| Year |
Citation |
Score |
| 2023 |
Bhardwaj M, Kamble P, Mundhe P, Jindal M, Thakur P, Bajaj P. Multifaceted personality and roles of heme enzymes in industrial biotechnology. 3 Biotech. 13: 389. PMID 37942054 DOI: 10.1007/s13205-023-03804-8 |
0.387 |
|
| 2022 |
Rajakumara E, Saniya D, Bajaj P, Rajeshwari R, Giri J, Davari MD. Hijacking Chemical Reactions of P450 Enzymes for Altered Chemical Reactions and Asymmetric Synthesis. International Journal of Molecular Sciences. 24. PMID 36613657 DOI: 10.3390/ijms24010214 |
0.371 |
|
| 2019 |
Bajaj P, Mahajan R. Cellulase and xylanase synergism in industrial biotechnology. Applied Microbiology and Biotechnology. PMID 31628521 DOI: 10.1007/S00253-019-10146-0 |
0.311 |
|
| 2018 |
Moore EJ, Steck V, Bajaj P, Fasan R. Chemoselective Cyclopropanation over Carbene Y-H insertion Catalyzed by an Engineered Carbene Transferase. The Journal of Organic Chemistry. PMID 29905476 DOI: 10.1021/Acs.Joc.8B00946 |
0.636 |
|
| 2017 |
Tripathy RK, Aggarwal G, Bajaj P, Kathuria D, Bharatam PV, Pande AH. Towards Understanding the Catalytic Mechanism of Human Paraoxonase 1: Experimental and In Silico Mutagenesis Studies. Applied Biochemistry and Biotechnology. PMID 28161867 DOI: 10.1007/S12010-017-2424-5 |
0.397 |
|
| 2016 |
Bajaj P, Sreenilayam G, Tyagi V, Fasan R. Gram-Scale Synthesis of Chiral Cyclopropane-Containing Drugs and Drug Precursors with Engineered Myoglobin Catalysts Featuring Complementary Stereoselectivity. Angewandte Chemie (International Ed. in English). PMID 27885768 DOI: 10.1002/Anie.201608680 |
0.597 |
|
| 2016 |
Tyagi V, Sreenilayam G, Bajaj P, Tinoco A, Fasan R. Biocatalytic Synthesis of Allylic and Allenyl Sulfides through a Myoglobin-Catalyzed Doyle-Kirmse Reaction. Angewandte Chemie (International Ed. in English). PMID 27647732 DOI: 10.1002/Anie.201607278 |
0.603 |
|
| 2016 |
Bajaj P, Tripathy RK, Aggarwal G, Datusalia AK, Sharma SS, Pande AH. Refolded Recombinant Human Paraoxonase 1 Variant Exhibits Prophylactic Activity Against Organophosphate Poisoning. Applied Biochemistry and Biotechnology. PMID 27131877 DOI: 10.1007/S12010-016-2091-Y |
0.399 |
|
| 2016 |
Aggarwal G, Prajapati R, Tripathy RK, Bajaj P, Iyengar AR, Sangamwar AT, Pande AH. Toward Understanding the Catalytic Mechanism of Human Paraoxonase 1: Site-Specific Mutagenesis at Position 192. Plos One. 11: e0147999. PMID 26829396 DOI: 10.1371/Journal.Pone.0147999 |
0.399 |
|
| 2015 |
Parikh H, Bajaj P, Tripathy RK, Pande AH. IMPROVING PROPERTIES OF RECOMBINANT SSOPOX BY SITE-SPECIFIC PEGYLATION. Protein and Peptide Letters. PMID 26428299 DOI: 10.2174/0929866522666151002122751 |
0.316 |
|
| 2015 |
Bajaj P, Tripathy RK, Aggarwal G, Pande AH. Expression and purification of biologically active recombinant human paraoxonase 1 from inclusion bodies of Escherichia coli. Protein Expression and Purification. PMID 26003526 DOI: 10.1016/J.Pep.2015.05.011 |
0.38 |
|
| 2015 |
Beladiya C, Tripathy RK, Bajaj P, Aggarwal G, Pande AH. Expression, purification and immobilization of recombinant AiiA enzyme onto magnetic nanoparticles. Protein Expression and Purification. 113: 56-62. PMID 25982248 DOI: 10.1016/J.Pep.2015.04.014 |
0.343 |
|
| 2014 |
Bajaj P, Tripathy RK, Aggarwal G, Pande AH. Human paraoxonase 1 as a pharmacologic agent: limitations and perspectives. Thescientificworldjournal. 2014: 854391. PMID 25386619 DOI: 10.1155/2014/854391 |
0.389 |
|
| 2014 |
Bajaj P, Aggarwal G, Tripathy RK, Pande AH. Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1. Biochimie. 105: 202-10. PMID 25107406 DOI: 10.1016/J.Biochi.2014.07.024 |
0.371 |
|
| 2014 |
Bajaj P, Pande AH. Stabilization studies on bacterially produced human paraoxonase 1 for improving its shelf life. Applied Biochemistry and Biotechnology. 172: 3798-809. PMID 24574251 DOI: 10.1007/S12010-014-0806-5 |
0.306 |
|
| 2013 |
Bajaj P, Tripathy RK, Aggarwal G, Pande AH. Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme. Protein Science : a Publication of the Protein Society. 22: 1799-807. PMID 24123308 DOI: 10.1002/Pro.2380 |
0.419 |
|
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