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T3516
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Showing 1-30 of 760 results for "T3516" within Papers
Virulence, 11(1), 1402-1414 (2020-10-24)
The respiratory tract is a major entry site for microbial pathogens. To combat bacterial infections, the immune system has various defense mechanisms at its disposal, including antimicrobial peptides (AMPs). To search for novel AMPs from the respiratory tract, a peptide
Cell death and differentiation, 27(1), 192-209 (2019-05-28)
Amyloid-Ī² (AĪ²) oligomers largely initiate the cascade underlying the pathology of Alzheimer's disease (AD). Galectin-3 (Gal-3), which is a member of the galectin protein family, promotes inflammatory responses and enhances the homotypic aggregation of cancer cells. Here, we examined the
Proceedings of the National Academy of Sciences of the United States of America, 115(42), E9782-E9791 (2018-10-04)
Human genetic studies have given evidence of familial, disease-causing mutations in the analogous amino acid residue shared by three related RNA binding proteins causative of three neurological diseases. Alteration of aspartic acid residue 290 of hnRNPA2 to valine is believed
Diabetologia, 63(11), 2385-2395 (2020-07-31)
Aggregation of the beta cell secretory product human islet amyloid polypeptide (hIAPP) results in islet amyloid deposition, a pathological feature of type 2 diabetes. Amyloid formation is associated with increased levels of islet IL-1Ī² as well as beta cell dysfunction
Nanoscale research letters, 13(1), 303-303 (2018-10-01)
The deposition of amyloid-Ī² (AĪ²) plaques and formation of neurotoxic reactive oxygen species (ROS) is a significant pathological signature of Alzheimer's disease (AD). Herein, a novel strategy is reported for combining the unique AĪ² absorption property of selenium nanoparticles with
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 26(1), 24-33 (2019-02-12)
Systemic AA amyloidosis is still, up to this day, a life-threatening complication of chronic inflammatory diseases. Despite the success of anti-inflammatory treatment, the prognosis of some AA patients is still poor, which is why therapies directed at the amyloidogenic pathway
sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.
Biophysical journal, 113(5), 991-1001 (2017-09-07)
Investigation of the molecular mechanisms underlying amyloid-related human diseases attracts close attention. These diseases, the number of which currently is above 40, are characterized by formation of peptide or protein aggregates containing a cross-Ī² structure. Most of the amyloidogenesis mechanisms
Journal of inorganic biochemistry, 205, 110996-110996 (2020-01-19)
Several abnormal events may concur as major risk factors for Alzheimer's disease (AD) pathogenesis. For instance, dysregulation of brain's metal homeostasis and amyloid-mediated membrane damage are established toxic mechanisms causing neuronal death. In this study, we assess the amyloidogenic propensity
International journal of biological macromolecules, 95, 281-287 (2016-11-23)
Current medications for the complex neurological disorder, Alzheimer's disease (AD), can neither stop disease progression nor revert back disease pathogenesis. The present study demonstrates the applicability of a phytoecdysteroid, Ī²-ecdysone, as a multi-potent agent in AD therapeutics. Ī²-ecdysone strongly binds
Molecular biology reports, 46(4), 4279-4292 (2019-05-22)
Ī±-Synuclein is a presynaptic neuronal protein that is abundant in the human brain and is linked genetically and neuropathologically to Parkinson's disease (PD). The E46K mutation of the Ī±-synuclein gene has been linked to autosomal dominant early-onset of PD. Crocin
Molecules (Basel, Switzerland), 24(3) (2019-02-02)
Transthyretin-related amyloidosis is a slowly progressive disorder caused by deposition of insoluble amyloid plaques formed by fibrillization of mutant or defective transthyretin (TTR) monomers that leads to neurodegeneration and organ failure. Thus, any compound exhibiting TTR amyloid formation inhibitory activity
Scientific reports, 10(1), 9115-9115 (2020-06-06)
Exogenous insulin, used as a therapeutic agent for diabetes, forms insoluble deposits containing amyloid fibrillar structures near the administration site. We have analyzed the in vitro anti-amyloid activity of four green tea constituents: (-)-epigallocatechin gallate (EGCG), (-)-epicatechin (EC), gallic acid
Journal of photochemistry and photobiology. B, Biology, 181, 89-97 (2018-03-11)
Insulin is known to form amyloid aggregates when agitated in a hydrophobic container. Amyloid aggregation is routinely measured by the fluorescence of the conformational dye thioflavin T, which, when incorporated into amyloid fibers, fluoresces at 480āÆnm. The kinetics of amyloid
PloS one, 10(11), e0141708-e0141708 (2015-11-05)
Inhibition of Ī²-amyloid (AĪ²) aggregation in the cerebral cortex of the brain is a promising therapeutic and defensive strategy in identification of disease modifying agents for Alzheimer's disease (AD). Since natural products are considered as the current alternative trend for
FEBS letters, 589(24 Pt B), 3807-3815 (2015-11-27)
Myoglobin (Mb) undergoes pronounced heme loss under denaturing conditions wherein the proximal histidine gets protonated. Our data show that macromolecular crowding agents (both synthetic and protein based) can appreciably influence the extent of heme retention in Mb. Interestingly, glucose and
Biochimica et biophysica acta. Molecular basis of disease, 1864(9 Pt B), 3060-3068 (2018-07-01)
Parkinson's disease (PD) and other synucleinopathies are characterized by accumulation of misfolded aggregates of Ī±-synuclein (Ī±-syn). The normal function of Ī±-syn is still under investigation, but it has been generally linked to synaptic plasticity, neurotransmitter release and the maintenance of
Science advances, 7(9) (2021-02-28)
Microglia participate in central nervous system (CNS) development and homeostasis and are often implicated in modulating disease processes. However, less is known about the role of microglia in the biology of the neurovascular unit (NVU). In particular, data are scant
Journal of materials chemistry. B, 8(11), 2256-2268 (2020-02-27)
Amyloid Ī²-peptide (AĪ²) aggregation induced by metal ions such as Cu2+ has been recognized as a crucial step in the pathogenesis of Alzheimer's disease (AD), so development of multifunctional agents that are able to inhibit AĪ² aggregation and modulate Cu2+-AĪ²
Biofouling, 31(6), 535-541 (2015-08-13)
Increasing drying time adversely affects attachment of tissue proteins and prion-associated amyloid to surgical stainless steel, and reduces the efficacy of commercial cleaning chemistries. This study tested the efficacy of commercial humidity retention bags to reduce biofouling on surgical stainless
EMBO reports, 20(2) (2018-12-01)
The murine cytomegalovirus protein M45 protects infected mouse cells from necroptotic death and, when heterologously expressed, can protect human cells from necroptosis induced by tumour necrosis factor receptor (TNFR) activation. Here, we show that the N-terminal 90 residues of the
Chemistry (Weinheim an der Bergstrasse, Germany), 26(66), 15150-15158 (2020-05-29)
Gold supra-pyramid structures were obtained by the addition of acidic solution of cucurbit[8]uril (CB[8]) to an aqueous solution of citrate stabilized gold nanoparticles (AuNP). The reaction resulted in the precipitation of supra-pyramid from the solution after just 1ā
min of shaking.
Acta biomaterialia, 112, 164-173 (2020-05-29)
Alzheimer's disease (AD) is the most common form of dementia and is associated with the accumulation of amyloid-Ī² (AĪ²), a peptide whose aggregation has been associated with neurotoxicity. Drugs targeting AĪ² have shown great promise in 2D in vitro models
Journal of inorganic biochemistry, 171, 67-75 (2017-04-04)
Aggregation of amyloid Ī²-proteins (AĪ²) induced by Cu
Microbial cell factories, 12, 17-17 (2013-02-16)
The understanding of protein aggregation is a central issue in different fields of protein science, from the heterologous protein production in biotechnology to amyloid aggregation in several neurodegenerative and systemic diseases. To this goal, it became more and more evident
Scientific reports, 7(1), 12482-12482 (2017-10-04)
Thioflavin T (ThT) is standardly used as a fluorescent marker to detect aggregation of amyloid fibrils by conventional fluorescence microscopy, including polarization resolved imaging that brings information on the orientational order of the fibrils. These techniques are however diffraction limited
Chembiochem : a European journal of chemical biology, 16(3), 446-454 (2015-02-03)
Contact between the human immunodeficiency virus (HIV-1) and its target cell is initiated by the interaction of viral gp120 with cellular CD4. An assembled peptide (CD4bs-M) that presents the CD4 binding site of gp120 was previously shown to inhibit the
ACS chemical neuroscience, 10(6), 2730-2740 (2019-03-30)
Proline residues play a prominent role in protein folding and aggregation. We investigated the influence of single prolines and their combination on oligomerization and the amyloid fibrillation reaction of human stefin B (stB). The proline mutants influenced the distribution of
Small (Weinheim an der Bergstrasse, Germany), 16(43), e2002804-e2002804 (2020-10-03)
The fibrillization and deposition of Ī²-amyloid protein (AĪ²) are recognized to be the pathological hallmarks of Alzheimer's disease (AD), which signify the need for the effective detection and inhibition of AĪ² accumulation. Development of multifunctional agents that can inhibit AĪ²
Steroids, 153, 108529-108529 (2019-11-02)
Alzheimer's disease (AD) is multi-factorial disorder characterized by impaired memory and cognition deficit. AD is characterized by impaired cholinergic transmission, extracellular amyloid beta deposits, neurofibrillary tangles and oxidative stress. A multi-target directed ligand (MTDL) approach is required to devise a
ACS chemical neuroscience, 10(3), 1813-1825 (2019-01-19)
Misfolding and aggregation of amyloid proteins into fibrillar aggregates is a central pathogenic event in neurodegenerative disorders such as Alzheimer's (AD) and Parkinson's diseases (PD). Currently, there is a lack of reliable sensors for detecting the range of protein aggregates
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