Results 1 to 10 of about 11,653 (194)

Allostery Frustrates the Experimentalist [PDF]

Journal of Molecular Biology, 2023
Proteins interact with other proteins, with nucleic acids, lipids, carbohydrates and various small molecules in the living cell. These interactions have been quantified and structurally characterized in numerous studies such that we today have a comprehensive picture of protein structure and function.
Per Jemth, Stefano Gianni
exaly   +5 more sources

Supramolecular Allostery Achieves Tunable Luminescence Aromatic Bridged Phenothiazine Noncovalent Frameworks. [PDF]

Adv Sci (Weinh)
Tunable luminescent supramolecular organic framework enabled by multiple allosteric effects, composed of a tetracation vinylphenylpyridinium‐modified aromatic‐bridged phenothiazine guest and cucurbit[8]uril, not only exhibits unique guest oxidation‐driven NIR luminescence blue‐shift and effectively enhances the quantum yield by 46‐fold to 22.2% but ...
Lu X, Chen J, Yu J.
europepmc   +2 more sources

Allostery is a widespread cause of loss-of-function variant pathogenicity [PDF]

Nature Communications
Allosteric communication between non-contacting sites in proteins plays a fundamental role in biological regulation and drug action. While allosteric gain-of-function variants are known drivers of oncogene activation, the broader importance of allostery ...
Xiaotian Liao, Ben Lehner
doaj   +2 more sources

Pathological Allostery in ADAMTS13: Autoantibody-Induced Modulation and Its Role in Immune Thrombotic Thrombocytopenic Purpura (iTTP) [PDF]

Pharmaceuticals
Background/Objectives: ADAMTS13 is a plasma metalloprotease that cleaves von Willebrand Factor (vWF), a multimeric glycoprotein involved in platelet recruitment during primary hemostasis.
Madison Gil, Konstantine Halkidis
doaj   +2 more sources

Allostery and cooperativity revisited [PDF]

Protein Science, 2008
Abstract Although phenomenlogical models that account for cooperativity in allosteric systems date back to the early and mid‐60's (e.g., the KNF and MWC models), there is resurgent interest in the topic due to the recent experimental and computational studies that attempted to reveal, at an atomistic level, how allostery actually ...
Qiang Cui
exaly   +3 more sources

The ensemble nature of allostery [PDF]

Nature, 2014
Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new ...
Vincent J. Hilser, Hesam N Motlagh
exaly   +3 more sources

Possible mechanism and clinical potentials of allostery

Clinical and Translational Medicine, 2014
Allostery is involved in the dynamic regulation of biological functions in proteins. Advances in allostery research have recently drawn great interest and brought allostery closer to the clinic.
Peixin Huang
exaly   +2 more sources

Allostery in Biomolecular Condensates. [PDF]

J Mol Biol
Allosteric proteins and membrane-less biomolecular condensates are physics-governed pivotal functional components. Allosteric regulation is an inherent physical property of dynamic proteins, and dynamic proteins are allosteric. Thus, in biomolecular condensates (like everywhere else in the cell), allostery is at play, and often missing in condensate ...
Nussinov R, Regev C, Jang H.
europepmc   +4 more sources

Sulfur-Oxygen Competitive Coordination Allosteric Hydrogel for Triboelectric Nanogenerator-Based Intelligent Tactile Recognition. [PDF]

Adv Sci (Weinh)
A dynamic Ag+─S coordinated hydrogel with a sulfur–oxygen competitive coordination allosteric switch enables reversible tuning between soft–adhesive and stiff–robust states. Integrated with a lightweight 1DCNN classifier, the smart glove system achieves 99.70% laboratory and 93.35% real‐wear material recognition accuracy, offering a paradigm for self ...
Lan S, Zhang L, Dong Y, Mao Y, Hu W.
europepmc   +2 more sources

Time-Dependent Voronoi Analysis of Amino Acid Side-Chain Packing in Simulations. [PDF]

J Comput Chem
Protein volume fluctuation is largely driven by loosely packed amino acid side chains while the backbone is comparatively restrained. We present a Voronoi‐based framework for quantifying and tracking local side‐chain volume and reorganization of neighbors. Paired snapshots show Voronoi tessellations for a side chain during molecular dynamics simulation
Bettencourt SB, Hwang W.
europepmc   +2 more sources