Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019)

doi:10.3390/books978-3-0365-7320-5

dc.contributor.editor	Kuwajima, Kunihiro
dc.contributor.editor	Okamoto, Yuko
dc.contributor.editor	Knowles, Tuomas
dc.contributor.editor	Vendruscolo, Michele
dc.date.accessioned	2023-06-23T09:43:24Z
dc.date.available	2023-06-23T09:43:24Z
dc.date.issued	2023
dc.identifier	ONIX_20230623_9783036573212_34
dc.identifier.uri	https://directory.doabooks.org/handle/20.500.12854/100802
dc.description.abstract	This Special Issue is dedicated to the memory of the late Professor Sir Christopher M. Dobson (1949–2019), who made outstanding contributions to the advancement of studies on protein folding and its related areas and played an irreplaceable role in the promotion of protein science. This reprint contains 24 recent research papers (17 original papers and 7 review papers) on protein folding, misfolding, and amyloid formation, which often lead to various human diseases.
dc.language	English
dc.subject.classification	thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general	en_US
dc.subject.classification	thema EDItEUR::P Mathematics and Science::PS Biology, life sciences	en_US
dc.subject.other	14-3-3 proteins
dc.subject.other	molecular chaperone
dc.subject.other	amyloid β
dc.subject.other	α-synuclein
dc.subject.other	NMR spectroscopy
dc.subject.other	amyloid fibril
dc.subject.other	amyloidogenesis
dc.subject.other	aggregation
dc.subject.other	adsorption
dc.subject.other	Aβ 1-40 peptide
dc.subject.other	boundary of liquid phase
dc.subject.other	self-assembly
dc.subject.other	extraction
dc.subject.other	solubilization
dc.subject.other	toxic oligomers
dc.subject.other	Parkinson’s disease
dc.subject.other	familial mutations
dc.subject.other	α-helical structure
dc.subject.other	amyloid-beta
dc.subject.other	mutants
dc.subject.other	cholesterol
dc.subject.other	simulations
dc.subject.other	X-ray crystallography
dc.subject.other	phospholipase A1
dc.subject.other	homodimer
dc.subject.other	dimerization domain
dc.subject.other	catalytic triad
dc.subject.other	plant protein
dc.subject.other	molecular dynamics simulation
dc.subject.other	replica permutation method
dc.subject.other	amyloid-β
dc.subject.other	disaggregation
dc.subject.other	β-sheet
dc.subject.other	α-helix
dc.subject.other	interface
dc.subject.other	inhibitor
dc.subject.other	polyphenol
dc.subject.other	high-temperature reversible oligomerization
dc.subject.other	amyloidogenicity
dc.subject.other	oligomeric interface residues
dc.subject.other	thermal denaturation
dc.subject.other	mutational analysis
dc.subject.other	RHIM
dc.subject.other	TRIF
dc.subject.other	necroptosis
dc.subject.other	functional amyloid
dc.subject.other	fibrils
dc.subject.other	RIPK
dc.subject.other	turbulent mixing
dc.subject.other	continuous flow
dc.subject.other	fluorescence
dc.subject.other	reaction mechanism
dc.subject.other	protein folding
dc.subject.other	protein–ligand interactions
dc.subject.other	protein design
dc.subject.other	reverse fold
dc.subject.other	minimum frustration
dc.subject.other	protein structure prediction
dc.subject.other	sequence-structure alignment
dc.subject.other	template-based modeling
dc.subject.other	conditional random fields
dc.subject.other	boosted regression trees
dc.subject.other	CASP
dc.subject.other	hydrogen/deuterium exchange
dc.subject.other	dimethylsulfoxide
dc.subject.other	nuclear magnetic resonance
dc.subject.other	chaperonin
dc.subject.other	GroEL
dc.subject.other	protease
dc.subject.other	Lon protease
dc.subject.other	proteomics
dc.subject.other	proteostasis
dc.subject.other	Hfq hexamer
dc.subject.other	mutations
dc.subject.other	unfolding intermediates
dc.subject.other	thermodynamics
dc.subject.other	amyloid
dc.subject.other	insulin B chain
dc.subject.other	nucleation
dc.subject.other	prefibrillar aggregates
dc.subject.other	protofibrils
dc.subject.other	bacterial amyloid
dc.subject.other	biofilm
dc.subject.other	curli
dc.subject.other	FapC
dc.subject.other	imperfect repeats
dc.subject.other	neurodegeneration
dc.subject.other	oligomerisation
dc.subject.other	native-like
dc.subject.other	micelle
dc.subject.other	globular protein
dc.subject.other	rigid native state
dc.subject.other	molten globule
dc.subject.other	intrinsically disordered
dc.subject.other	functional state
dc.subject.other	unfolded state
dc.subject.other	coil
dc.subject.other	post-translational modifications
dc.subject.other	membrane
dc.subject.other	chaperone
dc.subject.other	statistical mechanical model
dc.subject.other	WSME model
dc.subject.other	folding kinetics
dc.subject.other	folding intermediates
dc.subject.other	protein dynamics
dc.subject.other	amyloid fibrils
dc.subject.other	amorphous aggregation
dc.subject.other	β2-microglobulin
dc.subject.other	protein misfolding
dc.subject.other	solubility
dc.subject.other	supersaturation
dc.subject.other	ultrasonication
dc.subject.other	cryo-electron microscopy
dc.subject.other	fibril
dc.subject.other	ganglioside
dc.subject.other	cancer
dc.subject.other	prion
dc.subject.other	folding
dc.subject.other	pathway
dc.subject.other	interdiction
dc.subject.other	peptide
dc.subject.other	enhanced sampling method
dc.subject.other	molecular force fields
dc.subject.other	van der Waals interaction
dc.subject.other	CHARMM36m
dc.subject.other	NBFIX
dc.subject.other	intrinsically disordered proteins
dc.subject.other	crowding simulations
dc.title	Frontiers in Protein Folding and Related Areas – in Memory of Professor Sir Christopher M. Dobson (1949–2019)
dc.type	book
oapen.identifier.doi	10.3390/books978-3-0365-7320-5
oapen.relation.isPublishedBy	46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn	9783036573212
oapen.relation.isbn	9783036573205
oapen.pages	418
oapen.place.publication	Basel

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