(Q46402210)

21 December 2017

title

Conversion of yeast phosphoglycerate kinase into amyloid-like structure (English)

1 reference

21 December 2017

author name string

Damaschun G

1

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21 December 2017

Damaschun H

2

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21 December 2017

Fabian H

3

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21 December 2017

Gast K

4

1 reference

21 December 2017

Kröber R

5

1 reference

21 December 2017

Wieske M

6

1 reference

21 December 2017

Zirwer D

7

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21 December 2017

language of work or name

English

0 references

publication date

1 May 2000

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21 December 2017

published in

Proteins

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21 December 2017

volume

39

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21 December 2017

issue

3

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21 December 2017

page(s)

204-211

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21 December 2017

From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

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The environmental dependency of protein folding best explains prion and amyloid diseases

21 January 2018

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The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

21 January 2018

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Protein aggregation: folding aggregates, inclusion bodies and amyloid

21 January 2018

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Structural and kinetic features of amyloid beta-protein fibrillogenesis.

21 January 2018

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Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease

21 January 2018

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Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

21 January 2018

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Association-induced folding of globular proteins

21 January 2018

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Amyloid fibril formation by an SH3 domain

21 January 2018

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Designing conditions for in vitro formation of amyloid protofilaments and fibrils

21 January 2018

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Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin

21 January 2018

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Application of dynamic light scattering to studies of protein folding kinetics.

21 January 2018

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The folding and mutual interaction of the domains of yeast 3-phosphoglycerate kinase

21 January 2018

1 reference

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53 Scattering studies of ribosomes and ribosomal components

21 January 2018

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Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study.

21 January 2018

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The use and misuse of FTIR spectroscopy in the determination of protein structure

21 January 2018

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In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation

21 January 2018

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Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease.

21 January 2018

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Amyloid: microscopic demonstration, classification and clinical correlation

21 January 2018

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Supramolecular structure of the recombinant murine small heat shock protein hsp25

21 January 2018

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The structure of amyloid fibrils by electron microscopy and X-ray diffraction

21 January 2018

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Analysis of x-ray diffraction patterns from amyloid of biopsied vitreous humor and kidney of transthyretin (TTR) Met30 familial amyloidotic polyneuropathy (FAP) patients: axially arrayed TTR monomers constitute the protofilament

21 January 2018

1 reference

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Proteins can adopt totally different folded conformations

21 January 2018

1 reference

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Protein secondary structures in water from second-derivative amide I infrared spectra

21 January 2018

1 reference

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Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands

21 January 2018

1 reference

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Röntgenuntersuchung gelöster Fadenmoleküle

21 January 2018

1 reference

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10.1002/(SICI)1097-0134(20000515)39:3<204::AID-PROT20>3.0.CO;2-8

21 January 2018

Identifiers

DOI

1 reference

21 December 2017

release_jpnjtmhc5jhrxlt3b4jmvc6hly

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/jpnjtmhc5jhrxlt3b4jmvc6hly

mapped directly with Wikidata item

24 November 2022

based on heuristic

PubMed ID

10737941

1 reference

21 December 2017