Results 101 to 110 of about 10,740 (213)
Biophysical ChemistryThe fields of allostery and amyloid-related pathologies, such as Parkinson's disease (PD), have been extensively explored individually, but less is known about how amyloids control allostery. Recent advancements have revealed that amyloids can drive allosteric effects in both intrinsically disordered proteins, such as alpha-synuclein (αS), and multi ...
Jaskiran, Garcha +3 more
openaire +2 more sources
CRISPR/Cas13a: Compensatory Target Activation Mechanism
Advanced Science, Volume 13, Issue 32, 9 June 2026.CRISPR/Cas13a‐CTAM as a novel compensatory target activation mechanism that enables synergistic activation of Cas13a via two independently editable short RNA effectors. This dual‐effector system maintains enzymatic activity comparable to traditional single‐effector while significantly enhancing flexibility, sensitivity, and application scope.
Bowen Jiang +8 more
wiley +1 more source
Dynamic disorder is crucial for mitochondrial protein import
Protein Science, Volume 35, Issue 6, June 2026.Abstract The import of proteins into mitochondria poses fundamental mechanistic challenges: aggregation‐prone precursor proteins must be maintained in aqueous compartments and threaded through narrow pores without becoming stuck or mislocalized. Recent evidence from mitochondrial protein import studies and other chaperone systems underscores the ...
Jakob Schneider +3 more
wiley +1 more source
Use of biomolecular emulator for characterizing flexible proteins by small‐angle x‐ray scattering
Protein Science, Volume 35, Issue 6, June 2026.Abstract Flexible proteins populate heterogeneous conformational ensembles that are essential for their function. Small‐angle x‐ray scattering (SAXS) is widely used to study protein structure in solution and to characterize conformational heterogeneity.
Yoni Haitin, Bar Manori, Moshe Giladi
wiley +1 more source
Multi-scale Modelling of Allostery in Protein Homodimers [PDF]
, 2015 Allostery is a form of signalling within biomolecules such that ligand binding to a protein affects its activity at a second site. Allostery was described by early models to be driven by structural changes in the protein. However, more recently there has
BURNELL, DAVID
core
Cooperativity and allostery in haemoglobin function. [PDF]
, 2008 Tetrameric haemoglobins display a cooperative ligand binding behaviour, which has been attributed to the functional interrelationship between multiple ligand binding sites.
CIACCIO, CHIARA +7 more
core +1 more source
Insights into the activation mechanism of class I HDAC complexes by inositol phosphates
Nature Communications, 2016 Class I histone deacetylase complexes can be activated by inositol phosphates. Here, the authors investigate the stereochemical requirements for activation; use the crystal structure to understand substrate recognition, and suggest an entropically driven
Peter J. Watson +9 more
doaj +1 more source
ERK autoinhibition mechanism informs a drug combination strategy
Protein Science, Volume 35, Issue 6, June 2026.Abstract ERK is a key regulator in the MAPK pathway, controlling essential cell processes through dual‐phosphorylation‐based activation. We investigate the conformational equilibrium between inactive and active ERK states, which is controlled allosterically by its structurally unique C‐terminal L16 segment.
Clil Regev, Hyunbum Jang, Ruth Nussinov
wiley +1 more source
Correlated Motions and Allostery [PDF]
, 2011 Allostery describes altered protein function at one site due to a perturbation at another site. One mechanism of allostery involves correlated motions, which can occur even in the absence of substantial conformational change.
McClendon, Christopher
core
Mapping Polymerization and Allostery of Hemoglobin S Using Point Mutations [PDF]
, 2013 Hemoglobin is a complex system that undergoes conformational changes in response to oxygen, allosteric effectors, mutations, and environmental changes.
Weinkam, Patrick, Sali, Andrej
core +1 more source