Results 21 to 30 of about 50,252 (279)

Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid β protein

open access: yesBMC Cell Biology, 2005
Background The amyloid precursor protein (APP) is transported via the secretory pathway to the cell surface, where it may be cleaved within its ectodomain by α-secretase, or internalized within clathrin-coated vesicles. An alternative proteolytic pathway
Lopez-Coviella Ignacio   +3 more
doaj   +1 more source

Penetration into Cancer Cells via Clathrin-Dependent Mechanism Allows L-Asparaginase from Rhodospirillum rubrum to Inhibit Telomerase

open access: yesPharmaceuticals, 2020
The anticancer effect of L-asparaginases (L-ASNases) is attributable to their ability to hydrolyze L-asparagine in the bloodstream and cancer cell microenvironment.
Anna A. Plyasova   +7 more
doaj   +1 more source

Defects in expression of genes related to synaptic vesicle traffickingin frontal cortex of Alzheimer’s disease

open access: yesNeurobiology of Disease, 2003
Loss of synapses correlates with cognitive decline in Alzheimer’s disease (AD). However, molecular mechanisms underlying the synaptic dysfunction and loss are not well understood.
Pamela J Yao   +6 more
doaj   +1 more source

Structure and function of bacterial dynamin-like proteins [PDF]

open access: yes, 2012
Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core   +1 more source

Autism and mild epilepsy associated with a de novo missense pathogenic variant in the GTPase effector domain of DNM1

open access: yesAmerican Journal of Medical Genetics Part C: Seminars in Medical Genetics, EarlyView., 2023
Abstract Dynamin 1 is a GTPase protein involved in synaptic vesicle fission, which facilitates the exocytosis of neurotransmitters necessary for normal signaling. Pathogenic variants in the DNM1 gene are associated with intractable epilepsy, often manifested as infantile spasms at onset, developmental delay, and a movement disorder, and are located in ...
Davide Mei   +4 more
wiley   +1 more source

Smed-dynA-1 is a planarian nervous system specific dynamin 1 homolog required for normal locomotion

open access: yesBiology Open, 2014
Dynamins are GTPases that are required for separation of vesicles from the plasma membrane and thus are key regulators of endocytosis in eukaryotic cells. This role for dynamin proteins is especially crucial for the proper function of neurons, where they
Jared A. Talbot   +3 more
doaj   +1 more source

Dynamin Is Functionally Coupled to Insulin Granule Exocytosis [PDF]

open access: yes, 2007
The insulin granule integral membrane protein marker phogrin-green fluorescent protein was co-localized with insulin in Min6B1 beta-cell secretory granules but did not undergo plasma membrane translocation following glucose stimulation.
Gaisano, HY   +7 more
core   +2 more sources

Surface expression and limited proteolysis of ADAM10 are increased by a dominant negative inhibitor of dynamin

open access: yesBMC Cell Biology, 2011
Background The amyloid precursor protein (APP) is cleaved by β- and γ-secretases to generate toxic amyloid β (Aβ) peptides. Alternatively, α-secretases cleave APP within the Aβ domain, precluding Aβ formation and releasing the soluble ectodomain, sAPPα ...
Slack Barbara E   +2 more
doaj   +1 more source

Dynamin‐mediated lipid acquisition is essential for Chlamydia trachomatis development [PDF]

open access: yesMolecular Microbiology, 2014
SummaryChlamydia trachomatis is an obligate intracellular pathogen responsible for a high burden of human disease. Here, a loss‐of‐function screen using a set of lentivirally transduced shRNAs identified 14 human host cell factors that modulate C. trachomatis infectivity. Notably, knockdown of dynamin, a host GTPase, decreased C.
Gurumurthy, R.   +7 more
openaire   +3 more sources

Isoaspartate accumulation in mouse brain is associated with altered patterns of protein phosphorylation and acetylation, some of which are highly sex-dependent. [PDF]

open access: yesPLoS ONE, 2013
Isoaspartate (isoAsp) formation is a major source of protein damage that is kept in check by the repair function of protein L-isoaspartyl methyltransferase (PIMT).
Zhenxia Qin   +4 more
doaj   +1 more source

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