Results 31 to 40 of about 477,265 (189)

The PI3K/Akt signaling pathway regulates the expression of Hsp70, which critically contributes to Hsp90-chaperone function and tumor cell survival in multiple myeloma

open access: yesHaematologica, 2013
Despite therapeutic advances multiple myeloma remains largely incurable, and novel therapeutic concepts are needed. The Hsp90-chaperone is a reasonable therapeutic target, because it maintains oncogenic signaling of multiple deregulated pathways. However,
Manik Chatterjee   +10 more
doaj   +1 more source

In Vitro and In Vivo Chaperone Effect of (R)-2-amino-6-(1R, 2S)-1,2-dihydroxypropyl)-5,6,7,8-tetrahydropterin-4(3H)-one on the C1473G Mutant Tryptophan Hydroxylase 2

open access: yesBiomolecules, 2023
Tryptophan hydroxylase 2 (TPH2) is the key and rate-limiting enzyme of serotonin (5-HT) synthesis in the mammalian brain. The 1473G mutation in the Tph2 gene decreases TPH2 activity in the mouse brain by twofold.
Alla B. Arefieva   +4 more
doaj   +1 more source

Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis

open access: yesFrontiers in Cellular Neuroscience, 2017
The functional unit for inter-neuronal communication in the central nervous system is the neuronal synapse. The number of postsynaptic neurotransmitter receptors at the cell surface is an important determinant of synaptic efficacy and plasticity.
Nancy J. Leidenheimer
doaj   +1 more source

The development and use of small molecule inhibitors of glycosphingolipid metabolism for lysosomal storage diseases

open access: yesJournal of Lipid Research, 2014
Glycosphingolipid (GSL) storage diseases have been the focus of efforts to develop small molecule therapeutics from design, experimental proof of concept studies, and clinical trials.
James A. Shayman, Scott D. Larsen
doaj   +1 more source

ZMYND10 functions in a chaperone relay during axonemal dynein assembly

open access: yeseLife, 2018
Molecular chaperones promote the folding and macromolecular assembly of a diverse set of ‘client’ proteins. How ubiquitous chaperone machineries direct their activities towards specific sets of substrates is unclear.
Girish R Mali   +15 more
doaj   +1 more source

The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation [PDF]

open access: yes, 2011
Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant ...
Bowman, Andrew   +17 more
core   +1 more source

Pharmacological Chaperones for the Treatment of α-Mannosidosis [PDF]

open access: yesJournal of Medicinal Chemistry, 2019
α-Mannosidosis (AM) results from deficient lysosomal α-mannosidase (LAMAN) activity and subsequent substrate accumulation in the lysosome, leading to severe pathology. Many of the AM-causative mutations compromise enzyme folding and could be rescued with purpose-designed pharmacological chaperones (PCs).
Rocío Rísquez-Cuadro   +6 more
openaire   +5 more sources

Phenylalanine Hydroxylase Misfolding and Pharmacological Chaperones [PDF]

open access: yesCurrent Topics in Medicinal Chemistry, 2013
Phenylketonuria (PKU) is a loss-of-function inborn error of metabolism. As many other inherited diseases the main pathologic mechanism in PKU is an enhanced tendency of the mutant phenylalanine hydroxylase (PAH) to misfold and undergo ubiquitin-dependent degradation. Recent alternative approaches with therapeutic potential for PKU aim at correcting the
Underhaug, Jarl   +2 more
openaire   +2 more sources

Pharmacological Chaperone Design for Reducing Risk Factor of Parkinson’s Disease from Traditional Chinese Medicine [PDF]

open access: yes, 2015
Dysfunction of β-glucocerebrosidase (GCase) has no hydrolytic activity in patients of Gaucher's disease and increasing the risk factor for Parkinson’s disease occurrence.
Chen, Calvin Yu-Chian   +2 more
core   +1 more source

Chaperone/usher machinery [PDF]

open access: yes, 2012
Many virulence organelles of Gram-negative bacterial pathogens are assembled via the periplasmic chaperone/usher (CU) pathway. The assembly process is a complex task, involving secretion of organelle subunits via the two membranes and periplasm, subunit ...
Yu, Xiaodi
core   +1 more source

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