The Amazing World of IDPs in Human Diseases

It is now clearly established that some proteins or protein regions are devoid of any stable secondary and/or tertiary structure under physiological conditions, but still possess fundamental biological functions. These intrinsically disordered proteins (IDPs) or regions (IDRs) have peculiar features...

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Detalhes bibliográficos
Corporate Authors: Monti, Simona Maria, De Simone, Giuseppina, Langella, Emma
Formato: Livro
Idioma:Inglês
Publicado em: MDPI - Multidisciplinary Digital Publishing Institute 2021
Assuntos:
bic Book Industry Communication::G Reference, information & interdisciplinary subjects::GP Research & information: general
bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences
alpha-synuclein
NMR
secondary structure propensity
pre-structured motifs (PreSMos)
intrinsically disordered protein
ubiquitin-proteasome system
intrinsically disordered proteins
protein misfolding
molecular recognition features
cancer
neurodegenerative diseases
protein degradation
EPR spectroscopy
isothermal titration calorimetry
protein-ligand interaction
site-directed spin labeling
protein structural dynamics
WASp interacting protein
protein–protein interactions
actin
cytoskeleton remodeling
SH3 domain
proline-rich motif
single nucleotide variants
interface core and rim
human disease
intrinsically disordered regions
linear motifs
gene duplications
de novo
evolutionary origin
circular dichroism
flexibility
fluorescence
importin
isothermal titration calorimetry (ITC)
molecular docking
nuclear magnetic resonance (NMR)
nuclear protein 1 (NPR1)
peptide
Methyl-CpG-binding protein 2 (MeCP2)
Rett syndrome
intrinsically disordered protein (IDP)
protein stability
protein-DNA interaction
proteostasis
ubiquitin independent degradation
NADH-26S proteasome
n/a
Acesso em linha:https://directory.doabooks.org/handle/20.500.12854/76426
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