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Hire Dr. Rajaraman K.
USD 150 /hr
Free lance biochemist and structural biologist
Subject Matter Expertise
Vice President Discovery Research
March 2018 - Present
Post Doctoral Associate
Whitehead Institute for Biomedical Research
October 2001 - May 2010
Centre for Cellular and Molecular Biology CSIR
June 1995 - May 2001
- Certification details not provided.
(2019). Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif . Journal of molecular biology.
(2017). Conformation as the Therapeutic Target for Neurodegenerative Diseases . Current Alzheimer research.
(2016). NPT088 reduces both amyloid-β and tau pathologies in transgenic mice . Alzheimer's & dementia (New York, N. Y.).
(2015). Remodeling Amyloid Fibers: Baker's Yeast Shows Us the Way . Chemistry & biology.
(2014). A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies . Journal of molecular biology.
(2012). Conserved features of intermediates in amyloid assembly determine their benign or toxic states . Proceedings of the National Academy of Sciences of the United States of America.
(2011). Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins . Molecular cell.
(2011). The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication . The EMBO journal.
(2008). Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs . Proceedings of the National Academy of Sciences of the United States of America.
(2007). A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures . Proceedings of the National Academy of Sciences of the United States of America.
(2004). Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro . Proceedings of the National Academy of Sciences of the United States of America.
(2001). Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation . FEBS letters.
(1998). The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin . Biochemical and biophysical research communications.
(1998). Structural perturbation of alpha-crystallin and its chaperone-like activity . International journal of biological macromolecules.
(1996). Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin . The Journal of biological chemistry.