RAYCHAUDHURI LAB @ CSIR-CCMB, Hyderabad
 
Publications from CSIR-CCMB
  • Cytoplasmic sequestration of the RhoA effector mDiaphanous1 by Prohibitin2 promotes muscle differentiation.Saleh A, Subramaniam G, Raychaudhuri S, Dhawan JScientific Reports. 2019. 9(1):8302. doi: 10.1038/s41598-019-44749-4

  • Aggregation of Respiratory Complex Subunits Marks the Onset of Proteotoxicity in Proteasome Inhibited Cells.Rawat S, Anusha V, Jha M, Sreedurgalakshmi K, Raychaudhuri S.J Mol Biol.. 2019. pii: S0022-2836(19)30031-2. doi: 10.1016/j.jmb.2019.01.022.

  • Identification of a splice variant of optineurin which is defective in autophagy and phosphorylation Moharir SC, Bansal M, Ramachandran G, Ramaswamy R, Rawat S, Raychaudhuri S, Swarup G.Biochim Biophys Acta Mol Cell Res.. 2018; 1865(11 Pt A):1526-1538

  • Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity. Raychaudhuri S, Banerjee R, Mukhopadhyay S, Bhattacharyya NP. Journal of Biosciences. 2014; 39(4): 114.[DOI 10.1007/s12038-014-9442-z] *Corresponding author.

Publications from SR
  • Interplay of Acetyltransferase EP300 and the Proteasome System in Regulating Heat Shock Transcription Factor 1. Raychaudhuri S, Loew C, Koerner R, Pinkert S, Theis M, Hayer-Hartl M, Buchholz F, Hartl FU. Cell. 2014; 156: 975-985.

  • Firefly luciferase mutants as sensors of proteome stress. Gupta R, Kasturi P, Bracher A, Loew C, Zheng M, Villella A, Garza D, Hartl FU, Raychaudhuri S*. Nature Methods. 2011; 8(10):879-84. PMID: 21892152. *Corresponding author.

  • Protein Folding in the Cytoplasm and the Heat Shock Response. Vabulas M, Raychaudhuri S, Hayer-Hartl M, Hartl FU. Cold Spring Harb Perspect Biol. 2010; 2(12):a004390. PMID: 21123396

  • Identification of HYPK interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death. Roy Choudhury K, Raychaudhuri S, Bhattacharyya NP. PLoS One. 2012; 7(12): e51415.

  • Spectroscopic studies reveal the mode of variation in the residual structure of an intrinsically unstructured protein HYPK. Raychaudhuri S, Roy Choudhury K, Palchoudhuri S, Chopra S, Bhattacharyya NP, Mukhopadhyay D. J Biophysical Chemistry. 2011; 2 (4), 434-442.

  • The role of intrinsically unstructured proteins in neurodegenerative diseases. Raychaudhuri S, Dey S, Bhattacharyya NP, Mukhopadhyay D. PLoS One. 2009; 4(5):e5566. PMID: 19440375

  • Huntingtin interacting protein HYPK is intrinsically unstructured. Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. Proteins. 2008; 71(4):1686-98.PMID: 18076027

  • HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Raychaudhuri S, Sinha M, Mukhopadhyay D, Bhattacharyya NP. Hum Mol Genet. 2008;17(2):240-55. PMID: 17947297 **Recommended by F1000 Biology.

  • Increased caspase-2, calpain activations and decreased mitochondrial complex II activity in cells expressing exogenous huntingtin exon 1 containing CAG repeat in the pathogenic range. Majumder P, Raychaudhuri S, Chattopadhyay B, Bhattacharyya NP. Cell Mol Neurobiol. 2007; 27(8):1127-45. PMID: 17902043
 

    Copyright (C) 2014, Swasti Raychaudhuri. All rights reserved.