Results 31 to 40 of about 190,260 (351)

Probing GPCR Dimerization Using Peptides

Frontiers in Endocrinology, 2022
G protein-coupled receptors (GPCRs) are the largest class of membrane proteins and the most common and extensively studied pharmacological target. Numerous studies over the last decade have confirmed that GPCRs do not only exist and function in their ...
Zara Farooq, Zara Farooq, Lesley A. Howell, Peter J. McCormick   +3 more
doaj   +1 more source

Role of Oligomeric Proanthocyanidins Derived from an Extract of Persimmon Fruits in the Oxidative Stress-Related Aging Process

Molecules, 2014
Many researchers have focused on the oligomeric form of proanthocyanidins with a lower level of polymerization found in foodstuffs such as grape seeds and blackberries.
Takako Yokozawa, Chan Hum Park, Jeong Sook Noh, Seong Soo Roh   +3 more
doaj   +1 more source

Synthesis and Antibacterial Properties of Oligomeric Dehydrogenation Polymer from Lignin Precursors

Molecules, 2022
The lignin precursors of coniferin and syringin were synthesised, and guaiacyl-type and guaiacyl-syringyl-type oligomeric lignin dehydrogenation polymers (DHP and DHP-GS) were prepared with the bulk method.
Xin Wei, Sheng Cui, Yimin Xie
doaj   +1 more source

Toxic oligomer species of amyloid-β in Alzheimer's disease, a timing issue

Swiss Medical Weekly, 2014
A decade following the paradigm-shifting concept that endogenous forms of soluble, non-fibrillar amyloid-β (Aβ) might constitute the major bioactive entity causing synaptic loss and cognitive decline in Alzheimer’s disease (AD), our understanding ...
Sylvain E. Lesne
doaj   +1 more source

Rational Generation of Monoclonal Antibodies Selective for Pathogenic Forms of Alpha-Synuclein

Biomedicines, 2022
Misfolded toxic forms of alpha-synuclein (α-Syn) have been implicated in the pathogenesis of synucleinopathies, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA).
Ebrima Gibbs, Beibei Zhao, Andrei Roman, Steven S. Plotkin, Xubiao Peng, Shawn C. C. Hsueh, Adekunle Aina, Jing Wang, Clay Shyu, Calvin K. Yip, Sung-Eun Nam, Johanne M. Kaplan, Neil R. Cashman   +12 more
doaj   +1 more source

Oligomer size distributions.

, 2023
(A) Oligomer size distribution before the laser irradiation. Averages during (B) 991–1000 pulses, (C) 1991–2000 pulses, and (D) 3991–4000 pulses.
Hisashi Okumura (1743820), Heishun Zen (8847713), Satoru G. Itoh (1772761), Kazuhiro Nakamura (652922)   +3 more
core   +1 more source

Reducing-End Functionalization of 2,5-Anhydro-d-mannofuranose-Linked Chitooligosaccharides by Dioxyamine: Synthesis and Characterization

Molecules, 2020
The nitrous acid depolymerization of chitosan enables the synthesis of singular chitosan oligosaccharides (COS) since their reducing-end unit is composed of 2,5-anhydro-d-mannofuranose (amf).
Maxence Coudurier, Jimmy Faivre, Agnès Crépet, Catherine Ladavière, Thierry Delair, Christophe Schatz, Stéphane Trombotto   +6 more
doaj   +1 more source

Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer’s Disease

Molecules, 2022
The brains of Alzheimer’s disease (AD) patients contain numerous amyloid plaques that are diagnostic of the disease. The plaques are primarily composed of the amyloidogenic peptides proteins Aβ40 and Aβ42, which are derived by the processing of the ...
Terrone L. Rosenberry, Huan-Xiang Zhou, Scott M. Stagg, Anant K. Paravastu   +3 more
doaj   +1 more source

GalaxyHomomer: a web server for protein homo-oligomer structure prediction from a monomer sequence or structure

Nucleic Acids Res., 2017
Homo-oligomerization of proteins is abundant in nature, and is often intimately related with the physiological functions of proteins, such as in metabolism, signal transduction or immunity.
M. Baek, Taeyong Park, Lim Heo, Chiwook Park, Chaok Seok   +4 more
semanticscholar   +1 more source

Three Structural Features of Functional Food Components and Herbal Medicine with Amyloid β42 Anti-Aggregation Properties

Molecules, 2019
Aggregation of amyloid β42 (Aβ42) is one of the hallmarks of Alzheimer’s disease (AD). There are numerous naturally occurring products that suppress the aggregation of Aβ42, but the underlying mechanisms remain to be elucidated ...
Kazuma Murakami, Kazuhiro Irie
doaj   +1 more source