(Q38347673)

English

Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS).

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Europe PubMed Central

PubMed publication ID

2 September 2017

Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ANS). (English)

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Europe PubMed Central

PubMed publication ID

2 September 2017

prion protein family

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Yraima Cordeiro

1

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Europe PubMed Central

PubMed publication ID

2 September 2017

5

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Europe PubMed Central

PubMed publication ID

2 September 2017

object named as

Débora Foguel

4

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author name string

Luís Maurício T R Lima

2

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Europe PubMed Central

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2 September 2017

Mariana P B Gomes

3

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Europe PubMed Central

PubMed publication ID

2 September 2017

language of work or name

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publication date

21 November 2003

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Europe PubMed Central

PubMed publication ID

2 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

2 September 2017

279

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Europe PubMed Central

PubMed publication ID

2 September 2017

7

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Europe PubMed Central

PubMed publication ID

2 September 2017

5346-5352

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

1 reference

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Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein

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A novel generation of heparan sulfate mimetics for the treatment of prion diseases.

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Cellular heparan sulfate participates in the metabolism of prions

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DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation

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DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid

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Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro

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RNA molecules stimulate prion protein conversion

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Novel therapeutic uses for porphyrins and phthalocyanines in the transmissible spongiform encephalopathies

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Elimination of prions by branched polyamines and implications for therapeutics

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The anti-prion activity of Congo red. Putative mechanism

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Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation

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Potent inhibition of scrapie prion replication in cultured cells by bis-acridines

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Inhibition of viral capsid assembly by 1,1'-bi(4-anilinonaphthalene-5-sulfonic acid).

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Virus inactivation by anilinonaphthalene sulfonate compounds and comparison with other ligands

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Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease

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Prion protein gene variation among primates

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Conformational transitions in peptides containing two putative alpha-helices of the prion protein.

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The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state

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Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase.

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Prion diseases: a nucleic-acid accomplice?

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New perspectives for prion therapeutics meeting. Prion disease treatment's early promise unravels.

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Tetracyclines affect prion infectivity

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Influence of backbone conformation on protein aggregation

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The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL.

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Stabilization of partially folded conformation during alpha-synuclein oligomerization in both purified and cytosolic preparations

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Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

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Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells

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Quinacrine does not prolong survival in a murine Creutzfeldt-Jakob disease model

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Molecular genetics of transmissible spongiform encephalopathies

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Prion Protein Interaction with Glycosaminoglycan Occurs with the Formation of Oligomeric Complexes Stabilized by Cu(II) Bridges

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Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401

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Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding

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Identifiers

10.1074/JBC.M312262200

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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