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Relevant bibliographies by topics / Protein oligomers

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Journal articles

Academic literature on the topic 'Protein oligomers'

Author: Grafiati

Published: 10 March 2023

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Journal articles on the topic "Protein oligomers"

1

Schmid, J. A., H. Just, and H. H. Sitte. "Impact of oligomerization on the function of the human serotonin transporter." Biochemical Society Transactions 29, no. 6 (2001): 732–36. http://dx.doi.org/10.1042/bst0290732.

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The formation of oligomeric structures has been proposed for a large number of membrane proteins, including G-protein-coupled receptors and ion channels. Biochemical studies employing gel filtration, cross-linking or co-immunoprecipitation techniques showed that the serotonin [5-hydroxytryptamine (5-HT)] transporter is also capable of forming oligomers. We investigated whether the human serotonin transporter (hSERT) can be visualized as an oligomer in the plasma membrane of intact cells. To test this working hypothesis, we generated fusion proteins of hSERT and spectral variants of green fluor

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2

Eisenberg, David, Arthur Laganowsky, Cong Liu, et al. "Structural Studies of the Amyloid State of Proteins." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C797. http://dx.doi.org/10.1107/s205327331409202x.

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Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each associated with a particular protein in fibrillar form. At the morphological level, these fibers appear similar and are termed "amyloid." We found that the adhesive segments of amyloid fibers are short protein sequences which form pairs of interdigitated, in-register beta sheets. These amyloid fibrils were long suspected to be the disease agents, but evidence suggests that in the neurodegenerative diseases, smaller, often transient and polymorphic oligomers are the toxic entities. We have identified a segm

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3

Tanner, John J. "Empirical power laws for the radii of gyration of protein oligomers." Acta Crystallographica Section D Structural Biology 72, no. 10 (2016): 1119–29. http://dx.doi.org/10.1107/s2059798316013218.

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The radius of gyration is a fundamental structural parameter that is particularly useful for describing polymers. It has been known since Flory's seminal work in the mid-20th century that polymers show a power-law dependence, where the radius of gyration is proportional to the number of residues raised to a power. The power-law exponent has been measured experimentally for denatured proteins and derived empirically for folded monomeric proteins using crystal structures. Here, the biological assemblies in the Protein Data Bank are surveyed to derive the power-law parameters for protein oligomer

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4

Vaikath, Nishant, Indulekha Sudhakaran, Ilham Abdi, et al. "Structural and Biophysical Characterization of Stable Alpha-Synuclein Oligomers." International Journal of Molecular Sciences 23, no. 23 (2022): 14630. http://dx.doi.org/10.3390/ijms232314630.

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The aggregation of α-synuclein (α-syn) into neurotoxic oligomers and fibrils is an important pathogenic feature of synucleinopatheis, including Parkinson’s disease (PD). A further characteristic of PD is the oxidative stress that results in the formation of aldehydes by lipid peroxidation. It has been reported that the brains of deceased patients with PD contain high levels of protein oligomers that are cross-linked to these aldehydes. Increasing evidence also suggests that prefibrillar oligomeric species are more toxic than the mature amyloid fibrils. However, due to the heterogenous and meta

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5

Kreiser, Ryan P., Aidan K. Wright, Natalie R. Block, et al. "Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers." International Journal of Molecular Sciences 21, no. 22 (2020): 8651. http://dx.doi.org/10.3390/ijms21228651.

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The aberrant aggregation of proteins is implicated in the onset and pathogenesis of a wide range of neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Mounting evidence indicates that misfolded protein oligomers produced as intermediates in the aggregation process are potent neurotoxic agents in these diseases. Because of the transient and heterogeneous nature of these elusive aggregates, however, it has proven challenging to develop therapeutics that can effectively target them. Here, we review approaches aimed at reducing oligomer toxicity, including (1) modulating

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6

de Klerk, G. J., and D. Engelen. "Assembly of Agrostemma githago (corn-cockle) storage proteins and their precursor proteins into oligomers." Biochemical Journal 230, no. 1 (1985): 269–72. http://dx.doi.org/10.1042/bj2300269.

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The major fraction of seed storage proteins of Agrostemma githago (corn-cockle), a non-leguminous dicot, occurs as material with S20,w values of approximately 11S and approximately 2S, and a minor fraction as oligomers with S20,w values of approximately 6.5S. The 11S proteins are of the legumin type and consist of disulphide-linked α- and β-subunits of Mr approximately 39 000 and approximately 23 000 respectively. The oligomeric assembly of the precursor polypeptides of the 11S proteins was examined. The approximately 65 000-Mr precursor polypeptides of two 11S proteins, which consist of 38 00

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7

Stoneman, Michael R., Naomi Raicu, Gabriel Biener, and Valerică Raicu. "Fluorescence-based Methods for the Study of Protein-Protein Interactions Modulated by Ligand Binding." Current Pharmaceutical Design 26, no. 44 (2020): 5668–83. http://dx.doi.org/10.2174/1381612826666201116120934.

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Background: The growing evidence that G protein-coupled receptors (GPCRs) not only form oligomers but that the oligomers also may modulate the receptor function provides a promising avenue in the area of drug design. Highly selective drugs targeting distinct oligomeric sub-states offer the potential to increase efficacy while reducing side effects. In this regard, determining the various oligomeric configurations and geometric sub-states of a membrane receptor is of utmost importance. Methods: In this report, we have reviewed two techniques that have proven to be valuable in monitoring the qua

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8

Larson, Megan E., Susan J. Greimel, Fatou Amar та ін. "Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits". Proceedings of the National Academy of Sciences 114, № 23 (2017): E4648—E4657. http://dx.doi.org/10.1073/pnas.1704698114.

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Mounting evidence indicates that soluble oligomeric forms of amyloid proteins linked to neurodegenerative disorders, such as amyloid-β (Aβ), tau, or α-synuclein (αSyn) might be the major deleterious species for neuronal function in these diseases. Here, we found an abnormal accumulation of oligomeric αSyn species in AD brains by custom ELISA, size-exclusion chromatography, and nondenaturing/denaturing immunoblotting techniques. Importantly, the abundance of αSyn oligomers in human brain tissue correlated with cognitive impairment and reductions in synapsin expression. By overexpressing WT huma

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9

Wang, Yu, Karen S. L. Lam, Ming-hon Yau, and Aimin Xu. "Post-translational modifications of adiponectin: mechanisms and functional implications." Biochemical Journal 409, no. 3 (2008): 623–33. http://dx.doi.org/10.1042/bj20071492.

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Adiponectin is an insulin-sensitizing adipokine with anti-diabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. This adipokine is secreted from adipocytes into the circulation as three oligomeric isoforms, including trimeric, hexameric and the HMW (high-molecular-mass) oligomeric complex consisting of at least 18 protomers. Each oligomeric isoform of adiponectin exerts distinct biological properties in its various target tissues. The HMW oligomer is the major active form mediating the insulin-sensitizing effects of adiponectin, whereas the central actions of this adipo

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10

NEMOTO, Takayuki, and Nobuko SATO. "Oligomeric forms of the 90-kDa heat shock protein." Biochemical Journal 330, no. 2 (1998): 989–95. http://dx.doi.org/10.1042/bj3300989.

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Two isoforms of the 90-kDa heat shock protein, HSP90α and HSP90β, are present in the cytosol of mammalian cells. Analysis by polyacrylamide gel electrophoresis under nondenaturing conditions (native PAGE) revealed that HSP90α predominantly exists as a homodimer and that HSP90β is present mainly as a monomer [Minami, Kawasaki, Miyata, Suzuki and Yahara (1991) J. Biol. Chem. 266, 10099-10103]. However, only the dimeric form has been observed under other analytical conditions such as gradient centrifugation. In this study, therefore, we investigated native forms of HSP90 by use of immunochemical

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