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Protein misfolding, evolution and disease
scientific article (publication date: September 1999)
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instance of
scholarly article
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review article
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Europe PubMed Central
title
Protein misfolding, evolution and disease
(English)
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main subject
protein evolution
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author name string
C M Dobson
series ordinal
1
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language of work or name
English
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publication date
September 1999
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published in
Trends in Biochemical Sciences
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volume
24
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issue
9
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page(s)
329-32
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cites work
From computer simulations to human disease: emerging themes in protein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Retrograde protein translocation: ERADication of secretory proteins in health and disease
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Defective protein folding as a basis of human disease
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Amyloidosis
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7 January 2021
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The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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Glutamine repeats and neurodegenerative diseases: molecular aspects
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The structure of amyloid fibrils by electron microscopy and X-ray diffraction
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Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
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Deadly conformations--protein misfolding in prion disease
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7 January 2021
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Prion diseases and the BSE crisis
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7 January 2021
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Molecular genetics of transmissible spongiform encephalopathies
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7 January 2021
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Prion protein and the transmissible spongiform encephalopathies
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7 January 2021
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Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.
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7 January 2021
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Protein aggregation: folding aggregates, inclusion bodies and amyloid
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7 January 2021
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Amyloid fibril formation by an SH3 domain
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
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7 January 2021
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Designing conditions for in vitro formation of amyloid protofilaments and fibrils
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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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The fundamentals of protein folding: bringing together theory and experiment
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Physical properties of cytoplasm
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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inferred from DOI database lookup
Conserved residues and the mechanism of protein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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inferred from DOI database lookup
Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis
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Crossref
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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inferred from DOI database lookup
Prions of yeast and fungi. Proteins as genetic material
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Crossref
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Proteins, RNAs and chaperones in enzyme evolution: a folding perspective
1 reference
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https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Lectins as chaperones in glycoprotein folding
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reference URL
https://api.crossref.org/works/10.1016%2FS0968-0004%2899%2901445-0
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7 January 2021
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Identifiers
DOI
10.1016/S0968-0004(99)01445-0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1530987
OpenCitations bibliographic resource ID
1530987
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1530987
PubMed publication ID
10470028
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1530987
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