The pro‐sequence of parathyroid hormone prevents premature amyloid fibril formation
Sign Up to like & getrecommendations! Published in 2023 at "FEBS Letters"
DOI: 10.1002/1873-3468.14587
Abstract: The parathyroid hormone (PTH) regulates the calcium and phosphate level in blood after secretion from parathyroid chief cells. The pre‐ and pro‐sequences of precursor preproPTH get cleaved during PTH maturation. In secretory granules, PTH forms… read more here.
Keywords: hormone; prevents premature; parathyroid; parathyroid hormone ... See more keywords
A Competition of Secondary and Primary Nucleation Controls Amyloid Fibril Formation of the Parathyroid Hormone.
Sign Up to like & getrecommendations! Published in 2023 at "Macromolecular bioscience"
DOI: 10.1002/mabi.202200525
Abstract: Functional amyloids belong to an increasing class of non-toxic biologic material, in contrast to the prominent disease-related amyloids. Here, we report on the fibril formation of the parathyroid hormone PTH84 as a representative candidate following… read more here.
Keywords: nucleation; formation parathyroid; secondary nucleation; parathyroid hormone ... See more keywords
Polyphenol‐solubility alters amyloid fibril formation of α‐synuclein
Sign Up to like & getrecommendations! Published in 2021 at "Protein Science"
DOI: 10.1002/pro.4130
Abstract: Amyloid fibril formation is associated with various amyloidoses, including neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Amyloid fibrils form above the solubility of amyloidogenic proteins or peptides upon breaking supersaturation, followed by a nucleation… read more here.
Keywords: formation synuclein; formation; fibril formation; solubility ... See more keywords
Multivalent interacting glycodendrimer to prevent amyloid-peptide fibril formation induced by Cu(II): A multidisciplinary approach
Sign Up to like & getrecommendations! Published in 2018 at "Nano Research"
DOI: 10.1007/s12274-017-1734-9
Abstract: Amyloid peptide fibrillogenesis induced by Cu(II) ions is a key event in the pathogenesis of Alzheimer’s disease. Dendrimers have been found to be active in preventing fibril formation. Therefore, they hold promise for the treatment… read more here.
Keywords: amyloid peptide; glycodendrimer; formation; formation induced ... See more keywords
Effect of site-specific amino acid D-isomerization on β-sheet transition and fibril formation profiles of Tau microtubule-binding repeat peptides.
Sign Up to like & getrecommendations! Published in 2019 at "Biochemical and biophysical research communications"
DOI: 10.1016/j.bbrc.2018.11.043
Abstract: d-amino acid-containing proteins have been found in several human tissues, and the spontaneous accumulation of d-amino acids in proteins is thought to be involved in age-dependent diseases including dementia. Tau, a microtubule-associated protein, is a… read more here.
Keywords: acid isomerization; fibril formation; tau; amino acid ... See more keywords
The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death.
Sign Up to like & getrecommendations! Published in 2019 at "Biochimie"
DOI: 10.1016/j.biochi.2019.12.005
Abstract: Type 2 diabetes mellitus is a disease characterized by the formation of amyloid fibrillar deposits consisting mainly in human islet amyloid polypeptide (hIAPP), a peptide co-produced and co-secreted with insulin. hIAPP and insulin are synthesized… read more here.
Keywords: flanking peptides; hiapp; formation; fibril formation ... See more keywords
Kinetics of protein fibril formation: Methods and mechanisms.
Sign Up to like & getrecommendations! Published in 2017 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2016.06.052
Abstract: Amyloid fibril formation is a self-assembly reaction induced by favourable conformational changes of proteins leading to a stable, structurally organized aggregates. The deposition of stable protein fibrils in organs and tissues results in many diseases… read more here.
Keywords: methods mechanisms; formation methods; formation; fibril formation ... See more keywords
Diameter of the vial plays a crucial role in the amyloid fibril formation: Role of interface area between hydrophilic-hydrophobic surfaces.
Sign Up to like & getrecommendations! Published in 2017 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2017.03.070
Abstract: Number of incurable diseases associated with neurodegenerative syndromes like Alzheimer's, and Parkinson's, are owing to protein aggregation which leads to amyloid fibril formation. In vitro, such fibrillation depends on concentration, temperature, pH, ionic strength, organic… read more here.
Keywords: fibrillation; fibril formation; diameter vial; role ... See more keywords
Effect of natural biopolymers on amyloid fibril formation and morphology.
Sign Up to like & getrecommendations! Published in 2018 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2017.07.171
Abstract: Amyloid fibrils are associated with the pathogenesis of protein misfolding diseases such as Alzheimer's disease. These fibrils typically exhibit different morphologies when grown in vitro, and this has been known to affect their biological properties… read more here.
Keywords: effect natural; formation; fibril formation; amyloid fibrils ... See more keywords
Regulation of heteronuclear Pt-Ru complexes on the fibril formation and cytotoxicity of human islet amyloid polypeptide.
Sign Up to like & getrecommendations! Published in 2018 at "Journal of inorganic biochemistry"
DOI: 10.1016/j.jinorgbio.2018.08.012
Abstract: The deposition of human islet amyloid polypeptide (hIAPP) is considered as a causative factor of type 2 diabetes mellitus (T2DM). Developing effective inhibitors against the fibril formation of hIAPP is a potential way to treat… read more here.
Keywords: islet amyloid; human islet; metal; fibril formation ... See more keywords
The effect of three polyphenols and some other antioxidant substances on amyloid fibril formation by Human cystatin C
Sign Up to like & getrecommendations! Published in 2020 at "Neurochemistry International"
DOI: 10.1016/j.neuint.2020.104806
Abstract: Human cystatin C (CysC) is an amyloid forming protein involved in the hereditary cerebral amyloid angiopathy (HCCAA) that affects arteries in the brain and the peripheral nervous system. In this study we measured the influence… read more here.
Keywords: human cystatin; effect; fibril formation; effect three ... See more keywords