Results 71 to 80 of about 5,185,837 (206)

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett, Daggett, Valerie, van der Kamp, Marc W, Marc W. van der Kamp   +3 more
core   +1 more source

Human biomarker navigator

iMeta, EarlyView.
The Human Biomarker Navigator integrates the disease continuum, biomarker dynamics, cross‐organ biomarker networks, biomarker classification, and technology‐driven paradigms. It maps how biomarkers link multi‐system physiology and pathology across the nervous, respiratory, endocrine, circulatory, immune, digestive, urinary, reproductive, and ...
Meng‐Yao Li, Qian Zhang, Zijie Wang, Zeping Gui, Jing Liu, Jingda Li, Maojun Jiang, Zukang Chang, Qingqing Han, Bendong Yang, Tariq Saeed, Jun Li, Jinghan Jia, Chenghu Song, Tong Shao, Tianhuan Peng, Xueying Zhang, Pingping Guo, Jun Luo, Gangao Yang, Yuan Wan, Gokhan Zengin, Quan Yuan, Lingru Li, Xiaohui Fan, Yang Luo, Lvyun Zhu, Yanfei Zheng, Wenjun Mao, Wenlong Sun   +29 more
wiley   +1 more source

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]

, 2003
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C., Weiss, S., Riley, M. L., Gauczynski, S., Leucht, C.   +4 more
core   +1 more source

Histochemical approaches to assess cell-to-cell transmission of misfolded proteins in neurodegenerative diseases

European Journal of Histochemistry, 2013
Formation, aggregation and transmission of abnormal proteins are common features in neurodegenerative disorders including Parkinson’s disease, Alzheimer’s disease, amyotrophic lateral sclerosis, and Huntington’s disease. The mechanisms underlying protein
G. Natale, E. Pompili, F. Biagioni, S. Paparelli, P. Lenzi, F. Fornai   +5 more
doaj   +1 more source

Therapeutic Impact of GLP‐1 Receptor Agonists on Parkinson's Disease: A Scoping Review

Neurology and Clinical Neuroscience, EarlyView.
ABSTRACT No disease‐modifying treatment exists for Parkinson's disease (PD). Glucagon‐like peptide‐1 receptor agonists (GLP‐1 RAs) have gained attention as promising candidates for neuroprotection, given documented expression of GLP‐1 receptors within the central nervous system and the contribution of brain insulin resistance to dopaminergic ...
João Pedro Henriques, João Pedro Stringhetta Rahal, Rafael da Cunha Gomes Ribeiro, Enzo Bogucheski Ribeiro Machado, Carlos Antonio Negrato   +4 more
wiley   +1 more source

Gene expression profiling en association with prion-related lesions in the medulla oblongata of symptomatic natural scrapie animals. [PDF]

, 2011
The pathogenesis of natural scrapie and other prion diseases remains unclear. Examining transcriptome variations in infected versus control animals may highlight new genes potentially involved in some of the molecular mechanisms of prion-induced ...
Bossers, A., Rosa Bolea, Hicham Filali, Varona, L., Filalil, Hicham, Harders, F., Inmaculada Martin-Burriel, Alex Bossers, Zaragoza, P., Badiola, J.J., Juan J. Badiola, Bossers, Alex, Pumarola i Batlle, Martí, Lyahyai, Jaber, Lyahyai, J., Martín Burriel, Inmaculada, Pilar Zaragoza, Juan J Badiola, Bolea, Rosa, Filali, H., Bolea, R., Acín, Cristina, Luis Varona, Frank Harders, Filali, Hicham, Pumarola, M., Harders, Frank, Zaragoza, Pilar, Badiola, Juan J, Varona, Luis, Martí Pumarola, Jaber Lyahyai, Martin-Burriel, I., Badiola, Juan José, Pumarola, Martí   +34 more
core   +2 more sources

Neuroinflammation, Microglia, and Cell-Association during Prion Disease

Viruses, 2019
Prion disorders are transmissible diseases caused by a proteinaceous infectious agent that can infect the lymphatic and nervous systems. The clinical features of prion diseases can vary, but common hallmarks in the central nervous system (CNS) are ...
James A. Carroll, Bruce Chesebro
doaj   +1 more source

Polypeptides derived from α-Synuclein binding partners to prevent α-Synuclein fibrils interaction with and take-up by cells.

PLoS ONE, 2020
α-Synuclein (αSyn) fibrils spread from one neuronal cell to another. This prion-like phenomenon is believed to contribute to the progression of the pathology in Parkinson's disease and other synucleinopathies. The binding of αSyn fibrils originating from
Elodie Monsellier, Maya Bendifallah, Virginie Redeker, Ronald Melki   +3 more
doaj   +1 more source

Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Prions are infectious proteins that bear misfolded conformations capable of converting folded states into misfolded aggregates under physiologically relevant conditions. In mammals, prions cause deadly maladies including Creutzfeldt‐Jakob and chronic wasting disease. To date, several prion proteins have been identified in eukaryotes, primarily
Katherine Shreeve, Jinoh Jang, Mridula Srivathsan, Siyu Li, Taylor D. Scott, Silvia Cavagnero   +5 more
wiley   +1 more source

The presence of valine at residue 129 in human prion protein accelerates amyloid formation [PDF]

, 2005
The polymorphism at residue 129 of the human PRNP gene modulates disease susceptibility and the clinicopathological phenotypes in human transmissible spongiform encephalopathies.
Tahiri-Alaoui, Abdessamad, Gill, A, Shaw, Michael, Shaw, M, Baskakov, I, Breydo, L, James, W, Tahiri-Alaoui, A, Disterer, Petra, Gill, Andrew, Baskakov, Ilia, Breydo, Leonid, Disterer, P, James, William   +13 more
core   +1 more source