Intrinsically disordered proteins: an overview
R Trivedi, HA Nagarajaram - International journal of molecular sciences, 2022 - mdpi.com
Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …
structure under physiological conditions; instead, they adopt multiple interconverting …
Unusual biophysics of intrinsically disordered proteins
VN Uversky - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2013 - Elsevier
Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …
protein functionality requires close consideration of the fact that many functional proteins do …
Critical assessment of protein intrinsic disorder prediction
M Necci, D Piovesan, SCE Tosatto - Nature methods, 2021 - nature.com
Intrinsically disordered proteins, defying the traditional protein structure–function paradigm,
are a challenge to study experimentally. Because a large part of our knowledge rests on …
are a challenge to study experimentally. Because a large part of our knowledge rests on …
On the binding affinity of macromolecular interactions: daring to ask why proteins interact
PL Kastritis, AMJJ Bonvin - Journal of The Royal Society …, 2013 - royalsocietypublishing.org
Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …
underlying cellular function. The binding affinity, defined as the strength of these …
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids
Protein intrinsic disorder is becoming increasingly recognized in proteomics research. While
lacking structure, many regions of disorder have been associated with biological function …
lacking structure, many regions of disorder have been associated with biological function …
Understanding protein non-folding
VN Uversky, AK Dunker - Biochimica et Biophysica Acta (BBA)-Proteins …, 2010 - Elsevier
This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …
form rigid 3-D structures under physiological conditions, either along their entire lengths or …
A decade and a half of protein intrinsic disorder: biology still waits for physics
VN Uversky - Protein Science, 2013 - Wiley Online Library
The abundant existence of proteins and regions that possess specific functions without
being uniquely folded into unique 3D structures has become accepted by a significant …
being uniquely folded into unique 3D structures has become accepted by a significant …
Intrinsically Disordered Proteins in Human Diseases: Introducing the D2 Concept
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under
physiological conditions in vitro. They are highly abundant in nature and their functional …
physiological conditions in vitro. They are highly abundant in nature and their functional …
P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer's disease
KM Farmer, G Ghag, N Puangmalai… - Acta neuropathologica …, 2020 - Springer
The transcription factor, p53, is critical for many important cellular functions involved in
genome integrity, including cell cycle control, DNA damage response, and apoptosis …
genome integrity, including cell cycle control, DNA damage response, and apoptosis …
Intrinsically disordered proteins from A to Z
VN Uversky - The international journal of biochemistry & cell biology, 2011 - Elsevier
The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …