEBS J. 276, 3392-3402.

55. Sheikh, I.A., Singh, A.K., Singh, N., Sinha, M., Singh, S.B., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. and Singh, T.P. (2009) Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 Å resolution. J. Biol. Chem. 284, 14849-14856.

54. Sharma, P., Singh, N., Sinha, M., Sharma, S., Perbandt, M., Betzel, C., Kaur, P., Srinivasan, A. and Singh, T. P. (2009) Tryptophan as a three-way switch in regulating the function of the secretory signalling glycoprotein (SPS-40) from mammary glands: structure of SPS-40 complexed with 2-methylpentane-2,4-diol at 1.6 Å resolution. Acta Crystallogr. D65, 375-378.

53. Singh, A.K., Singh, N., Sharma, S., Shin, K., Takase, M., Kaur, P., Srinivasan, A. and Singh, T.P. (2009) Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A resolution. Biophys. J. 96, 646-654.

52. Lumb, V., Das, M.K., Mittra, P., Ahmed, A., Kumar, M., Kaur, P., Dash, A.P., Singh, S.S. and Sharma, Y.D. (2009) Emergence of an Unusual Sulfadoxine-Pyrimethamine Resistance Pattern and a Novel K540N Mutation in Dihydropteroate Synthetase in Plasmodium falciparum Isolates Obtained from Car Nicobar Island, India, after the 2004 Tsunami. J. Infect. Dis. 199,1064-1073.

51. Hassan, M.I., Bilgrami, S., Kumar, V., Singh, N., Yadav, S., Kaur, P. and Singh, T.P. (2008) Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma. J. Mol. Biol. 384, 663-672

50. Thakur, A., Alam, M.T., Bora, H., Kaur, P. and Sharma, Y.D. (2008) Plasmodium vivax: Sequence polymorphism and effect of natural selection at apical membrane antigen 1 (PvAMA1) among Indian population. Gene 419, 35-42.

49. Ethayathulla, A. S., Bessho, Y., Shinkai, A., Padmanabhan, B., Singh, T.P., Kaur P. and Yokoyama S. (2008) Purification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima. Acta Crystallogr. F64, 498-500.

48. Mir, R., Sinha, M., Sharma, S., Singh, N., Kaur, P., Srinivasan, A. and Singh, T.P. (2008) Isolation, purification, crystallization and preliminary crystallographicstudies of sagitoxin, an oligomeric cardiotoxin from the venom of Naja naja saggitifera Acta Crystallogr. F64, 545-547.

47. Sharma, P., Singh, N., Sinha, M., Sharma, S., Perbandt, M., Betzel, C., Kaur, P., Srinivasan, A. and Singh, T.P. (2008) Crystal Structure of the Peptidoglycan recognition protein at 1.8 A resolution reveals dual strategy to combat infection through two independent functional homodimers. J. Mol. Biol. 378, 921-930.

46. Singh, A.K., Singh, N., Sharma, S., Singh, S.B., Kaur, P., Bhushan, A., Srinivasan, A. and Singh, T.P. (2008) Crystal structure of lactoperoxidase at 2.4A resolution. J. Mol. Biol. 376:1060-1075.

45. Saravanan, K., Hariprasad, G., Jitesh, O., Das, U., Dey, S., Sharma, S., Kaur, P., Singh, T.P., and Srinivasan, A. (2007). Endothelin and its receptor interactions: role of extracellular receptor domain and length of peptide ligands. Protein Pept. Lett. 14 : 779-783.

44. Das, U., Hariprasad, G., Ethayathullah, A.S., Manral, P., Das, T.K., Pasha, S., Mann, A., Ganguli, M., Verma, A.K., Bhat, R., Chandrayan, S.K., Ahmed, S., Sharma, S., Kaur, P., Singh, T.P., Srinivasan, A. (2007). Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key. PLoS ONE. 2(11) : e1176.

43. Das, U., Hariprasad, G., Pasha, S., Mann, A., Ganguli, M., Sharma, S., Kaur, P., Singh, T.P. and Srinivasan, A.. (2007) Interface peptide of Alzheimer's amyloid beta: Application in purification. Biochem Biophys Res Commun. 362, 538-542.

42. Hariprasad, G., Singh, B., Das, U., Ethayathulla, A.S., Kaur, P., Singh, T.P. and Srinivasan, A. (2007). Cloning, sequence analysis and homology modeling of a novel phospholipase A2 from Heterometrus fulvipes (Indian black scorpion). DNA Seq. 18, 242-246

41. Singh, N., Somvanshi, R.K., Sharma, S., Dey, S., Kaur. P. and Singh, T. P. (2007) Structural elements of ligand recognition site in secretory phospholipase A2 and structure-based design of specific inhibitors. Curr. Top. Med. Chem. 7, 757-764.

40. Singh, B., Das, U., Ethayathulla, A.S., Kaur, P., Singh, T.P. and Srinivasan, A. (2007) Cloning, sequence analysis and homology modeling of a novel phospholipase A(2) from Heterometrus fulvipes (Indian black scorpion). DNA Seq. 18, 242-246.

39. Ethayathulla, A.S., Srivastava, D.B., Kumar, J., Saravanan, K., Bilgrami, S., Sharma, S., Kaur, P., Srinivasan, A. and Singh, T.P. (2007) Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution. Acta Crystallogr. F63, 258-265.

38. Kumar J.</snm></au>,<orf id="a"> </fnm> <snm>Ethayathulla A. S.</snm></au>,<orf id="a"> <au><fnm></fnm><snm>Srivastava</snm></au>,<orf id="a"> D.B., <au,<orf id="a"><snm>Singh</snm></au>,<orf id="a"> N., <au><fnm><au><fnm></fnm><snm>Sharma</snm></au>,<orf id="a"> S., <snm>Kaur, P., Srinivasan A. </snm></au><orf id="a">and </fnm><snm>Singh, T.P.</snm></au><orf id="a"><cor email="tps@aiims.aiims.ac.in"></cor> (2007) <!DOCTYPE IUCR-ART PUBLIC "IUCr//DTD IUCr article dtd V1.1//EN"><iucr-art jid="D000000" aid="xx0000" access="pay" docsubty="FA" crt="International Union of Crystallography" language="0"><jnlinfo name="Acta Crystallographica Section D" yr="2004" issue="1" volume="60" abbrtitle="Acta Cryst. D" coden="ABCRE6" editor="J. P. Glusker" issn="0907-4449" fpage="0" lpage="0"><fm><atl>Carbohydrate Binding Properties of Goat Secretory Glycoprotein (SPG-40) and its Functional Implications: Crystal Structures of the Native Glycoprotein and its Four Complexes with Chitin - Like Oligosaccharides Acta Crystallogr. D63, 437-446.</atl>

37. Sherawat, M., Kaur, P., Perbandt, M., Betzel, C., Slusarchyk, W.A., Bisacchi, G.S., Chang, C., Jacobson, B.L., Einspahr, H.M. and Singh, T.P. (2007) Structure of the complex of trypsin with a highly potent synthetic inhibitor at 0.97 A resolution. Acta Crystallogr. D63, 500-507.

36. Jabeen, T., Singh, N., Singh, R.K., Jasti, J., Sharma, S., Kaur, P., Srinivasan, A. and Singh, T.P. (2006). Crystal structure of a heterodimer of phospholipase A2 from Naja naja sagittifera at 2.3 Å resolution reveals the presence of a new PLA2-like protein with a novel Cys32 - Cys49 disulphide bridge with a bound sugar at the substrate-binding site. Proteins 62, 329-337.

35. Balasubramanya, T., Chandra, V., Kaur, P. and Singh T. P. (2005). Crystal structure of the complex of the secretory phospholipase A2 from Daboia russelli pulchella with an endogenic indole derivative, 2-carbamoylmethyl-5-propyl-octahydro-indol-7-yl-acetic acid at 1.8 Å resolution. Biochim. Biophys. Acta 1752, 177-185.

34. Bilgrami, S., Yadav, S., Kaur P., Sharma, S. Perbandt, M., Betzel, Ch., and Singh T. P. (2005) Crystal Structure of the Disintegrin Heterodimer from Saw-Scaled Viper (Echis carinatus) at 1.9 Å Resolution. Biochemistry 44, 11058-11066.

33. Jabeen, T., Sharma, S., Singh, N., Singh, R. K., Kaur, P., Perbandt, M., Betzel, Ch., Srinivasan, A. and Singh, T.P. (2005) Crystal structure of a calcium-induced dimer of two isoforms of cobra Phospholipase A2 at 1.6 Å resolution. Proteins: Struc. Func. Genetics 59, 856-863.

32. Mishra, V., Bilgrami, S., Sharma, R.S., Kaur, P., Yadav, S., Krauspenhaar, R., Betzel, Ch., Voelter, W., Babu, C. R. and Singh, T.P. (2005) Crystal Structure Of Himalayan Mistletoe Ribosome Inactivating Protein Reveals The Presence Of A Natural Inhibitor And A New Functionally Active Sugar-Binding Site. J. Biol. Chem. 280, 20712-20721.

31. Singh, G., Jasti, J., Saravanan, K., Sharma, S., Kaur, P., Srinivasan A. and Singh. (2005) Crystal structure of the complex formed between a group I Phospholipase A2 and a naturally occurring fatty acid at 2.7 Å resolution. Protein Sc. 14, 395-400.

30. Singh, R. K., Ethayathulla, A.S., Jabeen, T., Sharma, S., Kaur, P., and Singh, T.P. (2005) Aspirin induces its anti-inflammatory effects through its specific binding to Phospholipase A2: Crystal structure of the complex formed between Phospholipase A2 and aspirin at 1.9 Å Resolution. J. Drug Targeting 13, 113-119.

29. Singh, R. K., Jabeen, T., Sharma, S., Kaur, P., Srinivasan A. and Singh, T.P. (2005) Crystal structure of a novel phospholipase A2 from crude venom of Indian cobra sub-species Naja naja sagittifera at 1.48 Å resolution. Ind. J. Biochem. Biophys., 42, 279-286.

28. Bilgrami, S., Tomar S., Yadav, S., Kaur ,P., Kumar, J., Jabeen, T., Sharma, S. and Singh T. P. (2004) Crystal Structure of Schistatin, a Disintegrin Homodimer from Saw-scaled Viper (Echis carinatus) at 2.5 Å Resolution. J. Mol. Biol. 341, 829-834.

27. Singh, R. K., Vikram P., Makker J., Jabeen T., Sharma S., Dey S., Kaur P., Srinivasan A. and Singh T. P. (2003). Design of Specific Peptide Inhibitors for Group I Phospholipase A2: Structure of a Complex Formed between Phospholipase A2 from Naja naja sagittifera (Group I) and a Designed Peptide Inhibitor Val-Ala-Phe-Arg-Ser (VAFRS) at 1.9 Å Resolution Reveals Unique Features. Biochemistry 42, 11701-11706.

26. Mohanty, A.K., Singh, G., Paramasivam, M., Saravanan, K., Jabeen, T., Sharma, S., Yadav, S., Kaur, P., Kumar, P., Srinivasan, A. and Singh T. P. (2003) Crystal Structure of a Novel Regulatory 40 kDa Mammary Gland Protein (MGP-40) secreted during Involution. J. Biol. Chem. 278, 14451-14460.

25. Kumar, J., Weber, W., Munchau, S., Yadav, S., Singh, S.B., Saravan, K., Paramsivam, M., Sharma, S., Kaur, P., Bhushan, A., Srinivasan, A., Betzel, Ch and Singh, T.P. (2003) Crystal Structure of human seminal lactoferrin at 3.4 Å resolution. Ind. J. Biochem. Biophy. 40, 14-21.

24. Chandra V., Jasti J., Kaur P., Dey S., Perbandt. M., Srinivasan A., Betzel A., and Singh T.P. (2002). Crystal structure of a complex formed between a snake venom phospholipase A2 and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys (FLSYK) at 1.8 a resolution. J. Biol. Chem. 277, 41079-41085.

23. Chandra V., Jasti J., Kaur P., Srinivasan, A., Betzel, Ch. and T. P. Singh (2002) Structural Basis of Phospholipase A2 Inhibition for the Synthesis of Prostaglandins by the Plant Alkaloid Aristolochic Acid from a 1.7 Å Biochemistry 41, 10914-10919.

22. Chandra V., Jasti J., Kaur P., Dey S., Srinivasan, A., Betzel, Ch.and. Singh, T P. (2002). Design of specific peptide inhibitors of phospholipase A2: Crystal structure of a complex formed between russell's viper phospholipase A2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS) Acta Crystallogr D59 1813-1819.

21. Chandra, V., Jasti,J., Kaur, P., Betzel, Ch., Srinivasan, A. and Singh, T. P. (2002) First structural evidence of a specific inhibition of phospholipase A2 by a-Tocopherol and its implications in inflammation: Crystal structure of the complex formed between phospholipase A2 and -Tocopherol at 1.8 Å resolution. J. Mol. Biol. 320, 215-222.

20. Chandra, V., Kaur, P., Jasti, J., Betzel, Ch. and Singh, T. P. (2001) Regulation of catalytic function by molecular association: Crystal structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 Å resolution. Acta Crystallogr. D57, 1793-1798.

19. Betzel, Ch., Gourinath, S., Kumar, P., Kaur, P., Perbandt, M., Eschenburg, S. and Singh T. P. (2001) Structure of a serine protease Proteinase K from Tritirachium album limber at 0.98 Å resolution. Biochemistry 40, 3080-3088.

18. Chandra, V., Kaur, P., Srinivasan, A., and Singh, T.P. (2000). Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from daboia russelli pulchella at 2.4Å resolution. J. Mol. Biol. 296, 1117-1126.

17. Nagpal, A., Chandra, V., Kaur P., Singh, T.P. (1999) Purification, crystallization and preliminary crystallographic analysis of a natural complex of phospholipase A2 from Echis carinatus (saw-scaled viper). Acta Crystallogr. D55, 1240-1241.

16. Bhatia, S., Kumar, P., Kaur, P. and Singh, T.P. (1999) Design of Peptides with a,b-Dehydro-Residues: Synthesis, and Crystal and Molecular Structure of a 310 - helical Tetrapeptide Boc-L-Val-DPhe-DPhe-L-Ile-OCH3. J. Peptide Res. 54, 249-255.

15. Sharma, A.K., Karthikeyan, S., Kaur, P., Singh, T.P. and Yadav, M.P. (1996). Purification, Crystallization and Preliminary Crystallographic Analysis of Mare Lactoferrin. Acta Crystallogr. D52, 1196-1198.

14. Singh, T.P. and Kaur, P. (1996). Conformation and Design of Peptides with a, b-Dehdyro-Amino Acid Residues. Prog. Biophys. Mol. Biol. 66, 141-165.

13. Dey, S., Kaur, P., and Singh, T.P.(1996). Backbone-side-chain Interactions in Serine: Synthesis, Crystal Structure and Solution Conformation of a Linear model Peptide N-Boc-L-Ser-L-Phe-OCH3. Int. J. Peptide Prot. Res. 48, 299-303.

12. Bhatia, S., Dey, S., Kaur, P. and Singh, T.P. (1996). Design of Peptides Using a, b- dehydro-residues: Synthesis, Crystal structure and Molecular Conformation of Boc-L-Val-DPhe-DPhe-Ala-OCH3. J. Peptide Sci., 2, 357-363.

11. Sharma, P., Narula, P. and Singh, T.P. (1994) a, b-Dehydro-amino acid Residues in the Design of Peptide Structures- Synthesis, Crystal Structure and Molecular Conformation of Two Homologous Peptides; N-Ac-Dehydro-Phe-L-Leu-OCH3 and N-Ac-Dehydro-Phe-L-NorVal-OCH3 Biopolymers 34, 1243-1249.

10. Singh, S., Jha, N.K., Narula, P. and Singh, T.P. (1995) Structure and Conformation of cis – Dichloro[bis(diphenyl-phosphino)ethane] palladium (II) Acta Crystallogr. C51, 593-595.

9. Singh, T.P. and Narula, P. (1993) Molecular Design of Peptides: Synthesis, Molecular Structure and b-turn II' formation of N-Boc-L-Phe-dehydro-Abu-NH-CH3 in Crystals Int. J. Peptide Protein Res. 41, 394-398.

8. Narula, P., Khandelwal B. and Singh, T.P. (1991) Synthesis, Crystal Structure and Molecular Conformation of N-Ac-dehydro-Phe-L-Val-L-Val-OCH3 Biopolymers 31, 987-992.

7. Singh, T.P., Narula, P. and Patel, H.C. (1990) a, b-dehydro-residues in the Design of Peptide and Protein Structures Acta Crystallogr. B46, 539-545.

6. Narula, P., Patel, H.C., Singh, T.P. and Chauhan, V.S. (1990) Synthesis, Crystal Structure and Molecular Conformation of N-Boc-L-Phe-dehydro-Leu-L-Val-OCH3 Biopolymers 29, 935-941.

5. Singh, T.P., Narula, P., Chauhan, V.S. and Kaur, P. (1989) Crystal Structure and Molecular Conformation of N-Boc-Gly-dehydro-Phe-NH-CH3 Biopolymers 28, 1287-1295.

4. Singh, T.P., Narula, P., Chauhan, V.S.,Sharma, A.K. and Hinrichs, W. (1989) Structure of N-Boc-L-Pro-dehydro-Leu-NH-CH3 Int. J. Peptide Protein Res. 33, 167-172.

3. Narula, P., Patel, H.C., Singh, T.P. Chauhan, V.S. and Sharma, A.K. (1988) Crystal Structure and Molecular Conformation of N-Boc-L-Pro-dehydro-Leu-OCH3 Biopolymers 27, 1595-1603.

2. Narula, P., Patel, H.C., Srinivasan, A. and Singh, T.P. (1988) Structure of Kainic Acid Monohydrate Ind. J. Phy. 62A, 439-445.

1. Narula, P., Haridas M. and Singh, T.P. (1987) Crystal and Molecular Structure of Sulfadimethoxine C12H14N4O4S Ind. J. Phy. 61A, 132-142.

(b) Chapter in Book

Singh, T. P., Padmanabhan, B., Narula, P., Saxena, A.K., Betzel, Ch., Sharma, P. and Dey, S. (1995) Design of Specific Peptide Structures and Subtilisin Enzyme Inhibitors Using alpha,beta- Dehydro-Residues In Advances in Experimental Medicine and Biology: Subtilisin Enzymes: Practical Protein Engineering, Vol 379, (Eds. Bott, R. and Betzel, Ch.) p. 11-20, Plenum Press, New York.
Kumar M, Tiwari P and Kaur P (2016) Comparative evaluation of docking programs: a case study with small peptidic ligands Software and Techniques for Bio-Molecular Modelling STBMM-2016 (2016) Editor Azat Mukhametov pp 156-170 Publisher Austin Group Open Access ISBN: 978-0-9971499-4-4
Kulsum U Kapil A Singh H Kaur P (2018) NGSPanPipe: A Pipeline for Pan-genome Identification in Microbial Strains from Experimental Reads. Adv Exp. Med. Biol: Infectious Diseases and Nanomedicine III. Springer1052:39-49

(c) Abstracts In Indexed Journals

21. Kaur, P., Sharma, P., Yamini, S., Dube, D., Pandey, N., Sinha,. M., Sharma S, Singh T. P. (2013) Molecular Basis of Ligand Recognition by Mammalian Peptidoglycan Recognition Protein Biophysical J. 104(2) 547a.

20 Kaur, P., Pandey, N., Singh, A. K., Sinha,. M., Sharma S, Singh T. P. (2011) First structural evidence for the order of preference of inorganic substrates by lactoperoxidase. Acta Crystallogr. A67, C768-C769.

19 Sharma, P., Dube, D., Sinha,. M., Kaur, P., Sharma S, Singh T. P. (2011) Structural basis of recognition of pathogen-associated molecular patterns by PGRP-S Acta Crystallogr. A67, C546.

18. Hariprasad, G., Das, U., Kumar, M., Kaur, P., Singh, T.P. and Srinivasan. A. (2011) Structural insights for aminoglycoside induced nephrotoxicity: Molecular modeling studies of the calreticulin-gentamicin complex. FASEB J. 25, 572.5.

17. Hariprasad, G., Srinivasan, A., Kumar, M,, Kaur, P., Singh, T.P. and Kumar, P. (2010) Human group III PLA2 as a drug target: structural analysis and inhibitor binding studies. FASEB J. 24, 681.7.

16. Jain, R., Sharma, P., Singh, N., Sharma, S., Kaur, P. and Singh, T.P. (2008) Crystal Structure of the complex of cameline Peptidoglycan Recognition Protein with disaccharide at 3.2 Å resolution B559. Biophysical J. 94 (2, S1), 1090.

15. Singh, M., Kumar, J., Sharma, S. and Kaur, P. (2008) Homology Modeling of Signalling Glycoprotein from Camel (SPU-40) and Its Functional Characterization B587. Biophysical J. 94 (2, S1), 1099.

14. Kaur, P., Sharma, P., Singh, N., Sinha, M., Jain, R., Vikram G., Kaur, A., Sharma, S., Srinivasan A. and Singh, T.P. (2008) Crystal structure of complexes of peptidoglycan recognition protein with carbohydrates P04.15.365. Acta Crystallogr. A64, C345.

13. Sharma, P., Singh, N., Sinha, M., Sharma, S., Perbandt, M., Betzel, C, Kaur, P., Srinivasan A. and Singh, T.P. (2008) Crystal structure of the peptidoglycan recognition protein at 1.8 Å resolution P04.11.267 Acta Crystallogr. A64, C314.

12. Singh M., Kumar J., Sharma S. and Kaur P. (2008) Homology Modeling of Signalling Glycoprotein from Camel (SPU-40) and Its Functional Characterization. Biophysical J. 94, 3284

11. Jain R., Sharma P., Singh N., Sharma S., Kaur P. and Singh, T.P. (2008) Crystal Structure of the Complex of Cameline Peptidoglycan Recognition Protein with Disaccharide at 3.2Å Resolution Biophysical J. 94, 3256.

10. Prem Kumar R., Singh N., Sharma S., Kaur P., Srinivasan A., and Singh T. P. (2007) Crystal structures of complexes of phospholipase A2 with natural and synthetic inhibitors. FASEB J. 21, 649.6.

9. Somvanshi, R.K. Ethayathulla, A.S., Singh, N., Gopal, R., Singh, A.K., Sharma, S., Kaur, P. Dey, S. and Singh, T.P. (2006) Design of Specific Anti-Inflammatory Agents Using Structure-Based Approach: Crystal Structure of Complex Formed between Phospholipase A2 and Tetrapeptide Inhibitor Dehydro Val-Ala-Arg-Ser (V-A-R-S) Inflammation Research 55, S124.

8. Yadav S., Hassan, I., Kumar, V., Bilgrami, S., Kaur, P. and Singh, T.P. (2006) Clinical and Structural Proteomics of Human Seminal Plasma. Molecular Cellular Proteomics 5, S63.

7. Kaur P., Bilgrami S., Yadav S., Ethayathulla A. S., Prem kumar R., Sharma S., Perbandt M., Betzel C. and Singh T. P. (2005) Crystal Structure of a Disintegrin Heterodimer from Echis carinatus at 1.9 Å Resolution. Acta Crystallogr. A61, C245.

6. Mohanty, A.K., Singh, G., Paramasivam, M., .Sharma, S., Yadav, S., Kaur, P., Srinivasan, A. and Singh T. P. (2002) Structure of Novel Glycoprotein (BP-39) expressed during non-lactating period. Acta Crystallogr. A58S, C307.

5. Chandra V., Kaur P. and Singh T.P. (1999) Structure Of Phospholipase A2 from Daboia Russelli Pulchella At 2.5Å Resolution. Acta Crystallogr. A55 Suppl., Abstract P07.04.001, 298

4. Chandra V., Kaur P., Betzel Ch. and Singh T.P. (1999) Crystal Structure Function Relationship Of Neurotoxic Phospholipase A2 From Daboia Russelli Pulchella At 2.45 Å. J. BioSc. 24,39.

3. Kaur, P., Sharma, A.K., Karthikeyan, S. Mitra, S.N., and Singh T.P. (1996) Structure of Mare Lactoferrin at 4.0Å resolution Prog. Biophys. Mol. Biol. 63 Suppl. 1, 29.

2. Narula, P., Dey, S., Sharma, P. and Singh, T.P. (1993) Molecular Design of Peptides: Synthesis, Molecular Structure and -turn II' formation of N-Boc-L-Phe-dehydro-Abu-NH-CH3 in crystals Acta Crystallogr. A49 Suppl., 142.

1. Singh, T.P., Narula, P. and Patel, H.C. (1990) Dehydro-residues in the Design of Peptide and Protein Structures Acta Crystallogr. A46 Suppl., C145.