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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Year of Publication:2021
Language:English
Physical Description:1 electronic resource (196 p.)
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spelling Monti, Simona Maria edt
The Amazing World of IDPs in Human Diseases
Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021
1 electronic resource (196 p.)
text txt rdacontent
computer c rdamedia
online resource cr rdacarrier
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 due to their plasticity such as the capacity to bind their biological targets with high specificity and low affinity, and the possibility of interaction with numerous partners. A correlation between intrinsic disorder and various human diseases such as cancer, diabetes, amyloidoses and neurodegenerative diseases is now evident, highlighting the great importance of the topic. In this volume, we have collected recent high-quality research about IDPs and human diseases. We have selected nine papers which deal with a wide range of topics, from neurodegenerative disease to cancer, from IDR-mediated interactions to bioinformatics tools, all related to IDP peculiar features. Recent advances in the IDPs/IDRs issue are here presented, contributing to the progress of knowledge of the intrinsic disorder field in human disease.
English
Research & information: general bicssc
Biology, life sciences bicssc
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
3-0365-1028-1
3-0365-1029-X
De Simone, Giuseppina edt
Langella, Emma edt
Monti, Simona Maria oth
De Simone, Giuseppina oth
Langella, Emma oth
language English
format eBook
author2 De Simone, Giuseppina
Langella, Emma
Monti, Simona Maria
De Simone, Giuseppina
Langella, Emma
author_facet De Simone, Giuseppina
Langella, Emma
Monti, Simona Maria
De Simone, Giuseppina
Langella, Emma
author2_variant s m m sm smm
s g d sg sgd
e l el
author2_role HerausgeberIn
HerausgeberIn
Sonstige
Sonstige
Sonstige
title The Amazing World of IDPs in Human Diseases
spellingShingle The Amazing World of IDPs in Human Diseases
title_full The Amazing World of IDPs in Human Diseases
title_fullStr The Amazing World of IDPs in Human Diseases
title_full_unstemmed The Amazing World of IDPs in Human Diseases
title_auth The Amazing World of IDPs in Human Diseases
title_new The Amazing World of IDPs in Human Diseases
title_sort the amazing world of idps in human diseases
publisher MDPI - Multidisciplinary Digital Publishing Institute
publishDate 2021
physical 1 electronic resource (196 p.)
isbn 3-0365-1028-1
3-0365-1029-X
illustrated Not Illustrated
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