Maji SK - Search Results

1

Navalkar A, Ghosh S, Pandey S, Paul A, Datta D, Maji SK. Navalkar A, et al. Among authors: maji sk. Biochemistry. 2020 Jan 21;59(2):146-155. doi: 10.1021/acs.biochem.9b00796. Epub 2019 Oct 21. Biochemistry. 2020. PMID: 31603660 Review.

2

Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid β-protein aggregation and toxicity.

Singh PK, Maji SK. Singh PK, et al. Among authors: maji sk. Cell Biochem Biophys. 2012 Sep;64(1):29-44. doi: 10.1007/s12013-012-9364-z. Cell Biochem Biophys. 2012. PMID: 22628076

3

The Parkinson's disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro.

Ghosh D, Mondal M, Mohite GM, Singh PK, Ranjan P, Anoop A, Ghosh S, Jha NN, Kumar A, Maji SK. Ghosh D, et al. Among authors: maji sk. Biochemistry. 2013 Oct 8;52(40):6925-7. doi: 10.1021/bi400999d. Epub 2013 Sep 23. Biochemistry. 2013. PMID: 24047453

4

Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation.

Jha NN, Anoop A, Ranganathan S, Mohite GM, Padinhateeri R, Maji SK. Jha NN, et al. Among authors: maji sk. Biochemistry. 2013 Dec 10;52(49):8800-10. doi: 10.1021/bi401398k. Epub 2013 Nov 22. Biochemistry. 2013. PMID: 24236650

5

Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.

Sahay S, Anoop A, Krishnamoorthy G, Maji SK. Sahay S, et al. Among authors: maji sk. Biochemistry. 2014 Feb 11;53(5):807-9. doi: 10.1021/bi401543z. Epub 2014 Jan 27. Biochemistry. 2014. PMID: 24450731

6

Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion.

Anoop A, Ranganathan S, Das Dhaked B, Jha NN, Pratihar S, Ghosh S, Sahay S, Kumar S, Das S, Kombrabail M, Agarwal K, Jacob RS, Singru P, Bhaumik P, Padinhateeri R, Kumar A, Maji SK. Anoop A, et al. Among authors: maji sk. J Biol Chem. 2014 Jun 13;289(24):16884-903. doi: 10.1074/jbc.M114.548354. Epub 2014 Apr 29. J Biol Chem. 2014. PMID: 24782311 Free PMC article.

7

Investigating the intrinsic aggregation potential of evolutionarily conserved segments in p53.

Ghosh S, Ghosh D, Ranganathan S, Anoop A, P SK, Jha NN, Padinhateeri R, Maji SK. Ghosh S, et al. Among authors: maji sk. Biochemistry. 2014 Sep 30;53(38):5995-6010. doi: 10.1021/bi500825d. Epub 2014 Sep 17. Biochemistry. 2014. PMID: 25181279

8

The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding.

Ghosh D, Sahay S, Ranjan P, Salot S, Mohite GM, Singh PK, Dwivedi S, Carvalho E, Banerjee R, Kumar A, Maji SK. Ghosh D, et al. Among authors: maji sk. Biochemistry. 2014 Oct 21;53(41):6419-21. doi: 10.1021/bi5010365. Epub 2014 Oct 10. Biochemistry. 2014. PMID: 25268550

9

Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules.

Jacob RS, Das S, Ghosh S, Anoop A, Jha NN, Khan T, Singru P, Kumar A, Maji SK. Jacob RS, et al. Among authors: maji sk. Sci Rep. 2016 Mar 23;6:23370. doi: 10.1038/srep23370. Sci Rep. 2016. PMID: 27004850 Free PMC article.

10

Evidence of a Prion-Like Transmission of p53 Amyloid in Saccharomyces cerevisiae.

Sengupta S, Maji SK, Ghosh SK. Sengupta S, et al. Among authors: maji sk. Mol Cell Biol. 2017 Aug 28;37(18):e00118-17. doi: 10.1128/MCB.00118-17. Print 2017 Sep 15. Mol Cell Biol. 2017. PMID: 28630281 Free PMC article. Retracted.

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