Intracellular peptide library screening to derive inhibitors of Parkinson's disease associated α-synuclein aggregation

Autor: Cheruvara, Harish

Aggregation of α-synuclein (α-syn) into toxic fibrils is a pathogenic hallmark of Parkinson’s disease (PD). This research aimed to develop peptides capable of inhibiting α-syn aggregation using a semi-rational design combined with a multiplexed

Externí odkaz: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.679515

Intracellular Screening of a Peptide Library to Derive a Potent Peptide Inhibitor of α-Synuclein Aggregation

Autor: Cheruvara, Harish ^‡, Allen-Baume, Victoria L. ^‡, Kad, Neil M. ^{§, 1}, Mason, Jody M. ^{¶, 1, 2}

Publikováno v: In Journal of Biological Chemistry 20 March 2015 290(12):7426-7435

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Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomers

Autor: Acerra, Nicola, Kad, Neil. M., Cheruvara, Harish, Mason, Jody M.

Publikováno v: Acerra, N, Kad, N M, Cheruvara, H & Mason, J M 2014, ' Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ 42 oligomers ', Protein Science, vol. 23, no. 9, pp. 1262-1274 . https://doi.org/10.1002/pro.2509

The β-amyloid (Aβ) peptide aggregates into a number of soluble and insoluble forms, with soluble oligomers thought to be the primary factor implicated in Alzheimer's disease pathology. As a result, a wide range of potential aggregation inhibitors h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______1378::850ba11942dc58d0d19e27dd4df1c466
https://purehost.bath.ac.uk/ws/files/136920942/Intracellular_selection_of_peptide_inhibitors_that_target_disulphide_bridged_A_42_oligomers.pdf

High-Throughput Production and Optimization of Membrane Proteins After Expression in Mammalian Cells.

Autor: Gamage N; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK.; Structural Biology, The Rosalind Franklin Institute, Harwell Science & Innovation Campus, Didcot, UK., Cheruvara H; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK., Harrison PJ; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK., Birch J; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK., Hitchman CJ; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK.; Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK., Olejnik M; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK., Owens RJ; Structural Biology, The Rosalind Franklin Institute, Harwell Science & Innovation Campus, Didcot, UK.; The Wellcome Centre for Human Genetics, Division of Structural Biology, University of Oxford, Oxford, UK., Quigley A; Membrane Protein Laboratory, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK. andrew.quigley@diamond.ac.uk.; Research Complex at Harwell (RCaH), Harwell Science and Innovation Campus, Didcot, UK. andrew.quigley@diamond.ac.uk.

Publikováno v: Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2023; Vol. 2652, pp. 79-118.