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English
Optimization of Hydrophobic Domains in Peptides that Undergo Transformation from α-Helix to β-Fibril
scientific article published on 01 January 1999
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
title
Optimization of hydrophobic domains in peptides that undergo transformation from alpha-helix to beta-fibril
(English)
1 reference
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Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
main subject
hydrophobicity
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author
Hisakazu Mihara
series ordinal
3
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Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
author name string
Y Takahashi
series ordinal
1
1 reference
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Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
A Ueno
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
language of work or name
English
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publication date
1 January 1999
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
published in
Bioorganic & Medicinal Chemistry
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
volume
7
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Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
issue
1
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
page(s)
177-185
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Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
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For protein misassembly, it's the "I" decade
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Engineering peptides and proteins that undergo alpha-to-beta transitions
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Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition
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Prion Diseases and the BSE Crisis
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NMR structure of the mouse prion protein domain PrP(121-231)
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NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)
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Prion (PrPSc)-specific epitope defined by a monoclonal antibody
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A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform 1 1Edited by M. Yaniv
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Amyloid beta-protein and the genetics of Alzheimer's disease
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Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides
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Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
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High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
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High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein
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The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
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Context-dependent secondary structure formation of a designed protein sequence
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Protein alchemy: Changing β-sheet into α-helix
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De novo protein design: from molten globules to native-like states
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Native-like and structurally characterized designed alpha-helical bundles
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Amphiphilic Secondary Structure: Design of Peptide Hormones
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Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes
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Direct conversion of an oligopeptide from a beta-sheet to an alpha-helix: a model for amyloid formation
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Super-Secondary Structure with Amphiphilicβ-Strands Probed by Pyrenylalanine
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Conformational switching in designed peptides: the helix/sheet transition
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X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
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Haem binding and catalytic activity of two-α-helix peptide annealed by trifluoroethanol
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Prediction of protein conformation
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Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
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Putting prions to the test
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Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR
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Deprotection of the S-trimethylacetamidomethyl (Tacm) group using silver tetrafluoroborate: application to the synthesis of porcine brain natriuretic peptide-32 (pBNP-32).
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Identifiers
DOI
10.1016/S0968-0896(98)00236-3
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
PubMed publication ID
10199667
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10199667
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10199667%20AND%20SRC:MED&resulttype=core&format=json
retrieved
4 December 2019
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