Articles with "aggregation prone" as a keyword



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A Novel Approach for the Production of Aggregation-Prone Proteins Using the Spidroin-Derived NT* Tag.

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Published in 2022 at "Methods in molecular biology"

DOI: 10.1007/978-1-0716-1859-2_6

Abstract: Spiders have evolved proteins that can be kept in a highly concentrated soluble form in the silk gland yet rapidly assemble into stable silk fibers under certain environmental conditions. The transition between soluble and fibrillar… read more here.

Keywords: aggregation; tag; aggregation prone; production aggregation ... See more keywords

Efficient production of aggregation prone 4-α-glucanotransferase by combined use of molecular chaperones and chemical chaperones in Escherichia coli.

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Published in 2019 at "Journal of biotechnology"

DOI: 10.1016/j.jbiotec.2019.01.014

Abstract: In this study, a combined optimization strategy, based on co-expression of molecular chaperones and supplementation of osmolytes, was used to reduce the formation of inclusion bodies and enhance the expression of the soluble form of… read more here.

Keywords: aggregation prone; production; molecular chaperones; cell ... See more keywords
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Multi-Level High-Throughput Screening for Discovery of Ligands That Inhibit Insulin Aggregation.

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Published in 2022 at "Molecular pharmaceutics"

DOI: 10.1021/acs.molpharmaceut.2c00219

Abstract: We have developed a multi-level virtual screening protocol to identify lead molecules from the FDA inactives database that can inhibit insulin aggregation. The method is based on the presence of structural and interaction specificity in… read more here.

Keywords: aggregation; aggregation prone; multi level; insulin aggregation ... See more keywords
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Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

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Published in 2020 at "Nature Communications"

DOI: 10.1038/s41467-020-16564-3

Abstract: As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but identifying these within the dynamic ensemble of monomeric conformations is difficult.… read more here.

Keywords: aggregation; aggregation prone; terminus; asyn ... See more keywords
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The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis

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Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2200468119

Abstract: Significance Protein aggregation is a major problem for human health. However, our understanding of how folded proteins aggregate into amyloid lags behind. Using the tripartite β-lactamase assay (TPBLA) with our test protein, β2-microglobulin (β2m), we… read more here.

Keywords: aggregation; aggregation prone; effect mutation; prone protein ... See more keywords
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Interaction of selected biomolecules and metabolites with amyloidogenic proteins

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Published in 2020 at "Journal of Biomolecular Structure and Dynamics"

DOI: 10.1080/07391102.2020.1760138

Abstract: Abstract The current manuscript reports docking and molecular interaction analyses of three FDA approved acetylcholinesterase inhibitors, nitrogenous bases and nucleotides with amyloidogenic proteins like hen egg white lysozyme (HEWL) and amyloid β peptide. After prediction… read more here.

Keywords: amyloidogenic proteins; aggregation prone; prone regions; interaction selected ... See more keywords
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Aggregation-Prone Structural Ensembles of Transthyretin Collected With Regression Analysis for NMR Chemical Shift

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Published in 2021 at "Frontiers in Molecular Biosciences"

DOI: 10.3389/fmolb.2021.766830

Abstract: Monomer dissociation and subsequent misfolding of the transthyretin (TTR) is one of the most critical causative factors of TTR amyloidosis. TTR amyloidosis causes several human diseases, such as senile systemic amyloidosis and familial amyloid cardiomyopathy/polyneuropathy;… read more here.

Keywords: aggregation; aggregation prone; analysis; prone structural ... See more keywords
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Discovering Novel Small Molecule Compound for Prevention of Monoclonal Antibody Self-Association

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Published in 2022 at "Antibodies"

DOI: 10.3390/antib11020040

Abstract: Designing an antibody with the desired affinity to the antigen is challenging, often achieved by lengthening the hydrophobic CDRs, which can lead to aggregation and cause major hindrance to the development of successful biopharmaceutical products.… read more here.

Keywords: compound; aggregation; discovering novel; aggregation prone ... See more keywords
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A Capped Peptide of the Aggregation Prone NAC 71–82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations

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Published in 2020 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms21051629

Abstract: Although Lewy bodies and Lewy neurites are hallmarks of Parkinson’s disease (PD) and dementia with Lewy bodies (DLB), misfolded α-synuclein oligomers are nowadays believed to be key for the development of these diseases. Attempts to… read more here.

Keywords: capped peptide; aggregation prone; aggregation; nac amino ... See more keywords