Results 101 to 110 of about 23,829 (240)

The binding mechanisms of intrinsically disordered proteins

, 2014
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins are very common and instrumental for cellular signaling.
Gianni, Stefano, Jemth, Per, Jemth P., Dogan, Jakob, Dogan J, Dogan, Jakob,, Jemth, Per,   +6 more
core   +1 more source

Bone Grafts: Everything You Need to Know

Journal of Periodontal Research, EarlyView.
This review classifies bone grafts (autograft, allograft, xenograft, synthetic) by source and osteogenic/inductive/conductive potential, linking material properties and mechanisms to clinical indications in periodontal and dental regeneration. Key challenges—limited osteoinduction, poor vascularisation, unbalanced resorption, handling difficulties, and
Håvard Jostein Haugen, Javier Sanz, Giuseppe Perale, Augustine Mark Saiz, Mario Romandini, Maryam Rahmati   +5 more
wiley   +1 more source

Archaic chaos: intrinsically disordered proteins in Archaea [PDF]

, 2010
Background: Many proteins or their regions known as intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack unique 3D structure in their native states under physiological conditions yet fulfill key biological functions ...
Williams, Robert W., Uversky, Vladimir N., Dunker, A. Keith, Oldfield, Christopher J., Bin Xue, Robert W Williams, Vladimir N Uversky, A Dunker, Xue, Bin, Christopher J Oldfield, A Keith Dunker   +10 more
core   +1 more source

PolyProline Predictor: A web server for empirical sequence‐based prediction of polyproline II helices

Protein Science, Volume 35, Issue 7, July 2026.
Abstract Polyproline II (PPII) helices are extended left‐handed secondary structures increasingly recognized for their roles in molecular recognition, signaling and within intrinsically disordered regions of proteins. Despite their functional importance, predicting regions with propensity to form PPII helices from sequence alone remains challenging due
Rubén López‐Sánchez, David Pantoja‐Uceda, Miguel Mompeán, Douglas V. Laurents   +3 more
wiley   +1 more source

Cold stability of intrinsically disordered proteins

, 2009
Contrary to globular proteins, intrinsically disordered proteins (IDPs) lack a folded structure and they do not lose solubility at elevated temperatures. Although this should also be true at low temperatures, cold stability of IDPs has not been addressed
Friedrich, Peter, Tantos, Agnes, Tompa, Peter   +2 more
core   +1 more source

Ensemble docking for intrinsically disordered proteins

bioRxiv
Intrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable ...
A. Dhar, Thomas R. Sisk, Paul Robustelli
semanticscholar   +1 more source

Intrinsically Disordered Proteins in Cellular Signaling and Regulation

Nature reviews. Molecular cell biology, 2014
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same polypeptide to undertake different interactions with different consequences.
Peter E. Wright, H. J. Dyson
semanticscholar   +1 more source

Lipid Dynamics in the Amyloid Cascade Hypothesis: Evaluating the Biological Relevance of In Vitro Models

ChemBioChem, Volume 27, Issue 11, 15 June 2026.
This review reconsiders the amyloid cascade by placing lipid dynamics at its core. It shows that free lipids, governed by critical micellar concentration, act as pathological chaperones that redirect amyloid aggregation toward membrane‐damaging species.
Sofia Serravalle, Fabio Lolicato, Carmelo Tempra, Martina Pannuzzo, Michele F. M. Sciacca, Danilo Milardi, Carmelo La Rosa   +6 more
wiley   +1 more source

Comprehensive Biophysical Profiling Evidences Self‐Oligomerization of Bacterially Expressed Pc Protein

ChemBioChem, Volume 27, Issue 11, 15 June 2026.
Polycomb (Pc), a core component of Polycomb Repressive Complex 1 (PRC1), is largely intrinsically disordered yet forms buffer‐ and concentration‐dependent higher‐order assemblies. Integrative biophysical analysis and cryo‐electron microscopy reveal dynamic, heterogeneous oligomers, whereas AlphaFold modeling suggests that structural organization is ...
Maria Zahid, Sabin Prajapati, Ghazaleh Alamdari, Kai Tittmann, Selin Kara   +4 more
wiley   +1 more source

Intrinsic Fluorescence of Intrinsically Disordered Proteins

, 2012
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, Paolo Neyroz, Stefano Ciurli, CIURLI, STEFANO LUCIANO   +3 more
core   +1 more source