About: Protein stabilization by macromolecular crowding through enthalpy rather than entropy

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scientific article published on 16 June 2014

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 2014 (uk) scientific article published on 16 June 2014 (en) artículu científicu espublizáu en xunu de 2014 (ast) գիտական հոդված հրատարակված 2014 թվականի հունիսի 16-ին (hy)
publication date	wds:Q88006361-890B0DC1-B288-44AE-A76A-21EB8F9FEE78
publication date	2014-06-16 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q88006361-10C1E366-B1B3-461E-AAFE-4172926F5F06
language of work or name	English
author name string	wds:Q88006361-53351042-ECC2-46B9-B1AC-F62CFD2289A7 wds:Q88006361-8F881F49-9C61-412F-857C-DDF6A627B945 wds:Q88006361-D4B2B40F-CC1F-4406-B185-B8E504780EA6 wds:Q88006361-D8E84F1E-AB7D-42CF-BFC0-31A5AB82FBC6 wds:Q88006361-E0BABA34-9E11-425A-9BBE-4031F127C322 wds:Q88006361-E7908533-BB76-4F13-B578-0D601C8CFA26
author name string	Christian Herrmann Michael Senske Benjamin Born Martina Havenith Lisa Törk Simon Ebbinghaus
rdfs:label	Protein stabilization by macromolecular crowding through enthalpy rather than entropy (en) Protein stabilization by macromolecular crowding through enthalpy rather than entropy (nl)
skos:prefLabel	Protein stabilization by macromolecular crowding through enthalpy rather than entropy (en) Protein stabilization by macromolecular crowding through enthalpy rather than entropy (nl)
name	Protein stabilization by macromolecular crowding through enthalpy rather than entropy (en) Protein stabilization by macromolecular crowding through enthalpy rather than entropy (nl)
title	wds:Q88006361-75D9CD38-EDF6-4510-97CF-772C3D4775B6
title	Protein stabilization by macromolecular crowding through enthalpy rather than entropy (en)
page(s)	wds:Q88006361-C3DC0094-E727-4F91-B6A9-0C26B3D82892
page(s)	9036-9041
instance of	wds:Q88006361-2FD834ED-CD16-4C9E-AAA8-308EA17CC91A
instance of	scholarly article
PubMed ID	wds:Q88006361-5FE345A6-2632-44BE-A46D-9CF3CF4CBAB6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24888734
PubMed ID	24888734
published in	wds:Q88006361-7F96A825-CF73-4D84-A28C-AA8D3978675C
published in	Journal of the American Chemical Society
issue	wds:Q88006361-2F4F5A1A-3BF6-4761-996A-61C973990B75
volume	wds:Q88006361-8AB3F6F8-779A-4A5A-8DDA-2C17E25D422E
issue	25
volume	136
DOI	wds:Q88006361-D25E0868-BA3A-4823-9D34-C82030C2DD9C
DOI	http://dx.doi.org/10.1021/JA503205Y
DOI	10.1021/JA503205Y
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q88006361
is cites work of	Analysis of the size dependence of macromolecular crowding shows that smaller is better Thermodynamics of protein destabilization in live cells Stability of Protein-Specific Hydration Shell on Crowding Calcineurin in a Crowded World Trehalose Glycopolymer Enhances Both Solution Stability and Pharmacokinetics of a Therapeutic Protein. Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology The Differential Response of Proteins to Macromolecular Crowding Crowding induces complex ergodic diffusion and dynamic elongation of large DNA molecules Crowding in Cellular Environments at an Atomistic Level from Computer Simulations Excluded-volume effects in living cells Beyond the excluded volume effects: mechanistic complexity of the crowded milieu Molecular crowding and early evolution. Protein folding in the cell, from atom to organism Chemical Interactions of Polyethylene Glycols (PEGs) and Glycerol with Protein Functional Groups: Applications to Effects of PEG and Glycerol on Protein Processes Observed crowding effects on Mycobacterium tuberculosis 2-trans-enoyl-ACP (CoA) reductase enzyme activity are not due to excluded volume only The unfolding of iRFP713 in a crowded milieu The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP Protein folding, binding, and droplet formation in cell-like conditions Cosolutes, Crowding, and Protein Folding Kinetics. Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding. Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments. Crowders and Cosolvents-Major Contributors to the Cellular Milieu and Efficient Means to Counteract Environmental Stresses. The pH Dependence of Saccharides' Influence on Thermal Denaturation of Two Model Proteins Supports an Excluded Volume Model for Stabilization Generalized to Allow for Intramolecular Electrostatic Interactions Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding Cosolute and Crowding Effects on a Side-By-Side Protein Dimer Intracellular pH modulates quinary structure. Enthalpic stabilization of an SH3 domain by D O Large cosolutes, small cosolutes, and dihydrofolate reductase activity. Measuring the effects of macromolecular crowding on antibody function with biolayer interferometry Glucose-Responsive Trehalose Hydrogel for Insulin Stabilization and Delivery Crowding-Induced Elongated Conformation of Urea-Unfolded Apoazurin: Investigating the Role of Crowder Shape in Silico Engineering aspects of immobilized lipases on esterification: A special emphasis of crowding, confinement and diffusion effects Wanted: scalable tracers for diffusion measurements Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding. An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility. Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders Structural Perspective on Revealing and Altering Molecular Functions of Genetic Variants Linked with Diseases In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase Role of protein interactions in stabilizing canonical DNA features in simulations of DNA in crowded environments Protein Folding Modulation in Cells Subject to Differentiation and Stress Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function Mixed Macromolecular Crowding: A Protein and Solvent Perspective Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder
is cites work of	wds:Q35818679-DA64EB58-E122-4E7C-A1AE-076EA019BC3F wds:Q36987193-88C5E256-6A21-48F2-AD92-4CA00A96236B wds:Q46919872-9A36BD6E-DF60-4B61-93E7-D9BCCFF141CC wds:Q57854068-E58709BA-4413-426A-AEC2-A86A9B1038E2 wds:Q64067978-7BB18A6F-BF69-4D27-9103-A3F37CDFDA13 wds:Q26830682-7BB45D0D-E3E3-4053-A42A-C2543EC19C3E wds:Q30395880-03C74D05-A23F-43A0-8F6D-C6FE54AE4408 wds:Q35221715-0EAA2B9B-4BE4-4873-95FE-CE7F0B908735

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