Results 41 to 50 of about 33,531 (157)

Integrated genomics and proteomics define huntingtin CAG length-dependent networks in mice. [PDF]

, 2016
To gain insight into how mutant huntingtin (mHtt) CAG repeat length modifies Huntington's disease (HD) pathogenesis, we profiled mRNA in over 600 brain and peripheral tissue samples from HD knock-in mice with increasing CAG repeat lengths.
A Dobin, A Hodges, A Kuhn, A Pal, A Reiner, A Valencia, Andreas Tebbe, B Zhang, B Zhang, BM Bolstad, C Zuccato, CA Ross, Christoph Schaab, Daniel J Lavery, David Howland, DI Shirasaki, Doxa Chatzopoulou, DV Zaykin, EH Aylward, Eliana Marisa Ramos, ES Deneris, ES Lein, Fuying Gao, G Fishell, GA Smith, Giovanni Coppola, HT Orr, I Al-Ramahi, IS Seong, Ismael Al-Ramahi, J Cox, J Cox, J Labbadia, JA Miller, JC Jacobsen, JE Phillips, Jeffrey P Cantle, Jeffrey S Aaronson, JF Gusella, JF Gusella, Jim Rosinski, JM Dowen, JM Van Raamsdonk, JP Vonsattel, Juan Botas, K Becanovic, K Monahan, K Sharma, Karla El-Zein, LB Menalled, LB Menalled, LB Menalled, LS Kaltenbach, M Biagioli, M Heiman, M MACDONALD, M Mann, M Mielcarek, MA Pouladi, MC Oldham, MI Love, MK Lobo, MT Lin, N Wang, Nan Wang, P Giles, P Grange, P Langfelder, P Langfelder, P Langfelder, P Langfelder, P Langfelder, Peter Langfelder, PF Durrenberger, RC Gentleman, S Anders, S Horvath, S Toyoda, Sandeep Deverasetty, Seung Kwak, Steve Horvath, T Geiger, T Lu, WE Johnson, WV Chen, X Gu, X Gu, X William Yang, XH Lu, Xiao-Hong Lu, Y Benjamini, Y Guo, Y Shen, Y Wang, Yining Zhao   +94 more
core   +1 more source

The Potential for Extracellular Vesicles in Nanomedicine: A Review of Recent Advancements and Challenges Ahead

Advanced Biology, EarlyView.
Extracellular vesicles (EVs) play a dual role in diagnostics and therapeutics, offering innovative solutions for treating cancer, cardiovascular, neurodegenerative, and orthopedic diseases. This review highlights EVs’ potential to revolutionize personalized medicine through specific applications in disease detection and treatment.
Farbod Ebrahimi, Anjali Kumari, Samaneh Ghadami, Saqer Al Abdullah, Kristen Dellinger   +4 more
wiley   +1 more source

Effects of flanking sequences and cellular context on subcellular behavior and pathology of mutant HTT [PDF]

, 2020
Huntington’s disease (HD) is caused by an expansion of a poly glutamine (polyQ) stretch in the huntingtin protein (HTT) that is necessary to cause pathology and formation of HTT aggregates.
Agrawal, Namita, Barbaro, Brett A., Bornemann, Douglas J., Burke, John, Chin, Theodore M., Chongtham, Anjalika, Lukacsovich, Tamas, Marsh, J. Lawrence, Purcell, Judith, Syed, Adeela, Worthge, Shane   +10 more
core  

PAK in Alzheimer disease, Huntington disease and X-linked mental retardation. [PDF]

, 2012
Developmental cognitive deficits including X-linked mental retardation (XLMR) can be caused by mutations in P21-activated kinase 3 (PAK3) that disrupt actin dynamics in dendritic spines.
Cole, Greg M, Frautschy, Sally A, Ma, Qiu-Lan, Yang, Fusheng   +3 more
core   +1 more source

Transient Interdomain Interactions Modulate the Monomeric Structural Ensemble and Self‐Assembly of Huntingtin Exon 1

Advanced Science, EarlyView.
Polyglutamine (polyQ) tract expansion (≥ 36 amino acids) within the N‐terminal region of the Huntingtin protein (Httex1) causes Huntington's disease (HD), for which the underlying causes are not well‐understood. The authors performed computer simulations to understand the cause of HD at the molecular level.
Priyesh Mohanty, Tien Minh Phan, Jeetain Mittal   +2 more
wiley   +1 more source

Solving the Amyloid Paradox: Unveiling the Complex Pathogenicity of Amyloid Fibrils

Aggregate, EarlyView.
This review addresses the gap between strong evidence for the involvement of amyloid fibrils in neurodegeneration and the failure of anti‐amyloid therapies, a phenomenon herein termed the “amyloid paradox.” To address this paradox, we provide a comprehensive summary of the current understanding of fibrils' pathogenic properties and mechanisms ...
Maksim I. Sulatsky, Olesya V. Stepanenko, Olga V. Stepanenko, Anna I. Sulatskaya   +3 more
wiley   +1 more source

Fibrillogenesis of Huntingtin and Other Glutamine Containing Proteins [PDF]

, 2012
This chapter focuses on the aggregation of glutamine containing peptides and proteins with an emphasis on huntingtin protein, whose aggregation leads to the development of Huntington's disease. The kinetics that leads to the formation of amyloids, the structure of aggregates of various types and the morphological mechanical properties of amyloid ...
Alexey V. Krasnoslobodtsev, Yuri L. Lyubchenko, Sorin Luca   +2 more
openaire   +3 more sources

Mitochondria and Endoplasmic Reticulum Contact Site as a Regulator of Proteostatic Stress Responses in Neurodegenerative Diseases

BioEssays, EarlyView.
Recent findings indicate that mitochondria‐associated membranes (MAMs), where the endoplasmic reticulum directly contacts the mitochondria, are a novel microdomain essential for cellular homeostasis, including proteostasis. We summarize the disruption of protein homeostasis and MAM alteration in neurodegenerative diseases, then discuss challenges and ...
Seiji Watanabe, Koji Yamanaka
wiley   +1 more source

The contribution of extracellular RNA and its derived biomaterials in disease management

BMEMat, EarlyView.
The implications of exRNA's biological function and the structural uniqueness of RNA help establish a close connection between RNA, material, and modern medicine. Abstract The RNA found in the circular system is known as extracellular RNA (exRNA). This kind of RNA has been found to play a biological role similar to that of a messenger. They can be used
Yu Wei, Zhangyi Wang, Zixuan Qin, Qianqian Wan, Yutao Li, Franklin R. Tay, Chenyu Wang, Tong Zhang, Lina Niu   +8 more
wiley   +1 more source

Alteration in Fluidity of Cell Plasma Membrane in Huntington Disease Revealed by Spectral Phasor Analysis. [PDF]

, 2018
Huntington disease (HD) is a late-onset genetic neurodegenerative disorder caused by expansion of cytosine-adenine-guanine (CAG) trinucleotide in the exon 1 of the gene encoding the polyglutamine (polyQ).
Digman, Michelle A, Malacrida, Leonel, Sameni, Sara, Tan, Zhiqun   +3 more
core   +2 more sources