Pramanik D - Search Results

1

Hydrogen Evolution from Aqueous Solutions Mediated by a Heterogenized [NiFe]-Hydrogenase Model: Low pH Enables Catalysis through an Enzyme-Relevant Mechanism.

Ahmed ME, Chattopadhyay S, Wang L, Brazzolotto D, Pramanik D, Aldakov D, Fize J, Morozan A, Gennari M, Duboc C, Dey A, Artero V. Ahmed ME, et al. Among authors: pramanik d. Angew Chem Int Ed Engl. 2018 Dec 3;57(49):16001-16004. doi: 10.1002/anie.201808215. Epub 2018 Nov 11. Angew Chem Int Ed Engl. 2018. PMID: 30307683

2

Artificial maturation of [FeFe] hydrogenase in a redox polymer film.

Felbek C, Hardt S, Papini C, Pramanik D, Artero V, Fontecave M, Fourmond V, Plumeré N, Léger C. Felbek C, et al. Among authors: pramanik d. Chem Commun (Camb). 2021 Feb 19;57(14):1750-1753. doi: 10.1039/d0cc08168j. Chem Commun (Camb). 2021. PMID: 33469641

3

Engineering an [FeFe]-Hydrogenase: Do Accessory Clusters Influence O₂ Resistance and Catalytic Bias?

Caserta G, Papini C, Adamska-Venkatesh A, Pecqueur L, Sommer C, Reijerse E, Lubitz W, Gauquelin C, Meynial-Salles I, Pramanik D, Artero V, Atta M, Del Barrio M, Faivre B, Fourmond V, Léger C, Fontecave M. Caserta G, et al. Among authors: pramanik d. J Am Chem Soc. 2018 Apr 25;140(16):5516-5526. doi: 10.1021/jacs.8b01689. Epub 2018 Apr 17. J Am Chem Soc. 2018. PMID: 29595965

4

Self-assembled monolayers of Aβ peptides on Au electrodes: an artificial platform for probing the reactivity of redox active metals and cofactors relevant to Alzheimer's disease.

Pramanik D, Sengupta K, Mukherjee S, Dey SG, Dey A. Pramanik D, et al. J Am Chem Soc. 2012 Jul 25;134(29):12180-9. doi: 10.1021/ja303930f. Epub 2012 Jul 11. J Am Chem Soc. 2012. PMID: 22709431

5

Interaction of NO with Cu and heme-bound Aβ peptides associated with Alzheimer's disease.

Ghosh C, Pramanik D, Mukherjee S, Dey A, Dey SG. Ghosh C, et al. Among authors: pramanik d. Inorg Chem. 2013 Jan 7;52(1):362-8. doi: 10.1021/ic302131n. Epub 2012 Dec 7. Inorg Chem. 2013. PMID: 23214455

6

Self-assembly of stable oligomeric and fibrillar aggregates of Aβ peptides relevant to Alzheimer's disease: morphology dependent Cu/heme toxicity and inhibition of PROS generation.

Sengupta K, Chatterjee S, Pramanik D, Dey SG, Dey A. Sengupta K, et al. Among authors: pramanik d. Dalton Trans. 2014 Sep 21;43(35):13377-83. doi: 10.1039/c4dt01991a. Dalton Trans. 2014. PMID: 25076262

7

Analogues of oxy-heme Aβ: reactive intermediates relevant to Alzheimer's disease.

Seal M, Mukherjee S, Pramanik D, Mittra K, Dey A, Dey SG. Seal M, et al. Among authors: pramanik d. Chem Commun (Camb). 2013 Feb 4;49(11):1091-3. doi: 10.1039/c2cc37626a. Chem Commun (Camb). 2013. PMID: 23282799

8

Active site environment of heme-bound amyloid β peptide associated with Alzheimer's disease.

Pramanik D, Dey SG. Pramanik D, et al. J Am Chem Soc. 2011 Jan 12;133(1):81-7. doi: 10.1021/ja1084578. Epub 2010 Dec 9. J Am Chem Soc. 2011. PMID: 21141958

9

Heme-Cu bound aβ peptides: spectroscopic characterization, reactivity, and relevance to Alzheimer's disease.

Pramanik D, Ghosh C, Dey SG. Pramanik D, et al. J Am Chem Soc. 2011 Oct 5;133(39):15545-52. doi: 10.1021/ja204628b. Epub 2011 Sep 13. J Am Chem Soc. 2011. PMID: 21870836

10

Apomyoglobin sequesters heme from heme bound Aβ peptides.

Pramanik D, Mukherjee S, Dey SG. Pramanik D, et al. Inorg Chem. 2013 Oct 7;52(19):10929-35. doi: 10.1021/ic401771j. Epub 2013 Sep 24. Inorg Chem. 2013. PMID: 24063254

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