关于 "Cytoskeleton & Motor Proteins" 的结果57+ 个结果

Reverse sequence of Aβ 1-40.

Abeta 5-42 is produced from amyloid precursor protein by action of caspases. It is deposited in Alzheimer's disease brain as well, but less prone to aggregation.

Cleavage of APP by alpha- and gamma secretase (i.

Protein Kinase C Peptide Substrate 依赖于第二信使和特定的适配蛋白靶向特定的细胞间室，接受细胞外信号，激活 G 蛋白偶联受体，酪氨酸激酶受体或酪氨酸激酶偶联受体。Protein Kinase C Peptide Substrate 参与调控多种生理功能，包括神经。内分泌、外分泌、炎症和免疫系统的激活。

N-terminally biotin-labeled Aβ42.

Microtubule-associated protein tau (26-44) 是一个合成肽链，具有连接到谷氨酰胺的胺基和与赖氨酸连接的羧基。

C-Reactive Protein (CRP) 174-185 是 C-反应蛋白的 174-185 片段。C-Reactive Protein 可作为炎症的标记，是心血管风险的标志物，可能促进动脉粥样硬化形成。

Acyl Carrier Protein (ACP) (65-74) 是一种有活性的酰基载体蛋白 ACP 片段。

与内盐相比，Aβ42 的盐酸盐在 pH 7.4 时更容易聚集。

Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice.

Aβ 2-42 could be a biomarker for differentiating AD from other degenerative dementias, such as frontotemporal dementias (FTD). The peptide promotes phagocytosis by macrophages.

The N-terminally truncated Aβ42 may be formed in increased amounts as AD progresses. Aβ 3-42 is the precursor of the Pyr-peptide. (Pyr³)-Aβ 3-42 positive plaques are resistant to age-dependent degradation likely due to their high stability and propensity to aggregate.

Aβ 4-42 could be one of the earliest and most prominent Aβ species deposited in AD brain. Sequencing of amyloid plaque cores showed that 64% of the isolated Aβ had a phenylalanine at its N-terminus, and indeed, IP/MS experiments identified Aβ 4-42 as a major Aβ species in AD patients. Additionally, Aβ 4-42 was found to be a component of cotton wool plaques in familial AD patients with the V261I PS1 mutation. Aβ 4-42 was discovered as well in amyloid deposits from vascular dementia and familial Danish dementia patients. These observations indicate that Aβ 4-42 may contribute to the development of multiple CNS diseases.

The Dutch mutation (E22Q) of amyloid β-peptide aggregates more readily than the wild-type peptide and the resulting fibrils show increased neurotoxicity. The mutant peptide E22Q induced apoptosis of cerebral endothelial cells at a concentration of 25 μm, whereas WT Aβ 1-40 and the Italian mutant E22K (H-6698) showed no effect.

The Dutch mutation (E22Q) aggregates more readily than the wild-type sequence. The resulting fibrils show increased neurotoxicity.

Contrary to β-amyloid peptides mutated at position 22 (Dutch, Italian, Arctic mutants) the Flemish mutation (A21G) shows a decreased tendency to aggregate and a reduced neurotoxicity. In the studies of Betts and Tsubuki, A21G was degraded significantly more slowly by neprilysin than the wild-type Aβ 1-40 and the E22 mutants. The relative resistance to proteolytic degradation may account for the pathogenicity of the Aβ mutant.

The Flemish mutation (A21G) shows a decreased tendency to aggregate and a reduced neurotoxicity. A21G is pathogenic as it is degraded significantly more slowly by neprilysin than WT Abeta42.

The highly neurotoxic arctic mutant (E22G) of Aβ has been used to study the mechanisms underlying the formation of soluble and insoluble β-amyloid aggregates. As the wild-type Aβ, the arctic mutant preferably assembles in the presence of GM1 ganglioside.

The arctic mutant of amyloid β peptide 1-42, in which Glu²² is substituted by Gly, is distinctly more amyloidogenic than the wild-type Aβ 1-42.