| Year |
Citation |
Score |
| 2023 |
Nandi S, Dey M. Identification of residues involved in allosteric signal transmission from amino acid binding site of pyruvate kinase muscle isoform 2. Plos One. 18: e0282508. PMID 36897854 DOI: 10.1371/journal.pone.0282508 |
0.609 |
|
| 2020 |
Nandi S, Dey M. Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2. The Journal of Biological Chemistry. 295: 5390-5403. PMID 33509582 DOI: 10.1074/jbc.RA120.013030 |
0.382 |
|
| 2020 |
Nandi S, Razzaghi M, Srivastava D, Dey M. Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. The Journal of Biological Chemistry. 295: 17425-17440. PMID 33453989 DOI: 10.1074/jbc.RA120.015800 |
0.779 |
|
| 2020 |
Nandi S, Razzaghi M, Srivastava D, Dey M. Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. The Journal of Biological Chemistry. PMID 32989054 DOI: 10.1074/jbc.RA120.015800 |
0.78 |
|
| 2020 |
Nandi S, Dey M. Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2. The Journal of Biological Chemistry. PMID 32144209 DOI: 10.1074/Jbc.Ra120.013030 |
0.699 |
|
| 2019 |
Srivastava D, Nandi S, Dey M. Mechanistic and Structural Insights into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2. Biochemistry. PMID 31386812 DOI: 10.1021/Acs.Biochem.9B00349 |
0.797 |
|
| 2019 |
Nandi S, Dey M. Biochemical and structural investigation of the dynamic regulation mechanism of pyruvate kinase muscle isoform 2 using amino acids Acta Crystallographica Section a Foundations and Advances. 75: a406-a406. DOI: 10.1107/S010876731909603X |
0.616 |
|
| 2018 |
Dey M, Brummett AE. Isolation and Assays of Bacterial Dimethylsulfoniopropionate Lyases. Methods in Enzymology. 605: 291-323. PMID 29909828 DOI: 10.1016/Bs.Mie.2018.02.020 |
0.758 |
|
| 2017 |
Srivastava D, Razzaghi M, Henzl MT, Dey M. Structural Investigation of a Dimeric Variant of Pyruvate Kinase Muscle Isoform 2. Biochemistry. PMID 29182273 DOI: 10.1021/Acs.Biochem.7B01013 |
0.78 |
|
| 2017 |
Schnicker NJ, Razzaghi M, Guha Thakurta S, Chakravarthy S, Dey M. Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu. Biochemistry. PMID 28981257 DOI: 10.1021/Acs.Biochem.7B00601 |
0.759 |
|
| 2017 |
Dey M. Enzymology of Microbial Dimethylsulfoniopropionate Catabolism. Advances in Protein Chemistry and Structural Biology. 109: 195-222. PMID 28683918 DOI: 10.1016/Bs.Apcsb.2017.05.001 |
0.331 |
|
| 2017 |
Schnicker NJ, De Silva SM, Todd JD, Dey M. Structural and Biochemical Insights into Dimethylsulfoniopropionate Cleavage by Cofactor-bound DddK from the Prolific Marine Bacterium Pelagibacter. Biochemistry. PMID 28511016 DOI: 10.1021/Acs.Biochem.7B00099 |
0.781 |
|
| 2016 |
Brummett AE, Dey M. New Mechanistic Insight from Substrate and Product Bound Structures of the Metal-dependent Dimethylsulfoniopropionate Lyase DddQ. Biochemistry. PMID 27755868 DOI: 10.1021/Acs.Biochem.6B00585 |
0.775 |
|
| 2016 |
Schnicker NJ, Dey M. Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis. Acta Crystallographica. Section D, Structural Biology. 72: 675-81. PMID 27139630 DOI: 10.1107/S2059798316004198 |
0.81 |
|
| 2016 |
Schnicker NJ, Dey M. Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns. The Journal of Biological Chemistry. PMID 27129244 DOI: 10.1074/Jbc.M116.725432 |
0.805 |
|
| 2015 |
Brummett AE, Schnicker NJ, Crider A, Todd JD, Dey M. Biochemical, Kinetic, and Spectroscopic Characterization of Ruegeria pomeroyi DddW--A Mononuclear Iron-Dependent DMSP Lyase. Plos One. 10: e0127288. PMID 25993446 DOI: 10.1371/Journal.Pone.0127288 |
0.771 |
|
| 2015 |
Bewley KD, Dey M, Bjork RE, Mitra S, Chobot SE, Drennan CL, Elliott SJ. Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials. Plos One. 10: e0122466. PMID 25874934 DOI: 10.1371/Journal.Pone.0122466 |
0.576 |
|
| 2014 |
Dey M, Guionneau P, Hinge VK, Rao CP. Structural comparisons of the binding cores formed by 1,3-di-amide derivatives of p-tert-Butylcalix[4]arene: Arms Stabilization through intra-molecular interactions including N-H···O, O-H···Cl and π···Cl types Proceedings of the National Academy of Sciences India Section a - Physical Sciences. 84: 297-303. DOI: 10.1007/s40010-014-0145-5 |
0.486 |
|
| 2014 |
Mallik S, Dey M, Dutta M, Ghosh AK, Bandyopadhyay D. Flavin mononucleotide Phosphatase from goat liver: A possible target for divalent heavy metal cations International Journal of Pharmacy and Pharmaceutical Sciences. 6: 708-714. |
0.306 |
|
| 2013 |
Chang WC, Dey M, Liu P, Mansoorabadi SO, Moon SJ, Zhao ZK, Drennan CL, Liu HW. Mechanistic studies of an unprecedented enzyme-catalysed 1,2-phosphono-migration reaction. Nature. 496: 114-8. PMID 23552950 DOI: 10.1038/Nature11998 |
0.605 |
|
| 2011 |
Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL. Structural basis of regiospecificity of a mononuclear iron enzyme in antibiotic fosfomycin biosynthesis. Journal of the American Chemical Society. 133: 11262-9. PMID 21682308 DOI: 10.1021/Ja2025728 |
0.617 |
|
| 2011 |
Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM. Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis. Journal of the American Chemical Society. 133: 5626-8. PMID 21438550 DOI: 10.1021/Ja110492P |
0.603 |
|
| 2010 |
Dey M, Li X, Kunz RC, Ragsdale SW. Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue. Biochemistry. 49: 10902-11. PMID 21090696 DOI: 10.1021/Bi101562M |
0.779 |
|
| 2010 |
Dey M, Li X, Zhou Y, Ragsdale SW. Evidence for organometallic intermediates in bacterial methane formation involving the nickel coenzyme F₄₃₀. Metal Ions in Life Sciences. 7: 71-110. PMID 20877805 DOI: 10.1039/Bk9781847551771-00071 |
0.614 |
|
| 2010 |
Cedervall PE, Dey M, Pearson AR, Ragsdale SW, Wilmot CM. Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues . Biochemistry. 49: 7683-93. PMID 20707311 DOI: 10.1021/Bi100458D |
0.637 |
|
| 2009 |
Sarangi R, Dey M, Ragsdale SW. Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase. Biochemistry. 48: 3146-56. PMID 19243132 DOI: 10.1021/Bi900087W |
0.602 |
|
| 2008 |
Kunz RC, Dey M, Ragsdale SW. Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase. Biochemistry. 47: 2661-7. PMID 18220418 DOI: 10.1021/Bi701942W |
0.788 |
|
| 2007 |
Dey M, Kunz RC, Lyons DM, Ragsdale SW. Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme m reductase with brominated acids. Biochemistry. 46: 11969-78. PMID 17902704 DOI: 10.1021/Bi700925N |
0.785 |
|
| 2007 |
Dey M, Telser J, Kunz RC, Lees NS, Ragsdale SW, Hoffman BM. Biochemical and spectroscopic studies of the electronic structure and reactivity of a methyl-Ni species formed on methyl-coenzyme M reductase. Journal of the American Chemical Society. 129: 11030-2. PMID 17711283 DOI: 10.1021/Ja074556Z |
0.779 |
|
| 2006 |
Dey M, Kunz RC, Van Heuvelen KM, Craft JL, Horng YC, Tang Q, Bocian DF, George SJ, Brunold TC, Ragsdale SW. Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase. Biochemistry. 45: 11915-33. PMID 17002292 DOI: 10.1021/Bi0613269 |
0.746 |
|
| 2005 |
Dey M, Rao CP, Guionneau P. Structural characterization and reactivity of Cu(II) complex of p-tert-butyl-calix[4]arene bearing two imine pendants at lower rim Inorganic Chemistry Communications. 8: 998-1001. DOI: 10.1016/j.inoche.2005.08.002 |
0.484 |
|
| 2003 |
Dey M, Rao CP, Saarenketo PK, Rissanen K, Kolehmainen E, Guionneau P. Mn(IV) and Co(III)-complexes of –OH-rich ligands possessing O2N, O3N and O4N cores: syntheses, characterization and crystal structures Polyhedron. 22: 3515-3521. DOI: 10.1016/J.Poly.2003.09.015 |
0.505 |
|
| 2002 |
Dey M, Rao CP, Saarenketo PK, Rissanen K. Mono-, di- and tri-nuclear Ni(II) complexes of N-, O-donor ligands: structural diversity and reactivity Inorganic Chemistry Communications. 5: 924-928. DOI: 10.1016/S1387-7003(02)00602-0 |
0.495 |
|
| 2002 |
Dey M, Rao CP, Saarenketo PK, Rissanen K. Synthesis, structural diversity, inter-conversion and reactivity of Cu(II) complexes of hydroxy-rich molecules Inorganic Chemistry Communications. 5: 380-383. DOI: 10.1016/S1387-7003(02)00407-0 |
0.487 |
|
| 2002 |
Dey M, Rao C, Saarenketo P, Rissanen K, Kolehmainen E. Four-, Five- and Six-Coordinated ZnII Complexes of OH-Containing Ligands: Syntheses, Structure and Reactivity European Journal of Inorganic Chemistry. 2002: 2207-2215. DOI: 10.1002/1099-0682(200208)2002:8<2207::Aid-Ejic2207>3.0.Co;2-N |
0.528 |
|
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