Results 71 to 80 of about 109,107 (305)

β-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH [PDF]

, 2014
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β-microglobulin (βm),
Eric W. Hewitt, Xue, W-F, Beales Paul A., Sheynis, T, Radford, SE, Neil A. Ranson (610030), Sheena E. Radford (197775), Beales, Paul A, Goodchild Sophia C., Thompson, Rebecca, Xue Wei-Feng, Neil A. Ranson, Thompson Rebecca, Sheena E Radford, Sophia C. Goodchild, Sheynis Tania, Eric W Hewitt, Kevin W. Tipping (610028), Radford Sheena E., Tipping Kevin W., Sheena E. Radford, Hewitt, EW, Xue, Wei-Feng, Beales, PA, Radford, Sheena E, Tipping, KW, Sophia C Goodchild, Paul A Beales, Goodchild, SC, Ranson, Neil A, Rebecca Thompson, Wei-Feng Xue (610029), Ranson Neil A., Neil A Ranson, Tipping, Kevin W, Tania Sheynis (610026), Kevin W Tipping, Tania Sheynis, Sheynis, Tania, Wei-Feng Xue, Goodchild, Sophia C, Eric W. Hewitt (197779), Hewitt, Eric W, Hewitt Eric W., Sophia C. Goodchild (283440), Ranson, NA, Rebecca Thompson (610027), Paul A. Beales (435545), Thompson, R, Paul A. Beales   +49 more
core   +1 more source

QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study

Advanced Science, EarlyView.
The anti‐amyloidogenic peptide QBP1 effectively halts human islet amyloid polypeptide (hIAPP) aggregation, preventing the formation of toxic β‐structured intermediates. Through a combination of biophysical assays, molecular dynamics, and cell‐based studies, QBP1 is shown to preserve β‐cell viability and metabolic homeostasis, positioning it as a ...
María M. Tejero‐Ojeda, Ada Bernaus Vives, Michał Wojciechowski, Dinh Quoc Huy Pham, Mateusz Chwastyk, Mario Vallejo, Anna Novials, Douglas V. Laurents, Mariano Carrión‐Vázquez   +8 more
wiley   +1 more source

Protein Disulfide Isomerase Disassembles TDP‐43/G3BP1 Condensates and Antagonizes TDP‐43 Pathological Aggregates

Advanced Science, EarlyView.
Cytoplasmic aggregation of TDP‐43 is a common pathological feature in amyotrophic lateral sclerosis, frontotemporal lobar degeneration, and Alzheimer's disease with TDP‐43 pathology. This study reports that wild‐type PDI slows down phase separation of TDP‐43 through direct interaction with TDP‐43.
Jia‐Qi Liu, Hao Liu, Yu‐Xuan Sun, Yuying Li, Xiangyi Liu, Li‐Qiang Wang, Zhaofei Yang, Qi Fu, Xiaojiao Xu, Jie Chen, Yingshuang Zhang, Jun Zhou, Weidong Le, Mengchao Cui, Yi Liang   +14 more
wiley   +1 more source

The Beta Amyloid Dysfunction (BAD) Hypothesis for Alzheimer’s Disease

Frontiers in Neuroscience, 2019
Beta amyloid, Aβ 1–42, originally named as Amyloid A4 protein, is one of the most investigated peptides in neuroscience and has attracted substantial interest since its discovery as the main insoluble fibril-type protein in cerebrovascular amyloid ...
Heinz Hillen
doaj   +1 more source

Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin [PDF]

, 2005
Human islet amyloid polypeptide (hIAPP) forms amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). Pre-fibrillar hIAPP oligomers (in contrast to monomeric IAPP or mature fibrils) increase membrane permeability, suggesting an important ...
Bradshaw, Jeremy P., Bradshaw, Jeremy, Hauss, T, Ashley, Richard H., Balali-Mood, K, Bradshaw, J. P., Balali-Mood, K., Hauß, Thomas, Ashley, R.H., Balali-Mood, Kia, Ashley, R. A., Ashley, R H, Balali Mood, K., Hau , T., Bradshaw, J.P.   +14 more
core   +1 more source

Time‐Multiplexed Organic Electrochemical Transistor for Saliva‐Based Rapid Detection of Viral Proteins

Advanced Science, EarlyView.
A time‐multiplexed nanobody‐functionalized organic electrochemical transistor enables rapid and sensitive detection of three respiratory viral proteins from saliva. Sequentially addressed multi‐gate electrodes on a shared channel achieve around 1 fm detection within 15 min without sample preprocessing. Clinical validation demonstrates high specificity,
Tianrui Chang, Yuxiang Ren, Shofarul Wustoni, Atheer Alqatari, Adel Hama, Yazhou Wang, Long Chen, Jessica Parrado Agudelo, Luca Salvigni, Keying Guo, Ashraf Dada, Stefan T. Arold, Raik Grünberg, Sahika Inal   +13 more
wiley   +1 more source

Effects of methylglyoxal on amyloid‐beta peptide

The FASEB Journal, 2008
Diabetics exhibit elevated levels of carbohydrates and their oxidized byproducts such as methylglyoxal (MGO). With the excess production and accumulation of the amyloid‐beta peptide (ABP) in AD, the linkage between diabetes and AD may involve ABP and MGO. We studied the effects of MGO‐induced ABP modification on conformational properties. Human isoform
Randal Cerf Michelson, Norbert W Seidler
openaire   +1 more source

Oxidation destabilizes toxic amyloid beta peptide aggregation [PDF]

Scientific Reports, 2019
AbstractThe aggregation of insoluble amyloid beta (Aβ) peptides in the brain is known to trigger the onset of neurodegenerative diseases, such as Alzheimer’s disease. In spite of the massive number of investigations, the underlying mechanisms to destabilize the Aβ aggregates are still poorly understood. Some studies indicate the importance of oxidation
J. Razzokov, M. Yusupov, A. Bogaerts
openaire   +3 more sources

Small Extracellular Vesicles‐Derived Circ6718 Unlocks Stromal Remodeling and Serves as a Biomarker in Gastric Cancer

Advanced Science, EarlyView.
sEVs‐circ6718 serves as a promising serum biomarker for gastric cancer early diagnosis and prognosis, promoting malignant transformation in gastric cancer cells and GC‑MSC differentiation into CAFs. sEVs‑circ6718 holds potential as a biomarker for the early diagnosis and prognostic assessment of gastric cancer.
Fan Zhang, Xueyan Zang, Dongli Wang, Rong Li, Hui Qian, Wenrong Xu, Jiajia Jiang, Yongmin Yan   +7 more
wiley   +1 more source

Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine. [PDF]

PLoS Computational Biology, 2009
At the core of amyloid fibrils is the cross-beta spine, a long tape of beta-sheets formed by the constituent proteins. Recent high-resolution x-ray studies show that the unit of this filamentous structure is a beta-sheet bilayer with side chains within ...
Jiyong Park, Byungnam Kahng, Wonmuk Hwang   +2 more
doaj   +1 more source